|
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 ... |
95-764 |
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: 1372.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVASSHKSKKD---QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDhniPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 332 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 492 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 651
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 652 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 731
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 29436380 732 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-764 |
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: 1355.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 334
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 335 EQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 414
Cdd:cd14919 241 EQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 415 EALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 494
Cdd:cd14919 321 EALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 495 EGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCIIHYA 574
Cdd:cd14919 401 EGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCIIHYA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 575 GKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQL 654
Cdd:cd14919 481 GKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 655 AKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFM 734
Cdd:cd14919 561 AKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFM 640
|
650 660 670
....*....|....*....|....*....|
gi 29436380 735 DGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14919 641 DGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
95-764 |
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: 1344.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVASSHKSKKD----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKEsgkkKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYR-FLSNGHVTIPGQQDKDMFQETMEAMRIM 329
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 330 GIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQ 409
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 410 ADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 490 EEYQREGIEWNFIDFGLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPK-FQKPKQLKDKADF 568
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmsETALPGAFKTRKGMFRTVGQ 648
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 649 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 728
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 29436380 729 IPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01377 627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-764 |
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: 1320.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQ-------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 247
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQssialshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 248 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 408 EQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKAD 567
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSEtALPGAFKTRKGMFRTVG 647
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGE-SLHGAFKTRKGMFRTVG 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14932 560 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 29436380 728 SIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14932 640 AIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
95-764 |
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: 1262.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQ-------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 247
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQnslalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 248 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 408 EQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKAD 567
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSEtaLPGAFKTRKGMFRTVG 647
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 638
|
650 660 670
....*....|....*....|....*....|....*..
gi 29436380 728 SIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd15896 639 AIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
95-764 |
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: 1218.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 332 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 492 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYK 651
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 652 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 731
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 29436380 732 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
95-764 |
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: 1158.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVASShKSKKD-------------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 241
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSgavphpavnpavlIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 242 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQE 321
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 322 TMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYV 401
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 481
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 482 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKpKQ 561
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 562 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDrIIGLDQVAgMSETALpGAfKTRKG 641
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQF-GA-RTRKG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 642 MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 721
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 29436380 722 EILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14911 632 ELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
95-764 |
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: 1143.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQG---ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQdKDMFQETMEAMRIMGI 331
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 332 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 492 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14930 400 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETalPGAFKTRKGMFRTVGQLYK 651
Cdd:cd14930 480 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDG--PPGGRPRRGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 652 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 731
Cdd:cd14930 558 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 29436380 732 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14930 638 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
83-764 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1123.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 83 VEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMM 162
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 163 QDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKdQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 242
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN-VGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 243 FDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN-GHVTIPGQQDKDMFQE 321
Cdd:pfam00063 160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYTIDGIDDSEEFKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 322 TMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYV 401
Cdd:pfam00063 240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 481
Cdd:pfam00063 320 SKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 482 HTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQ 561
Cdd:pfam00063 400 HHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKPRL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 562 lKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVagmsETALPGAFKTRKG 641
Cdd:pfam00063 477 -QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAAN----ESGKSTPKRTKKK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 642 MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 721
Cdd:pfam00063 552 RFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 29436380 722 EILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:pfam00063 632 RILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
76-776 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 1025.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 76 NPPKFSKVEDMAELTCLNEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITD 155
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 156 TAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKkdqGELERQLLQANPILEAFGNAKTVKNDNSSRF 235
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV---GSVEDQILESNPILEAFGNAKTLRNNNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 236 GKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQ 314
Cdd:smart00242 158 GKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGcLTVDGID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 315 DKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNT-AAQKVSHLLGINVTDFTRGILTPR 393
Cdd:smart00242 238 DAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALTKRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 394 IKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTN 473
Cdd:smart00242 318 IKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNSFEQLCINYAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 474 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTH 553
Cdd:smart00242 397 EKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEKK--PPGILSLLDEECRFPKGTDQTFLEKLNQHHKKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 554 PKFQKPKQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqvagmsetalp 633
Cdd:smart00242 474 PHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG------------------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 634 GAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVV 713
Cdd:smart00242 535 VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLP 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29436380 714 FQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFRAGVLAHLEEERD 776
Cdd:smart00242 615 FDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
32-1151 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 927.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 32 VWVPSDKSGFEPASLKEEVGEEAIVEL---VENGKKVKVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKERYY 106
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEegkKEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 107 SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKK 186
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 187 VIQYLAYVASSHKSkkDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIR 266
Cdd:COG5022 172 IMQYLASVTSSSTV--EISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 267 QAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVT-IPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISG 345
Cdd:COG5022 250 QNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 346 VLQLGNIVFKKERNtDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERM 425
Cdd:COG5022 330 ILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNL 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 426 FRWLVLRINKALDKTKRQGaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFg 505
Cdd:COG5022 409 FDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY- 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 506 LDLQPCIDLIEKpAGPPGILALLDEECWFPKATDKSFVEKVMQ--EQGTHPKFQKPKQLKDKadFCIIHYAGKVDYKADE 583
Cdd:COG5022 487 FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVKHYAGDVEYDVEG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 584 WLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIigldqvagmsetalpgafkTRKGMFRTVGQLYKEQLAKLMATLRN 663
Cdd:COG5022 564 FLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENI-------------------ESKGRFPTLGSRFKESLNSLMSTLNS 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 664 TNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS----IPKGFMDGKQA 739
Cdd:COG5022 625 TQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNA 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 740 CVLMIKALELDSNLYRIGQSKVFFRAGVLAHLEEERDLKITDVIIGFQACCRGYLARKAFAKRQQQLTAMKVLQRNCAAY 819
Cdd:COG5022 705 VKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLR 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 820 LKLRNWQWWRLFTKVKPLLQVSRQEEEMMAKEEElvkVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLqaetelcAEA 899
Cdd:COG5022 785 RLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLAC---IIKLQKTIKREKKLRETEEVEFSLKAEVLIQKF-------GRS 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 900 EELRAR-LTAKKQELEEIChdlEARVEEEEERCQHLQAEKKKMQQniqeleeqleeeeSARQKLQLEKVTTEAKLKKLEE 978
Cdd:COG5022 855 LKAKKRfSLLKKETIYLQS---AQRVELAERQLQELKIDVKSISS-------------LKLVNLELESEIIELKKSLSSD 918
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 979 EQIILEDQNCKLAKEKKLL------EDRIAEFTTNLTEEE--EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTR 1050
Cdd:COG5022 919 LIENLEFKTELIARLKKLLnnidleEGPSIEYVKLPELNKlhEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFK 998
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1051 RKLegdsTDLSDQIAELQAQIAELKmQLAKKEEELQAALARVEEEAAQKNMaLKKIRELESQISELQEDLEseraSRNKA 1130
Cdd:COG5022 999 KEL----AELSKQYGALQESTKQLK-ELPVEVAELQSASKIISSESTELSI-LKPLQKLKGLLLLENNQLQ----ARYKA 1068
|
1130 1140
....*....|....*....|.
gi 29436380 1131 EKQKRDLGEELEALKTELEDT 1151
Cdd:COG5022 1069 LKLRRENSLLDDKQLYQLEST 1089
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
95-764 |
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: 883.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRH-EMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 174 GESGAGKTENTKKVIQYLAYVASSHKSKKD--QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSssASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL-----SNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd00124 161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNT--DQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 404
Cdd:cd00124 241 DVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 405 QTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQ-GASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd00124 321 LTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 484 MFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLK 563
Cdd:cd00124 401 VFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 564 DKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDkfvselwkdvdriigldqvagmsetalpgafktrkgmf 643
Cdd:cd00124 478 KLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ-------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 644 rtvgqlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd00124 519 ------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRI 592
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 29436380 724 LTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd00124 593 LAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
95-764 |
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: 790.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVAS---------SHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 245
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAAlgdgpgkkaQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 246 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETM 323
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVsmNPYD-YHFCSQGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 324 EAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQK 403
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 404 AQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 484 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKP--- 559
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPrpd 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 560 KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqVAGMSETALPGAFKTR 639
Cdd:cd14927 476 KKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY--------VGSDSTEDPKSGVKEK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 640 K---GMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQE 716
Cdd:cd14927 548 RkkaASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAD 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 29436380 717 FRQRYEILTPNSIPK-GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14927 628 FKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
96-764 |
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: 767.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 176 SGAGKTENTKKVIQYLAYVASS-----HKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdlakKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRI 328
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLIttNPYD-YPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 329 MGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 408 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVM-QEQGTHPKFQKPKQLKDKA 566
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGRA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 567 D--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqVAGMSETALPGAFKTRKG-MF 643
Cdd:cd14913 476 EahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT---------FATADADSGKKKVAKKKGsSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 644 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd14913 547 QTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRV 626
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 29436380 724 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14913 627 LNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
95-764 |
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: 760.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVASSHKSKKD-QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDgKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNK-YRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKeYHWVSQGVTVVDNMDDGEELQITDVAFDVLGFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 333 EEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 412
Cdd:cd14934 241 AEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCNN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 413 AIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 492
Cdd:cd14934 321 SIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 493 QREGIEWNFIDFGLDLQPCIDLIEKPAGppgILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKDK---ADF 568
Cdd:cd14934 400 KREGIEWVFIDFGLDLQACIDLLEKPMG---IFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGKgpeAHF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSdkfvselwkdvdriIGLDQVAGMSETALPGAFKTRKGM-FRTVG 647
Cdd:cd14934 477 ELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS--------------LGLLALLFKEEEAPAGSKKQKRGSsFMTVS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14934 543 NFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPN 622
|
650 660 670
....*....|....*....|....*....|....*..
gi 29436380 728 SIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14934 623 VIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
95-764 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 758.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQ---GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAkskGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL-EPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMG 330
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 331 IPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 410
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 411 DFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 490
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 491 EYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLK---DKA 566
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 567 DFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiGLDQVAGMSETAlpGAFKTRKGMFRTV 646
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD-----HAGQSGGGEQAK--GGRGKKGGGFATV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 647 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd14909 550 SSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNP 629
|
650 660 670
....*....|....*....|....*....|....*...
gi 29436380 727 NSIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14909 630 AGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
95-764 |
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: 732.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEhlKTDLLLEPYN--KYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14929 161 DIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEELLATEQAMDILGFL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 333 EEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 412
Cdd:cd14929 239 PDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 413 AIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 492
Cdd:cd14929 319 AVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 493 QREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKDK--ADFC 569
Cdd:cd14929 398 RKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKKfeAHFE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGmseTALPGAFKTRK--GMFRTVG 647
Cdd:cd14929 475 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YISTD---SAIQFGEKKRKkgASFQTVA 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14929 545 SLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPR 624
|
650 660 670
....*....|....*....|....*....|....*...
gi 29436380 728 SIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14929 625 TFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
841-1372 |
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: 724.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 841 SRQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDL 920
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 921 EARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDR 1000
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1001 IAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAK 1080
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1081 KEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE 1160
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1161 LRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGK 1240
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1241 GDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEE 1320
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 29436380 1321 NRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKK 1372
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK 532
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
96-764 |
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: 719.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 176 SGAGKTENTKKVIQYLAYVAS-SHKSKKDQ----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQtpgkGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRI 328
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItnNPYD-YAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 329 MGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 407
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 408 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 487
Cdd:cd14917 320 QQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 488 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKDK- 565
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGKp 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 566 -ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqVAGMSETALPGAFKTRKG-MF 643
Cdd:cd14917 476 eAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN---------YAGADAPIEKGKGKAKKGsSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 644 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd14917 547 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 626
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 29436380 724 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14917 627 LNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
96-764 |
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: 717.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSG-LIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVASSHKSKKdqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET---QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNG-HVTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01380 159 RTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGgSPVIDGVDDAAEFEETRKALTLLGISE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 334 EEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFA 413
Cdd:cd01380 239 EEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 414 IEALAKATYERMFRWLVLRINKALDKTKRQGA-SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 492
Cdd:cd01380 319 RDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 493 QREGIEWNFIDFgLDLQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPK--FQKPKQLKDKadFCI 570
Cdd:cd01380 399 VKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNTA--FIV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 571 IHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSsdkfvselwkdvdriigldqvagmsetalpgafKTRKgmfRTVGQLY 650
Cdd:cd01380 473 KHFADDVEYQVEGFLEKNRDTVSEEHLNVLKAS---------------------------------KNRK---KTVGSQF 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 651 KEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIP 730
Cdd:cd01380 517 RDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEW 596
|
650 660 670
....*....|....*....|....*....|....
gi 29436380 731 KGfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01380 597 LR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
96-764 |
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: 699.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 176 SGAGKTENTKKVIQYLAYVAS-SHKSKKD-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 249
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEnpnanKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 250 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtnNPYD-YAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNTA-AQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 407 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 487 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKDK 565
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 566 --ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldQVAGMSETALPGAFKTRKGMF 643
Cdd:cd14916 476 qeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDSGKGKGGKKKGSSF 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 644 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd14916 549 QTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 628
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 29436380 724 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14916 629 LNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
97-764 |
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: 698.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 97 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGES 176
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 177 GAGKTENTKKVIQYLAYVASSHKSKKD-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIM 329
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 330 GIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKE 408
Cdd:cd14918 242 GFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 409 QADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 489 QEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVM-QEQGTHPKFQKPKQLKDKAD 567
Cdd:cd14918 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 568 --FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldQVAGMSETALPGAfKTRKGMFRT 645
Cdd:cd14918 477 ahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY-------ASAEADSGAKKGA-KKKGSSFQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 646 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 725
Cdd:cd14918 549 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLN 628
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 29436380 726 PNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14918 629 ASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-764 |
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: 697.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 176 SGAGKTENTKKVIQYLAYVASSHKSKKD------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 249
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqpgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 250 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLkTDLLLEPYNKYR--FLSNGHVTIPGQQDKDMFQETMEAMR 327
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 407 KEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 487 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVM-QEQGTHPKFQKPKQLKDK 565
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPAKGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 566 AD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigLDQVAGMSETALPGAfKTRKGMF 643
Cdd:cd14923 476 AEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY-----AGAEAGDSGGSKKGG-KKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 644 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 723
Cdd:cd14923 550 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 29436380 724 LTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14923 630 LNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
96-764 |
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: 691.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 176 SGAGKTENTKKVIQYLAYVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLIttNPYD-YPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 405
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 406 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 486 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVM-QEQGTHPKFQKPKQLKD 564
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKVVKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 565 KAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETAlpgafKTRKGM 642
Cdd:cd14912 476 KAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAKKGG-----KKKGSS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 643 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14912 551 FQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 630
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 29436380 723 ILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14912 631 VLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
96-764 |
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: 687.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 176 SGAGKTENTKKVIQYLAYVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 405
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 406 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd14910 320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 486 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKD 564
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 565 K--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigldqvAGMSETALPGAFK--TRK 640
Cdd:cd14910 476 KveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSG----------AAAAEAEEGGGKKggKKK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 641 G-MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQ 719
Cdd:cd14910 546 GsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 29436380 720 RYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14910 626 RYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
96-764 |
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: 679.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 176 SGAGKTENTKKVIQYLAYVASSHKskkdqgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 256 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGE--HLKTDLLLEPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14883 156 DYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVLGIP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 333 EEEQMGLLRVISGVLQLGNIVFKK-ERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd14883 236 EEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEAR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 491
Cdd:cd14883 316 DNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 492 YQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCII 571
Cdd:cd14883 395 YEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEFGVK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDrIIGLDQVAGMSETALPGAfKTRKGMfRTVGQLYK 651
Cdd:cd14883 472 HYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGDTTSR-GTSKGK-PTVGDTFK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 652 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 731
Cdd:cd14883 549 HQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSA 628
|
650 660 670
....*....|....*....|....*....|...
gi 29436380 732 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14883 629 DHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
96-764 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 679.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 176 SGAGKTENTKKVIQYLAYVASSHKSKKD-------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAM 326
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLIttNPYD-FAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 405
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 406 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 486 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKD 564
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 565 KAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGMSETALPGAFKTRKGM 642
Cdd:cd14915 476 KAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-------GQTAEAEGGGGKKGGKKKGSS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 643 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14915 549 FQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYK 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 29436380 723 ILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14915 629 VLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
96-764 |
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: 655.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKgkKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 176 SGAGKTENTKKVIQYLAYVASshkskkDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGG------GSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 256 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIMGIPEE 334
Cdd:cd01383 154 TYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHELKEALDTVGISKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 335 EQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 414
Cdd:cd01383 234 DQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 415 EALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 494
Cdd:cd01383 314 DALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYEL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 495 EGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPkqlKDKAdFCIIHYA 574
Cdd:cd01383 394 DGIDWTKVDF-EDNQECLDLIEKK--PLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGE---RGGA-FTIRHYA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 575 GKVDYKADEWLMKNMDPLNDNIATLL----HQSSDKFVSELWKDVDRIigldqvagmsetALPGAFKTRKGMFRTVGQLY 650
Cdd:cd01383 467 GEVTYDTSGFLEKNRDLLHSDLIQLLsscsCQLPQLFASKMLDASRKA------------LPLTKASGSDSQKQSVATKF 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 651 KEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIp 730
Cdd:cd01383 535 KGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV- 613
|
650 660 670
....*....|....*....|....*....|....
gi 29436380 731 KGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01383 614 SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
96-764 |
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: 653.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 176 SGAGKTENTKKVIQYLAYVasshkSKKDQGELER---QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGA 252
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV-----SGGSESEVERvkdMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 253 NIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE-PYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 332 PEEEQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVG---RDYVQKAQTKE 408
Cdd:cd01378 237 TEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 409 QADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd01378 316 QAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 489 QEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFP-KATDKSFVEKVMQEQGTHPKFQKPKQLKD--K 565
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIEEK--PPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 566 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmsetalpgafKTRKGMFRT 645
Cdd:cd01378 473 GEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD-------------------LDSKKRPPT 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 646 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 725
Cdd:cd01378 534 AGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 29436380 726 PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01378 614 PKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
95-764 |
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: 641.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 174 GESGAGKTENTKKVIQYLAYVASshKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGG--RAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd01384 159 IRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELDGVDDAEEYRATRRAMDVVGIS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 333 EEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPD---NTAAQKVSHLLGINVTDFTRGiLTPRIKVGRD-YVQKAQTKE 408
Cdd:cd01384 239 EEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLKAAAELLMCDEKALEDA-LCKRVIVTPDgIITKPLDPD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 409 QADFAIEALAKATYERMFRWLVLRINKAL--DKTKRqgaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd01384 318 AATLSRDALAKTIYSRLFDWLVDKINRSIgqDPNSK---RLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 487 LEQEEYQREGIEWNFIDFgLDLQPCIDLIEKpaGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKqlKDKA 566
Cdd:cd01384 395 MEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LSRT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 567 DFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmsetalPGAFKTRKgmFRTV 646
Cdd:cd01384 470 DFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR---------------EGTSSSSK--FSSI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 647 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd01384 533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAP 612
|
650 660 670
....*....|....*....|....*....|....*...
gi 29436380 727 NsIPKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd01384 613 E-VLKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
95-764 |
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: 620.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVASSHKSkkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHSW------IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01381 155 EQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRDDAAEFADIRSAMKVLMFTD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 334 EEQMGLLRVISGVLQLGNIVFKK--ERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 411
Cdd:cd01381 235 EEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 412 FAIEALAKATYERMFRWLVLRINKALDKTKRQGAS--FIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd01381 315 DVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 490 EEYQREGIEWNFIDFgLDLQPCIDLI-EKPAgppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKAdF 568
Cdd:cd01381 395 EEYDKEGINWQHIEF-VDNQDVLDLIaLKPM---NIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTS-F 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFvselwkdVDRIIGLDQVAGMSetalpgafkTRKgmfR--TV 646
Cdd:cd01381 470 GINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKF-------LKQLFNEDISMGSE---------TRK---KspTL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 647 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd01381 531 SSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP 610
|
650 660 670
....*....|....*....|....*....|....*...
gi 29436380 727 NSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01381 611 GIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
95-764 |
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: 597.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 174 GESGAGKTENTKKVIQYLAYVASSHkskkdQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG-----AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLlepynkyrflsnghvTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01382 156 VSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL---------------KDPLLDDVGDFIRMDKAMKKIGLSD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 334 EEQMGLLRVISGVLQLGNIVFKKERNT-------DQASMPDNTAAqkvSHLLGINVTDF-----TRGILTPRIKVGRDYV 401
Cdd:cd01382 221 EEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYA---AELLGLDQDELrvsltTRVMQTTRGGAKGTVI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKrqGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 481
Cdd:cd01382 298 KVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 482 HTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKP-- 559
Cdd:cd01382 376 ERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPrk 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 560 ------KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagMSETALP 633
Cdd:cd01382 453 sklkihRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTN---------NNKDSKQ 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 634 gafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVV 713
Cdd:cd01382 524 ---KAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTS 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 29436380 714 FQEFRQRYEILTPNSIPKgfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01382 601 FHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
95-764 |
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: 572.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVASShkskkdQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAgeHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSLSGcIEVEGVDDVADFEEVVLAMEQLGFDD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 334 EEQMGLLRVISGVLQLGNIVFKKERNTDQAS---MPDNTAAQKVSHLLGINVTDFTRGILTPRIKV-GRDYVQKAQTKEQ 409
Cdd:cd14872 233 ADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 410 ADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd14872 313 ATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 490 EEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFC 569
Cdd:cd14872 393 ALYQSEGVKFEHIDF-IDNQPVLDLIEKK--QPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRTEFI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvagmsetalpGAFKTRKGmfrTVGQL 649
Cdd:cd14872 470 VKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE-----------------GDQKTSKV---TLGGQ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 650 YKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILtPNSI 729
Cdd:cd14872 530 FRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTI 608
|
650 660 670
....*....|....*....|....*....|....*.
gi 29436380 730 PKGFM-DGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14872 609 AKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
95-764 |
0e+00 |
|
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: 565.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVAsshksKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGANI 254
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN-----QRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVGAIT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNG-HVTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd01387 155 SQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLGFSS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 334 EEQMGLLRVISGVLQLGNIVFKKERNTDQ---ASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQA 410
Cdd:cd01387 235 EEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 411 DFAIEALAKATYERMFRWLVLRINKALDKTKRQGASfIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 490
Cdd:cd01387 315 LDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLS-IAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 491 EYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQlkDKADFCI 570
Cdd:cd01387 394 EYIREQIDWTEIAF-ADNQPVINLISKK--PVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM--PLPEFTI 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 571 IHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriigldQVAGMSETALP----GAFKTRKGMFRTV 646
Cdd:cd01387 469 KHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFS---------SHRAQTDKAPPrlgkGRFVTMKPRTPTV 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 647 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd01387 540 AARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVA 619
|
650 660 670
....*....|....*....|....*....|....*....
gi 29436380 727 NSIPKGfMDGKQACVLMIKALELD-SNLYRIGQSKVFFR 764
Cdd:cd01387 620 LKLPRP-APGDMCVSLLSRLCTVTpKDMYRLGATKVFLR 657
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
95-764 |
0e+00 |
|
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: 562.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQ----DREDQS 169
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 170 ILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQ-------------GELERQLLQANPILEAFGNAKTVKNDNSSRFG 236
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGegeaaseaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 237 KFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK 316
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 317 DMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmpDNTAAQKVSH---LLGINVTDFTRGILTPR 393
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLKLaaeLLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 394 IKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTN 473
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 474 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE-KPAGPPGILALLDeECWFPKAT--DKSFVEKVMQEQ 550
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHASF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 551 GT-------------HPKFQKPKQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSsdkfvselwkdvDR 617
Cdd:cd14890 476 GRksgsggtrrgssqHPHFVHPKFDADK-QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQS------------RR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 618 IIgldqvAGMSetalpgafktrkgmfrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGV 697
Cdd:cd14890 543 SI-----REVS-----------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGM 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29436380 698 LEGIRICRQGFPNRVVFQEFRQRYEILTPNSipkgfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14890 601 MEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
95-762 |
3.52e-180 |
|
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: 549.01 E-value: 3.52e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY------KGKKRHEMPPHIYAITDTAYRSMMQDRE-- 166
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 167 --DQSILCTGESGAGKTENTKKVIQYLAYVASshKSKKDQGELER-----QLLQANPILEAFGNAKTVKNDNSSRFGKFI 239
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS--ATTHGQNATERenvrdRVLESNPILEAFGNARTNRNNNSSRFGKFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 240 RINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHVTIPGQQDKD 317
Cdd:cd14901 159 RLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVDDSV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 318 MFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVF-KKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKV 396
Cdd:cd14901 239 QYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 397 GRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAS-FIGILDIAGFEIFDLNSFEQLCINYTNEK 475
Cdd:cd14901 319 GGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFANEK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 476 LQQLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVMQEQG 551
Cdd:cd14901 399 LQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 552 THPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSElwkdvdriigldqvagmseta 631
Cdd:cd14901 472 KHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS--------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 632 lpgafktrkgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNR 711
Cdd:cd14901 531 -------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVR 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 29436380 712 VVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNL-----YRIGQSKVF 762
Cdd:cd14901 598 FPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIehlppFQVGKTKVF 653
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
95-764 |
9.96e-180 |
|
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: 548.22 E-value: 9.96e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 174 GESGAGKTENTKKVIQYLAYVAsshkskkdqGELE----RQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 249
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA---------GGLNdstiKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 250 VGANIETYLLEKSRAIRQAKEERTFHIFYYLLsgAGEHLKTDLLLEPYNKYRFL-SNGHVTIPGQQDKDMFQETMEAMRI 328
Cdd:cd14903 152 VGAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGMSDRKHFARTKEALSL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 329 MGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASM--PDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14903 230 IGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 407 KEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:cd14903 310 KDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 487 LEQEEYQREGIEWNFIDFgLDLQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKVMqeqGTHPKFQK----PKql 562
Cdd:cd14903 389 TVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefPR-- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdrIIGLDQVAGMSETALPGAFKTRKGM 642
Cdd:cd14903 460 TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGARRRRGGALT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 643 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14903 537 TTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFW 616
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 29436380 723 ILTPNSiPKGFMDGKQACVLMIKALELDS-NLYRIGQSKVFFR 764
Cdd:cd14903 617 LFLPEG-RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
95-764 |
4.51e-178 |
|
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: 545.05 E-value: 4.51e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVasshkSKKDQGE-LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01385 81 ESGSGKTESTNFLLHHLTAL-----SQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHvTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd01385 156 VEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLnqSDCY-TLEGEDEKYEFERLKQAMEMVGF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 332 PEEEQMGLLRVISGVLQLGNIVFKKER-NTDQASMPDNTAAQK-VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQ 409
Cdd:cd01385 235 LPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDiISELLRVKEETLLEALTTKKTVTVGETLILPYKLPE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 410 ADFAIEALAKATYERMFRWLVLRINKAL----DKTKRQGASfIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 485
Cdd:cd01385 315 AIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 486 ILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPkQLKDK 565
Cdd:cd01385 394 KLEQEEYKKEGISWHNIEY-TDNTGCLQLISKK--PTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKP-QVMEP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 566 AdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdvdriIGLDQVAGMSETALPGAFKT-----RK 640
Cdd:cd01385 470 A-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVAVFRWAVLRAFFRAmaafrEA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 641 GMFR-----------------------------TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQ 691
Cdd:cd01385 542 GRRRaqrtaghsltlhdrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQ 621
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29436380 692 LRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILtpnsIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd01385 622 LRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
95-764 |
1.29e-175 |
|
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: 536.58 E-value: 1.29e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKK-RHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 174 GESGAGKTENTKKVIQYLayvasSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14897 81 GESGAGKTESTKYMIKHL-----MKLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQD-------KDMFQETMEAM 326
Cdd:cd14897 156 IDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseeleyyRQMFHDLTNIM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14897 236 KLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 407 KEQADFAIEALAKATYERMFRWLVLRINKAL----DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 482
Cdd:cd14897 316 LRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFND 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 483 TMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKql 562
Cdd:cd14897 396 YVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFKK--PLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASP-- 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriigldqvagmsetalpgafktrkgm 642
Cdd:cd14897 471 GNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT----------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 643 frtvgQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14897 522 -----SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYK 596
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 29436380 723 ILTPNSiPKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd14897 597 EICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
96-764 |
3.44e-175 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 535.32 E-value: 3.44e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 176 SGAGKTENTKKVIQYLAYVasshkSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-----GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 256 TYLLEKSRAIRQAKEERTFHIFYYLLSG-AGEHLKTDLLLEPYNKYRFLSNGHVTIPG----QQDKDMFQETMEAMRIMG 330
Cdd:cd01379 157 EYLLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLPENKPPRYLQNDGLTVQDivnnSGNREKFEEIEQCFKVIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 331 IPEEEQMGLLRVISGVLQLGNIVFK---KERNTDQASM-PDNTAAQKVSHLLGINVTDFtRGILTPRIKVGR-DYVQKAQ 405
Cdd:cd01379 237 FTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRiSNPEALNNVAKLLGIEADEL-QEALTSHSVVTRgETIIRNN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 406 TKEQADFAIEALAKATYERMFRWLVLRINKAL--DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd01379 316 TVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 484 MFILEQEEYQREGIEWNFIDFGlDLQPCID-LIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQGTHPkFQKPKql 562
Cdd:cd01379 396 IFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKSKY-YWRPK-- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSElwkdvdriigldqvagmsetalpgafktrkgm 642
Cdd:cd01379 469 SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ-------------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 643 frTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd01379 517 --TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYY 594
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 29436380 723 ILTPNSIPKGFMDgKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd01379 595 FLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
95-764 |
5.20e-173 |
|
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: 530.14 E-value: 5.20e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 174 GESGAGKTENTKKVIQYLAYVASSH---KSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 250
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSlelSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIM 329
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 330 GIPEEEQMGLLRVISGVLQLGNIVFKkerNTDQASMPDNTAAQKVSHLLGINVTDFTRgILTPRIKVGR-DYVQKAQTKE 408
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTD-ALTQRSMFLRgEEILTPLNVQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 409 QADFAIEALAKATYERMFRWLVLRINKALdkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd14873 317 QAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 489 QEEYQREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDkaDF 568
Cdd:cd14873 395 QLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVN--NF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 569 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWkdvdriiglDQVAGMSETALPGAFKTRKGmfRTVGQ 648
Cdd:cd14873 469 GVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF---------EHVSSRNNQDTLKCGSKHRR--PTVSS 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 649 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 728
Cdd:cd14873 538 QFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL 617
|
650 660 670
....*....|....*....|....*....|....*.
gi 29436380 729 IPKGFMDGKqaCVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14873 618 ALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
95-764 |
1.64e-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: 528.95 E-value: 1.64e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEM---PPHIYAITDTAYRSMMQDR----ED 167
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 168 QSILCTGESGAGKTENTKKVIQYLA----YVASSHKSKKDQG---ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANaheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH-VTIPGQQDKDMF 319
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 320 QETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFkkERNTDQ----ASMPDNTAAQKVSHLLGINVTDFTRGILTPRIK 395
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 396 VGRDYV-QKAQTKEQADFAIEALAKATYERMFRWLVLRINKAldkTKRQG------------ASFIGILDIAGFEIFDLN 462
Cdd:cd14892 319 TARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINAC---HKQQTsgvtggaasptfSPFIGILDIFGFEIMPTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 463 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFP-KATDKS 541
Cdd:cd14892 396 SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 542 FVEKVMQEQ-GTHPKFQKPKQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDkfvselwkdvdriig 620
Cdd:cd14892 473 LLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK--------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 621 ldqvagmsetalpgafktrkgmFRTvgqlykeQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEG 700
Cdd:cd14892 536 ----------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEV 586
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 701 IRICRQGFPNRVVFQEFRQRYEILTPNS-IPKGFMDGKQACVLMIKALE-----LDSNLYRIGQSKVFFR 764
Cdd:cd14892 587 VRIRREGFPIRRQFEEFYEKFWPLARNKaGVAASPDACDATTARKKCEEivaraLERENFQLGRTKVFLR 656
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
95-726 |
1.84e-171 |
|
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: 526.57 E-value: 1.84e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKgKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 174 GESGAGKTENTKKVIQYLAYVASSHKSKKDQgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD--------- 244
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSL--VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSklkskrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 245 VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN------------------- 305
Cdd:cd14888 158 DRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGAdakpisidmssfephlkfr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 306 -----GHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQ---KVSHL 377
Cdd:cd14888 238 yltksSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDdleKVASL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 378 LGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFE 457
Cdd:cd14888 318 LGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIFGFE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 458 IFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKA 537
Cdd:cd14888 398 CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFVPGG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 538 TDKSFVEKVMQEQGTHPKFQKPKqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD-VD 616
Cdd:cd14888 475 KDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSAyLR 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 617 RIIGLdqvagmsetalpgafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNG 696
Cdd:cd14888 553 RGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGG 617
|
650 660 670
....*....|....*....|....*....|
gi 29436380 697 VLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd14888 618 VLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
97-764 |
5.95e-159 |
|
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: 493.65 E-value: 5.95e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 97 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMM----QDREDQSILC 172
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 173 TGESGAGKTENTKKVIQYLAYVAsshkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGA 252
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHVKGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 253 NIETYLLEKSRAIRQAKEERTFHIFYYLLSG-AGEHLKTDLLLEPyNKYRFLSNGHvtipGQQD-----KDMFQETMEAM 326
Cdd:cd14889 156 KINEYLLEKSRVVHQDGGEENFHIFYYMFAGiSAEDRENYGLLDP-GKYRYLNNGA----GCKRevqywKKKYDEVCNAM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKkerntdqasmPDNTAAQKVSH-------------------LLG--INVTDF 385
Cdd:cd14889 231 DMVGFTEQEEVDMFTILAGILSLGNITFE----------MDDDEALKVENdsngwlkaaagqfgvseedLLKtlTCTVTF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 386 TRGiltprikvgrDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQG--ASFIGILDIAGFEIFDLNS 463
Cdd:cd14889 301 TRG----------EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 464 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFV 543
Cdd:cd14889 371 FEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFV 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 544 EKVMQEQGTHPKFQKPKQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWK-DVDRIIGLD 622
Cdd:cd14889 448 DKLNIHFKGNSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLM 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 623 QVAGMSETALPGAFKTRKgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIR 702
Cdd:cd14889 526 PRAKLPQAGSDNFNSTRK---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIR 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29436380 703 ICRQGFPNRVVFQEFRQRYEIL--TPNsIPKgfmdGKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd14889 603 IRREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
95-727 |
2.61e-153 |
|
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: 479.14 E-value: 2.61e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRH--------EMPPHIYAITDTAYRSMMQDR 165
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 166 EDQSILCTGESGAGKTENTKKVIQYL--------------AYVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDN 231
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLtqlsqqeqnseevlTLTSSIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 232 SSRFGKFIRINFD-VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDL-LLEPYNKYRFLS---NG 306
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDRYDYlkkSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 307 HVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQA--SMPDNTAAQKVSHLLGINVTD 384
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSpcCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 385 FTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL-------DKTKRQGASFIGILDIAGFE 457
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 458 IFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFP 535
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 536 KATDKSFVEKVMQEQGTHPKFQKPKQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDV 615
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 616 DRiigldqvagmSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCN 695
Cdd:cd14907 557 DG----------SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYL 626
|
650 660 670
....*....|....*....|....*....|..
gi 29436380 696 GVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14907 627 GVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
96-730 |
2.45e-152 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 474.79 E-value: 2.45e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMY-----------KGKKRHEMPPHIYAITDTAYRSMMQ 163
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 164 ----DREDQSILCTGESGAGKTENTKKVIQYLAYV-----ASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSR 234
Cdd:cd14900 82 glngVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 235 FGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEhlktdlllepynkyrflsnghvtipGQQ 314
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE-------------------------AAR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 315 DKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTD-QASMPDNTAAQKV------SHLLGINVTDFTR 387
Cdd:cd14900 217 KRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 388 GILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL---DKTKRQGAS-FIGILDIAGFEIFDLNS 463
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 464 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFV 543
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSDTTLA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 544 EKVMQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDplndniatLLHQSSdkfvselwkdVDriigldq 623
Cdd:cd14900 454 SKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------VD------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 624 vagmsetalpgafktrkgMFRTVGQlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRI 703
Cdd:cd14900 509 ------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRV 569
|
650 660
....*....|....*....|....*..
gi 29436380 704 CRQGFPNRVVFQEFRQRYEILTPNSIP 730
Cdd:cd14900 570 ARAGFPIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
95-764 |
2.13e-148 |
|
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: 464.90 E-value: 2.13e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERyySGLI----YTYSGLFCVVINPYKNLPiysEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDRE---D 167
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 168 QSILCTGESGAGKTENTKKVIQYL------------AYVASSHKSKKDQG-ELERQLLQANPILEAFGNAKTVKNDNSSR 234
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLttravggkkasgQDIEQSSKKRKLSVtSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 235 FGKFIRINFDVNGY-IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS-NGHVTIPG 312
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 313 QQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKK----ERNTDQASMPDNTAAQKVSHLLGINVTDFTRG 388
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 389 ILTPRIkVGRDYVQKAQ-TKEQADFAIEALAKATYERMFRWLVLRINKALDKtKRQGASFIGILDIAGFEIFDL-NSFEQ 466
Cdd:cd14891 316 ITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 467 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKV 546
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNETL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 547 MQEQGTHPKFQKPKQlKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHqSSDKFVselwkdvdriigldqva 625
Cdd:cd14891 471 HKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLA-SSAKFS----------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 626 gmsetalpgafktrkgmfrtvgqlykEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICR 705
Cdd:cd14891 532 --------------------------DQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLK 585
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 706 QGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIK-ALELDSNLYRIGQSKVFFR 764
Cdd:cd14891 586 VGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTLTQAILwAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
95-764 |
2.09e-147 |
|
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: 462.87 E-value: 2.09e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 174 GESGAGKTENTKKVIQYLAYVASSHKSKKDQgelerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:cd14904 156 CETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSLIGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 332 PEEEQMGLLRVISGVLQLGNIVFkKERNTDQASMPDNTAAQKVSHLLGINVTDF-----TRGILT--PRIKVGRDYVQKA 404
Cdd:cd14904 236 DNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIeealcNRSVVTrnESVTVPLAPVEAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 405 QTKeqadfaiEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTM 484
Cdd:cd14904 315 ENR-------DALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 485 FILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKV---MQEQGTHPKFQKPKQ 561
Cdd:cd14904 388 FKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 562 lkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvaGMSETALPGAFKTRKG 641
Cdd:cd14904 464 --KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APSETKEGKSGKGTKA 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 642 MfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 721
Cdd:cd14904 533 P-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRY 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 29436380 722 EILTPNSIPKGfmDGKQACVLMIKALELDSNL-YRIGQSKVFFR 764
Cdd:cd14904 612 AIMFPPSMHSK--DVRRTCSVFMTAIGRKSPLeYQIGKSLIYFK 653
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
95-747 |
2.58e-144 |
|
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: 456.66 E-value: 2.58e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYK--------GKKRHEMPPHIYAITDTAYRSMMQ-D 164
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 165 REDQSILCTGESGAGKTENTKKVIQYLAYV----ASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgrdqSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVT---IPGQQDKD 317
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPSfarKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 318 --MFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKE-RNTDQASMPDNTAAQ--KVSHLLGINVTDFTRGILTP 392
Cdd:cd14902 241 aqLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 393 RIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALD--------KTKRQGASFIGILDIAGFEIFDLNSF 464
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 465 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVE 544
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDK--SNGLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 545 KVMQEQGThpkfqkpkqlkdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSelwkdvdrIIGLDQV 624
Cdd:cd14902 478 KFYRYHGG------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVV--------AIGADEN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 625 AGMSETALPGAFKTRKGMFRT--VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIR 702
Cdd:cd14902 538 RDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVR 617
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 29436380 703 ICRQGFPNRVVFQEFRQRYEIL-----TPNSIPK-GFMDGKQA--CVLMIKAL 747
Cdd:cd14902 618 IARHGYSVRLAHASFIELFSGFkcflsTRDRAAKmNNHDLAQAlvTVLMDRVL 670
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
95-764 |
3.06e-144 |
|
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: 453.85 E-value: 3.06e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLayvaSSHKSKKDQGELeRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGANI 254
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL----SSLYQDQTEDRL-RQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHV-TIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd14896 155 SHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGLGLCA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 334 EEQMGLLRVISGVLQLGNIVFKKERNTDQ--ASMPDNTAAQKVSHLLGINvTDFTRGILTPRIKV-GRDYVQKAQTKEQA 410
Cdd:cd14896 235 EELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYGRVSRPLPVEGA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 411 DFAIEALAKATYERMFRWLVLRINKALDKTKRQGA-SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd14896 314 IDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 490 EEYQREGIEWNFIDfGLDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQlkDKADFC 569
Cdd:cd14896 394 EECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--PLPVFT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGmsetalpgafktrkgmfrTVGQL 649
Cdd:cd14896 469 VRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP------------------TLASR 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 650 YKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSI 729
Cdd:cd14896 531 FQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQ 610
|
650 660 670
....*....|....*....|....*....|....*
gi 29436380 730 PkGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14896 611 E-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
95-764 |
1.33e-140 |
|
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: 1.33e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYK--GKKRHE-------MPPHIYAITDTAYRSMMQD- 164
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 165 REDQSILCTGESGAGKTENTKKVIQYLAYVASSHK-SKKDQGELER-----QLLQANPILEAFGNAKTVKNDNSSRFGKF 238
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEgAPNEGEELGKlsimdRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 239 IRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGE--------HLKTDLLLEPYNKYRFLSNGHVTI 310
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 311 PGQ-QDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTAAQK----VSHLLGINVTDF 385
Cdd:cd14908 241 LREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 386 TRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGA-SFIGILDIAGFEIFDLNSF 464
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 465 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFP-KATDKSFV 543
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQAK--KKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 544 EKVM--------QEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLM-KNMDPLNdniatllhqssdkfvselwkd 614
Cdd:cd14908 477 SRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP--------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 615 vdriigldqvagmsetalpgafKTRKGMFRTvGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRC 694
Cdd:cd14908 536 ----------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRY 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 695 NGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnSIPK----GFMDGKQACVLMIKALELDSNLYR--------------- 755
Cdd:cd14908 593 GGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlsWSMERLDPQKLCVKKMCKDLVKGVlspamvsmknipedt 671
|
730
....*....|.
gi 29436380 756 --IGQSKVFFR 764
Cdd:cd14908 672 mqLGKSKVFMR 682
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
96-764 |
1.25e-136 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 435.92 E-value: 1.25e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPiyseeivEMYKGKKRHE-------MPPHIYAITDTAYRSMMQ----- 163
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 164 --DREDQSILCTGESGAGKTENTKKVIQYLAYVASSHK----SKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGK 237
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTatssSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 238 FIRINF-----DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYN--KYRFLSNG--HV 308
Cdd:cd14895 155 FVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGqcYQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 309 TIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTD---------------QASMPDNTAAQK 373
Cdd:cd14895 235 RNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTVQQH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 374 ---VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTK--------- 441
Cdd:cd14895 315 ldiVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpnkaa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 442 -RQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIEkpAG 520
Cdd:cd14895 395 nKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE--QR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 521 PPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKqlKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIAT 598
Cdd:cd14895 472 PSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAELFS 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 599 LLHQSSDKFVSELWKDVDriigLDQVAGMSETALPgaFKTRKGMFRTV--GQLYKEQLAKLMATLRNTNPNFVRCIIPNH 676
Cdd:cd14895 550 VLGKTSDAHLRELFEFFK----ASESAELSLGQPK--LRRRSSVLSSVgiGSQFKQQLASLLDVVQQTQTHYIRCIKPND 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 677 EKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELdsnlyri 756
Cdd:cd14895 624 ESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL------- 696
|
....*...
gi 29436380 757 GQSKVFFR 764
Cdd:cd14895 697 GKTRVFLR 704
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
93-807 |
3.43e-136 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 438.31 E-value: 3.43e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 93 NEASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHE-MPPHIYAITDTAYRSMMQDREDQSIL 171
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 172 CTGESGAGKTENTKKVIQYLAYVASSHKSKKDQgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 251
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFASSKSGNMDLKIQ----NAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRY 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 252 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGI 331
Cdd:PTZ00014 264 GSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 332 PEEEQMGLLRVISGVLQLGNIVF--KKERNTDQASM--PDNTAA-QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:PTZ00014 344 SESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWS 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 407 KEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 486
Cdd:PTZ00014 424 KDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFE 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 487 LEQEEYQREGIEWNFIDFgLDLQPCIDLI-EKPAgppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDK 565
Cdd:PTZ00014 503 RESKLYKDEGISTEELEY-TSNESVIDLLcGKGK---SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDSNK 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 566 aDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGldqvagmsetalpgafKTRKGMFrt 645
Cdd:PTZ00014 579 -NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG----------------KLAKGQL-- 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 646 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 725
Cdd:PTZ00014 640 IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 726 PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR---AGVLAHLEEERDLKITDVIIGFQACCRGYLARKAFAKR 802
Cdd:PTZ00014 720 LAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKN 799
|
....*
gi 29436380 803 QQQLT 807
Cdd:PTZ00014 800 IKSLV 804
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
95-764 |
1.63e-130 |
|
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: 418.64 E-value: 1.63e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVASSHKSKkdqgeLERQLLQA-NPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV-----LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKyrflSNGHVTIPGQQDKDM------FQETMEAMR 327
Cdd:cd01386 156 IQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQKPEDKqkaaaaFSKLQAAMK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGI------------LTPRIK 395
Cdd:cd01386 232 TLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSSGQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 396 VGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALdKTKRQGASFIGILDIAGFEifdlN----------SFE 465
Cdd:cd01386 312 ESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSL-SSSHHSTSSITIVDTPGFQ----NpahsgsqrgaTFE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 466 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAG------------PPGILALLDEECW 533
Cdd:cd01386 387 DLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQqalvrsdlrdedRRGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 534 FPKATDKSFVEKVMQEQG--THPKFQKPKQLKDKA-DFCIIHYAGK--VDYKADEWLMK-NMDPLNDNIATLLHQSSDKF 607
Cdd:cd01386 467 YPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQKET 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 608 vselwkdvdriigldqvagmsetalpgAFKTRKGMFRTVgqlyKEQLAKLMATLRNTNPNFVRCIIPNHE------KKAG 681
Cdd:cd01386 547 ---------------------------AAVKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHNagkderSTSS 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 682 KLDPHLVLD------QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGF-----MDGKQACVLMIKALELD 750
Cdd:cd01386 596 PAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLE 675
|
730
....*....|....
gi 29436380 751 SNLYRIGQSKVFFR 764
Cdd:cd01386 676 KSSYRIGLSQVFFR 689
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
95-762 |
8.72e-127 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 407.45 E-value: 8.72e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRH-EMPPHIYAITDTAYRSMMQDREDQSILCT 173
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 174 GESGAGKTENTKKVIQYLAYVASSHKSKKDQgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 253
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAKSGNMDLRIQ----TAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 254 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLsNGHVT-IPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14876 157 VVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFL-NPKCLdVPGIDDVADFEEVLESLKSMGLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 333 EEEQMGLLRVISGVLQLGNIVFKKErntDQASMPDntAA----------QKVSHLLGINVTDFTRGILTPRIKVGRDYVQ 402
Cdd:cd14876 236 EEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKVTKAGGQEIE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 403 KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 482
Cdd:cd14876 311 GRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFID 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 483 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFqKPKQL 562
Cdd:cd14876 390 IVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF-KPAKV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGldqvagmsetalpgafKTRKGM 642
Cdd:cd14876 466 DSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKG----------------KIAKGS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 643 FrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14876 530 L--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFK 607
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 29436380 723 ILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVF 762
Cdd:cd14876 608 FLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
95-762 |
1.02e-126 |
|
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: 407.70 E-value: 1.02e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKR-HEMPPHIYAITDTAYRSMMQDRE--DQSI 170
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 171 LCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGELER---QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 247
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERieqRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 248 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIpgqqDKDMFQETMEAMR 327
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL----EEDCFEVTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 328 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVS---HLLGINVTDFTRGILTPRIKVGRDYV--Q 402
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVRtsaLLLKLPEDHLLETLQIRTIRAGKQQQvfK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 403 KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNH 482
Cdd:cd14880 317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 483 TMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQL 562
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALpgafktrkgm 642
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAPV---------- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 643 fRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14880 544 -LTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 29436380 723 ILTPN--SIPKGFMDGKQAcvlmikalELDSNLYRIGQSKVF 762
Cdd:cd14880 623 LLRRLrpHTSSGPHSPYPA--------KGLSEPVHCGRTKVF 656
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
95-760 |
2.01e-124 |
|
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: 403.21 E-value: 2.01e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKR-HEMPPHIYAITDTAYRSMMQDREDQSILC 172
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 173 TGESGAGKTENTKKVIQYLAYVASSHKSKK-----DQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-VN 246
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNnnnnnNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRsSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 247 GYIVGANIETYLLEKSR-AIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEP-YNKYRFL--------------SNGHVTI 310
Cdd:cd14906 161 GKIDGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqsSNKNSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 311 PGQQDKD-MFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQAS--MPDNTAA-QKVSHLLGINVTDFT 386
Cdd:cd14906 241 NNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 387 RGILTPRIKV-GRDYVQ-KAQTKEQADFAIEALAKATYERMFRWLVLRINKALDK----------TKRQGASFIGILDIA 454
Cdd:cd14906 321 QALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 455 GFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGILALLDEECWF 534
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDECIM 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 535 PKATDKSFVEKVMQEQGTHPKFQkpKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKd 614
Cdd:cd14906 478 PKGSEQSLLEKYNKQYHNTNQYY--QRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ- 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 615 vdriigldqvagMSETALPGAFKTRKGMFRTVGQlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRC 694
Cdd:cd14906 555 ------------QQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRN 621
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29436380 695 NGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSK 760
Cdd:cd14906 622 VGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
95-764 |
6.10e-116 |
|
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: 378.38 E-value: 6.10e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYS-GLIYTYSGLFCVVINPYKNLPIYSEEIVEMY-KGKKRHEMPPHIYAITDTAYRSM-MQDREDQSIL 171
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 172 CTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERQ----LLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-VN 246
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQRSIADKidenLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDpTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 247 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDL-LLEPYNKYRFLSNGHVTI----PGQ--QDKDMF 319
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTFVrrgvDGKtlDDAHEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 320 QETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTAAQKVSHLLGINVTDFTRGILtprIKVGRD 399
Cdd:cd14875 241 QNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSKTS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 400 YVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALD-KTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQ 478
Cdd:cd14875 317 LVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 479 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVMQE-QGTHPKFQ 557
Cdd:cd14875 397 HYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQwANKSPYFV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 558 KPKQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdvdriigLDQVAGMSEtalpgafk 637
Cdd:cd14875 474 LPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL---------LSTEKGLAR-------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 638 tRKgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEF 717
Cdd:cd14875 536 -RK---QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQF 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 29436380 718 RQRYEILTPNSIPKGFMDGK--QACVLMI----KALELDSNLYRIGQSKVFFR 764
Cdd:cd14875 612 CRYFYLIMPRSTASLFKQEKysEAAKDFLayyqRLYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
95-764 |
6.54e-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: 369.99 E-value: 6.54e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRH-----EMPPHIYAITDTAYRSMMQDREDQ 168
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 169 SILCTGESGAGKTENTKKVIQYLAYVASSHKSKkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSSTD-----VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 249 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHV-TIPGQQDKDMFQETMEAMR 327
Cdd:cd14886 156 LKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGIDDQKEFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 328 IMgIPEEEQMGLLRVISGVLQLGNIVFKKERN--TDQASMPDNTAA-QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 404
Cdd:cd14886 236 KL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETIISP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 405 QTKEQADFAIEALAKATYERMFRWLVLRINKALdKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTM 484
Cdd:cd14886 315 VTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 485 FILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPAgpPGILALLDEECWFPKATDKSFVE---KVMQEQGTHPKfqKPKQ 561
Cdd:cd14886 394 FKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPN--LSIFSFLEEQCLIQTGSSEKFTSsckSKIKNNSFIPG--KGSQ 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 562 LKdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLdqvagmsetalpgafktRKG 641
Cdd:cd14886 469 CN----FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN-----------------MKG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 642 MFrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 721
Cdd:cd14886 528 KF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRN 605
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 29436380 722 EILT--PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14886 606 KILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
95-721 |
1.01e-111 |
|
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: 368.65 E-value: 1.01e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMY----------KGKKRHEMPPHIYAITDTAYRSMMQ 163
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 164 DREDQSILCTGESGAGKTENTKKVIQYLA------------YVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDN 231
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnnnltnSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 232 SSRFGKFIRINF-DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSG-----AGEHLKTDLLLEPYNKYRFLSN 305
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 306 GHVTI--PGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVF-----KKERNT--DQASMPDNTAA----- 371
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 372 QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL-------------- 437
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 438 DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEK 517
Cdd:cd14899 401 VDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 518 PagPPGILALLDEECWFPKATDKSFVEKV---MQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLND 594
Cdd:cd14899 480 R--PIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 595 NIATLLHQSSDKFVSELWKDVDRiiglDQVAGMSETALPGAFKTRKGMFRT----VGQLYKEQLAKLMATLRNTNPNFVR 670
Cdd:cd14899 558 SAAQLLAGSSNPLIQALAAGSND----EDANGDSELDGFGGRTRRRAKSAIaavsVGTQFKIQLNELLSTVRATTPRYVR 633
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 29436380 671 CIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 721
Cdd:cd14899 634 CIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
95-764 |
1.50e-103 |
|
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: 346.64 E-value: 1.50e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYS--------GLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDRE 166
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 167 DQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 246
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG-LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 247 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLlepynkyrflsnghvtiPGQQDKDMF--QETME 324
Cdd:cd14887 160 GKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSS-----------------AGEGDPESTdlRRITA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 325 AMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTA--------AQKVSHLL-------GINVTDFTRGI 389
Cdd:cd14887 223 AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLKVTEASRKH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 390 LT--------PRIKVGRDYV------------QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKR------- 442
Cdd:cd14887 303 LKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsd 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 443 ------QGASFIGILDIAGFEIF---DLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI--DFGLDLQPC 511
Cdd:cd14887 383 edtpstTGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFSFPLA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 512 IDLIEKPA---------------------GPPGILALLDE------ECWFPKATDKSFVEKVMQEQGTHPKFQK--PKQL 562
Cdd:cd14887 463 STLTSSPSstspfsptpsfrsssafatspSLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINSAKYKNitPALS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 563 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLhQSSDKFVSElwkdvdriIGLDQVAGMSetalpgAFKTRKgm 642
Cdd:cd14887 543 RENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTRL--------VGSKKNSGVR------AISSRR-- 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 643 fRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 722
Cdd:cd14887 606 -STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYE 684
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 29436380 723 ILTPNSIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 764
Cdd:cd14887 685 TKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
96-726 |
9.54e-99 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 328.40 E-value: 9.54e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNlpIYSEEIVEMYKGKKRHeMPPHIYAITDTAYRSMMQdREDQSILCTGE 175
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 176 SGAGKTENTKKVIQYLAYVASSHKSkkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvnGYIVGANIE 255
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTTS------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 256 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDlllepYNKYRF-LSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 334
Cdd:cd14898 150 TYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSStAGNKESIVQLSEKYKMTCSAMKSLGIANFKSI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 335 EQMGLlrvisGVLQLGNIVFKKERNTDQASmpdNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAI 414
Cdd:cd14898 225 EDCLL-----GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 415 EALAKATYERMFRWLVLRINKALDKTkrqGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 494
Cdd:cd14898 297 NSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 495 EGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKvMQEQGTHpkfqkpkQLKDKADFCII--H 572
Cdd:cd14898 374 EGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVK-IKKYLNG-------FINTKARDKIKvsH 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 573 YAGKVDYKADEWLMKNMDplndniatllhqssdkfvselwKDVDRIIGLDQVAgmsetalpgafktRKGMFRTVGQLYKE 652
Cdd:cd14898 442 YAGDVEYDLRDFLDKNRE----------------------KGQLLIFKNLLIN-------------DEGSKEDLVKYFKD 486
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29436380 653 QLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 726
Cdd:cd14898 487 SMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGI 560
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
92-763 |
2.27e-98 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 329.51 E-value: 2.27e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 92 LNEASVLHNLKERYYSGLIYTY---SGLfcVVINPYKNLPIYSEEIVEMYK-------GKKRHEMPPHIYAITDTAYRSM 161
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 162 MQDREDQSILCTGESGAGKTENTKKVI-QYLAYVASSHKSKKdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLrQLLRLSSHSKKGTK----LSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL--SNGHVT--IPGQQDK 316
Cdd:cd14879 155 LQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHPLplGPGSDDA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 317 DMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVF--KKERNTDQASMpDNTAA-QKVSHLLGINVTDFtRGILTPR 393
Cdd:cd14879 235 EGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVAAFLGVSPEDL-ETSLTYK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 394 IK-VGRD----YVQKAQTKEQADfaieALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFD---LNSFE 465
Cdd:cd14879 313 TKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRSstgGNSLD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 466 QLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIEKPAGppGILALLDEEC-WFPKATD 539
Cdd:cd14879 389 QFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGKPG--GLLGILDDQTrRMPKKTD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 540 KSFVEKVMQEQGTHPKF---QKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLndniatllhqSSDkFVSelwkdvd 616
Cdd:cd14879 461 EQMLEALRKRFGNHSSFiavGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVL----------SPD-FVN------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 617 riigldqvagmsetalpgafktrkgMFRTVGQLyKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNG 696
Cdd:cd14879 523 -------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLG 576
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29436380 697 VLEGIRICRQGFPNRVVFQEFRQRYEILTPnsipkgFMDGKQACVLMIKALELDSNLYRIGQSKVFF 763
Cdd:cd14879 577 LPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
95-764 |
1.50e-97 |
|
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: 326.97 E-value: 1.50e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEivemYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYlaYVASShkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14937 77 ESGSGKTEASKLVIKY--YLSGV----KEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEE 334
Cdd:cd14937 151 EIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNMHDM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 335 EQmGLLRVISGVLQLGNIVFK---KERNTDQASMPDNT--AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQ 409
Cdd:cd14937 231 KD-DLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 410 ADFAIEALAKATYERMFRWLVLRINKALDKTKrQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 489
Cdd:cd14937 310 SVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKET 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 490 EEYQREGIEWNFIDFGLDlQPCIDLIEkpaGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKaDFC 569
Cdd:cd14937 389 ELYKAEDILIESVKYTTN-ESIIDLLR---GKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINK-NFV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 570 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvagMSETAlpgafkTRKGMfrtVGQL 649
Cdd:cd14937 464 IKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE----------VSESL------GRKNL---ITFK 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 650 YKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRIcRQGFPNRVVFQEFRQRYEILTPNSI 729
Cdd:cd14937 525 YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTS 603
|
650 660 670
....*....|....*....|....*....|....*
gi 29436380 730 PKGFMDGKQACVLMIKAlELDSNLYRIGQSKVFFR 764
Cdd:cd14937 604 KDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
95-764 |
1.40e-94 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 319.45 E-value: 1.40e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 171
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 172 CTGESGAGKTENTKKVIQYLAYVASSHKSKkdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVNGYIV 250
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTT-----FDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 251 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGH----VTIPGQQDKDMFQETMEAM 326
Cdd:cd14878 156 GARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMredvSTAERSLNREKLAVLKQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 327 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 406
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 407 KEQADFAIEALAKATYERMFRWLVLRINKAL---DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 483
Cdd:cd14878 316 IQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 484 MFILEQEEYQREGIEWNFIDFGLDLQPCID-LIEKPAgppGILALLDEECWFPKATDKSFVEKV---MQEQGTHPKFQKP 559
Cdd:cd14878 396 LFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPS---GFLSLLDEESQMIWSVEPNLPKKLqslLESSNTNAVYSPM 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 560 KQ------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdvdriigldqvagmsetal 632
Cdd:cd14878 473 KDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL--------------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 633 pgaFKTRkgmFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRV 712
Cdd:cd14878 532 ---FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRL 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 29436380 713 VFQEFRQRYEILTPNSI-PKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd14878 606 SFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
95-716 |
3.18e-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: 287.96 E-value: 3.18e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHE-------MPPHIYAITDTAYRSMMQDRE 166
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 167 DQSILCTGESGAGKTENTKKVIQYLAYVasshKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-- 244
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEev 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 245 -------VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSG-AGEHLKTDLLLEPYNKYRFLSN----------G 306
Cdd:cd14884 157 entqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLNPdeshqkrsvkG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 307 HVTIPG----------QQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKkerntdqasmpdntaaqKVSH 376
Cdd:cd14884 237 TLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-----------------AAAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 377 LLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGA----------- 445
Cdd:cd14884 300 CLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediysine 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 446 SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKpagppgIL 525
Cdd:cd14884 380 AIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK------IF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 526 ALLDE-----ECWFPKATDKSFV-----EKVMQEQGTH------PKFQK---PKQLKDKADFCIIHYAGKVDYKADEWLM 586
Cdd:cd14884 453 RRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVsygfvlNHDADgtaKKQNIKKNIFFIRHYAGLVTYRINNWID 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 587 KNMDPLNDNIATLLHQSSDKFVSElwkdvdriigldqvagmsetalpGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNP 666
Cdd:cd14884 533 KNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDM 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 29436380 667 NFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQE 716
Cdd:cd14884 590 YYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
96-750 |
3.77e-82 |
|
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: 283.16 E-value: 3.77e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYknlpiyseeiveMYKGKKRH-------EMPPHIYAITDTAYRSMMQDREDQ 168
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 169 SILCTGESGAGKTENTKKVIQYLAYVASshkskkdqGELE----RQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFd 244
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG--------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 245 VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYN--KYRFLSNGHVTIPGQQDKDMFQET 322
Cdd:cd14881 141 TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARFQAW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 323 MEAMRIMGIPeeeQMGLLRVISGVLQLGNIVFKkERNTDQASMPDNTAAQKVSHLLGINVTDFTRGiLTPRIK-VGRDYV 401
Cdd:cd14881 221 KACLGILGIP---FLDVVRVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRG-LTTRTHnARGQLV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 402 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKaldkTKRQGAS--------FIGILDIAGFEIFDLNSFEQLCINYTN 473
Cdd:cd14881 296 KSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCINLCA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 474 EKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIEkpAGPPGILALLDEECwFPKATDKSFVEKVMQEQGT 552
Cdd:cd14881 372 ETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQ 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 553 HPKFQKPKQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFvselwkdvdriigldqvagmsetal 632
Cdd:cd14881 448 NPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF------------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 633 pgAFKTRKGMFRTvgqlykeQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRV 712
Cdd:cd14881 502 --GFATHTQDFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRM 572
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 29436380 713 VFQEFRQRYEILTPNSIPKGFMDGKQAC--VLMIKALELD 750
Cdd:cd14881 573 RFKAFNARYRLLAPFRLLRRVEEKALEDcaLILQFLEAQP 612
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
95-729 |
3.70e-70 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 248.63 E-value: 3.70e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 95 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYkgkkrhemppHIYAITDTAYRSMMQDRED-QSILCT 173
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 174 GESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERqllqanpILEAFGNAKTVKNDNSSRFGKFIRINFDVNgYIVGAN 253
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSIDLLYKRN-VLTGLN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 254 IE-TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 332
Cdd:cd14874 143 LKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 333 EEEQMGLLRVISGVLQLGNIVFKKERNTD---QASMPDNTAAQK-VSHLLGINVTDFTRgILTPRIKVGrdyvqKAQTKE 408
Cdd:cd14874 223 DDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKwVAFLLEVDFDQLVN-FLLPKSEDG-----TTIDLN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 409 QADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsfIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 488
Cdd:cd14874 297 AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 489 QEEYQREGIEWNF-IDFGLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQlKDKAD 567
Cdd:cd14874 375 LVDYAKDGISVDYkVPNSIENGKTVELLFKK--PYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-KERLE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 568 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqvagmsetalpgAFKTRKgMFRTVG 647
Cdd:cd14874 452 FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY-------------------SSNTSD-MIVSQA 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 648 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 727
Cdd:cd14874 512 QFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPG 591
|
..
gi 29436380 728 SI 729
Cdd:cd14874 592 DI 593
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
96-717 |
1.32e-69 |
|
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: 248.08 E-value: 1.32e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKgkKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVASShKSKKdqgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 254
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDLS-RSKY----LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 255 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN-GHVTIPGQQDKDMFQETMEAMRIMGIPE 333
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFDFPS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 334 EEQMGLLRVISGVLQLGNIVFKKERNtdQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAqtkeqadfa 413
Cdd:cd14905 235 EKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR--------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 414 iEALAKATYERMFRWLVLRINKALDKTkrQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQ 493
Cdd:cd14905 304 -DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 494 REGIEW-NFIDFGlDLQPCIDLIEKpagppgILALLDEECWFPKATDKSFVEKVMQEQGTHPKF-QKPKQlkdkadFCII 571
Cdd:cd14905 381 TERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK------FGIE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 572 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFV---SELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFR---- 644
Cdd:cd14905 448 HYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLfsrDGVFNINATVAELNQMFDAKNTAKKSPLSIVKVLLScgsn 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 645 --------------------------TVGQLYKeQLAKLMATLRNTNPN--FVRCIIPNHEKKAGKLDPHLVLDQLRCNG 696
Cdd:cd14905 528 npnnvnnpnnnsgggggggnsgggsgSGGSTYT-TYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTFDVKSVNEQIKSLC 606
|
650 660
....*....|....*....|....*
gi 29436380 697 VLEGIRICRQGFP----NRVVFQEF 717
Cdd:cd14905 607 LLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
96-764 |
1.50e-69 |
|
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: 246.96 E-value: 1.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 175
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 176 SGAGKTENTKKVIQYLAYVAsshksKKDQGELERqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 255
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG-----DGNRGATGR-VESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 256 TYLLEKSRAIRQAKEERTFHIFYYLLSG--AGEHLKtDLLLEPYNKYRFLSNGHVTIPG---------QQDKDMFQETME 324
Cdd:cd14882 156 MYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLRIPPEVPPSklkyrrddpEGNVERYKEFEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 325 AMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKerNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 404
Cdd:cd14882 235 ILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 405 QTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKrqgASF-----IGILDIAGFEIFDLNSFEQLCINYTNEKLQQL 479
Cdd:cd14882 313 HTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQLMVNTLNEQMQYH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 480 FNHTMFI---LEQEEYQREGIEWNFIDFGLDLQpciDLIEKPAgppGILALLDEECwfPKATDKSFV-EKVMQEQGTHPK 555
Cdd:cd14882 390 YNQRIFIsemLEMEEEDIPTINLRFYDNKTAVD---QLMTKPD---GLFYIIDDAS--RSCQDQNYImDRIKEKHSQFVK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 556 fqkpkqLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriiglDQVAGMsetalpga 635
Cdd:cd14882 462 ------KHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM-------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 636 fKTRKGMFRTVGQlykEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQ 715
Cdd:cd14882 521 -RTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQ 596
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 29436380 716 EFRQRYEILTPNSIPKGFMDgKQACVLMIKALELDSnlYRIGQSKVFFR 764
Cdd:cd14882 597 EFLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
98-722 |
2.41e-68 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 246.04 E-value: 2.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 98 LHNLKERYYSGLIYTYSGLFCVVINPYKNLPIY----------SEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDRED 167
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYtpdhmqaynkSREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 168 QSILCTGESGAGKTENTKKVIQYLAYVASS----HKSKKDQGELE---RQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 240
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHpigQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 241 INFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAgEH---LKTDLLL-EPYNKYRFLSN-----GHVTIP 311
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQadplaTNFALD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 312 GQQDKDMfqetMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVF-------KKERNTDQASMPDNTA------AQ--KVSH 376
Cdd:cd14893 243 ARDYRDL----MSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQScalkdpAQilLAAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 377 LLGIN--VTD---FTRGILTpriKVGRDYVQ--KAQTKEQADFAIEALAKATYERMFRWLVLRINKAL----DKTKR--- 442
Cdd:cd14893 319 LLEVEpvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKsni 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 443 ----QGasfIGILDIAGFEIFD--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQ 509
Cdd:cd14893 396 vinsQG---VHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 510 PCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKAD------------FCIIHYAGKV 577
Cdd:cd14893 473 KCLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 578 DYKADEWLMKNMDPLNDNIATLLHQSSDKfvselwkdVDRIIGLDQVA------GMSETALPGAF--KTRKGMFR----- 644
Cdd:cd14893 551 TYNGKGLSSKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAaassekAAKQTEERGSTssKFRKSASSaresk 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 645 -----TVGQLYKEQLAKLMAtLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQ 719
Cdd:cd14893 623 nitdsAATDVYNQADALLHA-LNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFR 701
|
...
gi 29436380 720 RYE 722
Cdd:cd14893 702 RYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
117-248 |
5.95e-59 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 200.26 E-value: 5.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 117 FCVVINPYKNLPIYSEEIV-EMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVA 195
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29436380 196 SSHKSKKD----------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 248
Cdd:cd01363 81 FNGINKGEtegwvylteiTVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
96-762 |
9.26e-59 |
|
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: 216.63 E-value: 9.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 96 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYK-GKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 174
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 175 ESGAGKTENTKKVIQYLAYVASSHKS------------------KKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFG 236
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRlptnlndqeednihneenTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 237 KFIRINFDvNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK 316
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 317 DMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNI-----VFKKE---------------------RNTDQASMPDNTA 370
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkaFRKKSllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 371 AQKV-SHLLGINVTDFTRGILTPRIkVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKR--QGASF 447
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 448 IGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgpPGILAL 527
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPT--EGSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 528 LDEECWFPKATDKS-FVEKVMQEQGTHPKFQKPKQLK-DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSD 605
Cdd:cd14938 478 LLENVSTKTIFDKSnLHSSIIRKFSRNSKYIKKDDITgNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 606 KFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQ----LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKA- 680
Cdd:cd14938 558 EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 681 GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnsipkgfmDGKQACVLMIKALELDSNLYRIGQSK 760
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 29436380 761 VF 762
Cdd:cd14938 710 IF 711
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
101-705 |
9.23e-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: 118.69 E-value: 9.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 101 LKERYYSGLIYTYSGLFCV-VINPYKNL------PIYSEEIVEMYKGKKRHE--MPPHIYAI------------------ 153
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIakqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 154 --TDTAYRSMMQDReDQSILCTGESGAGKTENTKKVIQYLAYVA---------------------------SSHKS---- 200
Cdd:cd14894 87 psTISSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseetckvsgstrqpkiklftSSTKStiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 201 ---------------------------------------------------------KKDQGELERQL------------ 211
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeKLEHLEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 212 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVNGY---IVGANIETYLLEKSRAIRQA------KEERTFHI 276
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 277 FYYLLSGAGEH-----LKTDLLLEPYN--KYRFLSNGHVTIPG--------QQDKDMFQETMEAMRIMGIPEEEQMGLLR 341
Cdd:cd14894 326 LYAMVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 342 VISGVLQLGNIVFKKERNTDQASMPDN---TAAQKVSHLLGI-NVTDFTRGILTPRIKV--GRDYVQKAQTKEQADFAIE 415
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 416 ALAKATYERMFRWLVLRINKAL-------DKTKRQ---------GASFIGILDIAGFEIFDLNSFEQLCINYTNEKLqql 479
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL--- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 480 fnhtmfileqeeYQREGiewNFIDFGLDLQPCI-------DLIEKPAGPPGILALLDEECWFPKAT----------DKSF 542
Cdd:cd14894 563 ------------YAREE---QVIAVAYSSRPHLtardsekDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLF 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 543 VEKVMQEQGThpKFQKPKQLKDKAD-----------FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSEL 611
Cdd:cd14894 628 VRNIYDRNSS--RLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRM 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 612 WKDVDRiIGLD-----QVAGMSETALPGAfKTRKGMFRTVGQLYKEQLAKLMatlrntnPNFVRCIIPNHEKKAGKLDPH 686
Cdd:cd14894 706 LNESSQ-LGWSpntnrSMLGSAESRLSGT-KSFVGQFRSHVNVLTSQDDKNM-------PFYFHCIRPNAKKQPSLVNND 776
|
810
....*....|....*....
gi 29436380 687 LVLDQLRCNGVLEGIRICR 705
Cdd:cd14894 777 LVEQQCRSQRLIRQMEICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
970-1258 |
6.32e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 116.19 E-value: 6.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 970 EAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKT 1049
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1050 RRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNK 1129
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1130 AEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvnilkktlEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTK 1209
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE--------EEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 29436380 1210 RVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQ 1258
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1035-1374 |
1.84e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.18 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1035 RLRREEKQRqELEKTRRKLEgdstDLSDQIAELQAQIAELKMQ--LAKKEEELQAalarvEEEAAQKNMALKKIRELESQ 1112
Cdd:COG1196 171 KERKEEAER-KLEATEENLE----RLEDILGELERQLEPLERQaeKAERYRELKE-----ELKELEAELLLLKLRELEAE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1113 ISELQEDLESERASRNKAEKQKRDLGEELEALKTELEdtldstAAQQELRSKREQEVNILKKTLEEEAKthEAQIQEMRQ 1192
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELE------ELELELEEAQAEEYELLAELARLEQD--IARLEERRR 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1193 KHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELA 1272
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1273 DKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAK 1352
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340
....*....|....*....|..
gi 29436380 1353 HNLEKQIATLHAQVADMKKKKK 1374
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
989-1360 |
8.26e-22 |
|
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: 102.83 E-value: 8.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 989 KLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQ 1068
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1069 AQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTEL 1148
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1149 EDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAqIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGE 1228
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEA-LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1229 LANEVkvllqgkGDSEHKRKKVEAQLQELQVKFNEgervrteladkvtKLQVELDNVtgllsqsDSKSSKLTKDFSALES 1308
Cdd:TIGR02168 920 LREKL-------AQLELRLEGLEVRIDNLQERLSE-------------EYSLTLEEA-------EALENKIEDDEEEARR 972
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 29436380 1309 QLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIA 1360
Cdd:TIGR02168 973 RLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE 1024
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
856-1372 |
3.10e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.78 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 856 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQ 935
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 936 AEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKS 1015
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1016 KSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEE 1095
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1096 AAQKNMALKKIRELESQISELQEDLESERASRN---------KAEKQKRDLGEELEALKTEL--EDTLDSTAAQQELRSK 1164
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLagavavligVEAAYEAALEAALAAALQNIvvEDDEVAAAAIEYLKAA 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1165 REQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSE 1244
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1245 HKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDfsALESQLQDTQELLQEENRQK 1324
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER--ELAEAEEERLEEELEEEALE 727
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 29436380 1325 LSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKK 1372
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
882-1229 |
1.41e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 98.99 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 882 KLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQK 961
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 962 LQLEKVTTEAKLKKLEEEqiiLEDQNCKLAKEKKLLEDRIAEFttNLTEEEEKSKSLAKLKNKH---EAMITDLEERLRR 1038
Cdd:TIGR02169 749 LEQEIENVKSELKELEAR---IEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVsriEARLREIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1039 EEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQE 1118
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1119 DLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQElrskreqevnilkktlEEEAKTHEAQIQEMRQKHSQAV 1198
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE----------------IPEEELSLEDVQAELQRVEEEI 967
|
330 340 350
....*....|....*....|....*....|....*...
gi 29436380 1199 EELA-------EQLEQTKRVKANLEKAKQTLENERGEL 1229
Cdd:TIGR02169 968 RALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
858-1223 |
2.08e-20 |
|
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: 98.21 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 858 REKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEIC---HDLEARVEEEEERCQHL 934
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqiSALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 935 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEK 1014
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1015 SKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAELKMQLAKKEEELQAALARVEE 1094
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE-------ELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1095 EAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEEL-EALKTELEDTLDSTAAQQELRSKREQEVNILK 1173
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 29436380 1174 KTLEEEAKTHEAQIQEMrqkhsqavEELAEQLEQTKRVKANLEKAKQTLE 1223
Cdd:TIGR02168 979 NKIKELGPVNLAAIEEY--------EELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
870-1370 |
5.65e-20 |
|
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: 97.05 E-value: 5.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 870 EMETLQSQLMA-EKLQLQEQLQAETELCAEAEELRARLTAKKQELEE---------------------ICHDLEARVEEE 927
Cdd:TIGR02168 221 ELRELELALLVlRLEELREELEELQEELKEAEEELEELTAELQELEEkleelrlevseleeeieelqkELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 928 EERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTN 1007
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1008 LTEEEEKSKSLAKLKNKHEAMITDLEERL----RREEKQRQELEKTRRKLEgdstdlSDQIAELQAQIAELKMQLAKKEE 1083
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLerleDRRERLQQEIEELLKKLE------EAELKELQAELEELEEELEELQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1084 ELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEAlKTELEDTLDSTAAQQELRS 1163
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN-QSGLSGILGVLSELISVDE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1164 KREQEV---------NILKKTLEEEAKTHEAQIQ------------------------EMRQKHSQAVEELAEQLEQTKR 1210
Cdd:TIGR02168 534 GYEAAIeaalggrlqAVVVENLNAAKKAIAFLKQnelgrvtflpldsikgteiqgndrEILKNIEGFLGVAKDLVKFDPK 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1211 VKANL-----------------EKAKQTLENER-----GELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVR 1268
Cdd:TIGR02168 614 LRKALsyllggvlvvddldnalELAKKLRPGYRivtldGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKI 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1269 TELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEE 1348
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
570 580
....*....|....*....|..
gi 29436380 1349 EEAKHNLEKQIATLHAQVADMK 1370
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLK 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
933-1255 |
6.28e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 93.58 E-value: 6.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 933 HLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKvtteaKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEE 1012
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLVLRLEELRE-----ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1013 EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAELKMQLAKKEEELQAALARV 1092
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE-------AQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1093 EEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTA-AQQELRSKREQEVNI 1171
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1172 LKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVE 1251
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
|
....
gi 29436380 1252 AQLQ 1255
Cdd:TIGR02168 514 NQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1018-1345 |
7.76e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 93.20 E-value: 7.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1018 LAKLKNKHEAMITDLEERLRR-------EEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQLAKKEEELQAALA 1090
Cdd:TIGR02168 637 LAKKLRPGYRIVTLDGDLVRPggvitggSAKTNSSILERRREIE----ELEEKIEELEEKIAELEKALAELRKELEELEE 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1091 RVEEeaaqknmALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvn 1170
Cdd:TIGR02168 713 ELEQ-------LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE-- 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1171 ilKKTLEEEAKTHEAQIQEMRQKHSqaveELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKV 1250
Cdd:TIGR02168 784 --IEELEAQIEQLKEELKALREALD----ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1251 EAQLQELQVKfnegervRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTK 1330
Cdd:TIGR02168 858 AAEIEELEEL-------IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
330
....*....|....*
gi 29436380 1331 LKQVEDEKNSFREQL 1345
Cdd:TIGR02168 931 LEGLEVRIDNLQERL 945
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
899-1256 |
2.04e-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: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 899 AEELRARLTAKKQELEEichdlearveeeeercqhLQAEKKKMQQNIQEleeqleeeesarqklqlekvtTEAKLKKLEE 978
Cdd:TIGR02168 665 SAKTNSSILERRREIEE------------------LEEKIEELEEKIAE---------------------LEKALAELRK 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 979 EQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST 1058
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1059 DLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLG 1138
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1139 EELEALKTELEDTLDSTAAQQELRSKREQEvnilKKTLEEEAKTHEAQIQEMRQKHsqavEELAEQLEQtkrVKANLEKA 1218
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRSE----LEELSEELRELESKRSELRREL----EELREKLAQ---LELRLEGL 934
|
330 340 350
....*....|....*....|....*....|....*...
gi 29436380 1219 KQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQE 1256
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
963-1315 |
2.10e-18 |
|
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: 91.67 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 963 QLEKVTTEaKLKKLEEEQIILEDQNCK---LAKEKKLLEDRIAEFTTNLTEEEEkskSLAKLknkhEAMITDLEERL-RR 1038
Cdd:TIGR02169 199 QLERLRRE-REKAERYQALLKEKREYEgyeLLKEKEALERQKEAIERQLASLEE---ELEKL----TEEISELEKRLeEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1039 EEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQknmalkkIRELESQISELQE 1118
Cdd:TIGR02169 271 EQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE-------IDKLLAEIEELER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1119 DLESERasrnkaeKQKRDLGEELEALKTELEDtldstaaqqeLRSKreqevnilkktLEEEAKTHeaqiQEMRQKHSQAV 1198
Cdd:TIGR02169 344 EIEEER-------KRRDKLTEEYAELKEELED----------LRAE-----------LEEVDKEF----AETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1199 EE---LAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKgdsehkrKKVEAQLQELQVKFNEGERVRTELADKV 1275
Cdd:TIGR02169 392 EKlekLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI-------NELEEEKEDKALEIKKQEWKLEQLAADL 464
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 29436380 1276 TKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQE 1315
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
854-1374 |
1.09e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 89.35 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 854 LVKVREKQLAA-ENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQ 932
Cdd:PRK03918 194 LIKEKEKELEEvLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK----LEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 933 HLQAEKKKMQQNIQELEEQLEEEESARqKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEE 1012
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1013 EKSKSLAKLKNKHEA--MITDLEERLRREEKQR-----QELEKTRRKLEGDSTDLSDQIAELQAQIAELKmqlaKKEEEL 1085
Cdd:PRK03918 349 ELEKRLEELEERHELyeEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIGELK----KEIKEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1086 QAALARVE-------------EEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKteLEDTL 1152
Cdd:PRK03918 425 KKAIEELKkakgkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK--LKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1153 DstaaqqELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQ--AVEELAEQLEQTKRVKANLEKAKQTLENERGELA 1230
Cdd:PRK03918 503 E------QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEikSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1231 NEVKVLlqGKGDSEHKRKKVEaQLQELQVKFNEGERVRTELADKVTKLQVELDNvtglLSQSDSKSSKLTKDFSALESQL 1310
Cdd:PRK03918 577 KELEEL--GFESVEELEERLK-ELEPFYNEYLELKDAEKELEREEKELKKLEEE----LDKAFEELAETEKRLEELRKEL 649
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29436380 1311 QDTQELLQEENRQKlsLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:PRK03918 650 EELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
854-1354 |
2.12e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 88.66 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 854 LVKVREKQLAAENRLTEMETLQSQL---MAEKLQLQEQLQAETELCAEAEELRARLTAKKQ------ELEEICHDLEARV 924
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAkkkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKadeakkKAEEKKKADEAKK 1438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 925 EEEEERCQH---LQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKlKKLEEEQIILEDQNCKLAKEKKLLEDRI 1001
Cdd:PTZ00121 1439 KAEEAKKADeakKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK-KKAEEAKKKADEAKKAAEAKKKADEAKK 1517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1002 AEFTTNL-----TEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRrklEGDSTDLSDQIAELQAQIAELK- 1075
Cdd:PTZ00121 1518 AEEAKKAdeakkAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK---AEEDKNMALRKAEEAKKAEEARi 1594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1076 ---MQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESErasRNKAEKQKRDlgEELEALKTELEdtl 1152
Cdd:PTZ00121 1595 eevMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE---KKKAEELKKA--EEENKIKAAEE--- 1666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1153 dstaAQQELRSKREQEVniLKKTLEEEAKTHEAQIQEMRQKhsQAVEELAEQLEQTKRVKANLEKAkqtlENERGELANE 1232
Cdd:PTZ00121 1667 ----AKKAEEDKKKAEE--AKKAEEDEKKAAEALKKEAEEA--KKAEELKKKEAEEKKKAEELKKA----EEENKIKAEE 1734
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1233 VKvllqgKGDSEHKRKKVEAQLQE------LQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSAL 1306
Cdd:PTZ00121 1735 AK-----KEAEEDKKKAEEAKKDEeekkkiAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFAN 1809
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 29436380 1307 ESQLQDTQELLQeeNRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHN 1354
Cdd:PTZ00121 1810 IIEGGKEGNLVI--NDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFN 1855
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
856-1374 |
9.61e-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: 86.28 E-value: 9.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 856 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQ 935
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 936 AEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKS 1015
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1016 KSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIA---ELKMQLAKKEEELQAAL--- 1089
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhGTVAQLGSVGERYATAIeva 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1090 --AR-----VEEEAAQKN---------------MALKKIRELESQISELQ------------------------------ 1117
Cdd:TIGR02169 545 agNRlnnvvVEDDAVAKEaiellkrrkagratfLPLNKMRDERRDLSILSedgvigfavdlvefdpkyepafkyvfgdtl 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1118 --EDLESERA--------------------------SRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEV 1169
Cdd:TIGR02169 625 vvEDIEAARRlmgkyrmvtlegelfeksgamtggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRL 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1170 NILKKTLEEEAKTH---EAQIQEMRQKHSQAVEELAEqleqtkrVKANLEKAKQTLENERGELANEVKVLlqgkGDSEHK 1246
Cdd:TIGR02169 705 DELSQELSDASRKIgeiEKEIEQLEQEEEKLKERLEE-------LEEDLSSLEQEIENVKSELKELEARI----EELEED 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1247 RKKVEAQLQELQVKFNEgERVRtELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLS 1326
Cdd:TIGR02169 774 LHKLEEALNDLEARLSH-SRIP-EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 29436380 1327 LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:TIGR02169 852 IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1035-1367 |
9.66e-17 |
|
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: 86.26 E-value: 9.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1035 RLRREEKQRQeLEKTRRKLEgdstDLSDQIAELQAQIAELKMQlAKKEEELQAAlaRVEEEAAQKNMALKKIRELESQIS 1114
Cdd:TIGR02168 171 KERRKETERK-LERTRENLD----RLEDILNELERQLKSLERQ-AEKAERYKEL--KAELRELELALLVLRLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1115 ELQEDLESERASRNKAEKQKRDLGEELEALKTEL-EDTLDSTAAQQELrskreQEVNILKKTLEEEAKTHEAQIQEMRQK 1193
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVsELEEEIEELQKEL-----YALANEISRLEQQKQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1194 hsqaVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVkvllqgkgdsehkrkkveaqlQELQVKFNEGERVRTELAD 1273
Cdd:TIGR02168 318 ----LEELEAQLEELESKLDELAEELAELEEKLEELKEEL---------------------ESLEAELEELEAELEELES 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1274 KVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLkqVEDEKNSFREQLEEEEEAKH 1353
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELE 450
|
330
....*....|....
gi 29436380 1354 NLEKQIATLHAQVA 1367
Cdd:TIGR02168 451 ELQEELERLEEALE 464
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
821-1343 |
1.54e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.96 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 821 KLRNWQWWRLFTKVKPLLQVSRQEEEMMAKE---EELVKVREKQLAAENRLTEMETLQSQLmaeKLQLQEQLQAEtELCA 897
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEArkaDELKKAEEKKKADEAKKAEEKKKADEA---KKKAEEAKKAD-EAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 898 EAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKlKKLE 977
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK-KKAE 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 978 EEQIILEDQNCKLAKEKKLLEdriaefttnLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQelEKTRRKLEgds 1057
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADE---------AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA--EEAKKKAE--- 1467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1058 tdlsdqiAELQAQIAELKMQLAKKEEELQaalaRVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRdl 1137
Cdd:PTZ00121 1468 -------EAKKADEAKKKAEEAKKADEAK----KKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK-- 1534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1138 gEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKA---- 1213
Cdd:PTZ00121 1535 -KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeak 1613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1214 NLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADK-----VTKLQVELDNVTGL 1288
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKkkaeeAKKAEEDEKKAAEA 1693
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 29436380 1289 LSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFRE 1343
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
856-1201 |
1.60e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.50 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 856 KVREKQLAAENRLTEMETLqsqlMAEKLQLQEQLQAETElcaEAEELRArLTAKKQELE--EICHDLEArveeeeercqh 933
Cdd:TIGR02169 174 KALEELEEVEENIERLDLI----IDEKRQQLERLRRERE---KAERYQA-LLKEKREYEgyELLKEKEA----------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 934 LQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKL--------EEEQIILEDQNCKLAKEKKLLEDRIAEFT 1005
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1006 TNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEEL 1085
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1086 QAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKR 1165
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 29436380 1166 EQEVNILKKTLEE-----EAKTHEAQIQEMRQKHSQAVEEL 1201
Cdd:TIGR02169 475 KEEYDRVEKELSKlqrelAEAEAQARASEERVRGGRAVEEV 515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
839-1144 |
1.78e-16 |
|
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: 85.49 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 839 QVSRQEEEMMAKEEELVKVREKQLAAEN-------RLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQ 911
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEeleqlrkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 912 ELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLA 991
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 992 KEKK-------LLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQI 1064
Cdd:TIGR02168 845 EQIEelsedieSLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1065 AELQAQIAELKMQLAKKEEELqAALARVEEEAAQKNMALK---------KIRELESQISEL-------QEDLESERASRN 1128
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERL-SEEYSLTLEEAEALENKIeddeeearrRLKRLENKIKELgpvnlaaIEEYEELKERYD 1003
|
330
....*....|....*.
gi 29436380 1129 KAEKQKRDLGEELEAL 1144
Cdd:TIGR02168 1004 FLTAQKEDLTEAKETL 1019
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
857-1357 |
2.02e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 85.12 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 857 VREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHD---LEARVEEEEERCQH 933
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSkrkLEEKIRELEERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 934 LQAEKKKMQQNIQELEEQLEEEESARqKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEE 1013
Cdd:PRK03918 271 LKKEIEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1014 KSKSLAKLKNKHEA--MITDLEERLRREEKQR-----QELEKTRRKLEGDSTDLSDQIAELQAQIAELKmqlaKKEEELQ 1086
Cdd:PRK03918 350 LEKRLEELEERHELyeEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIGELK----KEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1087 AALARVE-------------EEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKteLEDTLD 1153
Cdd:PRK03918 426 KAIEELKkakgkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK--LKELAE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1154 staaqqELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQ--AVEELAEQLEQTKRVKANLEKAKQTLENERGELAN 1231
Cdd:PRK03918 504 ------QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEikSLKKELEKLEELKKKLAELEKKLDELEEELAELLK 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1232 EVKVLlqGKGDSEHKRKKVEaQLQELQVKFNEGERVRTELADKVTKLQVELDNvtglLSQSDSKSSKLTKDFSALESQLQ 1311
Cdd:PRK03918 578 ELEEL--GFESVEELEERLK-ELEPFYNEYLELKDAEKELEREEKELKKLEEE----LDKAFEELAETEKRLEELRKELE 650
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29436380 1312 DTQELLQEENRQKLS------------LSTKLKQVEDEKNS-------FREQLEEEEEAKHNLEK 1357
Cdd:PRK03918 651 ELEKKYSEEEYEELReeylelsrelagLRAELEELEKRREEikktlekLKEELEEREKAKKELEK 715
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
906-1345 |
2.17e-16 |
|
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: 84.69 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 906 LTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILED 985
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 986 QNCKLAKEKKllEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIA 1065
Cdd:TIGR04523 296 EISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1066 ELQAQIAELK---MQLAKKEEELQAALARVEEEAAQKNmalKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELE 1142
Cdd:TIGR04523 374 KLKKENQSYKqeiKNLESQINDLESKIQNQEKLNQQKD---EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1143 ALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEE---EAKTHEAQIQEMRQKHSQ---AVEELAEQLEQTKRVKANLE 1216
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQkqkELKSKEKELKKLNEEKKEleeKVKDLTKKISSLKEKIEKLE 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1217 KAKQTLENERGELANEVKvllqgKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKS 1296
Cdd:TIGR04523 531 SEKKEKESKISDLEDELN-----KDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 29436380 1297 SKLTKDFSALESQLqdtqELLQEENRQklsLSTKLKQVEDEKNSFREQL 1345
Cdd:TIGR04523 606 EEKEKKISSLEKEL----EKAKKENEK---LSSIIKNIKSKKNKLKQEV 647
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
960-1365 |
6.64e-16 |
|
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: 83.15 E-value: 6.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 960 QKLQLEKVTTEAKLKKLEEEQIILEDQNcklAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKN--------KHEAMITD 1031
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQ---NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSeisdlnnqKEQDWNKE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1032 LEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELES 1111
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLES 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1112 QISELQEDLEserasrnKAEKQKRDLGEELEALKTELEDTLDStaaQQELRSKREQEVNILKKtLEEEAKTHEAQIQEMR 1191
Cdd:TIGR04523 392 QINDLESKIQ-------NQEKLNQQKDEQIKKLQQEKELLEKE---IERLKETIIKNNSEIKD-LTNQDSVKELIIKNLD 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1192 QKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELanevKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTEL 1271
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL----KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1272 ADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSAleSQLQDTQELLQEENRQKlslSTKLKQVEDEKNSFREQLEEEEEA 1351
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELKKENLEKEIDEKNKEI--EELKQTQKSLKKKQEEK---QELIDQKEKEKKDLIKEIEEKEKK 611
|
410
....*....|....
gi 29436380 1352 KHNLEKQIATLHAQ 1365
Cdd:TIGR04523 612 ISSLEKELEKAKKE 625
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
858-1374 |
8.31e-16 |
|
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: 83.18 E-value: 8.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 858 REKQLA-AENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAE----ELRARLTAKKQELEEICHDLEA---RVEEEEE 929
Cdd:TIGR02168 223 RELELAlLVLRLEELREELEELQEELKEAEEELEELTAELQELEekleELRLEVSELEEEIEELQKELYAlanEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 930 RCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLT 1009
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1010 EEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLsdQIAELQAQIAELKMQLAKKEEELQAAL 1089
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1090 ARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRD--------------------------------- 1136
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkallknqsglsgilgvlselisvdegyeaaie 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1137 --LGEELEAL------------------------------------------------------------KTELEDTL-- 1152
Cdd:TIGR02168 541 aaLGGRLQAVvvenlnaakkaiaflkqnelgrvtflpldsikgteiqgndreilkniegflgvakdlvkfDPKLRKALsy 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1153 --------DSTAAQQELRSK----------------------------------REQEVNILKKTLEE-EAKTHEAQI-- 1187
Cdd:TIGR02168 621 llggvlvvDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsaktnssileRRREIEELEEKIEElEEKIAELEKal 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1188 -------QEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEN----------ERGELANEVKVLLQGKGDS------- 1243
Cdd:TIGR02168 701 aelrkelEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQleeriaqlskELTELEAEIEELEERLEEAeeelaea 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1244 EHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQ 1323
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 29436380 1324 KLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
854-1370 |
1.32e-15 |
|
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: 82.53 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 854 LVKVREKQLAAENRLTE-----------METLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEA 922
Cdd:pfam01576 347 LQEMRQKHTQALEELTEqleqakrnkanLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESER 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 923 RVEEEEERCQHLQ------------AEKK--KMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNC 988
Cdd:pfam01576 427 QRAELAEKLSKLQselesvssllneAEGKniKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLE 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 989 KLAKEKKLLEDRI-------AEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDstdLS 1061
Cdd:pfam01576 507 EEEEAKRNVERQLstlqaqlSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQE---LD 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1062 DQIAELQAQiAELKMQLAKKEEELQAALA--------------RVEEEAAQKNM-----------ALKKIRELESQISEL 1116
Cdd:pfam01576 584 DLLVDLDHQ-RQLVSNLEKKQKKFDQMLAeekaisaryaeerdRAEAEAREKETralslaraleeALEAKEELERTNKQL 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1117 QEDLESERASRNKA-------EKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQE 1189
Cdd:pfam01576 663 RAEMEDLVSSKDDVgknvhelERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEE 742
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1190 MRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRT 1269
Cdd:pfam01576 743 KRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRD 822
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1270 EladkvtklqveldnvtgLLSQSDSKSSKLtkdfSALESQLQDTQELLQEENRQKlslstklKQVEDEKNSFREQLEEEE 1349
Cdd:pfam01576 823 E-----------------ILAQSKESEKKL----KNLEAELLQLQEDLAASERAR-------RQAQQERDELADEIASGA 874
|
570 580
....*....|....*....|.
gi 29436380 1350 EAKHNLEKQIATLHAQVADMK 1370
Cdd:pfam01576 875 SGKSALQDEKRRLEARIAQLE 895
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
859-1319 |
1.71e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.01 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 859 EKQLAAENRLTEMETLQSQlmAEKLQLQEQLQAE----TELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHL 934
Cdd:PRK02224 228 QREQARETRDEADEVLEEH--EERREELETLEAEiedlRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 935 QAEKKKMQQNIQELEeqlEEEESARQKLQLEKVTTEAKLKKLE---EEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEE 1011
Cdd:PRK02224 306 DADAEAVEARREELE---DRDEELRDRLEECRVAAQAHNEEAEslrEDADDLEERAEELREEAAELESELEEAREAVEDR 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1012 EEKSKSLaklknkhEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALAR 1091
Cdd:PRK02224 383 REEIEEL-------EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCP 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1092 VEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKqKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNI 1171
Cdd:PRK02224 456 ECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEE-RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEE 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1172 LKKTLE---EEAKTHEAqiqEMRQKHSQAvEELAEQLEQTKRVKANLEKAKQTLENERGELAN--EVKVLLQGKGDSEHK 1246
Cdd:PRK02224 535 KRERAEelrERAAELEA---EAEEKREAA-AEAEEEAEEAREEVAELNSKLAELKERIESLERirTLLAAIADAEDEIER 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1247 RKKVEAQLQELQVKFNE-----GERVRtELADKVTKLQVE------------LDNVTGLLSQSDSKSSKLTKDFSALESQ 1309
Cdd:PRK02224 611 LREKREALAELNDERRErlaekRERKR-ELEAEFDEARIEearedkeraeeyLEQVEEKLDELREERDDLQAEIGAVENE 689
|
490
....*....|
gi 29436380 1310 LQDTQELLQE 1319
Cdd:PRK02224 690 LEELEELRER 699
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
997-1370 |
1.97e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.01 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 997 LEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST---DLSDQIAELQAQIAE 1073
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERereELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1074 LkmqlakkEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQ--------------KRDLGE 1139
Cdd:PRK02224 291 L-------EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEaeslredaddleerAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1140 ELEALKTELEDTldstaaqQELRSKREQEVNILKKTLEEEAKTHEaQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKak 1219
Cdd:PRK02224 364 EAAELESELEEA-------REAVEDRREEIEELEEEIEELRERFG-DAPVDLGNAEDFLEELREERDELREREAELEA-- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1220 qTLENERGELANEVKVLLQGK--------GDSEHkrkkVEAqLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQ 1291
Cdd:PRK02224 434 -TLRTARERVEEAEALLEAGKcpecgqpvEGSPH----VET-IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA 507
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29436380 1292 SDSKSSKLTKDfSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMK 1370
Cdd:PRK02224 508 EDRIERLEERR-EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELK 585
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1037-1374 |
5.66e-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: 80.50 E-value: 5.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1037 RREEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQLAKKEE--ELQAALARVE--EEAAQKNMALKKIRELESQ 1112
Cdd:TIGR02169 170 RKKEKALEELEEVEENIE----RLDLIIDEKRQQLERLRREREKAERyqALLKEKREYEgyELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1113 ISELQEDLEserasrnKAEKQKRDLGEELEALKTELEDtldstaAQQELRSKREQEVNILKKTLEE---EAKTHEAQIQE 1189
Cdd:TIGR02169 246 LASLEEELE-------KLTEEISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKIGEleaEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1190 MRQKHSQAVEELA---EQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGER 1266
Cdd:TIGR02169 313 KERELEDAEERLAkleAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1267 VRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALES---QLQDTQELLQEENRQKlslSTKLKQVEDEKNSFRE 1343
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAkinELEEEKEDKALEIKKQ---EWKLEQLAADLSKYEQ 469
|
330 340 350
....*....|....*....|....*....|.
gi 29436380 1344 QLEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
999-1240 |
7.05e-15 |
|
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: 78.27 E-value: 7.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 999 DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL 1078
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1079 AKKEEELQAALArveeeAAQKNMALKKIRELESQiselQEDLESERASR--NKAEKQKRDLGEELEALKTELEDTLDSTA 1156
Cdd:COG4942 100 EAQKEELAELLR-----ALYRLGRQPPLALLLSP----EDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1157 AQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL 1236
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....
gi 29436380 1237 LQGK 1240
Cdd:COG4942 251 LKGK 254
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
838-1373 |
7.81e-15 |
|
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: 80.16 E-value: 7.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 838 LQVSRQEEEMMAKEEELVKVREKQlAAENRLTEMETLQSQLMAEKLQLQEQLQAETelcAEAEELRARLTAKK---QELE 914
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRRESQ-SQEDLRNQLQNTVHELEAAKCLKEDMLEDSN---TQIEQLRKMMLSHEgvlQEIR 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 915 EICHDLEarveeeeercqhlQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLK------KLEEEQIILEDQN- 987
Cdd:pfam15921 191 SILVDFE-------------EASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKgrifpvEDQLEALKSESQNk 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 988 --CKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQelektrRKLegdsTDLSDQIA 1065
Cdd:pfam15921 258 ieLLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYM------RQL----SDLESTVS 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1066 ELQAQIAELKMQLAKKEEELQAAL----ARVEEEAAQKNMALKKIRELESQISELQEDLEsERASRNKAEKQK------R 1135
Cdd:pfam15921 328 QLRSELREAKRMYEDKIEELEKQLvlanSELTEARTERDQFSQESGNLDDQLQKLLADLH-KREKELSLEKEQnkrlwdR 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1136 DLGEE--LEALKTELEDtldstaaqqelRSKREQEVNILKKTLEEEAKTH-EAQIQEMRQKHS--QAVEELAEQLEQTKR 1210
Cdd:pfam15921 407 DTGNSitIDHLRRELDD-----------RNMEVQRLEALLKAMKSECQGQmERQMAAIQGKNEslEKVSSLTAQLESTKE 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1211 V-----------KANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRteladkvtKLQ 1279
Cdd:pfam15921 476 MlrkvveeltakKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR--------NVQ 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1280 VELDNVTGLLSQSDsksskltKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQI 1359
Cdd:pfam15921 548 TECEALKLQMAEKD-------KVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKI 620
|
570
....*....|....
gi 29436380 1360 ATLHAQVADMKKKK 1373
Cdd:pfam15921 621 RELEARVSDLELEK 634
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1049-1340 |
9.81e-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: 79.73 E-value: 9.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1049 TRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRN 1128
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1129 KAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTL-EEEAKTHEAQIQEMRQKHSQ---AVEELAEQ 1204
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRieaRLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1205 LEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELdn 1284
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL-- 898
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 29436380 1285 vtgllsqsdsksSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNS 1340
Cdd:TIGR02169 899 ------------RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1031-1205 |
1.01e-14 |
|
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: 75.35 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1031 DLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMAlKKIRELE 1110
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1111 SqiseLQEDLESERASRNKAEKQKRDLGEELEALKTELEDTldstaaqQELRSKREQEVNILKKTLEEEAKTHEAQIQEM 1190
Cdd:COG1579 93 A----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|....*
gi 29436380 1191 RQKHSQAVEELAEQL 1205
Cdd:COG1579 162 EAEREELAAKIPPEL 176
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
833-1373 |
1.14e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 79.63 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 833 KVKPLLQVSRQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLM-------AEKLQLQEQLQAETELCAEAEELRAR 905
Cdd:TIGR00618 281 ETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLmkraahvKQQSSIEEQRRLLQTLHSQEIHIRDA 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 906 LTAKKQELEEICHDLEARveeeeercQHLqaekKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIIL-- 983
Cdd:TIGR00618 361 HEVATSIREISCQQHTLT--------QHI----HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLah 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 984 EDQNCKLAKEK-KLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSD 1062
Cdd:TIGR00618 429 AKKQQELQQRYaELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCG 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1063 QIAELQAqiaelKMQLAKKEEELQAALARVEEEAAQKNMALKKIR----ELESQISELQEDLESERASRNKAEKQKRDLG 1138
Cdd:TIGR00618 509 SCIHPNP-----ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSK 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1139 EELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEeeaktHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKA 1218
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQ-----PEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1219 KQTLEnergelanevkvLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNV---TGLLSQSDSK 1295
Cdd:TIGR00618 659 RVREH------------ALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIeeyDREFNEIENA 726
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29436380 1296 SSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQL-EEEEEAKHNLEKQIATLHAQVADMKKKK 1373
Cdd:TIGR00618 727 SSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLE 805
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
959-1345 |
4.80e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.41 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 959 RQKLQLEKVTTEAK-LKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLR 1037
Cdd:PRK03918 152 RQILGLDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1038 REEKQRQELEKTRR---KLEGDSTDLSDQIAELQAQIAELKmqlaKKEEELQAALARVEE--EAAQKNMALKKIRE---- 1108
Cdd:PRK03918 232 ELEELKEEIEELEKeleSLEGSKRKLEEKIRELEERIEELK----KEIEELEEKVKELKElkEKAEEYIKLSEFYEeyld 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1109 -----------LESQISELQE---DLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKK 1174
Cdd:PRK03918 308 elreiekrlsrLEEEINGIEErikELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1175 TLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKAN---LEKAKQTL--------ENERGELAN----EVKVLLQG 1239
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieeLKKAKGKCpvcgreltEEHRKELLEeytaELKRIEKE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1240 KGDSEHKRKKVEAQLQELQVKFNEGERVRT--ELADKVTKLQVELDNV--------TGLLSQSDSKSSKLTKDFSALESQ 1309
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYnleelekkAEEYEKLKEKLIKLKGEIKSLKKE 547
|
410 420 430
....*....|....*....|....*....|....*.
gi 29436380 1310 LQDTQELlqeeNRQKLSLSTKLKQVEDEKNSFREQL 1345
Cdd:PRK03918 548 LEKLEEL----KKKLAELEKKLDELEEELAELLKEL 579
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1042-1298 |
6.63e-14 |
|
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: 75.19 E-value: 6.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1042 QRQELEKTRRKLEgdstDLSDQIAELQAQIAELKmqlaKKEEELQAALARVEEEAAQKNmalKKIRELESQISELQEDLe 1121
Cdd:COG4942 18 QADAAAEAEAELE----QLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALA---RRIRALEQELAALEAEL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1122 serasrNKAEKQKRDLGEELEALKTELEDTLDstAAQQelRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEEL 1201
Cdd:COG4942 86 ------AELEKEIAELRAELEAQKEELAELLR--ALYR--LGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1202 AEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVE 1281
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250
....*....|....*..
gi 29436380 1282 LDNVTGLLSQSDSKSSK 1298
Cdd:COG4942 236 AAAAAERTPAAGFAALK 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
973-1374 |
7.48e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 76.60 E-value: 7.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 973 LKKLEEEQIILEDQNCKLAKEKKLLEDriaEFTTNLTEEEEKSKSLAKLKNKHEAM------ITDLEERLRREEKQRQEL 1046
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELEN---ELNLLEKEKLNIQKNIDKIKNKLLKLelllsnLKKKIQKNKSLESQISEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1047 EKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQ---EDLESE 1123
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKseiSDLNNQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1124 rasrnKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQ------- 1196
Cdd:TIGR04523 304 -----KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEieklkke 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1197 -------------AVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNE 1263
Cdd:TIGR04523 379 nqsykqeiknlesQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1264 GERVRTELADKVTKL--------------QVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLST 1329
Cdd:TIGR04523 459 LDNTRESLETQLKVLsrsinkikqnleqkQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 29436380 1330 KLKQVEDEKNSFREQLEeeeeaKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:TIGR04523 539 KISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEELKQTQK 578
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
970-1371 |
9.75e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 76.21 E-value: 9.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 970 EAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKT 1049
Cdd:TIGR04523 67 EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1050 RRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEEL---QAALARVEEEAAQKNMALKKIRELESQISELQEDLESERAS 1126
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1127 RNKAEKQKRDLGEELEALKTELEDTldstaaqqelrskrEQEVNILKKTLEEEAKTHEAQIQEMrQKHSQAVEELAEQLE 1206
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNT--------------QTQLNQLKDEQNKIKKQLSEKQKEL-EQNNKKIKELEKQLN 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1207 QTKRVKANLEKAKQTlenergELANEVKVLLqgkgdsehkrKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVT 1286
Cdd:TIGR04523 292 QLKSEISDLNNQKEQ------DWNKELKSEL----------KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1287 gllSQSDSKSSKLTKDFSALESQLQDTQELLQEENR---QKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLH 1363
Cdd:TIGR04523 356 ---SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNlesQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
....*...
gi 29436380 1364 AQVADMKK 1371
Cdd:TIGR04523 433 ETIIKNNS 440
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
854-1370 |
1.87e-13 |
|
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: 75.14 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 854 LVKVREKqlaaENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTakkQELEEICHDLEARVEEEEERCQH 933
Cdd:pfam05483 246 LIQITEK----ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLT---KELEDIKMSLQRSMSTQKALEED 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 934 LQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEeqiILEDQNCKLAKEkkllEDRIAEFTTNLTEEEE 1013
Cdd:pfam05483 319 LQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEKN----EDQLKIITMELQKKSS 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1014 KSKSLAKLKNKHEAMITDLEERLRREEK---QRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL----------AK 1080
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLtaiktseehyLK 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1081 KEEELQAALARVE----EEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALK---TELEDTLD 1153
Cdd:pfam05483 472 EVEDLKTELEKEKlkniELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEekeMNLRDELE 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1154 STaaQQELRSKREQEVNILKKTlEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEV 1233
Cdd:pfam05483 552 SV--REEFIQKGDEVKCKLDKS-EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAEN 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1234 KVLlqgkGDSEHKRKKVEAQLQELQVKFNE---------------GERVRTEL------ADKVTKLQVELD-----NVTG 1287
Cdd:pfam05483 629 KQL----NAYEIKVNKLELELASAKQKFEEiidnyqkeiedkkisEEKLLEEVekakaiADEAVKLQKEIDkrcqhKIAE 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1288 LLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVA 1367
Cdd:pfam05483 705 MVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
|
...
gi 29436380 1368 DMK 1370
Cdd:pfam05483 785 DKK 787
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
878-1356 |
2.63e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.08 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 878 LMAEKLQLQEQLQAETElCAEAEELRARLTAKKQELEEICHDLEarveeeeercqHLQAEKKKMQQNIQELEEQLEEEES 957
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIE-EKEEKDLHERLNGLESELAELDEEIE-----------RYEEQREQARETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 958 ARQKLQlekvTTEAKLKKLEEEqiILEDQncklaKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLR 1037
Cdd:PRK02224 249 RREELE----TLEAEIEDLRET--IAETE-----REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1038 REEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEElqaalARVEEEAAQKnmALKKIRELESQISELQ 1117
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREE-----AAELESELEE--AREAVEDRREEIEELE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1118 EDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAaqqELRSKREQEVNILKK--TLEEEAK-----------THE 1184
Cdd:PRK02224 391 EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA---ELEATLRTARERVEEaeALLEAGKcpecgqpvegsPHV 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1185 AQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERgelanEVKVLLQGKGDSEH----KRKKVEAQLQELQVK 1260
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAED-----RIERLEERREDLEEliaeRRETIEEKRERAEEL 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1261 FNEGERVRTELADK---VTKLQVELDNVTGLLSQSDSKSSKLTKDFSALEsQLQDTQELLQEENRQKLSLSTKLKQVEDE 1337
Cdd:PRK02224 543 RERAAELEAEAEEKreaAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAEL 621
|
490
....*....|....*....
gi 29436380 1338 KNSFREQLEEEEEAKHNLE 1356
Cdd:PRK02224 622 NDERRERLAEKRERKRELE 640
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
854-1263 |
3.19e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.72 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 854 LVKVREKQLAAENRLTEMETLQSQLMAEklqLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEA--RVEEEEERC 931
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEING---IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeEAKAKKEEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 932 QHLQAEKKKmqqniqeleeqleeeesarqkLQLEKVttEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTE- 1010
Cdd:PRK03918 375 ERLKKRLTG---------------------LTPEKL--EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEl 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1011 ---------------EEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST-----DLSDQIAELQAQ 1070
Cdd:PRK03918 432 kkakgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliklkELAEQLKELEEK 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1071 IAELKMQLAKKEEE-----------LQAALARVEEEAAQKNMALKKIRELESQISELQEDLES-ERASRNKAEKQKRDLG 1138
Cdd:PRK03918 512 LKKYNLEELEKKAEeyeklkeklikLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAElLKELEELGFESVEELE 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1139 EELEALKTELEDTLDSTAAQQELRSK---REQEVNILKKTLEEEAKTH------EAQIQEMRQKHSQ-AVEELAEQLEQT 1208
Cdd:PRK03918 592 ERLKELEPFYNEYLELKDAEKELEREekeLKKLEEELDKAFEELAETEkrleelRKELEELEKKYSEeEYEELREEYLEL 671
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29436380 1209 KRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVE------AQLQELQVKFNE 1263
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEklekalERVEELREKVKK 732
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
856-1136 |
4.55e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.33 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 856 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARL---TAKKQELEEICHDLEARveEEEERCQ 932
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIeelEEDLHKLEEALNDLEAR--LSHSRIP 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 933 HLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFttnLTEEE 1012
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL---EEELE 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1013 EKSKSLAKLKNKHEamitDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKE---------- 1082
Cdd:TIGR02169 872 ELEAALRDLESRLG----DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEdpkgedeeip 947
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29436380 1083 ------EELQAALARVEEEAAQK---NM--------ALKKIRELESQISELQEDLESERASRNKAEKQKRD 1136
Cdd:TIGR02169 948 eeelslEDVQAELQRVEEEIRALepvNMlaiqeyeeVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
869-1372 |
5.23e-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: 74.00 E-value: 5.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 869 TEMETLQSQLMAEKLQLQEQLqaeTELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQ---NI 945
Cdd:pfam15921 299 SQLEIIQEQARNQNSMYMRQL---SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgNL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 946 QELEEQLEEEESARQK-LQLEKVTTEAKLKKLEEEQII-------LEDQNCKLAKEKKLLEDRIAEFTTNLTEE----EE 1013
Cdd:pfam15921 376 DDQLQKLLADLHKREKeLSLEKEQNKRLWDRDTGNSITidhlrreLDDRNMEVQRLEALLKAMKSECQGQMERQmaaiQG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1014 KSKSLAKLKNKhEAMITDLEERLRreeKQRQELEKTRRKLEGDSTDLSDQIAELQaqiaelkmqlaKKEEELQAALARVE 1093
Cdd:pfam15921 456 KNESLEKVSSL-TAQLESTKEMLR---KVVEELTAKKMTLESSERTVSDLTASLQ-----------EKERAIEATNAEIT 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1094 EEAAQKNMALKKIRELESQISELQE-DLESERASRNKAEKQKrdlgeELEALKTELEDTLD-------STAAQQELRSKR 1165
Cdd:pfam15921 521 KLRSRVDLKLQELQHLKNEGDHLRNvQTECEALKLQMAEKDK-----VIEILRQQIENMTQlvgqhgrTAGAMQVEKAQL 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1166 EQEVNILKKTLEE---EAKTHEAQIQEMRQKHSQAveelaeQLEQTKRVKANLEK--AKQTLENERGELANEVKvllQGK 1240
Cdd:pfam15921 596 EKEINDRRLELQEfkiLKDKKDAKIRELEARVSDL------ELEKVKLVNAGSERlrAVKDIKQERDQLLNEVK---TSR 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1241 GDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQ---SDSKSSKLT-----------KDFSAL 1306
Cdd:pfam15921 667 NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmegSDGHAMKVAmgmqkqitakrGQIDAL 746
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29436380 1307 ESQLQDTQELLQEENRQKLSLstklkqvEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKK 1372
Cdd:pfam15921 747 QSKIQFLEEAMTNANKEKHFL-------KEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEK 805
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
974-1333 |
7.14e-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: 73.85 E-value: 7.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 974 KKLEEEQIILEDQNCKLAKEKKLLE--DRIAEFTTNLTEEEEKSKSLAKLKNKheamitdleERLRREEKQRQELEKTRR 1051
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIEetENLAELIIDLEELKLQELKLKEQAKK---------ALEYYQLKEKLELEEEYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1052 KLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAE 1131
Cdd:pfam02463 227 LYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1132 KQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvnilKKTLEEEAKTHEAQIQEMRQKhsqavEELAEQLEQTKRV 1211
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKE----LKELEIKREAEEEEEEELEKL-----QEKLEQLEEELLA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1212 KANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEaqLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQ 1291
Cdd:pfam02463 378 KKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQL--EDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 29436380 1292 SDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQ 1333
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1015-1236 |
1.16e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1015 SKSLAKLKNKHEAMITDLE--ERLRREEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQLAKKE-----EELQA 1087
Cdd:COG4913 231 VEHFDDLERAHEALEDAREqiELLEPIRELAERYAAARERLA----ELEYLRAALRLWFAQRRLELLEAEleelrAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1088 ALARVEEEAAQKNMALKKIRELESQIS--------ELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQ 1159
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29436380 1160 ELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL 1236
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFV 463
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
870-1345 |
1.59e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.64 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 870 EMETLQSQLMA-EKL-QLQEQLQAETELCAEAEELRARLTA-----KKQELEEICHDLEARVEEEEERCQHLQAEKKKMQ 942
Cdd:COG4913 243 ALEDAREQIELlEPIrELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 943 QNIQELEEQLEEEESAR-QKLQLEKVTTEAKLKKLEEEQIILEDQ----NCKLAKEKKLLEDRIAEFTTNLTEEEEKSKS 1017
Cdd:COG4913 323 EELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALlaalGLPLPASAEEFAALRAEAAALLEALEEELEA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1018 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAE-LQAQIAELK-----MQLAKKEEELQAALAR 1091
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPfvgelIEVRPEEERWRGAIER 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1092 ----------VEEEAAQKnmALKKIRELesqisELQEDLESERASRNKAEKQ-----KRDLGEELEALKTELEDTLDSTA 1156
Cdd:COG4913 483 vlggfaltllVPPEHYAA--ALRWVNRL-----HLRGRLVYERVRTGLPDPErprldPDSLAGKLDFKPHPFRAWLEAEL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1157 AQ----------QELR-----------------------SKREQEVNIL-------KKTLEEEAktheAQIQEMRQKHSQ 1196
Cdd:COG4913 556 GRrfdyvcvdspEELRrhpraitragqvkgngtrhekddRRRIRSRYVLgfdnrakLAALEAEL----AELEEELAEAEE 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1197 AVEELAEQLEQTKRVKANLEKAKQ---------TLENERGELANEVKVLLQGKGDSEhkrkKVEAQLQELQVKFNEGERV 1267
Cdd:COG4913 632 RLEALEAELDALQERREALQRLAEyswdeidvaSAEREIAELEAELERLDASSDDLA----ALEEQLEELEAELEELEEE 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1268 RTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQ--ELLQEENRQKLS--LSTKLKQVEDEKNSFRE 1343
Cdd:COG4913 708 LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVERELRenLEERIDALRARLNRAEE 787
|
..
gi 29436380 1344 QL 1345
Cdd:COG4913 788 EL 789
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
932-1260 |
1.67e-12 |
|
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: 72.08 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 932 QHLQAEKKKMQQNiqelEEQLEEEESARQKLQlEKVTTEAKLKKLEE----EQIILEDQNCKLAKEKKLLEDRIAEFttN 1007
Cdd:pfam17380 279 QHQKAVSERQQQE----KFEKMEQERLRQEKE-EKAREVERRRKLEEaekaRQAEMDRQAAIYAEQERMAMEREREL--E 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1008 LTEEEEKSKSLAKLKNKHEAM----ITDLE----ERLRREEKQRQELEKTRRK--LEgdstdlSDQIAELQAQIAELKMQ 1077
Cdd:pfam17380 352 RIRQEERKRELERIRQEEIAMeisrMRELErlqmERQQKNERVRQELEAARKVkiLE------EERQRKIQQQKVEMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1078 LAKKEEELQAALARVEEEAAQKnmaLKKIRELE----SQISELQEDLESERASRNKAEKQKRD--LGEEL--EALKTELE 1149
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERARE---MERVRLEEqerqQQVERLRQQEEERKRKKLELEKEKRDrkRAEEQrrKILEKELE 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1150 DTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEkakqTLENERgEL 1229
Cdd:pfam17380 503 ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE----AMERER-EM 577
|
330 340 350
....*....|....*....|....*....|.
gi 29436380 1230 ANEVKvllqgkgDSEHKRKKVEAQLQELQVK 1260
Cdd:pfam17380 578 MRQIV-------ESEKARAEYEATTPITTIK 601
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
863-1374 |
1.86e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 72.46 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 863 AAENRLTEMETLQSQLMAEKLQLQEQLQAeteLCAEAEELRARLTAKKQE-LEEIC--HDLEARVEEEEERCQHLQAEKK 939
Cdd:pfam15921 221 AISKILRELDTEISYLKGRIFPVEDQLEA---LKSESQNKIELLLQQHQDrIEQLIseHEVEITGLTEKASSARSQANSI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 940 KMQQNIQELEEQLEEEESARQKLQLEKVTTEAKlKKLEEEQIILEDQNCKLAKEKKLLEdriAEFTTNLTEEEEKSKSLA 1019
Cdd:pfam15921 298 QSQLEIIQEQARNQNSMYMRQLSDLESTVSQLR-SELREAKRMYEDKIEELEKQLVLAN---SELTEARTERDQFSQESG 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1020 KLKNKHEAMITDLEerlRREEKQRQELEKTRRKLEGDSTDlSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQK 1099
Cdd:pfam15921 374 NLDDQLQKLLADLH---KREKELSLEKEQNKRLWDRDTGN-SITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQ 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1100 NMALKKIRELESQISELQEDLESERasrnkaeKQKRDLGEELEALKTELEDT----LDSTAAQQEL-RSKREQEVNILKK 1174
Cdd:pfam15921 450 MAAIQGKNESLEKVSSLTAQLESTK-------EMLRKVVEELTAKKMTLESSertvSDLTASLQEKeRAIEATNAEITKL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1175 TLEEEAKTHEAQIQEMRQKHSQAVEELAE--QLEQTKRVKAnLEKAKQTLENER---GELANEVKVLLQGKGDSEHKRKK 1249
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEalKLQMAEKDKV-IEILRQQIENMTqlvGQHGRTAGAMQVEKAQLEKEIND 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1250 VEAQLQELQVKFNEGERVRTELADKVTKLqvELDNVTglLSQSDSKSSKLTKDFSalesqlQDTQELLQEENRQKLSLST 1329
Cdd:pfam15921 602 RRLELQEFKILKDKKDAKIRELEARVSDL--ELEKVK--LVNAGSERLRAVKDIK------QERDQLLNEVKTSRNELNS 671
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 29436380 1330 KLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:pfam15921 672 LSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLK 716
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1012-1336 |
3.01e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 71.74 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1012 EEKSKSLAKLKNKHEAMITDleerlrrEEKQRQELEKTRRKLEGDSTDLSDQIA-------ELQAQIAELKMQLAKKEEE 1084
Cdd:pfam01576 741 EEKRRQLVKQVRELEAELED-------ERKQRAQAVAAKKKLELDLKELEAQIDaankgreEAVKQLKKLQAQMKDLQRE 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1085 LQAALARVEEEAAQKNMALKKIRELESQISELQEDLESerasrnkAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSK 1164
Cdd:pfam01576 814 LEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAA-------SERARRQAQQERDELADEIASGASGKSALQDEKRR 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1165 REQEVNILKKTLEEEAKTHEAQIQEMRqKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELA---NEVKVLLQGKG 1241
Cdd:pfam01576 887 LEARIAQLEEELEEEQSNTELLNDRLR-KSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKaklQEMEGTVKSKF 965
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1242 DS-----EHKRKKVEAQL-QELQVKFNEGERVR-TELADKVTKLQVELDNVTGllSQSDSKSSKLTKDFSALESQLQDTQ 1314
Cdd:pfam01576 966 KSsiaalEAKIAQLEEQLeQESRERQAANKLVRrTEKKLKEVLLQVEDERRHA--DQYKDQAEKGNSRMKQLKRQLEEAE 1043
|
330 340
....*....|....*....|..
gi 29436380 1315 ELLQEENRQKLSLSTKLKQVED 1336
Cdd:pfam01576 1044 EEASRANAARRKLQRELDDATE 1065
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
859-1226 |
4.65e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 4.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 859 EKQLAAENRLTEMETLQSQL--MAEKL-QLQEQLQAETELCAEAEELRARLTAKKQELEEICHDL----EARVEEEEERC 931
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELaeLPERLeELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 932 QHLQAEKKKMQQNIQELEEQLEEEESARQKLQlEKVTTEAKLKKLEEEQIILEDQN--CKLAKEKKLLEDRIAEFTTNLT 1009
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLE-NELEAAALEERLKEARLLLLIAAalLALLGLGGSLLSLILTIAGVLF 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1010 EEEE----KSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDST-------DLSDQIAELQAQIAEL---- 1074
Cdd:COG4717 281 LVLGllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDlspeellELLDRIEELQELLREAeele 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1075 -KMQLAKKEEELQAALARV----EEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDlgEELEALKTELE 1149
Cdd:COG4717 361 eELQLEELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1150 DTLDSTAAQQELRSKREQEVNILKKTLEEEAktheaQIQEMRQKHSQAVEELAEQLEQTKRVK---ANLEKAKQTLENER 1226
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEEDG-----ELAELLQELEELKAELRELAEEWAALKlalELLEEAREEYREER 513
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
856-1373 |
5.31e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 70.77 E-value: 5.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 856 KVREKQLAAENRLTEMETLQSQLMAEKLQ-LQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHL 934
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQaKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 935 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEK 1014
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1015 SKSLAKLKNKHEAmitDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEE 1094
Cdd:pfam02463 337 IEELEKELKELEI---KREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1095 EAAQKNMALKKIRELESQISELQEDLESERA-----------------SRNKAEKQKRDLGEELEALKTELEDTLDSTAA 1157
Cdd:pfam02463 414 ARQLEDLLKEEKKEELEILEEEEESIELKQGklteekeelekqelkllKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1158 QQELRSKREQEVNILKKTLEEEAKTHEA-QIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL 1236
Cdd:pfam02463 494 KLEERSQKESKARSGLKVLLALIKDGVGgRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1237 LQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQEL 1316
Cdd:pfam02463 574 PLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVS 653
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 29436380 1317 LQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKK 1373
Cdd:pfam02463 654 LEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
971-1367 |
6.72e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 6.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 971 AKLKKLEEEQIILEDQNCKLA---KEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAM---------ITDLEERLRR 1038
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAelqEELEELEEELEELEAELEELREELEKLEKLLQLLPLYqelealeaeLAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1039 EEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQL-AKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQ 1117
Cdd:COG4717 151 LEERLEELRELEEELE----ELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1118 EDLESERASRNKAEKQKR-----------DLGEELEALKTELEDTLDSTAA------------------QQELRSKREQE 1168
Cdd:COG4717 227 EELEQLENELEAAALEERlkearlllliaAALLALLGLGGSLLSLILTIAGvlflvlgllallflllarEKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1169 VNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVK-ANLEKAKQTLENERGELANEVKVLLQGKGDSEhkr 1247
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQeLLREAEELEEELQLEELEQEIAALLAEAGVED--- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1248 kkvEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSskLTKDFSALESQLQDTQELLQEENRQKLSL 1327
Cdd:COG4717 384 ---EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELEELREELAEL 458
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 29436380 1328 STKLKQVEDEknsfrEQLEEEEEAKHNLEKQIATLHAQVA 1367
Cdd:COG4717 459 EAELEQLEED-----GELAELLQELEELKAELRELAEEWA 493
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
957-1322 |
7.45e-12 |
|
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: 68.94 E-value: 7.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 957 SARQKLQLEKVTTEAKLK-------KLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMI 1029
Cdd:pfam19220 41 RELPQAKSRLLELEALLAqeraaygKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1030 TDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIREL 1109
Cdd:pfam19220 121 EALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAEL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1110 ESQ-------ISELQEDLESERASRNKAEKQkrdLGEELEALKTEledtldstaaQQELRSKREqevnilkkTLEEEAKT 1182
Cdd:pfam19220 201 ETQldatrarLRALEGQLAAEQAERERAEAQ---LEEAVEAHRAE----------RASLRMKLE--------ALTARAAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1183 HEAQIQEMRqkhsQAVEELAEQLEQTKRVKANLEKAKQTLENERGELanevkvllqgkgdsehkrkkvEAQLQELQVKFN 1262
Cdd:pfam19220 260 TEQLLAEAR----NQLRDRDEAIRAAERRLKEASIERDTLERRLAGL---------------------EADLERRTQQFQ 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1263 EGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENR 1322
Cdd:pfam19220 315 EMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANR 374
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
859-1374 |
1.03e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 69.75 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 859 EKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETElcaEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEK 938
Cdd:pfam05483 201 ELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEIN---DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 939 KKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKlledriaeftTNLTEEEEKSKSL 1018
Cdd:pfam05483 278 KLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKE----------AQMEELNKAKAAH 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1019 AKLKNKHEAMITDLEERLRREEkqrQELEKTRRKLEGDSTDLSDQIAELQaQIAELKMQLAKKEEELQAALARVEEEAAQ 1098
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQ---QRLEKNEDQLKIITMELQKKSSELE-EMTKFKNNKEVELEELKKILAEDEKLLDE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1099 KNMALKKIRELESQISELQEDLESErasrnkaEKQKRDLGEELEALKTELEDTLDS-----TAAQQELRSKREQEVNILK 1173
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELIFLLQAR-------EKEIHDLEIQLTAIKTSEEHYLKEvedlkTELEKEKLKNIELTAHCDK 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1174 KTLEEEAKTHEAQIQEMRQKHSQavEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQ 1253
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQ--EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEN 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1254 LQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQellQEENRQKLSLSTKLKQ 1333
Cdd:pfam05483 575 ARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYE---IKVNKLELELASAKQK 651
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 29436380 1334 VEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:pfam05483 652 FEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1029-1368 |
1.08e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.41 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1029 ITDLEERLRREEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMAL--KKI 1106
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAElpERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1107 RELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQ 1186
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1187 IQEMRQKhsQAVEELAEQLEQTKR----------VKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQE 1256
Cdd:COG4717 229 LEQLENE--LEAAALEERLKEARLllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1257 LQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQlqdTQELLQEENRQKLSLSTKLKQVED 1336
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL---EEELQLEELEQEIAALLAEAGVED 383
|
330 340 350
....*....|....*....|....*....|..
gi 29436380 1337 EKnSFREQLeEEEEAKHNLEKQIATLHAQVAD 1368
Cdd:COG4717 384 EE-ELRAAL-EQAEEYQELKEELEELEEQLEE 413
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1063-1223 |
1.45e-11 |
|
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: 65.72 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1063 QIAELQAQIAELKMQLAKKEEELQAALARVEEeaaqknmALKKIRELESQISELQEDLESERASRNKAEKQkrdLGE--- 1139
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEA-------AKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNvrn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1140 --ELEALKTELEdtldSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEK 1217
Cdd:COG1579 88 nkEYEALQKEIE----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*.
gi 29436380 1218 AKQTLE 1223
Cdd:COG1579 164 EREELA 169
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1068-1374 |
1.46e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1068 QAQIAELkmqLAKKEEELQAALarveEEAA-------QKNMALKKIRE-------LESQISELQEDLESERASRNKAEKQ 1133
Cdd:TIGR02168 143 QGKISEI---IEAKPEERRAIF----EEAAgiskykeRRKETERKLERtrenldrLEDILNELERQLKSLERQAEKAERY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1134 KrDLGEELEALKTELEdTLDSTAAQQELRSKREQevnilKKTLEEEAKTHEAQIQEmrqkhsqaveeLAEQLEQTKRVKA 1213
Cdd:TIGR02168 216 K-ELKAELRELELALL-VLRLEELREELEELQEE-----LKEAEEELEELTAELQE-----------LEEKLEELRLEVS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1214 NLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSD 1293
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1294 SKSSKLTKDFSALESQLQDTQELLQEENRqklslstKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKK 1373
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRS-------KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
.
gi 29436380 1374 K 1374
Cdd:TIGR02168 431 E 431
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
957-1207 |
1.50e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.17 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 957 SARQKLQLEkvttEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFT--TNLTEEEEKSKS----LAKLKNKHEAMIT 1030
Cdd:COG4913 607 DNRAKLAAL----EAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASaereIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1031 D------LEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL----AKKEEELQAALARVEEEAAQKN 1100
Cdd:COG4913 683 SsddlaaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLeaaeDLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1101 MALKKIRELESQISELQEDLeseRASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVnilkktLEEea 1180
Cdd:COG4913 763 VERELRENLEERIDALRARL---NRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG------LPE-- 831
|
250 260
....*....|....*....|....*...
gi 29436380 1181 ktHEAQIQEMRQKHS-QAVEELAEQLEQ 1207
Cdd:COG4913 832 --YEERFKELLNENSiEFVADLLSKLRR 857
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
961-1374 |
1.56e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 69.38 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 961 KLQLEKVTTEAKlKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEamitdleerlRREE 1040
Cdd:pfam15921 73 KEHIERVLEEYS-HQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRES----------QSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1041 KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKE---EELQAALARVEEEAAQK-----NMALKKIRELESQ 1112
Cdd:pfam15921 142 DLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKiyehdSMSTMHFRSLGSA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1113 ISELQEDLESERASrnkAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKR---EQEVNIlkKTLEEEAKTHEAQ--- 1186
Cdd:pfam15921 222 ISKILRELDTEISY---LKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQlisEHEVEI--TGLTEKASSARSQans 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1187 -------IQEM-RQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKV--------------LLQGKGDSE 1244
Cdd:pfam15921 297 iqsqleiIQEQaRNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLanseltearterdqFSQESGNLD 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1245 HKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQE----LLQEE 1320
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMErqmaAIQGK 456
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 29436380 1321 NRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKER 510
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
994-1179 |
4.34e-11 |
|
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: 64.56 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 994 KKLLEdrIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAE 1073
Cdd:COG1579 7 RALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1074 lkmqlAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEdtld 1153
Cdd:COG1579 85 -----VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE---- 155
|
170 180
....*....|....*....|....*.
gi 29436380 1154 stAAQQELRSKREQevniLKKTLEEE 1179
Cdd:COG1579 156 --AELEELEAEREE----LAAKIPPE 175
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1062-1253 |
4.85e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 66.39 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1062 DQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLEserASRNKAEKQKRDLGEEL 1141
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1142 EALK---------------TELEDTLDSTAAQQELRSKREQEVNILKKtLEEEAKTHEAQIQEMRQKHSQAVEELAEQLE 1206
Cdd:COG3883 93 RALYrsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKA-DKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 29436380 1207 QTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQ 1253
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
842-1343 |
5.26e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 842 RQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELcAEAEELRARLTAKKQE----LEEIC 917
Cdd:PTZ00121 1140 RKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEEL-RKAEDARKAEAARKAEeerkAEEAR 1218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 918 HDLEARVEEEEERCQHL--------QAEKKKMQQNIQELEEQLEEEESARQ-------KLQLEKVTTEAKLKKLEEEQII 982
Cdd:PTZ00121 1219 KAEDAKKAEAVKKAEEAkkdaeeakKAEEERNNEEIRKFEEARMAHFARRQaaikaeeARKADELKKAEEKKKADEAKKA 1298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 983 LEDQNCKLAKeKKLLEDRIAEFTTNLTEEEEKSKSlaKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSD 1062
Cdd:PTZ00121 1299 EEKKKADEAK-KKAEEAKKADEAKKKAEEAKKKAD--AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1063 ---QIAELQAQIAELKM--QLAKKEEELQAALARVEEEAAQKNMA--LKKIRELESQISELQEDLESERAS---RNKAEK 1132
Cdd:PTZ00121 1376 akkKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAAKKKAdeAKKKAEEKKKADEAKKKAEEAKKAdeaKKKAEE 1455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1133 QKR--DLGEELEALKT--ELEDTLDSTAAQQELRSKREQ---EVNILKKTLEEEAKTHEAQIQEMRQKHSQAVE-ELAEQ 1204
Cdd:PTZ00121 1456 AKKaeEAKKKAEEAKKadEAKKKAEEAKKADEAKKKAEEakkKADEAKKAAEAKKKADEAKKAEEAKKADEAKKaEEAKK 1535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1205 LEQTKRVKaNLEKAKQTLENERGELANEVKVLLQGKGDSEHK----------RKKVEAQLQELQVKFNEGERVRTELADK 1274
Cdd:PTZ00121 1536 ADEAKKAE-EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKnmalrkaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29436380 1275 VTKLQVELDNVtgllSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFRE 1343
Cdd:PTZ00121 1615 AEEAKIKAEEL----KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
887-1344 |
1.08e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.33 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 887 EQLQAETELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQAEKKKMQQniqeleeqleeeesarqklQLEK 966
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLEK-------------------LLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 967 VTTEAKLKKLEEEQIILEDQncklakeKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDL----EERLRREEKQ 1042
Cdd:COG4717 128 LPLYQELEALEAELAELPER-------LEELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1043 RQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQL--AKKEEELQAALARVEEEAA----------------------- 1097
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALEERLKEARLLLLIAAAllallglggsllsliltiagvlf 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1098 --------QKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQev 1169
Cdd:COG4717 281 lvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE-- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1170 nilkktLEEEAKTHEAQIQE---MRQKHSQAVEELAEQLEQTKRVKaNLEKAKQTLENERGELANEVKVLLQGKGDSEhk 1246
Cdd:COG4717 359 ------LEEELQLEELEQEIaalLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEE-- 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1247 rkkVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNvtglLSQSDsksskltkDFSALESQLQDTQELLQEENRQKLS 1326
Cdd:COG4717 430 ---LEEELEELEEELEELEEELEELREELAELEAELEQ----LEEDG--------ELAELLQELEELKAELRELAEEWAA 494
|
490
....*....|....*...
gi 29436380 1327 LSTKLKQVEDEKNSFREQ 1344
Cdd:COG4717 495 LKLALELLEEAREEYREE 512
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
858-1229 |
1.08e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 858 REKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAE 937
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 938 KKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQ------------IILEDQNCKLAKEKKLLEDRIAEFT 1005
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEadyegflegvkaALLLAGLRGLAGAVAVLIGVEAAYE 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1006 TNLTEEEEKSksLAKLKNKHEAMITDLEERLRREEKQRQE---LEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKE 1082
Cdd:COG1196 538 AALEAALAAA--LQNIVVEDDEVAAAAIEYLKAAKAGRATflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1083 EELQAALARVEEEAAQKNMALKKIRELE-----------------SQISELQEDLESERASRNKAEKQKRDLGEELEALK 1145
Cdd:COG1196 616 YVLGDTLLGRTLVAARLEAALRRAVTLAgrlrevtlegeggsaggSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1146 TELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENE 1225
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
....
gi 29436380 1226 RGEL 1229
Cdd:COG1196 776 IEAL 779
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1053-1281 |
1.81e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 65.42 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1053 LEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALAR--VEEEAAQKNMALKKIRELESQISELQEDLESERASRNKA 1130
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1131 EKQkrdLGEELEALKTELEDTLDSTAAQQelRSKREQEVNILKKTLEEE---AKTHEAQIQEMRQKHSQAVEELAEQLEQ 1207
Cdd:COG3206 246 RAQ---LGSGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29436380 1208 TKRVkanLEKAKQTLENERGELANEVKVLlqgkgdsehkrKKVEAQLQELQVKFNEGERVRTELADKVTKLQVE 1281
Cdd:COG3206 321 ELEA---LQAREASLQAQLAQLEARLAEL-----------PELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
27-72 |
2.16e-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: 57.06 E-value: 2.16e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 29436380 27 AAKKLVWVPSDKSGFEPASLKEEVGEEAIVELvENGKKVKVNKDDI 72
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1026-1230 |
2.17e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.47 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1026 EAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKK 1105
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1106 IRELESQISELQEDLESE-------RASR-NKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLE 1177
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSEsfsdfldRLSAlSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29436380 1178 EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELA 1230
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
897-1125 |
2.37e-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: 64.01 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 897 AEAEELRARLTAKKQELEEICHDLEArveeeeercqhLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKL 976
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA-----------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 977 EEEQIILEDQnckLAKEKKLLEDRIAEFTTNLTEEE-------EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKT 1049
Cdd:COG4942 89 EKEIAELRAE---LEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29436380 1050 RRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERA 1125
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
856-1122 |
4.85e-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: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 856 KVREKQLAAE-NRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEarvEEEEERCQHL 934
Cdd:pfam17380 364 RIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQREVRRL 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 935 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNcklakeKKLLEDRIAEFTTNLTEEEEK 1014
Cdd:pfam17380 441 EEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR------RKILEKELEERKQAMIEEERK 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1015 SKSLAKLKNKHEAMITDLEERLRREEKQRQELE-KTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQaalaRVE 1093
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKA----RAE 590
|
250 260 270
....*....|....*....|....*....|
gi 29436380 1094 EEAAQKNMALKKIreLESQISELQ-EDLES 1122
Cdd:pfam17380 591 YEATTPITTIKPI--YRPRISEYQpPDVES 618
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
862-1371 |
5.48e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 64.09 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 862 LAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICH------DLEARVEEEEERCQHLQ 935
Cdd:pfam12128 206 LEDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHlhfgykSDETLIASRQEERQETS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 936 AEKKkmqqniQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEK------------------KLL 997
Cdd:pfam12128 286 AELN------QLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADietaaadqeqlpswqselENL 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 998 EDRIAEFTTN---LTEEEEKSKSLAKLKNKHEamITDLEERL--RREEKQRQELEKT----------RRKLEGDSTDLSD 1062
Cdd:pfam12128 360 EERLKALTGKhqdVTAKYNRRRSKIKEQNNRD--IAGIKDKLakIREARDRQLAVAEddlqaleselREQLEAGKLEFNE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1063 Q-------IAELQAQIA------ELKMQLAKKEEELQAA-----LARVEEEAAQKNMALKKIR----------------E 1108
Cdd:pfam12128 438 EeyrlksrLGELKLRLNqatatpELLLQLENFDERIERAreeqeAANAEVERLQSELRQARKRrdqasealrqasrrleE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1109 LESQISELQEDLESERAS-----RNKAEKQKRDLGEELEA---LKTELEDTLDSTAAQQE-------LRSKREQ--EVNI 1171
Cdd:pfam12128 518 RQSALDELELQLFPQAGTllhflRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGElnlygvkLDLKRIDvpEWAA 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1172 LKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENER---GELANEVKVLLQGKGDS--EHK 1246
Cdd:pfam12128 598 SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARldlRRLFDEKQSEKDKKNKAlaERK 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1247 RKKVEaQLQEL--QVKFNEG------ERVRTELADKVTKLQVELDNVTGLLsqsDSKSSKLTKDFSALESQLQDTQELLQ 1318
Cdd:pfam12128 678 DSANE-RLNSLeaQLKQLDKkhqawlEEQKEQKREARTEKQAYWQVVEGAL---DAQLALLKAAIAARRSGAKAELKALE 753
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 29436380 1319 EENRQKLslstKLKQVEDEKNSfreqleeeeeakhNLEKQIATLHAQVADMKK 1371
Cdd:pfam12128 754 TWYKRDL----ASLGVDPDVIA-------------KLKREIRTLERKIERIAV 789
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
872-1287 |
5.72e-10 |
|
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: 63.38 E-value: 5.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 872 ETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVeeeeercqhlqaekkkmqqniqeleeq 951
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRV--------------------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 952 leeeesarQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITD 1031
Cdd:pfam07888 83 --------AELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1032 LEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELES 1111
Cdd:pfam07888 155 MKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1112 QISELQEDLESERASRNKAEKqkrdLGEELEALKTELEDTldstaaQQELRSKREQ--EVNILKKTLEEEAKTHEAQIQE 1189
Cdd:pfam07888 235 LLEELRSLQERLNASERKVEG----LGEELSSMAAQRDRT------QAELHQARLQaaQLTLQLADASLALREGRARWAQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1190 MRQKHSQAVEELAEQLEqtkRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQE----LQVKFNEGE 1265
Cdd:pfam07888 305 ERETLQQSAEADKDRIE---KLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQElkasLRVAQKEKE 381
|
410 420
....*....|....*....|....*
gi 29436380 1266 RVRT---ELADKVTKLQVELDNVTG 1287
Cdd:pfam07888 382 QLQAekqELLEYIRQLEQRLETVAD 406
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
859-1235 |
5.83e-10 |
|
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: 64.22 E-value: 5.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 859 EKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERcqhlQAEK 938
Cdd:pfam02463 656 EGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRV----QEAQ 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 939 KKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQncKLAKEKKLLEDRIAEFTTNLTEEEEKSKSL 1018
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEE--REKTEKLKVEEEKEEKLKAQEEELRALEEE 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1019 AKLKNKH----EAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEE 1094
Cdd:pfam02463 810 LKEEAELleeeQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELE 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1095 EAAQKNMALKKIRELESQISELQEDLESERASRNKAEK----QKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVN 1170
Cdd:pfam02463 890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAeillKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAK 969
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29436380 1171 ILKKTLEEEAKTHEAQIQEMRQKhsqavEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKV 1235
Cdd:pfam02463 970 EELGKVNLMAIEEFEEKEERYNK-----DELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSI 1029
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
858-1371 |
5.97e-10 |
|
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: 64.07 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 858 REKQLAAENRlTEMETLQSQLMA---EKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHL 934
Cdd:pfam10174 43 KERALRKEEA-ARISVLKEQYRVtqeENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 935 QAEKKK--------------MQQNIQELEEQLEEEESARQKLqLEKVTTEAKLKKLEEE------------------QII 982
Cdd:pfam10174 122 QSEHERqakelfllrktleeMELRIETQKQTLGARDESIKKL-LEMLQSKGLPKKSGEEdwertrriaeaemqlghlEVL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 983 LEDQNCKLAKEKKLLEDRiaeftTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEkqrQELEKTRRKLEGDSTDLSD 1062
Cdd:pfam10174 201 LDQKEKENIHLREELHRR-----NQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTEDREE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1063 QIAELQA----------QIAELKMQLAKKEEELQAALARVEE------------EAAQKNMALKKIRE--LESQISELQE 1118
Cdd:pfam10174 273 EIKQMEVykshskfmknKIDQLKQELSKKESELLALQTKLETltnqnsdckqhiEVLKESLTAKEQRAaiLQTEVDALRL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1119 DLESERASRNKAEKQKRDLGEELEALKTELEDTLDstaaqqeLRSKREQEVNILKKTLE---EEAKTHEAQIQEMRqkhs 1195
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKD-------MLDVKERKINVLQKKIEnlqEQLRDKDKQLAGLK---- 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1196 QAVEELAEQLEQTKRVKANLEKA----KQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTEL 1271
Cdd:pfam10174 422 ERVKSLQTDSSNTDTALTTLEEAlsekERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDL 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1272 ADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQElLQEENRQKLSLSTKLKQVEDEKNSFREQ------- 1344
Cdd:pfam10174 502 KEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQEVARYKEEsgkaqae 580
|
570 580 590
....*....|....*....|....*....|....
gi 29436380 1345 -------LEEEEEAKHNLEKQIATLHAQVADMKK 1371
Cdd:pfam10174 581 verllgiLREVENEKNDKDKKIAELESLTLRQMK 614
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1106-1374 |
7.69e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1106 IRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEA 1185
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1186 QIQEMR----------QKHSQAVEELAEQLEQ-TKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQL 1254
Cdd:TIGR02169 245 QLASLEeeleklteeiSELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1255 QELQVKFNEGERVRTELADKVTKLQVELDNVTgllsqsdSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQV 1334
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLT-------EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 29436380 1335 EDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN 437
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
859-1340 |
8.28e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 8.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 859 EKQLAAENRLTEMETlqsqlmAEKLQLQEQLQAETELCAEAEELRARLTAKKQEleeichdlEARVEEEEERCQHLQAEK 938
Cdd:PTZ00121 1096 AFGKAEEAKKTETGK------AEEARKAEEAKKKAEDARKAEEARKAEDARKAE--------EARKAEDAKRVEIARKAE 1161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 939 KKMQQNIQELEEQLEEEESARQKLQLEKVTteaKLKKLEEEQIILEDQncKLAKEKKLLEDRIAEfttnlteEEEKSKSL 1018
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAARKAEEVRKAE---ELRKAEDARKAEAAR--KAEEERKAEEARKAE-------DAKKAEAV 1229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1019 AKLKnkheamitdlEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIaelKMQLAKKEEELQAALARVEEEAAQ 1098
Cdd:PTZ00121 1230 KKAE----------EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI---KAEEARKADELKKAEEKKKADEAK 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1099 KNMALKKIRELESQISELQEDLESER----------ASRNKAEKQKRD---LGEELEALKTELEDTLDSTAAQQELRSKR 1165
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKADEAKKkaeeakkkadAAKKKAEEAKKAaeaAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1166 EQEVNILKKTLEEEAKTHEAqiqemrQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGelANEVKVLLQGKGDSEH 1245
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEA------KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK--ADEAKKKAEEAKKADE 1448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1246 KRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDfsalESQLQDTQELLQEENRQKl 1325
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA----AEAKKKADEAKKAEEAKK- 1523
|
490
....*....|....*
gi 29436380 1326 slSTKLKQVEDEKNS 1340
Cdd:PTZ00121 1524 --ADEAKKAEEAKKA 1536
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
863-1100 |
9.34e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 9.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 863 AAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELeeicHDLEARVEEEEERCQHLQAEKKKMQ 942
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI----RALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 943 QNIqeleeqleeeesARQKLQLEKVTTEA-KLKKLEEEQIILEDQNCK--------LAKEKKLLEDRIAEFTTNLTEEEE 1013
Cdd:COG4942 97 AEL------------EAQKEELAELLRALyRLGRQPPLALLLSPEDFLdavrrlqyLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1014 KSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVE 1093
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
....*..
gi 29436380 1094 EEAAQKN 1100
Cdd:COG4942 245 AAGFAAL 251
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
963-1345 |
9.80e-10 |
|
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: 63.05 E-value: 9.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 963 QLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQ 1042
Cdd:COG5185 225 AKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1043 RQELEKTRRKLEgdstdlsdqiaelQAQIAELKMQLAKKEEELQAALARVEEEAAQKNmalkkiRELESQISELQEDLES 1122
Cdd:COG5185 305 IDIKKATESLEE-------------QLAAAEAEQELEESKRETETGIQNLTAEIEQGQ------ESLTENLEAIKEEIEN 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1123 ERASRNKAEKQkrdlgEELEALKTELEDTLDSTaaQQELRSKREQEVNILkKTLEEEAKTHEAQIQEMRQKHSQAVEELA 1202
Cdd:COG5185 366 IVGEVELSKSS-----EELDSFKDTIESTKESL--DEIPQNQRGYAQEIL-ATLEDTLKAADRQIEELQRQIEQATSSNE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1203 EQleqtkrvkanlEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKveaqlQELQVKFNEGERVRTELADKV----TKL 1278
Cdd:COG5185 438 EV-----------SKLLNELISELNKVMREADEESQSRLEEAYDEIN-----RSVRSKKEDLNEELTQIESRVstlkATL 501
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29436380 1279 QVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLK-----QVEDEKNSFREQL 1345
Cdd:COG5185 502 EKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNaktdgQAANLRTAVIDEL 573
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
865-1219 |
1.05e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 865 ENRLTEMETLQSQLMAEKLQLQEQLQAETE---LCAEAEELRARLTAK-KQELEEICHDLEARVEEEEERCQHLQAEKKK 940
Cdd:PRK03918 337 EERLEELKKKLKELEKRLEELEERHELYEEakaKKEELERLKKRLTGLtPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 941 MQQNIQELEEQLEEEESARQKLQL--EKVTTE----------AKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTT-- 1006
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAKGKCPVcgRELTEEhrkelleeytAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEli 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1007 -------------------NLTEEEEKSKSLAKLK---NKHEAMITDLEERLRRE---EKQRQELEKTRRKLEGDSTDLS 1061
Cdd:PRK03918 497 klkelaeqlkeleeklkkyNLEELEKKAEEYEKLKeklIKLKGEIKSLKKELEKLeelKKKLAELEKKLDELEEELAELL 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1062 DQIA--------ELQAQIAELK------MQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLES----- 1122
Cdd:PRK03918 577 KELEelgfesveELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElekky 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1123 -----ERASRNKAEKQKRDLG-----EELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEE-----------EAK 1181
Cdd:PRK03918 657 seeeyEELREEYLELSRELAGlraelEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERveelrekvkkyKAL 736
|
410 420 430
....*....|....*....|....*....|....*...
gi 29436380 1182 THEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAK 1219
Cdd:PRK03918 737 LKERALSKVGEIASEIFEELTEGKYSGVRVKAEENKVK 774
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1026-1370 |
1.25e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1026 EAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQ-AQIAELKMQLAKKEEEL---QAALARVEEEAAQKNM 1101
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELeerERRRARLEALLAALGL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1102 ALKKIRE-LESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDtldstaAQQELRSKREQEVNI------LKK 1174
Cdd:COG4913 374 PLPASAEeFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE------LEAEIASLERRKSNIparllaLRD 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1175 TLEEEAKTHEAQIQ------EMRQKHSQ---AVE------------------ELAEQLEQTK-RVKANLEKAKQTLENER 1226
Cdd:COG4913 448 ALAEALGLDEAELPfvgeliEVRPEEERwrgAIErvlggfaltllvppehyaAALRWVNRLHlRGRLVYERVRTGLPDPE 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1227 GE------LANEVKV-----------LL--------------------------QGKGDSEHKRKK-------------- 1249
Cdd:COG4913 528 RPrldpdsLAGKLDFkphpfrawleaELgrrfdyvcvdspeelrrhpraitragQVKGNGTRHEKDdrrrirsryvlgfd 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1250 VEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLS--QSDSKSSKLTKDFSALESQLQDtqelLQEENRQKLSL 1327
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAE----LEAELERLDAS 683
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 29436380 1328 STKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMK 1370
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1034-1368 |
1.36e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 63.05 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1034 ERLRREEKQRQELEKTRRKLegdsTDLSDQIAELQAQIAELKMQLAKKEEELQAA---LARVEEEAAQKnmalKKIRELE 1110
Cdd:COG3096 282 ELSERALELRRELFGARRQL----AEEQYRLVEMARELEELSARESDLEQDYQAAsdhLNLVQTALRQQ----EKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1111 SQISELQEDLESERASRNKAEKQKRDLGEELEA-------LKTELED---TLDS--TAA---QQELRSKRE-QEVNILKK 1174
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAaeeevdsLKSQLADyqqALDVqqTRAiqyQQAVQALEKaRALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1175 TLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEN-----ERGELANEVKVLLQGKGDSEH---K 1246
Cdd:COG3096 434 LTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKiagevERSQAWQTARELLRRYRSQQAlaqR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1247 RKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTgllsqsdskssKLTKDFSALESQLQDTQELLQEENRQKLS 1326
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-----------ELEELLAELEAQLEELEEQAAEAVEQRSE 582
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 29436380 1327 LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVAD 1368
Cdd:COG3096 583 LRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALAD 624
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
897-1335 |
1.54e-09 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 62.45 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 897 AEAEELRARLTAKKQELE--EICH-----DLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQK----LQLE 965
Cdd:pfam05557 2 AELIESKARLSQLQNEKKqmELEHkrariELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREqaelNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 966 KVTTEAKLKKLEEEQIILEDqncklAKEKKL-LEDRIAEFTTNLTEEEEKSKSLaklknKHEAMitDLEERLRREEKQRQ 1044
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLAD-----AREVIScLKNELSELRRQIQRAELELQST-----NSELE--ELQERLDLLKAKAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1045 ELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEE------------ELQAALARVEEEAAQKNMALKKIRELESQ 1112
Cdd:pfam05557 150 EAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvknskselaripELEKELERLREHNKHLNENIENKLLLKEE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1113 ISELQEDLESERASRNKA---EKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQ----EVNIL--KKTLEEEAKTH 1183
Cdd:pfam05557 230 VEDLKRKLEREEKYREEAatlELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQlqqrEIVLKeeNSSLTSSARQL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1184 EAQIQEMRQKHSQA---VEELAEQLEQTKRVKANLEKA-----------KQTLENERGELANE--VKVLLQGKGDSEHKR 1247
Cdd:pfam05557 310 EKARRELEQELAQYlkkIEDLNKKLKRHKALVRRLQRRvllltkerdgyRAILESYDKELTMSnySPQLLERIEEAEDMT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1248 KKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKltKDFSALESQLQDTQELLQEENRQKLSL 1327
Cdd:pfam05557 390 QKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSK--EEVDSLRRKLETLELERQRLREQKNEL 467
|
....*...
gi 29436380 1328 STKLKQVE 1335
Cdd:pfam05557 468 EMELERRC 475
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1018-1374 |
1.82e-09 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 62.07 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1018 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAA 1097
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1098 QKNMALKKIRELESQ---ISELQEDLESE-RASRNKAEKQKrdlgEELEALKTELEDTLDstaaQQELRSKREQEVNILK 1173
Cdd:pfam05557 84 YLEALNKKLNEKESQladAREVISCLKNElSELRRQIQRAE----LELQSTNSELEELQE----RLDLLKAKASEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1174 KTLE---EEAKTHEAQIQEMRQKHSQAVEELAEqleqTKRVKANLEKAKqTLENERGELANEVKVLLQGKGDSEhkrkKV 1250
Cdd:pfam05557 156 QNLEkqqSSLAEAEQRIKELEFEIQSQEQDSEI----VKNSKSELARIP-ELEKELERLREHNKHLNENIENKL----LL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1251 EAQLQELQVKFNEGERVRTELADkvtkLQVELdnvtgllsqsdsksSKLTKDFSALESQLQDTQELLqeenRQKLSLSTK 1330
Cdd:pfam05557 227 KEEVEDLKRKLEREEKYREEAAT----LELEK--------------EKLEQELQSWVKLAQDTGLNL----RSPEDLSRR 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 29436380 1331 LKQVE-------DEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:pfam05557 285 IEQLQqreivlkEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLK 335
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
937-1360 |
3.70e-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: 61.52 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 937 EKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSK 1016
Cdd:TIGR00618 164 EKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1017 SLAKLKNKHEAMIT---DLEERLRREEK---QRQELEKTRRKLEGDSTDLsdQIAELQAQIAELKMQLAKKEEELQAALA 1090
Cdd:TIGR00618 244 YLTQKREAQEEQLKkqqLLKQLRARIEElraQEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTELQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1091 RVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLgEELEALKTELEDTLdstaAQQELRSKREQEVN 1170
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR-EISCQQHTLTQHIH----TLQQQKTTLTQKLQ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1171 ILKK---TLEEEAKTHEAQIQEMR---------QKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQ 1238
Cdd:TIGR00618 397 SLCKeldILQREQATIDTRTSAFRdlqgqlahaKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1239 GKG---DSEHKRKKVEAQ----LQELQVKFNEGER-----------------VRTELADKVTKLQVELDNVTGllsQSDS 1294
Cdd:TIGR00618 477 TKEqihLQETRKKAVVLArlleLQEEPCPLCGSCIhpnparqdidnpgpltrRMQRGEQTYAQLETSEEDVYH---QLTS 553
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29436380 1295 KSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVED-----EKNSFREQLEEEEEAKHNLEKQIA 1360
Cdd:TIGR00618 554 ERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRlqdltEKLSEAEDMLACEQHALLRKLQPE 624
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1085-1310 |
4.15e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1085 LQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTEL---EDTLDSTAAQQ-E 1160
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELaalEAELAELEKEIaE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1161 LRSKREQEVNILKKTLEEEAKTHE-------------AQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERG 1227
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1228 ELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSklTKDFSALE 1307
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP--AAGFAALK 252
|
...
gi 29436380 1308 SQL 1310
Cdd:COG4942 253 GKL 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1056-1279 |
4.37e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1056 DSTDLSDQIAELQAQIAELkmqlakkeEELQAALarveEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKR 1135
Cdd:COG4913 219 EEPDTFEAADALVEHFDDL--------ERAHEAL----EDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1136 DLG-EELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHE-AQIQEMRQKHSQAVEELAEQLEQTKRVKA 1213
Cdd:COG4913 287 QRRlELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29436380 1214 NLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQ 1279
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
858-1224 |
4.57e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 858 REKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAE 937
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 938 KKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEE----------------------------EQIILEDQNCK 989
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavavligveaayeaaleaalaaaLQNIVVEDDEV 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 990 LAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMI---------------------------TDLEERLRREEKQ 1042
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGaavdlvasdlreadaryyvlgdtllgrTLVAARLEAALRR 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1043 RQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLES 1122
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1123 ERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQEL----RSKREQEVNILKKTLE----------EEAktheaqiQ 1188
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPeppdLEELERELERLEREIEalgpvnllaiEEY-------E 791
|
410 420 430
....*....|....*....|....*....|....*.
gi 29436380 1189 EMRQKHsqavEELAEQLEQtkrvkanLEKAKQTLEN 1224
Cdd:COG1196 792 ELEERY----DFLSEQRED-------LEEARETLEE 816
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
864-1275 |
4.59e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 864 AENRLTEMETLQSQLMAEKLQLQEQLQAETElcaeaEELRARLTAKKQELEEICHDL---EARVEEEEERCQHLQAEKKK 940
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNNQKEQDWN-----KELKSELKNQEKKLEEIQNQIsqnNKIISQLNEQISQLKKELTN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 941 MQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAK 1020
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1021 LKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELqaalarveeeaaqkN 1100
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL--------------K 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1101 MALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTEL---EDTLDSTAAQQELRSKrEQEVNILKKTLE 1177
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkdDFELKKENLEKEIDEK-NKEIEELKQTQK 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1178 EEAKTHEaQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQEL 1257
Cdd:TIGR04523 579 SLKKKQE-EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEI 657
|
410
....*....|....*...
gi 29436380 1258 QVKFNEGERVRTELADKV 1275
Cdd:TIGR04523 658 RNKWPEIIKKIKESKTKI 675
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1009-1225 |
6.20e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1009 TEEEEKSKSLAKLKNKheamITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAA 1088
Cdd:COG3883 16 PQIQAKQKELSELQAE----LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1089 LARVEE------------------EAAQKNMALKKIRELESQ-ISELQEDLESERASRNKAEKQKrdlgEELEALKTELE 1149
Cdd:COG3883 92 ARALYRsggsvsyldvllgsesfsDFLDRLSALSKIADADADlLEELKADKAELEAKKAELEAKL----AELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29436380 1150 DTLDSTAAQQElrskreqEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENE 1225
Cdd:COG3883 168 AAKAELEAQQA-------EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
958-1170 |
6.39e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.42 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 958 ARQKLQlekvTTEAKLKKLEEEQIILEdqnckLAKEKKLLEDRIAEFTTNLT-------EEEEKSKSLAKLKNKHEAMIT 1030
Cdd:COG3206 187 LRKELE----EAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAearaelaEAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1031 DLEE--RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAkkeEELQAALARVEEEAAQknmALKKIRE 1108
Cdd:COG3206 258 ELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ---QEAQRILASLEAELEA---LQAREAS 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29436380 1109 LESQISELQEDLESErasrNKAEKQKRDLGEELEALKTELEDTLdstAAQQELRSKREQEVN 1170
Cdd:COG3206 332 LQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLL---QRLEEARLAEALTVG 386
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
932-1130 |
6.42e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 932 QHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEqiiLEDQNCKLAKEKKLLEDRIAEF-----TT 1006
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREELGERARALyrsggSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1007 NLTEEEEKSKSLA----------KLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKM 1076
Cdd:COG3883 103 SYLDVLLGSESFSdfldrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29436380 1077 QLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKA 1130
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
765-1249 |
6.81e-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: 60.75 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 765 AGVLAHLEEERDLKITDVIIGFQ---ACCRGYLARKAFAKRQQQLTAMKVLQRNCAAYLKLRNWQWWRLFT---KVKPLL 838
Cdd:TIGR00618 410 ATIDTRTSAFRDLQGQLAHAKKQqelQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihlQETRKK 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 839 QVSRQEEEMMAKEEELVKVREKQLAAENRLT-EMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEIC 917
Cdd:TIGR00618 490 AVVLARLLELQEEPCPLCGSCIHPNPARQDIdNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 918 HDLEARVEEEeercQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLK-KLEEEQIILEDQNCklAKEKKL 996
Cdd:TIGR00618 570 QSFSILTQCD----NRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQpEQDLQDVRLHLQQC--SQELAL 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 997 LEDRIAEFTTNLTEEEEKSKSLAKLKNKheamitdlEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKM 1076
Cdd:TIGR00618 644 KLTALHALQLTLTQERVREHALSIRVLP--------KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1077 QLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDtldsta 1156
Cdd:TIGR00618 716 YDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQF------ 789
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1157 aQQELRSKREQEVNILKKTLEEEAKTHEA-------QIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEnergEL 1229
Cdd:TIGR00618 790 -FNRLREEDTHLLKTLEAEIGQEIPSDEDilnlqceTLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA----QL 864
|
490 500
....*....|....*....|
gi 29436380 1230 ANEVKVLLQGKGDSEHKRKK 1249
Cdd:TIGR00618 865 TQEQAKIIQLSDKLNGINQI 884
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
856-1374 |
7.99e-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: 60.45 E-value: 7.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 856 KVREKQLAAENRLTEMETLQSQLMAEKLQL---QEQLQAETELCAEAEELRARLTAKKQELEEICHDL-----EARVEEE 927
Cdd:TIGR00606 420 KERLKQEQADEIRDEKKGLGRTIELKKEILekkQEELKFVIKELQQLEGSSDRILELDQELRKAERELskaekNSLTETL 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 928 EERCQHLQAEKKKMQQNIQELEEQLEEEEsaRQKLQLEKVTTEAKLKKLEEEQI----------------------ILED 985
Cdd:TIGR00606 500 KKEVKSLQNEKADLDRKLRKLDQEMEQLN--HHTTTRTQMEMLTKDKMDKDEQIrkiksrhsdeltsllgyfpnkkQLED 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 986 QNCKLAKEKKLLEDRIAEFTTNLT-----------EEEEKSKSLAKLKNK---------HEAMITDLEERLRREEKQRQE 1045
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELAsleqnknhinnELESKEEQLSSYEDKlfdvcgsqdEESDLERLKEEIEKSSKQRAM 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1046 LE----------------------------KTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAA 1097
Cdd:TIGR00606 658 LAgatavysqfitqltdenqsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQS 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1098 QKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTldsTAAQQELRSKREQEVNILKKTLE 1177
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDV---TIMERFQMELKDVERKIAQQAAK 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1178 EEAKTHEAQIQEMRQKHSQAVEEL---AEQLEQTKRVKANLEKAKQTLENERGELANEvKVLLqgkGDSEHKRKKVEAQL 1254
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQHELdtvVSKIELNRKLIQDQQEQIQHLKSKTNELKSE-KLQI---GTNLQRRQQFEEQL 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1255 QELQVKFNEGERVRTELADKVTKLQVELDNvtgLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQV 1334
Cdd:TIGR00606 891 VELSTEVQSLIREIKDAKEQDSPLETFLEK---DQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDG 967
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 29436380 1335 EDEKnsfreqleeeeeaKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:TIGR00606 968 KDDY-------------LKQKETELNTVNAQLEECEKHQE 994
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
877-1373 |
1.06e-08 |
|
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: 59.98 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 877 QLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQniqeleeQLEEEE 956
Cdd:TIGR00618 167 ELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE-------ALQQTQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 957 SARQKLQlekvtteaKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFtTNLTEEEEKSKSLAKLKnKHEAMITDLEERL 1036
Cdd:TIGR00618 240 QSHAYLT--------QKREAQEEQLKKQQLLKQLRARIEELRAQEAVL-EETQERINRARKAAPLA-AHIKAVTQIEQQA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1037 RREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEelqaaLARVEEEAAQKNMALKKIRELESQISEL 1116
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH-----IRDAHEVATSIREISCQQHTLTQHIHTL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1117 QEDLESERASRNKAEKQKRDLGEelEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKH-- 1194
Cdd:TIGR00618 385 QQQKTTLTQKLQSLCKELDILQR--EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHlq 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1195 --SQAVEELaEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGK-----------GDSEHKRKKVEAQLQELQVKF 1261
Cdd:TIGR00618 463 esAQSLKER-EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGScihpnparqdiDNPGPLTRRMQRGEQTYAQLE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1262 NEGERVRTELADKVTKLQV------ELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVE 1335
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASlkeqmqEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKL 621
|
490 500 510
....*....|....*....|....*....|....*...
gi 29436380 1336 DEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKK 1373
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQER 659
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
998-1296 |
1.32e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 998 EDRIAEFTTNLTEEEEKSKSLA----KLKNKHE------------AMITDLEERLRREEKQRQELEKTRRKLEGDSTDLS 1061
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSfdvqKLQRLHQafsrfigshlavAFEADPEAELRQLNRRRVELERALADHESQEQQQR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1062 DQIAELQAQIAEL-KMQ----------LAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQED---LESERASR 1127
Cdd:PRK04863 865 SQLEQAKEGLSALnRLLprlnlladetLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDpeqFEQLKQDY 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1128 NKAEKQKRDLGEELEALKteledtldstaaqqELRSKR-----EQEVNILKKT--LEEEAKTHEAQIQEMRQKHSQAVEE 1200
Cdd:PRK04863 945 QQAQQTQRDAKQQAFALT--------------EVVQRRahfsyEDAAEMLAKNsdLNEKLRQRLEQAEQERTRAREQLRQ 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1201 LAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL-LQGKGDSEhkrKKVEAQLQELQVKFNEGERVRTELADKVTKLQ 1279
Cdd:PRK04863 1011 AQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLgVPADSGAE---ERARARRDELHARLSANRSRRNQLEKQLTFCE 1087
|
330
....*....|....*..
gi 29436380 1280 VELDNVTGLLSQSDSKS 1296
Cdd:PRK04863 1088 AEMDNLTKKLRKLERDY 1104
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
770-1335 |
1.35e-08 |
|
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: 59.60 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 770 HLEEERDLKITDVIIGFQA-CCRGYLARKAFAKRQQQLTAMK-VLQRNCAAYLKLRNWQwwrlfTKVKPLLQvSRQEEEM 847
Cdd:TIGR00618 351 HSQEIHIRDAHEVATSIREiSCQQHTLTQHIHTLQQQKTTLTqKLQSLCKELDILQREQ-----ATIDTRTS-AFRDLQG 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 848 MAKEEELVKVREKQLAAENRLTEMETLQSQLMAEKLQ--LQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVE 925
Cdd:TIGR00618 425 QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLqeSAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPC 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 926 EEEERCQHLQAEkkkmqqniqeleeqleeeesaRQKLQLEKVTTeAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFT 1005
Cdd:TIGR00618 505 PLCGSCIHPNPA---------------------RQDIDNPGPLT-RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1006 TNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDStdlSDQIAELQAQIAELKMQLAKKEEEL 1085
Cdd:TIGR00618 563 EQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQ---HALLRKLQPEQDLQDVRLHLQQCSQ 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1086 QAALARVEEEAAQKNMALKKIRELESQISELQEDLeseRASRNKAEKQKRDLGEELEALKTELEDTldstaaqQELRSKR 1165
Cdd:TIGR00618 640 ELALKLTALHALQLTLTQERVREHALSIRVLPKEL---LASRQLALQKMQSEKEQLTYWKEMLAQC-------QTLLREL 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1166 EQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKrvkanleKAKQTLENERGELANEVKVLLQGKGDSEH 1245
Cdd:TIGR00618 710 ETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR-------TVLKARTEAHFNNNEEVTAALQTGAELSH 782
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1246 KRKKVEAQLQELQVKFnegervrTELADKVTKLQVELDNVTGLLSQSDSKsskLTKDFSALESQLQDTQELLQEENRQKL 1325
Cdd:TIGR00618 783 LAAEIQFFNRLREEDT-------HLLKTLEAEIGQEIPSDEDILNLQCET---LVQEEEQFLSRLEEKSATLGEITHQLL 852
|
570
....*....|
gi 29436380 1326 SLSTKLKQVE 1335
Cdd:TIGR00618 853 KYEECSKQLA 862
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1009-1269 |
1.47e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 58.38 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1009 TEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAELKMQLAKKEEELQAA 1088
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLR-------EELEQAREELEQLEEELEQARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1089 LARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQE 1168
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1169 VNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRK 1248
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
250 260
....*....|....*....|.
gi 29436380 1249 KVEAQLQELQVKFNEGERVRT 1269
Cdd:COG4372 239 LDALELEEDKEELLEEVILKE 259
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
860-1372 |
1.52e-08 |
|
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: 59.38 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 860 KQLAAENRLTEMETLQSQ--LMAEKLQLQEQLQAETELCAEAEELRARLTAKkqelEEICHDLEARVEEEEERCQHLQAE 937
Cdd:pfam07111 76 RRLEEEVRLLRETSLQQKmrLEAQAMELDALAVAEKAGQAEAEGLRAALAGA----EMVRKNLEEGSQRELEEIQRLHQE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 938 kkkmQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQncklaKEKKLLEDRIAEfttnLTEEEEKSKS 1017
Cdd:pfam07111 152 ----QLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQ-----KEAELLRKQLSK----TQEELEAQVT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1018 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEEL------------ 1085
Cdd:pfam07111 219 LVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELtrkiqpsdslep 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1086 ------QAALARVEEEAAQKNMALK--------KIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDT 1151
Cdd:pfam07111 299 efpkkcRSLLNRWREKVFALMVQLKaqdlehrdSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1152 LDSTAAQQELRSKREQEVNilkkTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELAN 1231
Cdd:pfam07111 379 QMELSRAQEARRRQQQQTA----SAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMAR 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1232 EVKV--LLQGKGDSEHKRKKVEAQLQ-ELQVKFNEGERVRTELADKVTKLQVELDNVTgllSQSDSKSSKLTKDFSALES 1308
Cdd:pfam07111 455 KVALaqLRQESCPPPPPAPPVDADLSlELEQLREERNRLDAELQLSAHLIQQEVGRAR---EQGEAERQQLSEVAQQLEQ 531
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29436380 1309 QLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEA-KHNLEKQIAT----LHAQVADMKKK 1372
Cdd:pfam07111 532 ELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIyGQALQEKVAEvetrLREQLSDTKRR 600
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
859-1320 |
1.64e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 59.43 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 859 EKQLAAENR--------LTEMETLQSQLMAEKLQLQEQLQAET---------ELCAEAEELR----------ARLTAKKQ 911
Cdd:PRK10246 232 EKQLLTAQQqqqqslnwLTRLDELQQEASRRQQALQQALAAEEkaqpqlaalSLAQPARQLRphweriqeqsAALAHTRQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 912 ELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQlEKVTTEAKLKKLEEEQIILEDQNCKLA 991
Cdd:PRK10246 312 QIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNN-ELAGWRAQFSQQTSDREQLRQWQQQLT 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 992 KEKKLLeDRIAEFTTNLTeEEEKSKSLAKLKNKHEamitdLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQI 1071
Cdd:PRK10246 391 HAEQKL-NALPAITLTLT-ADEVAAALAQHAEQRP-----LRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAAL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1072 AELKMQLAKKEEELQAALARVEEEAaqknmalkKIRELESQISELQE---------------------DLESERASRNKA 1130
Cdd:PRK10246 464 NEMRQRYKEKTQQLADVKTICEQEA--------RIKDLEAQRAQLQAgqpcplcgstshpaveayqalEPGVNQSRLDAL 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1131 EKQKRDLGEE-------LEALKTEL---EDTLDSTAAQQELRSKREQEV----NILKKTLEE------EAKTHEAQIQEM 1190
Cdd:PRK10246 536 EKEVKKLGEEgaalrgqLDALTKQLqrdESEAQSLRQEEQALTQQWQAVcaslNITLQPQDDiqpwldAQEEHERQLRLL 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1191 RQKHS-QAveELAEQLEQTKRVKANLEKAKQTLENERGELAnevkVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRT 1269
Cdd:PRK10246 616 SQRHElQG--QIAAHNQQIIQYQQQIEQRQQQLLTALAGYA----LTLPQEDEEASWLATRQQEAQSWQQRQNELTALQN 689
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29436380 1270 ELAdkvtklqvELDNVTGLLSQSDSKSS-----------KLTKDFSALESQLQDTQELLQEE 1320
Cdd:PRK10246 690 RIQ--------QLTPLLETLPQSDDLPHseetvaldnwrQVHEQCLSLHSQLQTLQQQDVLE 743
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1026-1281 |
2.04e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 57.23 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1026 EAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKK 1105
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1106 IRELESQISELQEdlesERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQEL--RSKR-EQEVNILKKTLEEEAKT 1182
Cdd:COG1340 87 LNELREELDELRK----ELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELveKIKElEKELEKAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1183 HE--AQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLE--NERGELANEVKVLLQGKGDSEHKrkkveaQLQELQ 1258
Cdd:COG1340 163 KElrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADelRKEADELHKEIVEAQEKADELHE------EIIELQ 236
|
250 260
....*....|....*....|...
gi 29436380 1259 VKFNEGERVRTELADKVTKLQVE 1281
Cdd:COG1340 237 KELRELRKELKKLRKKQRALKRE 259
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
882-1196 |
2.40e-08 |
|
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: 59.03 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 882 KLQLQEQL-QAETELCAEAEElRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQ 960
Cdd:pfam01576 744 RRQLVKQVrELEAELEDERKQ-RAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRD 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 961 KLQLEKVTTEAKLKKLEEEQIILEDQ----------------------------NCKLAKEKKLLEDRIAEFTTNLTEEE 1012
Cdd:pfam01576 823 EILAQSKESEKKLKNLEAELLQLQEDlaaserarrqaqqerdeladeiasgasgKSALQDEKRRLEARIAQLEEELEEEQ 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1013 EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQI-AELKMQLAKKEEELQAALAR 1091
Cdd:pfam01576 903 SNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVkSKFKSSIAALEAKIAQLEEQ 982
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1092 VEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKreqevni 1171
Cdd:pfam01576 983 LEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRK------- 1055
|
330 340
....*....|....*....|....*
gi 29436380 1172 LKKTLEEEAKTHEAQIQEMRQKHSQ 1196
Cdd:pfam01576 1056 LQRELDDATESNESMNREVSTLKSK 1080
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1025-1277 |
2.49e-08 |
|
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: 57.08 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1025 HEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAqknmalk 1104
Cdd:pfam09787 42 STALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEA------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1105 kirELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQ--EVNILKKTLEEEAKT 1182
Cdd:pfam09787 115 ---ELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQltETLIQKQTMLEALST 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1183 heaqiqemrQKHSQAVEelaeqleqtkrvkanLEKAKQTLENERGELANEVKVLLQGKGDSEHKRkkveaqLQELQVKFN 1262
Cdd:pfam09787 192 ---------EKNSLVLQ---------------LERMEQQIKELQGEGSNGTSINMEGISDGEGTR------LRNVPGLFS 241
|
250
....*....|....*
gi 29436380 1263 EGERVRTELADKVTK 1277
Cdd:pfam09787 242 ESDSDRAGMYGKVRK 256
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
859-1131 |
3.22e-08 |
|
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: 57.38 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 859 EKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETE-LCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAE 937
Cdd:pfam19220 124 ERQLAAETEQNRALEEENKALREEAQAAEKALQRAEgELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQ 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 938 KKKMQQNIQELEEQLEEEESARQKL------QLEKVTTE--AKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTtnlt 1009
Cdd:pfam19220 204 LDATRARLRALEGQLAAEQAERERAeaqleeAVEAHRAEraSLRMKLEALTARAAATEQLLAEARNQLRDRDEAIR---- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1010 EEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAAL 1089
Cdd:pfam19220 280 AAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELT 359
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 29436380 1090 ARVEEEAAqknmalkkirELESQISELQEDLESERASRNKAE 1131
Cdd:pfam19220 360 KRFEVERA----------ALEQANRRLKEELQRERAERALAQ 391
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
858-1099 |
5.14e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 858 REKQL-AAENRLTEMETLQSQLMAEKLQLQEQLqaetelcaeaEELRARLTAKKQELeeicHDLEARVEEEEERCQHLQA 936
Cdd:COG4942 25 AEAELeQLQQEIAELEKELAALKKEEKALLKQL----------AALERRIAALARRI----RALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 937 EKKKMQQNIqeleeqleeeesARQKLQLEKVTTEA-KLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEE-EEK 1014
Cdd:COG4942 91 EIAELRAEL------------EAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEElRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1015 SKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKmqlaKKEEELQAALARVEE 1094
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEA 234
|
....*
gi 29436380 1095 EAAQK 1099
Cdd:COG4942 235 EAAAA 239
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
856-1359 |
6.01e-08 |
|
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: 57.67 E-value: 6.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 856 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQ 935
Cdd:pfam02463 297 ELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 936 AEKKKMQQNIQELEEQLEEEES---------------ARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDR 1000
Cdd:pfam02463 377 AKKKLESERLSSAAKLKEEELElkseeekeaqlllelARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1001 IAEFTTNLtEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAK 1080
Cdd:pfam02463 457 ELKLLKDE-LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1081 KEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE 1160
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEA 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1161 LRSKREQEVNILKKTLEEEAKTHEAQIQEMRQkhSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGK 1240
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESG--LRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEE 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1241 GDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEE 1320
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 29436380 1321 NRQKLSLS------------TKLKQVEDEKNSFREQLEEEEEAKHNLEKQI 1359
Cdd:pfam02463 774 KELAEEREkteklkveeekeEKLKAQEEELRALEEELKEEAELLEEEQLLI 824
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1012-1134 |
6.12e-08 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 57.53 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1012 EEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLakkEEELQAALAR 1091
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKE 581
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 29436380 1092 VEEEAAQknmALKKIRELESQISELQ--EDLESERASRNKAEKQK 1134
Cdd:PRK00409 582 AKKEADE---IIKELRQLQKGGYASVkaHELIEARKRLNKANEKK 623
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
859-1233 |
6.23e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 859 EKQLA-AENRLTEMETLQSQLM--AEKLQLQEQLQAE--TELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQH 933
Cdd:COG4913 344 EREIErLERELEERERRRARLEalLAALGLPLPASAEefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 934 LQAEKKKMQQNIQELEEQLEEEESA-RQKLQLekvtTEAKLK--------KLEEEQ---------------IILEDQNCK 989
Cdd:COG4913 424 LEAEIASLERRKSNIPARLLALRDAlAEALGL----DEAELPfvgelievRPEEERwrgaiervlggfaltLLVPPEHYA 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 990 LAKE--------KKLLEDRIAEFTTNLTEEEEKSKSLA-KLKNK-HEA--------------MITDLEERLRRE------ 1039
Cdd:COG4913 500 AALRwvnrlhlrGRLVYERVRTGLPDPERPRLDPDSLAgKLDFKpHPFrawleaelgrrfdyVCVDSPEELRRHpraitr 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1040 -----------EKQRQELEK--------TRRKLEgdstDLSDQIAELQAQIAELKMQLAKKEEELQA--ALARVEEEAAQ 1098
Cdd:COG4913 580 agqvkgngtrhEKDDRRRIRsryvlgfdNRAKLA----ALEAELAELEEELAEAEERLEALEAELDAlqERREALQRLAE 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1099 KNMALKKIRELESQISELQEDLESERASRNKAEKqkrdLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEE 1178
Cdd:COG4913 656 YSWDEIDVASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE 731
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 29436380 1179 EAKTHEAQIQEMRQKHSQAVEELAEQL---EQTKRVKANLEKAKQTLENERGELANEV 1233
Cdd:COG4913 732 LQDRLEAAEDLARLELRALLEERFAAAlgdAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1026-1160 |
6.59e-08 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 56.40 E-value: 6.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1026 EAMITDLEERLRRE--EKQRQELEKTRRKLEGDSTDLSD------------QIAELQAQIAELKMQLAKKEEELQAALAR 1091
Cdd:COG3524 164 EELVNQLSERAREDavRFAEEEVERAEERLRDAREALLAfrnrngildpeaTAEALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29436380 1092 VEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQkrdlgEELEALKTEL---EDTLDSTAAQQE 1160
Cdd:COG3524 244 LSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLASLL-----AEYERLELERefaEKAYTSALAALE 310
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
993-1218 |
8.25e-08 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 57.25 E-value: 8.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 993 EKKLLEDRiaeftTNLTEEEEKSKSLAklknkhEAMITDLEERLRREEKQRQELEKTRR-----------KLEGDSTDLs 1061
Cdd:PLN03188 1046 EKKLEQER-----LRWTEAESKWISLA------EELRTELDASRALAEKQKHELDTEKRcaeelkeamqmAMEGHARML- 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1062 DQIAELQaqiaELKMQLAKKEEELQAALARVEEEAAQ---KNMALKKIRELESQISELQedleSERasrnkaEKQKRDLG 1138
Cdd:PLN03188 1114 EQYADLE----EKHIQLLARHRRIQEGIDDVKKAAARagvRGAESKFINALAAEISALK----VER------EKERRYLR 1179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1139 EELEALKTELEDTLDSTAAQQEL--RSKREQEVNIL--KKTLEEEAKTHEA--QIQEMRQKHSQAVEELAEQLEQTKRVK 1212
Cdd:PLN03188 1180 DENKSLQAQLRDTAEAVQAAGELlvRLKEAEEALTVaqKRAMDAEQEAAEAykQIDKLKRKHENEISTLNQLVAESRLPK 1259
|
....*.
gi 29436380 1213 ANLEKA 1218
Cdd:PLN03188 1260 EAIRPA 1265
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1025-1232 |
8.68e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1025 HEAMITDLEERLrreEKQRQELEKTRRKLegdSTDLSDQIAELQAQIAELKmqlaKKEEELQAALARVEEEAAQKNMALK 1104
Cdd:COG4717 40 LAFIRAMLLERL---EKEADELFKPQGRK---PELNLKELKELEEELKEAE----EKEEEYAELQEELEELEEELEELEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1105 KIRELESQISEL--QEDLESERASRNKAEKQKRDLGEELEALKTELEDTL----DSTAAQQELRSKREQEVNILKKTLEE 1178
Cdd:COG4717 110 ELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEELReleeELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29436380 1179 EakthEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANE 1232
Cdd:COG4717 190 T----EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1061-1323 |
9.66e-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: 55.93 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1061 SDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEE 1140
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1141 LEALKTELEDTLDstAAQqelRSKREQEVNILkktLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTkrvkanlekakq 1220
Cdd:COG4942 99 LEAQKEELAELLR--ALY---RLGRQPPLALL---LSPEDFLDAVRRLQYLKYLAPARREQAEELRAD------------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1221 tlenergelanevkvllqgkgdsehkRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLT 1300
Cdd:COG4942 159 --------------------------LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
250 260
....*....|....*....|...
gi 29436380 1301 KDFSALESQLQDTQELLQEENRQ 1323
Cdd:COG4942 213 AELAELQQEAEELEALIARLEAE 235
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1018-1146 |
1.08e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 56.40 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1018 LAKLKNKHEAmiTDLEERLRREEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQLAKKE---EELQAALARVEE 1094
Cdd:COG2433 382 LEELIEKELP--EEEPEAEREKEHEERELTEEEEEIR----RLEEQVERLEAEVEELEAELEEKDeriERLERELSEARS 455
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 29436380 1095 EAAQKNMALKKIRELESQISELQEDLESERasrnkaeKQKRDLGEELEALKT 1146
Cdd:COG2433 456 EERREIRKDREISRLDREIERLERELEEER-------ERIEELKRKLERLKE 500
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
932-1345 |
1.12e-07 |
|
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: 56.59 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 932 QHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTT---EAKLKKLEEEQIILEDQNCKLAKekklLEDRIAEFTTNL 1008
Cdd:TIGR00606 203 QEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVksyENELDPLKNRLKEIEHNLSKIMK----LDNEIKALKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1009 TEEEEKSKSLAKLKNK----HEAMITDLEERLRRE----EKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQlak 1080
Cdd:TIGR00606 279 KQMEKDNSELELKMEKvfqgTDEQLNDLYHNHQRTvrekERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQ--- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1081 keeelqaalARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE 1160
Cdd:TIGR00606 356 ---------ADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1161 LRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQ------AVEELAEQLEQTKRVKANLEKAKQTLENErgELANEVK 1234
Cdd:TIGR00606 427 QADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKElqqlegSSDRILELDQELRKAERELSKAEKNSLTE--TLKKEVK 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1235 VLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDN-------VTGLLSQSDSKsSKLTKDFSALE 1307
Cdd:TIGR00606 505 SLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIksrhsdeLTSLLGYFPNK-KQLEDWLHSKS 583
|
410 420 430
....*....|....*....|....*....|....*...
gi 29436380 1308 SQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQL 1345
Cdd:TIGR00606 584 KEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQL 621
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1102-1374 |
1.37e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1102 ALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEdtldstAAQQELRskreqevnilkkTLEEEAK 1181
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA------ALARRIR------------ALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1182 THEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQtlenergelANEVKVLLQGKG--DSEHKRKKVEAQLQELQV 1259
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGR---------QPPLALLLSPEDflDAVRRLQYLKYLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1260 KFNEGERVRTELADKVTKLQVELDnvtgllsqsdsksskltkdfsalesQLQDTQELLQEE----NRQKLSLSTKLKQVE 1335
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERA-------------------------ELEALLAELEEEraalEALKAERQKLLARLE 205
|
250 260 270
....*....|....*....|....*....|....*....
gi 29436380 1336 DEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:COG4942 206 KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
854-1374 |
1.55e-07 |
|
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: 56.21 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 854 LVKVREKQLAAE-----NRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEE 928
Cdd:TIGR00606 346 LVEQGRLQLQADrhqehIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 929 ERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKL--EEEQIILEDQNCKLAKEKKLLEDRIAEFTT 1006
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIleLDQELRKAERELSKAEKNSLTETLKKEVKS 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1007 NLTEEEEKSKSLAKL------KNKHEAMITDLE----------ERLRREEKQ--------------RQELEKTRRKLEGD 1056
Cdd:TIGR00606 506 LQNEKADLDRKLRKLdqemeqLNHHTTTRTQMEmltkdkmdkdEQIRKIKSRhsdeltsllgyfpnKKQLEDWLHSKSKE 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1057 STDLSDQIAELQAQIAEL---KMQLAKKEEELQAALARVEEeaaqKNMALKKIRELESQISELQEDLESERASRN----- 1128
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLeqnKNHINNELESKEEQLSSYED----KLFDVCGSQDEESDLERLKEEIEKSSKQRAmlaga 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1129 --------------------------KAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKT 1182
Cdd:TIGR00606 662 tavysqfitqltdenqsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL 741
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1183 HEAQIQEMRQKHSQAVEELAeqleqtkRVKANLEKAKQTLE--NERGELA----NEVKVLLQGKGDSEHKRKKVEAQLQE 1256
Cdd:TIGR00606 742 KEKEIPELRNKLQKVNRDIQ-------RLKNDIEEQETLLGtiMPEEESAkvclTDVTIMERFQMELKDVERKIAQQAAK 814
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1257 LQVkfNEGERVRTELADKVTKLQVELDNVTgllsqsdsksskltkdfsaleSQLQDTQELLQEENRQKLSLSTKLKQVED 1336
Cdd:TIGR00606 815 LQG--SDLDRTVQQVNQEKQEKQHELDTVV---------------------SKIELNRKLIQDQQEQIQHLKSKTNELKS 871
|
570 580 590
....*....|....*....|....*....|....*...
gi 29436380 1337 EKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:TIGR00606 872 EKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKE 909
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1000-1324 |
1.61e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 56.06 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1000 RIAEFTTNLTEEEEKSKSLAKLKNkheAMITDLEERLRREEKQRQELEKTR-RKLEGDSTDLSDQIAeLQAQIAELKMQL 1078
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQLSD---FQLEDLVGMIQNAEKNILLLNQARlQALEDLEKILTEKEA-LQGKINILEMRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1079 AKKEEELQAalarveeeAAQKNMalkKIRELESQISELQEDLESERASRNKAEKQkrdLGEELEALKTE---LEDtlDST 1155
Cdd:PLN02939 180 SETDARIKL--------AAQEKI---HVEILEEQLEKLRNELLIRGATEGLCVHS---LSKELDVLKEEnmlLKD--DIQ 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1156 AAQQELRSKREQEVNILKktLEEEAKTHEAQIQEMRQKHSQAVEELAEQleQTKRVKANLEKAkQTLENERGELANEVK- 1234
Cdd:PLN02939 244 FLKAELIEVAETEERVFK--LEKERSLLDASLRELESKFIVAQEDVSKL--SPLQYDCWWEKV-ENLQDLLDRATNQVEk 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1235 --VLLQGKGDSEHKRKKVEAQLQELQV-KFNegervrtelADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQ 1311
Cdd:PLN02939 319 aaLVLDQNQDLRDKVDKLEASLKEANVsKFS---------SYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQ 389
|
330
....*....|...
gi 29436380 1312 DTQELLQEENRQK 1324
Cdd:PLN02939 390 DTLSKLKEESKKR 402
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
854-1258 |
1.96e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.11 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 854 LVKVREKQLAAENRLTEMetlqsqlmAEKLQLQEQLQA--ETELCAEAEELRARLTAKKQ---------ELEEICHDLEA 922
Cdd:COG3096 294 LFGARRQLAEEQYRLVEM--------ARELEELSARESdlEQDYQAASDHLNLVQTALRQqekieryqeDLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 923 rveeeeercQHLQAEKKKMQQniqeleeqleeeesARQKLQLEKVTTEAK-LK-KLEEEQIILEDQNCK----------L 990
Cdd:COG3096 366 ---------QEEVVEEAAEQL--------------AEAEARLEAAEEEVDsLKsQLADYQQALDVQQTRaiqyqqavqaL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 991 AKEKKLLEdrIAEFT-TNLTEEEEKSKslAKLKNKHEAMItDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQA 1069
Cdd:COG3096 423 EKARALCG--LPDLTpENAEDYLAAFR--AKEQQATEEVL-ELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTA 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1070 QiaelkmQLAKKEEELQAALARVEEEAAQknmalkkIRELEsQISELQEDLESERASRNKAEKQKRDLGEELEALKTELE 1149
Cdd:COG3096 498 R------ELLRRYRSQQALAQRLQQLRAQ-------LAELE-QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELE 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1150 DTLDStaAQQELRSKREQevnilKKTLEEEAKTHEAQIQEMRQKH------SQAVEELAEQLEQTKRVKANLEKAKQT-L 1222
Cdd:COG3096 564 AQLEE--LEEQAAEAVEQ-----RSELRQQLEQLRARIKELAARApawlaaQDALERLREQSGEALADSQEVTAAMQQlL 636
|
410 420 430
....*....|....*....|....*....|....*.
gi 29436380 1223 ENERGelanevkvLLQGKGDSEHKRKKVEAQLQELQ 1258
Cdd:COG3096 637 ERERE--------ATVERDELAARKQALESQIERLS 664
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1134-1365 |
2.52e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1134 KRDLGEELEALKTELeDTLDstAAQQELRSKREQeVNILKKtLEEEAKTHEAQIQEMRQ-----------KHSQAVEELA 1202
Cdd:COG4913 220 EPDTFEAADALVEHF-DDLE--RAHEALEDAREQ-IELLEP-IRELAERYAAARERLAEleylraalrlwFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1203 EQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKK-VEAQLQELQVKFNEGERVRTELADKVTKLQVE 1281
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1282 LDNVTgllsqsdsksskltKDFSALESQLQDTQELLQEEnrqklslstkLKQVEDEKNSFREQLEEEEEAKHNLEKQIAT 1361
Cdd:COG4913 375 LPASA--------------EEFAALRAEAAALLEALEEE----------LEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
....
gi 29436380 1362 LHAQ 1365
Cdd:COG4913 431 LERR 434
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1083-1239 |
3.37e-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: 53.00 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1083 EELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLD----STAAQ 1158
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikkYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1159 QELRSKRE-----QEVNILKK---TLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELA 1230
Cdd:COG1579 83 GNVRNNKEyealqKEIESLKRrisDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
....*....
gi 29436380 1231 NEVKVLLQG 1239
Cdd:COG1579 163 AEREELAAK 171
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1065-1340 |
4.11e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.92 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1065 AELQAQIAELKMQlaKKEEELQAALARVEEEAAQknmALKKIRELESQISELQEDLEserasrnKAEKQKRDLGEELEAL 1144
Cdd:PRK11281 39 ADVQAQLDALNKQ--KLLEAEDKLVQQDLEQTLA---LLDKIDRQKEETEQLKQQLA-------QAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1145 KTELEDTLDSTAAQQELRskreqevnilkkTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLEN 1224
Cdd:PRK11281 107 KDDNDEETRETLSTLSLR------------QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1225 ERGELANevkVLLQGKGDSEHKRKKVEAQLQ--ELQVKFNegervRTELADKvTKLQvELDNvtgllSQSDSKSSKLTKd 1302
Cdd:PRK11281 175 IRNLLKG---GKVGGKALRPSQRVLLQAEQAllNAQNDLQ-----RKSLEGN-TQLQ-DLLQ-----KQRDYLTARIQR- 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 29436380 1303 fsaLESQLQDTQELLqeeNRQKLSLSTklKQVEDEKNS 1340
Cdd:PRK11281 239 ---LEHQLQLLQEAI---NSKRLTLSE--KTVQEAQSQ 268
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
860-1318 |
4.17e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.36 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 860 KQLAAENRLTEMETLQSQL------MAEKLQLQEQLQAETELCAEAEElraRLTAKKQELEEICHDLE---------ARV 924
Cdd:pfam05557 123 AELELQSTNSELEELQERLdllkakASEAEQLRQNLEKQQSSLAEAEQ---RIKELEFEIQSQEQDSEivknskselARI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 925 EEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQlekvtteaKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEF 1004
Cdd:pfam05557 200 PELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLE--------REEKYREEAATLELEKEKLEQELQSWVKLAQDT 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1005 TTNLTEEEEKSKSLAKLKNK---HEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQ--LA 1079
Cdd:pfam05557 272 GLNLRSPEDLSRRIEQLQQReivLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRvlLL 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1080 KKEEE-LQAALARVEEEAAQKNMALKK---IRELESQISELQEDLESERASRNKAEkqkrdlgEELEALKteledtLDST 1155
Cdd:pfam05557 352 TKERDgYRAILESYDKELTMSNYSPQLlerIEEAEDMTQKMQAHNEEMEAQLSVAE-------EELGGYK------QQAQ 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1156 AAQQELRSKREQEVNilkktleEEAKTHEAQIQEMRQKhsqaVEELAEQLEQTKRVKANLEkakqtLENERGELA----- 1230
Cdd:pfam05557 419 TLERELQALRQQESL-------ADPSYSKEEVDSLRRK----LETLELERQRLREQKNELE-----MELERRCLQgdydp 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1231 NEVKVL-LQGKGDSEHKRKKVEaQLQELQVkfnEGERVRtelaDKVTKLQVELDNVTGLLSQSDSKSSK----LTKDFSA 1305
Cdd:pfam05557 483 KKTKVLhLSMNPAAEAYQQRKN-QLEKLQA---EIERLK----RLLKKLEDDLEQVLRLPETTSTMNFKevldLRKELES 554
|
490
....*....|...
gi 29436380 1306 LESQLQDTQELLQ 1318
Cdd:pfam05557 555 AELKNQRLKEVFQ 567
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
873-1275 |
4.56e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 873 TLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLeARVEEEEErcqhlQAEK-KKMQQNIQELEEQ 951
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHL-NLVQTALR-----QQEKiERYQADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 952 LEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQnckLAKEKKLLE--DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMI 1029
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQ---LADYQQALDvqQTRAIQYQQAVQALERAKQLCGLPDLTADNA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1030 TDLEERLRREEKQR-QELEKTRRKLegdstDLSDQIAELQAQIAELkmqlakkeeeLQAALARVEEEAAQkNMALKKIRE 1108
Cdd:PRK04863 441 EDWLEEFQAKEQEAtEELLSLEQKL-----SVAQAAHSQFEQAYQL----------VRKIAGEVSRSEAW-DVARELLRR 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1109 LESQ-------------ISELQEDLESER-ASRNKAEKQKR-----DLGEELEALKTELEDTLDStaAQQELRSKREQev 1169
Cdd:PRK04863 505 LREQrhlaeqlqqlrmrLSELEQRLRQQQrAERLLAEFCKRlgknlDDEDELEQLQEELEARLES--LSESVSEARER-- 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1170 nilKKTLEEEAKTHEAQIQEMRQKHSQ------AVEELAEQLEQTKRVKANLEKA-KQTLENERGelanevkvLLQGKGD 1242
Cdd:PRK04863 581 ---RMALRQQLEQLQARIQRLAARAPAwlaaqdALARLREQSGEEFEDSQDVTEYmQQLLERERE--------LTVERDE 649
|
410 420 430
....*....|....*....|....*....|....
gi 29436380 1243 SEHKRKKVEAQLQEL-QVKFNEGERVRTeLADKV 1275
Cdd:PRK04863 650 LAARKQALDEEIERLsQPGGSEDPRLNA-LAERF 682
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1184-1374 |
5.15e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1184 EAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELAnevkvllqgkgDSEHKRKKVEAQLQELQVKFNE 1263
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE-----------ALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1264 GervRTELADKVTKLQVELDNVTGLLSQSDSKS-SKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFR 1342
Cdd:COG3883 84 R---REELGERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190
....*....|....*....|....*....|..
gi 29436380 1343 EQLEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1088-1297 |
5.87e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1088 ALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKR-- 1165
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1166 -----EQEVNILKKTLE----EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL 1236
Cdd:COG3883 94 alyrsGGSVSYLDVLLGsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29436380 1237 LQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSS 1297
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
971-1160 |
6.73e-07 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 51.60 E-value: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 971 AKLKKLEEEQIILE----DQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQR-QE 1045
Cdd:pfam04012 15 EGLDKAEDPEKMLEqairDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEkKS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1046 LEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARveEEAAQKNMALKK----------IRELEsQISE 1115
Cdd:pfam04012 95 LEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKAR--LKAAKAQEAVQTslgslstssaTDSFE-RIEE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 29436380 1116 LQEDLESERASRNKAEkQKRDLGEELEALKTELEDTLDSTAAQQE 1160
Cdd:pfam04012 172 KIEEREARADAAAELA-SAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
873-1193 |
6.78e-07 |
|
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: 54.06 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 873 TLQSQLMAEKLQLQEQlqaETELCAEAEELRaRLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQL 952
Cdd:pfam10174 342 ILQTEVDALRLRLEEK---ESFLNKKTKQLQ-DLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 953 EEEESARQKLQLEKVTTEAKLKKLEE-------------EQIILEDQN-----CKLAKEKKLLEDRIAEFTTNLTEEE-- 1012
Cdd:pfam10174 418 AGLKERVKSLQTDSSNTDTALTTLEEalsekeriierlkEQREREDRErleelESLKKENKDLKEKVSALQPELTEKEss 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1013 -----EKSKSLAKLKNKHEAMITDLE----------ERLRREEKQRQELEKTRRKlegdSTDLSDQIAELQAQIAELKMQ 1077
Cdd:pfam10174 498 lidlkEHASSLASSGLKKDSKLKSLEiaveqkkeecSKLENQLKKAHNAEEAVRT----NPEINDRIRLLEQEVARYKEE 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1078 LAKKEEELQAALARVEEEAAQKNMALKKIRELESQIS--------------------------ELQEDL-ESERASRNKA 1130
Cdd:pfam10174 574 SGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLrqmkeqnkkvanikhgqqemkkkgaqLLEEARrREDNLADNSQ 653
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29436380 1131 EKQKRDLGEELEALKTELEDT-LDSTAAQQELRSKREQEVNilkktLEEEAKTHEAQIQEMRQK 1193
Cdd:pfam10174 654 QLQLEELMGALEKTRQELDATkARLSSTQQSLAEKDGHLTN-----LRAERRKQLEEILEMKQE 712
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
962-1181 |
7.77e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 53.75 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 962 LQLEKVTTEAKLKKLEEEQI---ILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEE--KSKSLAkLKNKHEAM------IT 1030
Cdd:PLN02939 175 LEMRLSETDARIKLAAQEKIhveILEEQLEKLRNELLIRGATEGLCVHSLSKELDvlKEENML-LKDDIQFLkaelieVA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1031 DLEERLRREEKQRQELEKTRRKLEgdSTDLSDQiaELQAQIAELKMQ-LAKKEEELQAALARVEEEAAQKNMALKKIREL 1109
Cdd:PLN02939 254 ETEERVFKLEKERSLLDASLRELE--SKFIVAQ--EDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDL 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29436380 1110 ESQISELQEDLESERASRNKAEKQKRdLGEELEALKTELEDTLDSTAAQQELRSKREQEV-NILKKTLEEEAK 1181
Cdd:PLN02939 330 RDKVDKLEASLKEANVSKFSSYKVEL-LQQKLKLLEERLQASDHEIHSYIQLYQESIKEFqDTLSKLKEESKK 401
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
999-1212 |
9.57e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 52.95 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 999 DRIAEfttnLTEEEEKSKSLAKLknkheamitdlEERLRREEKQRQ-ELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQ 1077
Cdd:COG2268 192 RKIAE----IIRDARIAEAEAER-----------ETEIAIAQANREaEEAELEQEREIETARIAEAEAELAKKKAEERRE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1078 lAKKEEELQAALARVEEEAAQKNMalkkirELESQISELQEDLESERASRNKAEKQ-KRDLGEELEALKTELEDTLDSTA 1156
Cdd:COG2268 257 -AETARAEAEAAYEIAEANAEREV------QRQLEIAEREREIELQEKEAEREEAElEADVRKPAEAEKQAAEAEAEAEA 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 29436380 1157 AQQELRSKREQEVniLKKTLEEEAKTHEAQIQEMR-QKHSQAVEELAEQLEQTKRVK 1212
Cdd:COG2268 330 EAIRAKGLAEAEG--KRALAEAWNKLGDAAILLMLiEKLPEIAEAAAKPLEKIDKIT 384
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1056-1167 |
1.10e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 52.36 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1056 DSTDLSDQIAELQAQIAELKMQLAKKE---------EELQAALARVEEEAAQKNMALKKIRELESQ--ISelQEDLESER 1124
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARLEaelgaeaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKgaVS--QQELDEAR 154
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 29436380 1125 ASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQ 1167
Cdd:COG1566 155 AALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAA 197
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
857-1144 |
1.18e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 857 VREKQLAAENRLTEMET----LQSQL--------MAEK--LQLQEQLQA---ETELC-------AEAEELRARLTAKKQE 912
Cdd:PRK04863 374 ADEQQEENEARAEAAEEevdeLKSQLadyqqaldVQQTraIQYQQAVQAlerAKQLCglpdltaDNAEDWLEEFQAKEQE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 913 LEEICHDLEARVEE-EEERCQHLQAekKKMQQNIQELEEQLEEEESARQKLqlekvtteaklKKLEEEQIiledqnckLA 991
Cdd:PRK04863 454 ATEELLSLEQKLSVaQAAHSQFEQA--YQLVRKIAGEVSRSEAWDVARELL-----------RRLREQRH--------LA 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 992 KEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITD---LEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQ 1068
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDedeLEQLQEELEARLESLSESVSEARERRMALRQQLEQLQ 592
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29436380 1069 AQIAELKmQLAKKEEELQAALARVEEeaaQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEAL 1144
Cdd:PRK04863 593 ARIQRLA-ARAPAWLAAQDALARLRE---QSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1006-1270 |
1.34e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.84 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1006 TNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIA-------ELQAQIAELKMQL 1078
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQelrekrdELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1079 AKKEEELQAALARVEE---EAAQKNMALKKIRELESQISELQEDLESERASRNKAEK---QKRDLGEELEALKTELEDTL 1152
Cdd:COG1340 81 DELNEKLNELREELDElrkELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKElveKIKELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1153 DSTAAQQELRSKREQ--EVNILKKTLEEEAKTHEAQIQEMRQKH---SQAVEELAEQLEQTKRVKANLEKAKQTLENERG 1227
Cdd:COG1340 161 KLKELRAELKELRKEaeEIHKKIKELAEEAQELHEEMIELYKEAdelRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 29436380 1228 ELANEVKVLLQGKGDSEHKRKK--VEAQLQELQVKFNEGERVRTE 1270
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKeeLEEKAEEIFEKLKKGEKLTTE 285
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1002-1374 |
1.70e-06 |
|
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: 52.67 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1002 AEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKK 1081
Cdd:pfam02463 657 GLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINE 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1082 EEELQaalaRVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLdstAAQQEL 1161
Cdd:pfam02463 737 ELKLL----KQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL---RALEEE 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1162 RSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKg 1241
Cdd:pfam02463 810 LKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDEL- 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1242 dsEHKRKKVEAQLQELQVKfnegERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELlQEEn 1321
Cdd:pfam02463 889 --ESKEEKEKEEKKELEEE----SQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEE-EEE- 960
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 29436380 1322 rqklslstKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:pfam02463 961 --------RNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1044-1362 |
1.78e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.61 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1044 QELEKTRRKLegdstdlsDQIAELQAQIAELKMQLAKKEEELQ------AALARVEEEAAQKNMALKKIRELESQISELQ 1117
Cdd:PRK11281 63 QDLEQTLALL--------DKIDRQKEETEQLKQQLAQAPAKLRqaqaelEALKDDNDEETRETLSTLSLRQLESRLAQTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1118 EDLESERASRNKAEKQkrdlgeeLEALKTELEDtldstaAQQEL--RSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHS 1195
Cdd:PRK11281 135 DQLQNAQNDLAEYNSQ-------LVSLQTQPER------AQAALyaNSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1196 QAVEELAEQLEQTKRVKANLekakQTLENERGELANEvkvllqgkgdsehKRKKVEAQLQELQVKFNEGERVRTElaDKV 1275
Cdd:PRK11281 202 ALLNAQNDLQRKSLEGNTQL----QDLLQKQRDYLTA-------------RIQRLEHQLQLLQEAINSKRLTLSE--KTV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1276 TKLQveldnvtgllsqsdsksskltkdfSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSF-------REQLEEE 1348
Cdd:PRK11281 263 QEAQ------------------------SQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLtqqnlrvKNWLDRL 318
|
330
....*....|....
gi 29436380 1349 EEAKHNLEKQIATL 1362
Cdd:PRK11281 319 TQSERNIKEQISVL 332
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
991-1323 |
2.16e-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: 52.65 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 991 AKEKKLLEDRIAEFTTNLTEEEEKsksLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQ--IAELQ 1068
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQ---LAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQekIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1069 AQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESE--RA-----SRNKAEKQKR------ 1135
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtRAiqyqqAVQALEKARAlcglpd 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1136 ----DLGEELEALKTElEDTLDST---------------------------------------AAQQELRSKREQevnil 1172
Cdd:COG3096 434 ltpeNAEDYLAAFRAK-EQQATEEvleleqklsvadaarrqfekayelvckiageversqawqTARELLRRYRSQ----- 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1173 kKTLEEEAKTHEAQIQEMRQKHS--QAVEELAEQLEQTKRVK----ANLEKAKQTLENERGELANEVKVLLQGKGDSEHK 1246
Cdd:COG3096 508 -QALAQRLQQLRAQLAELEQRLRqqQNAERLLEEFCQRIGQQldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1247 RKKVEAQLQELQVKfnegERVRTELADKVTKLQ----VELDNVTGLLSQSDSKSSKLTKdFSALESQLQDTQELLQEENR 1322
Cdd:COG3096 587 LEQLRARIKELAAR----APAWLAAQDALERLReqsgEALADSQEVTAAMQQLLERERE-ATVERDELAARKQALESQIE 661
|
.
gi 29436380 1323 Q 1323
Cdd:COG3096 662 R 662
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
880-1309 |
2.25e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.52 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 880 AEKLQLQEQLQAEtELCAEAEELRARLTAK----KQELEEICHDLEARVEEEEERCQHLQAEKKKMqqniqeleeQLEEE 955
Cdd:NF041483 220 AERLLNAASTQAQ-EATDHAEQLRSSTAAEsdqaRRQAAELSRAAEQRMQEAEEALREARAEAEKV---------VAEAK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 956 ESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKK-----LLEDRIAEFTTNLTEEEEKSKS---------LAKL 1021
Cdd:NF041483 290 EAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEALKaeaeqALADARAEAEKLVAEAAEKARTvaaedtaaqLAKA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1022 KNKHEAMITDLEERLRREEKQ-RQELEKTRRKLEGDSTDLSDQIAELQAQiaeLKMQLAKKEEELQAALARVEEEAaqkn 1100
Cdd:NF041483 370 ARTAEEVLTKASEDAKATTRAaAEEAERIRREAEAEADRLRGEAADQAEQ---LKGAAKDDTKEYRAKTVELQEEA---- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1101 malkkiRELESQISELQEDLESErASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEA 1180
Cdd:NF041483 443 ------RRLRGEAEQLRAEAVAE-GERIRGEARREAVQQIEEAARTAEELLTKAKADADELRSTATAESERVRTEAIERA 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1181 KTHEAQIQE-MRQKHSQAVEELAEQLEQTKRVKANLEKAKQTL--ENERGELANevkvllQGKGDSEHKRKKVEAQL--- 1254
Cdd:NF041483 516 TTLRRQAEEtLERTRAEAERLRAEAEEQAEEVRAAAERAARELreETERAIAAR------QAEAAEELTRLHTEAEErlt 589
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 29436380 1255 ---QELQVKFNEGERVRTELADKVTKLQVEL-DNVTGLLSQSDSKSSKLTKDFSALESQ 1309
Cdd:NF041483 590 aaeEALADARAEAERIRREAAEETERLRTEAaERIRTLQAQAEQEAERLRTEAAADASA 648
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
858-1192 |
2.33e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.82 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 858 REKQLAAENRLtEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAE 937
Cdd:pfam07888 59 KEKERYKRDRE-QWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEED 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 938 KKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKS 1017
Cdd:pfam07888 138 IKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1018 LAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSD-------QIAEL---QAQIAELKMQLAKKEEELQA 1087
Cdd:pfam07888 218 LTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrTQAELhqaRLQAAQLTLQLADASLALRE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1088 ALAR--VEEEAAQKNMALKK--IRELESQISELQEDLESERASRNKaekqkrdlgeeleaLKTELEDTLDSTAAQQELRS 1163
Cdd:pfam07888 298 GRARwaQERETLQQSAEADKdrIEKLSAELQRLEERLQEERMEREK--------------LEVELGREKDCNRVQLSESR 363
|
330 340
....*....|....*....|....*....
gi 29436380 1164 KREQEVNILKKTLEEEAKTHEAQIQEMRQ 1192
Cdd:pfam07888 364 RELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
999-1270 |
2.60e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 51.79 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 999 DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERL-RREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQ 1077
Cdd:pfam02029 34 ESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKReERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1078 LAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRD--LGEELEALKTELEDTLDST 1155
Cdd:pfam02029 114 SWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTEnfAKEEVKDEKIKKEKKVKYE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1156 AAQQELRSKREQEVnilkKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQlEQTKRVKAnlEKAKQTLENERGELANEVKV 1235
Cdd:pfam02029 194 SKVFLDQKRGHPEV----KSQNGEEEVTKLKVTTKRRQGGLSQSQEREE-EAEVFLEA--EQKLEELRRRRQEKESEEFE 266
|
250 260 270
....*....|....*....|....*....|....*
gi 29436380 1236 LLQgkgdseHKRKKVEAQLQELQVKFNEGERVRTE 1270
Cdd:pfam02029 267 KLR------QKQQEAELELEELKKKREERRKLLEE 295
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
858-1352 |
2.69e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.13 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 858 REKQLA-AENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLT------AKKQELEEICHDLEARVEEEEER 930
Cdd:pfam10174 183 RTRRIAeAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTviemkdTKISSLERNIRDLEDEVQMLKTN 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 931 ----CQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEeeqiILEDQNCKLAKEKKLLEDriaeftt 1006
Cdd:pfam10174 263 gllhTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLE----TLTNQNSDCKQHIEVLKE------- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1007 NLTEEEEKSkslAKLKNKHEAMITDLEER---LRREEKQRQELEKTRRKLEGDSTDLSD-------QIAELQAQIAELKM 1076
Cdd:pfam10174 332 SLTAKEQRA---AILQTEVDALRLRLEEKesfLNKKTKQLQDLTEEKSTLAGEIRDLKDmldvkerKINVLQKKIENLQE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1077 QLAKKE---EELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERasrnkaEKQKRDLGEELEALKTELEDTLD 1153
Cdd:pfam10174 409 QLRDKDkqlAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQR------EREDRERLEELESLKKENKDLKE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1154 STAAQQELRSKREQEVNILKKTLEEEA----------KTHEAQIQEMRQKHSQAVEEL--AEQLEQTKRVKANLEKAKQT 1221
Cdd:pfam10174 483 KVSALQPELTEKESSLIDLKEHASSLAssglkkdsklKSLEIAVEQKKEECSKLENQLkkAHNAEEAVRTNPEINDRIRL 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1222 LENE-----------RGELANEVKVLLQGKGDSEHKRKKVEA-------QLQELQVKFNEGERVRTELADKVTKLQVELD 1283
Cdd:pfam10174 563 LEQEvarykeesgkaQAEVERLLGILREVENEKNDKDKKIAElesltlrQMKEQNKKVANIKHGQQEMKKKGAQLLEEAR 642
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29436380 1284 NVTGLLSqSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAK 1352
Cdd:pfam10174 643 RREDNLA-DNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMK 710
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1056-1240 |
2.71e-06 |
|
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: 50.88 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1056 DSTDLSDQIAELQAQIAelkmqlakkeeELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEkqkr 1135
Cdd:pfam00529 52 DPTDYQAALDSAEAQLA-----------KAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQ---- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1136 dlgEELEALKTELEDTlDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTK-RVKAN 1214
Cdd:pfam00529 117 ---AQLAQAQIDLARR-RVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELsGAQLQ 192
|
170 180
....*....|....*....|....*..
gi 29436380 1215 LEKAKQTLENERGELAN-EVKVLLQGK 1240
Cdd:pfam00529 193 IAEAEAELKLAKLDLERtEIRAPVDGT 219
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1016-1337 |
2.92e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1016 KSLAKLKNKHEAMitdleerlRREEkqrQELEKTRRKLEGDSTDLSD-------------QIAELQAQIAELKMQLAKKE 1082
Cdd:PRK04863 300 RQLAAEQYRLVEM--------AREL---AELNEAESDLEQDYQAASDhlnlvqtalrqqeKIERYQADLEELEERLEEQN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1083 EELQAALARVEEEAAQKNMALKKIRELESQISELQE--DLESERASRNKAEKQKRD---------------LGEELEALK 1145
Cdd:PRK04863 369 EVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQalDVQQTRAIQYQQAVQALErakqlcglpdltadnAEDWLEEFQ 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1146 TELED-TLDSTAAQQELRS----------------------KREQEVNILKKTLE--EEAKTHEAQIQEMRQKHS----- 1195
Cdd:PRK04863 449 AKEQEaTEELLSLEQKLSVaqaahsqfeqayqlvrkiagevSRSEAWDVARELLRrlREQRHLAEQLQQLRMRLSeleqr 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1196 ----QAVEELAEQLEQtkRVKANLEKAKQtLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTE- 1270
Cdd:PRK04863 529 lrqqQRAERLLAEFCK--RLGKNLDDEDE-LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAw 605
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29436380 1271 --LADKVTKLQveldnvtgllsqsdSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDE 1337
Cdd:PRK04863 606 laAQDALARLR--------------EQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEE 660
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1032-1368 |
2.95e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1032 LEERLrreeKQRQELEKTRRKLEGDSTDLSdqiaELQAQIAELKMQLAKKEEELQAA---LARVEEEAAQKNmalkKIRE 1108
Cdd:PRK04863 285 LEEAL----ELRRELYTSRRQLAAEQYRLV----EMARELAELNEAESDLEQDYQAAsdhLNLVQTALRQQE----KIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1109 LESQISELQEDLESERASRNKAEKQKrdlgEELEALKTELEDTLDSTAAQ----------QELR-SKREQEVNILKKTLE 1177
Cdd:PRK04863 353 YQADLEELEERLEEQNEVVEEADEQQ----EENEARAEAAEEEVDELKSQladyqqaldvQQTRaIQYQQAVQALERAKQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1178 ---------EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTL-----ENERGELANEVKVLLQgkgds 1243
Cdd:PRK04863 429 lcglpdltaDNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVrkiagEVSRSEAWDVARELLR----- 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1244 EHKRKKVEA-QLQELQVKFNEGERvRTELADKVTKLQVELDNVTGLLSQSDSksskltkDFSALESQLQDTQELLQEENR 1322
Cdd:PRK04863 504 RLREQRHLAeQLQQLRMRLSELEQ-RLRQQQRAERLLAEFCKRLGKNLDDED-------ELEQLQEELEARLESLSESVS 575
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 29436380 1323 QKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVAD 1368
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGE 621
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
857-1367 |
3.46e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.72 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 857 VREKQLAAEnrlTEMETLQSQLMAEKLQLQEQLQAETE-LCAEAEELRARLTAKKQELEEIchdlearveEEEERCQHLQ 935
Cdd:PRK10246 189 VFEQHKSAR---TELEKLQAQASGVALLTPEQVQSLTAsLQVLTDEEKQLLTAQQQQQQSL---------NWLTRLDELQ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 936 AEKKKMQQniQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQiilEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKS 1015
Cdd:PRK10246 257 QEASRRQQ--ALQQALAAEEKAQPQLAALSLAQPARQLRPHWERI---QEQSAALAHTRQQIEEVNTRLQSTMALRARIR 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1016 KSLAKLKNKHEAMITDLEERLRREEKQR---QELEKTRRKLEGDSTDlSDQIAELQAQIAELKMQLAKKEEelqAALARV 1092
Cdd:PRK10246 332 HHAAKQSAELQAQQQSLNTWLAEHDRFRqwnNELAGWRAQFSQQTSD-REQLRQWQQQLTHAEQKLNALPA---ITLTLT 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1093 EEEAAQKNMALKKIRELESQISELQEDLeserasrnkAEKQKRdlgeelealKTELEDTLDSTAAQQELRskreqevnil 1172
Cdd:PRK10246 408 ADEVAAALAQHAEQRPLRQRLVALHGQI---------VPQQKR---------LAQLQVAIQNVTQEQTQR---------- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1173 kktleeeakthEAQIQEMRQKHSQAVEELAeqleqtkRVKA--NLEKAKQTLENERGELANEVKVLLQGKgdSEHkrkKV 1250
Cdd:PRK10246 460 -----------NAALNEMRQRYKEKTQQLA-------DVKTicEQEARIKDLEAQRAQLQAGQPCPLCGS--TSH---PA 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1251 EAQLQELQVKFNegERVRTELADKVTKLQVEldnVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTK 1330
Cdd:PRK10246 517 VEAYQALEPGVN--QSRLDALEKEVKKLGEE---GAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNIT 591
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 29436380 1331 LKQVED-----EKNSFREQLEEEEEAKHNLEKQIATLHAQVA 1367
Cdd:PRK10246 592 LQPQDDiqpwlDAQEEHERQLRLLSQRHELQGQIAAHNQQII 633
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1031-1234 |
3.52e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1031 DLEERLRREEKQRQELEKTRRKLE--GDS-TDLSDQIAELQ---AQIAELKMQLAKKEEELQAALARVE--EEAAQKNMA 1102
Cdd:COG3096 890 TLADRLEELREELDAAQEAQAFIQqhGKAlAQLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQIFalSEVVQRRPH 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1103 L--KKIRELESQISELQEDLeseRASRNKAEKQKRDLGEELEALKTELEDtldSTAAQQELRSKREQEVNILKKtLEEEA 1180
Cdd:COG3096 970 FsyEDAVGLLGENSDLNEKL---RARLEQAEEARREAREQLRQAQAQYSQ---YNQVLASLKSSRDAKQQTLQE-LEQEL 1042
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29436380 1181 KTHEAQI-QEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVK 1234
Cdd:COG3096 1043 EELGVQAdAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLR 1097
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1001-1226 |
4.96e-06 |
|
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: 50.72 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1001 IAEFTTNLTEEEEKSKSLAKlknkhEAMITDLEE------RLR--REEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIA 1072
Cdd:pfam15709 302 TFVVTGNMESEEERSEEDPS-----KALLEKREQekasrdRLRaeRAEMRRLEVERKRREQEEQRRLQQEQLERAEKMRE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1073 ELKMQLAKKEEELQAALARVEEEAAQknmalkkiRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTL 1152
Cdd:pfam15709 377 ELELEQQRRFEEIRLRKQRLEEERQR--------QEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAE 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29436380 1153 DSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVkANLEKAKQTLENER 1226
Cdd:pfam15709 449 AEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARL-ALEEAMKQAQEQAR 521
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1041-1276 |
5.38e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 50.84 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1041 KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAEL-KMQLAKKE-EELQAA---LARVEEEAAQKNMALKKIRELE----S 1111
Cdd:COG0497 165 RAWRALKKELEELRADEAERARELDLLRFQLEELeAAALQPGEeEELEEErrrLSNAEKLREALQEALEALSGGEggalD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1112 QISELQEDLesERASRnkAEKQKRDLGEELEALKTELEDtldstaAQQELRSKREQ-EVNilkktlEEE-AKTHE--AQI 1187
Cdd:COG0497 245 LLGQALRAL--ERLAE--YDPSLAELAERLESALIELEE------AASELRRYLDSlEFD------PERlEEVEErlALL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1188 QEMRQKHSQAVEEL-------AEQLEQTKRVKANLEKAKQTLENERGELANEVKVLlqgkgdSEhKRKK--------VEA 1252
Cdd:COG0497 309 RRLARKYGVTVEELlayaeelRAELAELENSDERLEELEAELAEAEAELLEAAEKL------SA-ARKKaakklekaVTA 381
|
250 260 270
....*....|....*....|....*....|.
gi 29436380 1253 QLQEL-------QVKFNEGERVRTELADKVT 1276
Cdd:COG0497 382 ELADLgmpnarfEVEVTPLEEPGPNGADQVE 412
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1141-1374 |
5.48e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1141 LEALKTELEDTLDstAAQQELRSKREQEVNILKKTLEEEakthEAQIQEMRQKHSQaVEELAEQLEQTKRVKANLEKAKQ 1220
Cdd:COG4717 40 LAFIRAMLLERLE--KEADELFKPQGRKPELNLKELKEL----EEELKEAEEKEEE-YAELQEELEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1221 TLENERGELANEVKVLlqgkgDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQveldnvtgllsqsdskssKLT 1300
Cdd:COG4717 113 ELREELEKLEKLLQLL-----PLYQELEALEAELAELPERLEELEERLEELRELEEELE------------------ELE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29436380 1301 KDFSALESQLQDTQELLQEENRQKLS-LSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:COG4717 170 AELAELQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1052-1206 |
5.58e-06 |
|
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: 48.03 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1052 KLEGDSTDLSDQIAELQAQIA----ELKMQLAKKEEELQAALARVEEEAAQK---------NMALKKIRELESQISELQE 1118
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGpvaqELVDRLEKETEALRERLQKDLEEVRAKlepyleelqAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1119 DLEsERASRnKAEKQKRDLGEELEALKTELEDTLDSTAAQ-----QELRSKREQEVNILKKTLEEEAKTHEAQ----IQE 1189
Cdd:pfam01442 81 ELR-KRLNA-DAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAEEVQAQlsqrLQE 158
|
170
....*....|....*..
gi 29436380 1190 MRQKHSQAVEELAEQLE 1206
Cdd:pfam01442 159 LREKLEPQAEDLREKLD 175
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
970-1318 |
7.60e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.67 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 970 EAKLKKLEEEQ------IILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQR 1043
Cdd:PRK01156 325 HAIIKKLSVLQkdyndyIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDP 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1044 QELEKTRRKLEGDSTDLSDQIAELQAQIAEL---KMQLAKKEEELQA-------------------------ALARVEEE 1095
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALrenLDELSRNMEMLNGqsvcpvcgttlgeeksnhiinhyneKKSRLEEK 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1096 AAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKrdlgeeLEALKTELEDTLDSTAAQQE--------------- 1160
Cdd:PRK01156 485 IREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNK------IESARADLEDIKIKINELKDkhdkyeeiknryksl 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1161 ----LRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVL 1236
Cdd:PRK01156 559 kledLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEI 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1237 LQGKGDSEHKRKKVE------AQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQL 1310
Cdd:PRK01156 639 QENKILIEKLRGKIDnykkqiAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI 718
|
....*...
gi 29436380 1311 QDTQELLQ 1318
Cdd:PRK01156 719 NDINETLE 726
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1019-1153 |
8.33e-06 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 50.47 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1019 AKLKNKHEAM---ITDLEERLRREEKQRQELEKtrrklegdstdlsDQIAELQAQIAELKMQLAKKEEELQAALARVEEE 1095
Cdd:COG0542 400 ARVRMEIDSKpeeLDELERRLEQLEIEKEALKK-------------EQDEASFERLAELRDELAELEEELEALKARWEAE 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 29436380 1096 aaqknmalkkiRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLD 1153
Cdd:COG0542 467 -----------KELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
930-1238 |
8.35e-06 |
|
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: 49.42 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 930 RCQHLQAEKKKM-QQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEeQIILEDQNCKLAKEKKLLEDRIAEFTTNL 1008
Cdd:pfam15905 25 KSQRFRKQKAAEsQPNLNNSKDASTPATARKVKSLELKKKSQKNLKESKD-QKELEKEIRALVQERGEQDKRLQALEEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1009 TEEEEKSKSLAKLKNKHEAMITDLEERLRrEEKQRQELEKTRRKLEGDSTDLSDQIAELqaqiaelkMQLAKK-EEELQA 1087
Cdd:pfam15905 104 EKVEAKLNAAVREKTSLSASVASLEKQLL-ELTRVNELLKAKFSEDGTQKKMSSLSMEL--------MKLRNKlEAKMKE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1088 ALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRN--KAEKQKR-DLGEELEALKTELEDTLDSTAAQQELRSK 1164
Cdd:pfam15905 175 VMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIeeKSETEKLlEYITELSCVSEQVEKYKLDIAQLEELLKE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29436380 1165 REQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQ 1238
Cdd:pfam15905 255 KNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1051-1339 |
8.99e-06 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 50.24 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1051 RKLEGDSTDlsdqIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKnmaLKKirELESQISE------LQEDLESER 1124
Cdd:PLN03229 422 KKREAVKTP----VRELEGEVEKLKEQILKAKESSSKPSELALNEMIEK---LKK--EIDLEYTEaviamgLQERLENLR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1125 ASRNKAEKQK----RDLGEELEALKTELEDTLDSTAAQQELRSKRE--QEVNILKKTLEEEAKTHEAQiQEMRQKhSQAV 1198
Cdd:PLN03229 493 EEFSKANSQDqlmhPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlNEFSRAKALSEKKSKAEKLK-AEINKK-FKEV 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1199 EELAEQLEQTKRVKANLEKA------------KQTLENERGELANEVKVLLQGKG-DSEHKRKKveaQLQELQVKFNEGE 1265
Cdd:PLN03229 571 MDRPEIKEKMEALKAEVASSgassgdeldddlKEKVEKMKKEIELELAGVLKSMGlEVIGVTKK---NKDTAEQTPPPNL 647
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29436380 1266 RVRTE-LADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSL---STKLKQVEDEKN 1339
Cdd:PLN03229 648 QEKIEsLNEEINKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEalnSSELKEKFEELE 725
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
984-1168 |
9.37e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 48.45 E-value: 9.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 984 EDQNCKLAKEKKLLED---RIAEFTTNLteEEEKSKSLAKLKNKHEAM-ITDLEERLRREEKQRQELEKTRRKLEGDSTD 1059
Cdd:pfam12795 33 DASKQRAAAYQKALDDapaELRELRQEL--AALQAKAEAAPKEILASLsLEELEQRLLQTSAQLQELQNQLAQLNSQLIE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1060 LSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALK-KIRELESQISELQEDLES-------ERASRNKAE 1131
Cdd:pfam12795 111 LQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQaELAALKAQIDMLEQELLSnnnrqdlLKARRDLLT 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 29436380 1132 KQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQE 1168
Cdd:pfam12795 191 LRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQLAE 227
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
865-1154 |
9.93e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 865 ENRLTEMETLQSQLMAEKLQLQEQLQaetELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQAEKKKMQQN 944
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELK---ELAEKRDELNAQVKELREEAQE----LREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 945 IQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEdRIAEfttnLTEEEEKSKSLAKLKNK 1024
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVE-KIKE----LEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1025 heamITDLEERLRREEKQRQELEKtrrklegDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALK 1104
Cdd:COG1340 162 ----LKELRAELKELRKEAEEIHK-------KIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 29436380 1105 KIRELESQISELQEDLESERASRNKAEKQKRDlgEELEALKTELEDTLDS 1154
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALKREKEK--EELEEKAEEIFEKLKK 278
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1110-1374 |
1.03e-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: 50.12 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1110 ESQISELQEDLESERASRNKAEK-----QKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvniLKKTLEEEAKTHE 1184
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKareveRRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERE---LERIRQEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1185 AQIQE----MRQKHSQAVEELA-EQLEQTKRVKANLEKAKQT--LENERGELANEVKVLLQG-KGDSEHKRKKVEAQLQE 1256
Cdd:pfam17380 363 ERIRQeeiaMEISRMRELERLQmERQQKNERVRQELEAARKVkiLEEERQRKIQQQKVEMEQiRAEQEEARQREVRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1257 LQVKfnEGERVRTELADKVTKLQVELDNvtgllsQSDSKSSKLTKDfsalesQLQDTQELLQEENRqklslstklKQVED 1336
Cdd:pfam17380 443 ERAR--EMERVRLEEQERQQQVERLRQQ------EEERKRKKLELE------KEKRDRKRAEEQRR---------KILEK 499
|
250 260 270
....*....|....*....|....*....|....*...
gi 29436380 1337 EKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:pfam17380 500 ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRRE 537
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1026-1320 |
1.05e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 50.21 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1026 EAMITDLEERLRREEKQRQE-LEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLakKEEELQAALARvEEEAAQKNMALK 1104
Cdd:NF041483 505 ERVRTEAIERATTLRRQAEEtLERTRAEAERLRAEAEEQAEEVRAAAERAAREL--REETERAIAAR-QAEAAEELTRLH 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1105 KirELESQISELQEDLeseRASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE------------------------ 1160
Cdd:NF041483 582 T--EAEERLTAAEEAL---ADARAEAERIRREAAEETERLRTEAAERIRTLQAQAEqeaerlrteaaadasaaraegenv 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1161 ---LRSKREQEVNILKKTLEEEAKTHEAQIQEMRQK-HSQAVEELAEQLEQTKRVKAnleKAKQTLENERGELANEVKvl 1236
Cdd:NF041483 657 avrLRSEAAAEAERLKSEAQESADRVRAEAAAAAERvGTEAAEALAAAQEEAARRRR---EAEETLGSARAEADQERE-- 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1237 lQGKGDSEH----KRKKVEAQLQELQVKFNEGERVRTEL--ADKVTKLQVElDNVTGLLSQSDSKSSKLTkdfSALESQL 1310
Cdd:NF041483 732 -RAREQSEEllasARKRVEEAQAEAQRLVEEADRRATELvsAAEQTAQQVR-DSVAGLQEQAEEEIAGLR---SAAEHAA 806
|
330
....*....|
gi 29436380 1311 QDTQELLQEE 1320
Cdd:NF041483 807 ERTRTEAQEE 816
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1110-1326 |
1.19e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1110 ESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDtldstaAQQELrskreqevnilkKTLEEEAKTHEAQIQE 1189
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE------LQAEL------------EALQAEIDKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1190 MRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENER-GELANEVKVLLQ-GKGDSE------HKRKKVEAQLQELQVKF 1261
Cdd:COG3883 77 AEAEIEERREELGERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKiADADADlleelkADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29436380 1262 NEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLS 1326
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1057-1279 |
1.21e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.75 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1057 STDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQIS-------ELQEDLESERASRNK 1129
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQelrekrdELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1130 AEKQKRDLGEELEALKTELEDTLDSTAAQQELRSK-----REQEVNILKKTLE----EEAKTHEAQIQEMRQKHSQAvEE 1200
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEierleWRQQTEVLSPEEEkelvEKIKELEKELEKAKKALEKN-EK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29436380 1201 LAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQ 1279
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1075-1221 |
1.31e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.47 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1075 KMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEdleserasrnkaekQKRDLGEELEALK---TELEDT 1151
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA--------------EVEELEAELEEKDeriERLERE 449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1152 LDSTAAQQELRSKREQEVNIlkktLEEEAKTHEAQIQEMRQKhsqaVEELAEQLEQTKRVKANLEKAKQT 1221
Cdd:COG2433 450 LSEARSEERREIRKDREISR----LDREIERLERELEEERER----IEELKRKLERLKELWKLEHSGELV 511
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
856-1236 |
1.36e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.84 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 856 KVREKQlaaENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEArveeeeercqHLQ 935
Cdd:pfam12128 475 RAREEQ---EAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLH----------FLR 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 936 AEKKKMQQNIQELEEQ----------LEEEESARQ-------KLQLEKV----------TTEAKLKKLEE----EQIILE 984
Cdd:pfam12128 542 KEAPDWEQSIGKVISPellhrtdldpEVWDGSVGGelnlygvKLDLKRIdvpewaaseeELRERLDKAEEalqsAREKQA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 985 DQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRRE----EKQRQELEKTRRKLEGDSTDL 1060
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERkdsaNERLNSLEAQLKQLDKKHQAW 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1061 SDQIaelQAQIAELKMQLAKK----EEELQAALARVEEEAAQKNMALKkireleSQISELQEDLESERASRNKAEKQKRD 1136
Cdd:pfam12128 702 LEEQ---KEQKREARTEKQAYwqvvEGALDAQLALLKAAIAARRSGAK------AELKALETWYKRDLASLGVDPDVIAK 772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1137 LGEELEALKTELEDTldstaaqqelrSKREQEV----NILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVK 1212
Cdd:pfam12128 773 LKREIRTLERKIERI-----------AVRRQEVlryfDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRR 841
|
410 420
....*....|....*....|....
gi 29436380 1213 ANLEKAKQTLENERGELANEVKVL 1236
Cdd:pfam12128 842 AKLEMERKASEKQQVRLSENLRGL 865
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
995-1322 |
1.39e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 48.76 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 995 KLLEDRIAEFTtnlteeeEKSKSLAKLKNKHEAMITDLEERLRREEKQRQEL-EKTRRklegdstDLSDQIAELQAQIAE 1073
Cdd:pfam00038 7 QELNDRLASYI-------DKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLyEKEIE-------DLRRQLDTLTVERAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1074 LKMQLAKKEEELQAALARVEEEAAQKnmalkkiRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELED--- 1150
Cdd:pfam00038 73 LQLELDNLRLAAEDFRQKYEDELNLR-------TSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEevr 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1151 -------------------TLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRv 1211
Cdd:pfam00038 146 elqaqvsdtqvnvemdaarKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRR- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1212 kanlekakqTLENERGELANevkvlLQGKGDSehkrkkVEAQLQELQvkfnegERvrteladkvtkLQVELDNVTGLLSQ 1291
Cdd:pfam00038 225 ---------TIQSLEIELQS-----LKKQKAS------LERQLAETE------ER-----------YELQLADYQELISE 267
|
330 340 350
....*....|....*....|....*....|.
gi 29436380 1292 sdsksskltkdfsaLESQLQDTQELLQEENR 1322
Cdd:pfam00038 268 --------------LEAELQETRQEMARQLR 284
|
|
| Cortex-I_coil |
pfam09304 |
Cortexillin I, coiled coil; Members of this family are predominantly found in the ... |
1050-1153 |
1.42e-05 |
|
Cortexillin I, coiled coil; Members of this family are predominantly found in the actin-bundling protein Cortexillin I from Dictyostelium discoideum. They adopt a structure consisting of an 18-heptad-repeat alpha-helical coiled-coil, and are a prerequisite for the assembly of Cortexillin I.
Pssm-ID: 312712 [Multi-domain] Cd Length: 107 Bit Score: 45.38 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1050 RRKLEGDSTDLSDQIAELQAQIAELKM---QLAKKEEELQAALARVEEEAAQKNmalKKIRELESQISELQEDLESERAS 1126
Cdd:pfam09304 4 KERLEASKNSLANKLAGLENSLESEKTsreQLIKQKDELESLLASLEQENAERE---KRLRELEAKLDEALKNLELEKLA 80
|
90 100
....*....|....*....|....*..
gi 29436380 1127 RNKAEKQKRDLGEELEALKTELEDTLD 1153
Cdd:pfam09304 81 RMELESRLSKTEKDKAILELKLAEALD 107
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1006-1213 |
1.44e-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: 49.37 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1006 TNLTEEEEKSKSLAKLKNKheamITDLEERLRREEKQrqELEKT--------RRKLEGDSTDLSDQIAELQAQIAELKMQ 1077
Cdd:pfam09731 229 DNVEEKVEKAQSLAKLVDQ----YKELVASERIVFQQ--ELVSIfpdiipvlKEDNLLSNDDLNSLIAHAHREIDQLSKK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1078 LA--KKEEELQAALARVEEEAAQKNMALKKIRELESQIS--ELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLD 1153
Cdd:pfam09731 303 LAelKKREEKHIERALEKQKEELDKLAEELSARLEEVRAadEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLK 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29436380 1154 STAAQQELRSKREQEVNIlKKTLEEEAKTHEAQIQEMRQK---HSQAVEELAEQLEQTKRVKA 1213
Cdd:pfam09731 383 DVLVEQEIELQREFLQDI-KEKVEEERAGRLLKLNELLANlkgLEKATSSHSEVEDENRKAQQ 444
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
960-1248 |
1.48e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 960 QKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRRE 1039
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1040 EKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAalARVEEEAAQKNMALKKIRELESQISELQED 1119
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA--LEQELQALSEAEAEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1120 LESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVE 1199
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 29436380 1200 ELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRK 1248
Cdd:COG4372 279 EIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
972-1363 |
1.57e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.45 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 972 KLKKLEEEQIILEDQ--NCKLAKEKKLledriaefttNLTEEEEKS-----KSLAKLKNKH----EAMITDLEERLR--R 1038
Cdd:PRK04778 30 RIDELEERKQELENLpvNDELEKVKKL----------NLTGQSEEKfeewrQKWDEIVTNSlpdiEEQLFEAEELNDkfR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1039 EEKQRQELEKTRRKLEgdstDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEeaAQKNMALKK------IRELESQ 1112
Cdd:PRK04778 100 FRKAKHEINEIESLLD----LIEEDIEQILEELQELLESEEKNREEVEQLKDLYRE--LRKSLLANRfsfgpaLDELEKQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1113 ISELQEDLE-----SERASRNKAEKQKRDLGEELEALKTELED--TLDSTAaQQELRSKREQEVNILKKTLEE----EAK 1181
Cdd:PRK04778 174 LENLEEEFSqfvelTESGDYVEAREILDQLEEELAALEQIMEEipELLKEL-QTELPDQLQELKAGYRELVEEgyhlDHL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1182 THEAQIQEMRQKHSQAVEELAEqLEqTKRVKANLEKAKQTLENERGELANEV---KVLLQGKGDSEHKRKKVEAQLQELQ 1258
Cdd:PRK04778 253 DIEKEIQDLKEQIDENLALLEE-LD-LDEAEEKNEEIQERIDQLYDILEREVkarKYVEKNSDTLPDFLEHAKEQNKELK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1259 vkfNEGERVR------TELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSLSTKLK 1332
Cdd:PRK04778 331 ---EEIDRVKqsytlnESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQ 407
|
410 420 430
....*....|....*....|....*....|.
gi 29436380 1333 QVEDEKNSFREQLEEEEEAKHNLEKQIATLH 1363
Cdd:PRK04778 408 GLRKDELEAREKLERYRNKLHEIKRYLEKSN 438
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
908-1332 |
1.83e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 48.92 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 908 AKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEE-SARQKLQLEKVtteakLKKLEEEQIILEDQ 986
Cdd:pfam05622 7 EEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTpGGKKYLLLQKQ-----LEQLQEENFRLETA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 987 NCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKheamITDLEERLRREEKQRQELEKTRRKLEgDSTDLSDQIAE 1066
Cdd:pfam05622 82 RDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDE----MDILRESSDKVKKLEATVETYKKKLE-DLGDLRRQVKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1067 LQAQIAELKMQLAKKEEELQAAlarveeeaaqkNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKT 1146
Cdd:pfam05622 157 LEERNAEYMQRTLQLEEELKKA-----------NALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1147 EledtldstaaQQELRSKREqevnILKKTLEE-----EAKTHEAQIQEMRQKHSQAVEELAEQLeQTKRVKANLEKakqt 1221
Cdd:pfam05622 226 E----------KERLIIERD----TLRETNEElrcaqLQQAELSQADALLSPSSDPGDNLAAEI-MPAEIREKLIR---- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1222 lenergeLANEVKVL-LQGKGDSEHKRKKVEAQLQELQVKFNEgerVRTEL---ADKVTKLQVELDNVTGLLSQSDSK-- 1295
Cdd:pfam05622 287 -------LQHENKMLrLGQEGSYRERLTELQQLLEDANRRKNE---LETQNrlaNQRILELQQQVEELQKALQEQGSKae 356
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 29436380 1296 -SSKLTKDFSALESQLQDTQELLQ------EENRQKLSLSTKLK 1332
Cdd:pfam05622 357 dSSLLKQKLEEHLEKLHEAQSELQkkkeqiEELEPKQDSNLAQK 400
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
861-1116 |
1.91e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 861 QLAAENRLTEMETLQSQLMAEKLQLQEQLQAetelcAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKK 940
Cdd:COG1196 564 EYLKAAKAGRATFLPLDKIRARAALAAALAR-----GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 941 MQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAK 1020
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1021 LKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKK-------EEELQAALARVE 1093
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaIEEYEELEERYD 798
|
250 260
....*....|....*....|...
gi 29436380 1094 EEAAQKNMALKKIRELESQISEL 1116
Cdd:COG1196 799 FLSEQREDLEEARETLEEAIEEI 821
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
999-1311 |
1.92e-05 |
|
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.
Pssm-ID: 462752 [Multi-domain] Cd Length: 307 Bit Score: 48.43 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 999 DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKtrrKLEGDSTDLSDQIAELQAQIAELKMQL 1078
Cdd:pfam09311 2 DMCSNYEKQLQAIQEQEAETRDQVKKLQEMLRQANDQLEKTMKDKKELED---KMNQLSEETSNQVSTLAKRNQKSETLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1079 akkeEELQAALARVEEEAA-QKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTEL--------E 1149
Cdd:pfam09311 79 ----DELQQAFSQAKRNFQdQLAVLMDSREQVSDELVRLQKDNESLQGKHSLHVSLQQAEKFDMPDTVQELqelvlkyrE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1150 DTLDSTAAQQELRSKREQEVNILKKTLEEEakthEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQtlenERGEL 1229
Cdd:pfam09311 155 ELIEVRTAADHMEEKLKAEILFLKEQIQAE----QCLKENLEETLQAEIENCKEEIASISSLKVELERIKA----EKEQL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1230 ANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNvtgllsqsdskSSKLTKDFSALESQ 1309
Cdd:pfam09311 227 ENGLTEKIRQLEDLQTTKGSLETQLKKETNEKAAVEQLVFEEKNKAQRLQTELDV-----------SEQVQRDFVKLSQT 295
|
..
gi 29436380 1310 LQ 1311
Cdd:pfam09311 296 LQ 297
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1074-1221 |
2.11e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1074 LKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQ--ISELQEDLESE-RASRNKAEKQKRDLGEELEALKTELED 1150
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKeeIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1151 tLDSTaaQQELrSKREQEVNILKKTLEEEAKTHEAQIQEMRQK--------HSQAVEELAEQLEQ------TKRVKANLE 1216
Cdd:PRK12704 105 -LEKR--EEEL-EKKEKELEQKQQELEKKEEELEELIEEQLQElerisgltAEEAKEILLEKVEEearheaAVLIKEIEE 180
|
....*
gi 29436380 1217 KAKQT 1221
Cdd:PRK12704 181 EAKEE 185
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
990-1115 |
2.36e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.04 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 990 LAKEKKL-LEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLrreekqrQELEKTRRKLEGDSTDLSDQIAELQ 1068
Cdd:PRK09039 71 LERQGNQdLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRA-------GELAQELDSEKQVSARALAQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 29436380 1069 AQIAELKMQLAKKEEELQAALARVEEEAAQ-------KNMAL-KKIRELESQISE 1115
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKiadlgrrLNVALaQRVQELNRYRSE 198
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
883-1218 |
2.51e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 48.53 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 883 LQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQqniqeleeqleEEESARQKL 962
Cdd:pfam05622 62 LLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMD-----------ILRESSDKV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 963 QLEKVTTEAKLKKLEEeqiiLEDqnckLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEA---MITDLE------ 1033
Cdd:pfam05622 131 KKLEATVETYKKKLED----LGD----LRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETykrQVQELHgklsee 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1034 ----ERLRREEKQRQE----LEKTRRKLEGDSTDLSDQIAEL---QAQIAELKMQLAKKEE---------------ELQA 1087
Cdd:pfam05622 203 skkaDKLEFEYKKLEEkleaLQKEKERLIIERDTLRETNEELrcaQLQQAELSQADALLSPssdpgdnlaaeimpaEIRE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1088 ALARVEEEaaQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTldsTAAQQELRSKREQ 1167
Cdd:pfam05622 283 KLIRLQHE--NKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEEL---QKALQEQGSKAED 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 29436380 1168 EVNILKKTLEEEAKTHEAQIQemRQKHSQAVEELAEQLEQTKRVK-ANLEKA 1218
Cdd:pfam05622 358 SSLLKQKLEEHLEKLHEAQSE--LQKKKEQIEELEPKQDSNLAQKiDELQEA 407
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1036-1167 |
2.77e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.04 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1036 LRRE-EKQRQELEKTRRKLegdsTDLSDQIA-------ELQAQIAELKMQLAKKEEE---LQAALARVEEEAAqknmalk 1104
Cdd:PRK09039 44 LSREiSGKDSALDRLNSQI----AELADLLSlerqgnqDLQDSVANLRASLSAAEAErsrLQALLAELAGAGA------- 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29436380 1105 kirELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTEL---EDTLDstAAQQELRSKREQ 1167
Cdd:PRK09039 113 ---AAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLaalEAALD--ASEKRDRESQAK 173
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1031-1345 |
2.83e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 48.33 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1031 DLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIA-----ELKMQLAKKEEELQAALARVE--EEAAQKNM-- 1101
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSyeedsELKPSGQGGLDEEEAFLDRTAkrEERRQKRLqe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1102 ALKKIRELESQISELQEDLESERASRNKAEKqkrdlgeelealkteledtldSTAAQQELRSKREQEVNILKKTLEEEAK 1181
Cdd:pfam02029 82 ALERQKEFDPTIADEKESVAERKENNEEEEN---------------------SSWEKEEKRDSRLGRYKEEETEIREKEY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1182 THEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELA--NEVKVLL-QGKGDSEHKRKKVEAQLQELQ 1258
Cdd:pfam02029 141 QENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKvkYESKVFLdQKRGHPEVKSQNGEEEVTKLK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1259 VKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKDFSAL-ESQLQDTQEL------------LQEENRQKL 1325
Cdd:pfam02029 221 VTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLrQKQQEAELELeelkkkreerrkLLEEEEQRR 300
|
330 340
....*....|....*....|..
gi 29436380 1326 SLSTKLKQV--EDEKNSFREQL 1345
Cdd:pfam02029 301 KQEEAERKLreEEEKRRMKEEI 322
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
960-1373 |
2.91e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.89 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 960 QKLQLEKVTTEAKLKKLE---EEQIILEDQNCKLAKEKKLLEDRIAEFTTnLTEEEEKSKSLAKLKNKHEAMITDLEErl 1036
Cdd:TIGR01612 1229 EKIDEEKKKSEHMIKAMEayiEDLDEIKEKSPEIENEMGIEMDIKAEMET-FNISHDDDKDHHIISKKHDENISDIRE-- 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1037 rreekqrqeleKTRRKLEGDS--TDLSDQIAELQAQIAELKMQLAKKEEELQ--AALARVEEEAAQKNMaLKKIRELESQ 1112
Cdd:TIGR01612 1306 -----------KSLKIIEDFSeeSDINDIKKELQKNLLDAQKHNSDINLYLNeiANIYNILKLNKIKKI-IDEVKEYTKE 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1113 ISELQEDLESERASRNKAEKQKRDlGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKK-----TLEEEAKTHEAQI 1187
Cdd:TIGR01612 1374 IEENNKNIKDELDKSEKLIKKIKD-DINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEesnidTYFKNADENNENV 1452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1188 Q------EMRQKHSQAV----------------EELAEQLEQTKRVKANLEKAKQTLENER---GELANEVKVLL----- 1237
Cdd:TIGR01612 1453 LllfkniEMADNKSQHIlkikkdnatndhdfniNELKEHIDKSKGCKDEADKNAKAIEKNKelfEQYKKDVTELLnkysa 1532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1238 --------QGKGDSE---------HKRKKVEAQLQELQVKFNEGERVRTElaDKVTK----------LQVELDNV-TGLL 1289
Cdd:TIGR01612 1533 laiknkfaKTKKDSEiiikeikdaHKKFILEAEKSEQKIKEIKKEKFRIE--DDAAKndksnkaaidIQLSLENFeNKFL 1610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1290 SQSD--SKSSKLTKDFSALESQLQ----DTQEllqeenrqklslsTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLH 1363
Cdd:TIGR01612 1611 KISDikKKINDCLKETESIEKKISsfsiDSQD-------------TELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD 1677
|
490
....*....|
gi 29436380 1364 AQVADMKKKK 1373
Cdd:TIGR01612 1678 ELDSEIEKIE 1687
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
650-674 |
2.96e-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: 45.80 E-value: 2.96e-05
10 20
....*....|....*....|....*
gi 29436380 650 YKEQLAKLMATLRNTNPNFVRCIIP 674
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
992-1161 |
3.18e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.65 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 992 KEKKL--LEDRIAEFTTNLTEEEEKSKSLaklknkhEAMITDLEERLRREEKQRQelektrrKLEGDSTDLSDQIAELQA 1069
Cdd:PRK09039 51 KDSALdrLNSQIAELADLLSLERQGNQDL-------QDSVANLRASLSAAEAERS-------RLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1070 QIAELKMQLAKKEEELQAALARVEEeaaqknmalkkireLESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELE 1149
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVEL--------------LNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLN 182
|
170
....*....|....
gi 29436380 1150 DTLdstaAQ--QEL 1161
Cdd:PRK09039 183 VAL----AQrvQEL 192
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
860-1097 |
3.34e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 860 KQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETElcaEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQAEKK 939
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNE---EYNELQAELEALQAEIDK----LQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 940 K----MQQNIQELEEQLEEEES-----ARQKLQLEKVTTEAKLKKLEEeqiiLEDQNCKLAKEKKLLEDRIAEFTTNLTE 1010
Cdd:COG3883 90 EraraLYRSGGSVSYLDVLLGSesfsdFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1011 EEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKtrrklegdstdlsdQIAELQAQIAELKMQLAKKEEELQAALA 1090
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA--------------ELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
....*..
gi 29436380 1091 RVEEEAA 1097
Cdd:COG3883 232 AAAAAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
839-1073 |
3.42e-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: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 839 QVSRQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLqaetelcaeaEELRARLTAKKQELEEich 918
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI----------AELRAELEAQKEELAE--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 919 dlearveeeeercqHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEeqiiLEDQNCKLAKEKKLLE 998
Cdd:COG4942 109 --------------LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29436380 999 DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAE 1073
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALIARLEAEAAA 238
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
989-1151 |
3.77e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 989 KLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQ 1068
Cdd:PHA02562 196 QIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1069 --------------------------AQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLES 1122
Cdd:PHA02562 276 kvikmyekggvcptctqqisegpdriTKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLIT 355
|
170 180 190
....*....|....*....|....*....|....*.
gi 29436380 1123 ERASRNKAEK-------QKRDLGEELEALKTELEDT 1151
Cdd:PHA02562 356 LVDKAKKVKAaieelqaEFVDNAEELAKLQDELDKI 391
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
884-1226 |
6.46e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 884 QLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARveeeEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQ 963
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA----RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 964 LEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQR 1043
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1044 QELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESE 1123
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1124 RASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAE 1203
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
330 340
....*....|....*....|...
gi 29436380 1204 QLEQTKRVKANLEKAKQTLENER 1226
Cdd:COG4372 348 VGLLDNDVLELLSKGAEAGVADG 370
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
854-1226 |
6.62e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.16 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 854 LVKVREKQLAAENRLTEMETLQSQLMAEklqLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEarveeeeercqh 933
Cdd:pfam06160 81 FKKAKKALDEIEELLDDIEEDIKQILEE---LDELLESEEKNREEVEELKDKYRELRKTLLANRFSYG------------ 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 934 lQAEKKkmqqniqeleeqleeeesarqklqLEKvtteaKLKKLEEEqiiledqncklakekklledrIAEFTTnLTEE-- 1011
Cdd:pfam06160 146 -PAIDE------------------------LEK-----QLAEIEEE---------------------FSQFEE-LTESgd 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1012 -EEKSKSLAKLKNkheaMITDLEERLRREEKQRQELEktrrklegdsTDLSDQIAELQAQIAELKMQ------------- 1077
Cdd:pfam06160 174 yLEAREVLEKLEE----ETDALEELMEDIPPLYEELK----------TELPDQLEELKEGYREMEEEgyalehlnvdkei 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1078 --LAKKEEELQAALARVEEEAAQKNmalkkIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDST 1155
Cdd:pfam06160 240 qqLEEQLEENLALLENLELDEAEEA-----LEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEEL 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29436380 1156 AAQQELRSKREQEVNILK------KTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENER 1226
Cdd:pfam06160 315 ERVQQSYTLNENELERVRglekqlEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLR 391
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
941-1226 |
6.64e-05 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 47.02 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 941 MQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKL---------------EEEQIILEDQNCKLAKEKKLLED--RIAE 1003
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELylakeedlkrqnavlQEAQVELDALQNQLALARAEMENikAVAT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1004 FTTNLTEE------EEKSKSLAKLKNKHEAMITDLEERL-RREEKQRQELEKTRRKLEGDSTDLSDQIAELQ-AQIAELK 1075
Cdd:pfam03528 86 VSENTKQEaidevkSQWQEEVASLQAIMKETVREYEVQFhRRLEQERAQWNQYRESAEREIADLRRRLSEGQeEENLEDE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1076 MQLAKKE-EELQAALARVEEEAAQKNMAL----KKIRELE-SQISELQEDLESERASRNKAE-------KQKRDLGEELE 1142
Cdd:pfam03528 166 MKKAQEDaEKLRSVVMPMEKEIAALKAKLteaeDKIKELEaSKMKELNHYLEAEKSCRTDLEmyvavlnTQKSVLQEDAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1143 ALKTELEDTldSTAAQQElRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRV------KANLE 1216
Cdd:pfam03528 246 KLRKELHEV--CHLLEQE-RQQHNQLKHTWQKANDQFLESQRLLMRDMQRMESVLTSEQLRQVEEIKKKdqeehkRARTH 322
|
330
....*....|
gi 29436380 1217 KAKQTLENER 1226
Cdd:pfam03528 323 KEKETLKSDR 332
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
960-1255 |
7.37e-05 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 46.98 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 960 QKLQLEKvttEAKLKKLEEEQII-------LEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDL 1032
Cdd:pfam15070 7 KQLQTER---DQYAENLKEEGAVwqqkmqqLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPPAGPSEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1033 EERLRRE-EKQRQELEKTRRKLEG---DSTDLSDQIAELQAQIAELKMQL---AKKEEELQAALARVEEEAAQKNMALKK 1105
Cdd:pfam15070 84 EQRLQEEaEQLQKELEALAGQLQAqvqDNEQLSRLNQEQEQRLLELERAAerwGEQAEDRKQILEDMQSDRATISRALSQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1106 IRELESQISELQED--------------LESERASRNKAEKQKRDLGEELEALKTELEdtLDSTAAqQELRSKREQEVNI 1171
Cdd:pfam15070 164 NRELKEQLAELQNGfvkltnenmeltsaLQSEQHVKKELAKKLGQLQEELGELKETLE--LKSQEA-QSLQEQRDQYLAH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1172 LKK--------TLEEEA--KTHEAQIQEM-RQKHSQ-----AVEELAEQLEQTKRVKANLEKAKQTLENERGELANEvkv 1235
Cdd:pfam15070 241 LQQyvaayqqlASEKEElhKQYLLQTQLMdRLQHEEvqgkvAAEMARQELQETQERLEALTQQNQQLQAQLSLLANP--- 317
|
330 340
....*....|....*....|
gi 29436380 1236 llqGKGDSEHKRKKVEAQLQ 1255
Cdd:pfam15070 318 ---GEGDGLESEEEEEEAPR 334
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1041-1367 |
8.00e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 8.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1041 KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDL 1120
Cdd:TIGR00618 124 KKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1121 ESERASRNKAEKQKRDLGEELEALKTELEDtldstaAQQELRSKREQevnilkktleeeaKTHEAQIQEMRQKHSQAVEE 1200
Cdd:TIGR00618 204 QLLTLCTPCMPDTYHERKQVLEKELKHLRE------ALQQTQQSHAY-------------LTQKREAQEEQLKKQQLLKQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1201 LAEQLEQTKRVKANLEKAkqtleNERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADkVTKLQV 1280
Cdd:TIGR00618 265 LRARIEELRAQEAVLEET-----QERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAA-HVKQQS 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1281 ELDNVTGLLSQSDSKSSKLtkdfsaleSQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIA 1360
Cdd:TIGR00618 339 SIEEQRRLLQTLHSQEIHI--------RDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQA 410
|
....*..
gi 29436380 1361 TLHAQVA 1367
Cdd:TIGR00618 411 TIDTRTS 417
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
969-1112 |
8.22e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 8.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 969 TEAKLKKLEEEQIILEDQNcKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEK 1048
Cdd:PRK01156 617 IDKSIREIENEANNLNNKY-NEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKA 695
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29436380 1049 TRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKeEELQAALARVEE--EAAQKNMALKKIRELESQ 1112
Cdd:PRK01156 696 NRARLESTIEILRTRINELSDRINDINETLESM-KKIKKAIGDLKRlrEAFDKSGVPAMIRKSASQ 760
|
|
| SF-assemblin |
pfam06705 |
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related ... |
1019-1212 |
8.84e-05 |
|
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related beta giardin proteins. During mitosis the SF-assemblin-based cytoskeleton is reorganized; it divides in prophase and is reduced to two dot-like structures at each spindle pole in metaphase. During anaphase, the two dots present at each pole are connected again. In telophase there is an asymmetrical outgrowth of new fibres. It has been suggested that SF-assemblin is involved in re-establishing the microtubular root system characteriztic of interphase cells after mitosis.
Pssm-ID: 284187 [Multi-domain] Cd Length: 247 Bit Score: 45.70 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1019 AKLKNKHEAmITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQI--AELQAQIAELKMQLAKKEEELQAALARVEEEA 1096
Cdd:pfam06705 5 VKLSNMNER-VSGFHDKMENEIEVKRVDEDTRVKMIKEAIAHLEKLiqTESKKRQESFEDIQEEFKKEIDNMQETIKEEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1097 AQKNMALKK-IRELESQISELQEDLESERASRNKAekqkrdlgeeLEALKTELEDTL-DSTAAQQELRSKREQEVNILKK 1174
Cdd:pfam06705 84 DDMAANFRKaLAELNDTINNVETNLQNEIAIHNDA----------IEALRKEALKSLnDLETGIATENAERKKMYDQLNK 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 29436380 1175 TLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVK 1212
Cdd:pfam06705 154 KVAEGFARISAAIDTEKNARDSAVSAATTELTNTKLVE 191
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
879-1089 |
1.06e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 879 MAEKLQLQEQLQA-ETELcAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLeeees 957
Cdd:COG1579 2 MPEDLRALLDLQElDSEL-DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 958 ARQKLQLEKVTTEAKLKKLEEEQIILEdqncklaKEKKLLEDRIAEFttnLTEEEEKSKSLAKLKNKHEAmitdLEERLR 1037
Cdd:COG1579 76 KKYEEQLGNVRNNKEYEALQKEIESLK-------RRISDLEDEILEL---MERIEELEEELAELEAELAE----LEAELE 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29436380 1038 REEKQRQElektrrklegdstdlsdQIAELQAQIAELKMQLAKKEEELQAAL 1089
Cdd:COG1579 142 EKKAELDE-----------------ELAELEAELEELEAEREELAAKIPPEL 176
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1057-1281 |
1.08e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 46.22 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1057 STDLSDQIAELQAQIAE--------------LKMQLaKKEEELQAALARveeeaaqknmalkKIRELESQISELQEDLES 1122
Cdd:PRK11637 42 ASDNRDQLKSIQQDIAAkeksvrqqqqqrasLLAQL-KKQEEAISQASR-------------KLRETQNTLNQLNKQIDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1123 ERASRNKAEKQK----RDLGEELEAL-----KTELEDTLDSTAAQQE---------LRSKREQEVNILKKTLEEEAkthe 1184
Cdd:PRK11637 108 LNASIAKLEQQQaaqeRLLAAQLDAAfrqgeHTGLQLILSGEESQRGerilayfgyLNQARQETIAELKQTREELA---- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1185 AQIQEMRQKHSQAVEELAEQLEQtkrvkanlekaKQTLENERGELANEVKVLlqgkgdsEHKRKKVEAQLQELQVkfNEg 1264
Cdd:PRK11637 184 AQKAELEEKQSQQKTLLYEQQAQ-----------QQKLEQARNERKKTLTGL-------ESSLQKDQQQLSELRA--NE- 242
|
250
....*....|....*..
gi 29436380 1265 ervrTELADKVTKLQVE 1281
Cdd:PRK11637 243 ----SRLRDSIARAERE 255
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
857-1373 |
1.14e-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: 46.96 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 857 VREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELrarLTAKKQELEEICHDLEARVEEEEERCQHLQA 936
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKV---FQGTDEQLNDLYHNHQRTVREKERELVDCQR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 937 EKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDR-IAEFTTNLTE-EEEK 1014
Cdd:TIGR00606 327 ELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERqIKNFHTLVIErQEDE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1015 SKSLAKLKNkheamitDLEERLRREEKQRQELEKTR----RKLEGDSTDLSDQIAELQAQIAELKM------QLAKKEEE 1084
Cdd:TIGR00606 407 AKTAAQLCA-------DLQSKERLKQEQADEIRDEKkglgRTIELKKEILEKKQEELKFVIKELQQlegssdRILELDQE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1085 LQAALARVEEEAAQKNMALKKIRELESQiselQEDLESERASRNKAEKQKrDLGEELEALKTELEDTLDSTAAQQELRSK 1164
Cdd:TIGR00606 480 LRKAERELSKAEKNSLTETLKKEVKSLQ----NEKADLDRKLRKLDQEME-QLNHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1165 REQEVNIL---------KKTLEEEAKTHEAQIQEMRQKHSQAVEELAeQLEQTKRVKANLEKAKQTLENERGELANEVKV 1235
Cdd:TIGR00606 555 KSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELA-SLEQNKNHINNELESKEEQLSSYEDKLFDVCG 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1236 LLQGKGDSEHKRKKVE---AQLQELQVKFNEGERVRTELADK----------VTKLQVELDNVTG-LLSQSDSKSSKLTK 1301
Cdd:TIGR00606 634 SQDEESDLERLKEEIEkssKQRAMLAGATAVYSQFITQLTDEnqsccpvcqrVFQTEAELQEFISdLQSKLRLAPDKLKS 713
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29436380 1302 DFSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKK 1373
Cdd:TIGR00606 714 TESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAK 785
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
867-1226 |
1.14e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.72 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 867 RLTEMETLQSQLMAEKLQLQE---QLQAE-TELCAEAEELRARLTAKKQELEE---IChDLEARVEEEEERCQHLQAEKK 939
Cdd:PRK10246 427 RLVALHGQIVPQQKRLAQLQVaiqNVTQEqTQRNAALNEMRQRYKEKTQQLADvktIC-EQEARIKDLEAQRAQLQAGQP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 940 -----KMQQNIQELEEQLEEEESARQKLQLEKvtteaKLKKLEEEQIILEDQNCKLAKEKKLLED---RIAEFTTNLTEE 1011
Cdd:PRK10246 506 cplcgSTSHPAVEAYQALEPGVNQSRLDALEK-----EVKKLGEEGAALRGQLDALTKQLQRDESeaqSLRQEEQALTQQ 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1012 -EEKSKSLAKLKNKHEamitDLEERLRREEKQRQELEKTRRKLEgdstdLSDQIAELQAQIAELKMQLAKKEEELQAALA 1090
Cdd:PRK10246 581 wQAVCASLNITLQPQD----DIQPWLDAQEEHERQLRLLSQRHE-----LQGQIAAHNQQIIQYQQQIEQRQQQLLTALA 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1091 RveeeaaqknMALkKIRELESQISELQEDlESERASRNKAEKQKRDLGEELEALKTELE-----DTLDSTAAQQELRSKR 1165
Cdd:PRK10246 652 G---------YAL-TLPQEDEEASWLATR-QQEAQSWQQRQNELTALQNRIQQLTPLLEtlpqsDDLPHSEETVALDNWR 720
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29436380 1166 EQEVNILkkTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQT--------------KRVKANLEKAKQTLENER 1226
Cdd:PRK10246 721 QVHEQCL--SLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASvfddqqaflaalldEETLTQLEQLKQNLENQR 793
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1047-1284 |
1.17e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 46.21 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1047 EKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQI----------SEL 1116
Cdd:pfam15742 33 EKELRYERGKNLDLKQHNSLLQEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKIRELELEVlkqaqsiksqNSL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1117 QEDLESERASRNKAEKQKRDLGEELE-ALKTELEDTLDSTAAQQELRSKREQevnilkktlEEEAKThEAQIQEMRQKH- 1194
Cdd:pfam15742 113 QEKLAQEKSRVADAEEKILELQQKLEhAHKVCLTDTCILEKKQLEERIKEAS---------ENEAKL-KQQYQEEQQKRk 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1195 --SQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRK---KVEAQLQELQvkfNEGERVRT 1269
Cdd:pfam15742 183 llDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKsnqELSEKLSSLQ---QEKEALQE 259
|
250
....*....|....*
gi 29436380 1270 ELADKVTKLQVELDN 1284
Cdd:pfam15742 260 ELQQVLKQLDVHVRK 274
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
972-1145 |
1.31e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.78 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 972 KLKKLEEEQIILEDQNCKL-AKE------KKLLEDRIAEFTTNLT----EEEEKSKSLAKLKNKHEAmITDLEERLRREE 1040
Cdd:smart00787 110 DVKLLMDKQFQLVKTFARLeAKKmwyewrMKLLEGLKEGLDENLEglkeDYKLLMKELELLNSIKPK-LRDRKDALEEEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1041 KQRQELEKTRRKLEGDSTD-LSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNmalkkirELESQISELQED 1119
Cdd:smart00787 189 RQLKQLEDELEDCDPTELDrAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKS-------ELNTEIAEAEKK 261
|
170 180
....*....|....*....|....*.
gi 29436380 1120 LESERASRNKAEKQKRDLGEELEALK 1145
Cdd:smart00787 262 LEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
856-1145 |
1.36e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 856 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEeeeercqhlQ 935
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA---------E 1684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 936 AEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEaKLKKLEEEQIILEDQNCKLAKEKKlledRIAEfttNLTEEEEKS 1015
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE-ELKKAEEENKIKAEEAKKEAEEDK----KKAE---EAKKDEEEK 1756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1016 KSLAKLKNKHEAMITDLEERLRR--EEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAAlarVE 1093
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEAviEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSA---IK 1833
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 29436380 1094 EEAAQKNMALKKIRELESQI----SELQEDLESErASRNKAEKQKRDLGEELEALK 1145
Cdd:PTZ00121 1834 EVADSKNMQLEEADAFEKHKfnknNENGEDGNKE-ADFNKEKDLKEDDEEEIEEAD 1888
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
905-1374 |
1.44e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 905 RLTAKKQELEEICHDLEARVEEEeercQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEEQIILE 984
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRAEISNI----DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLK 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 985 D---QNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDL----EERLRREEKQRQELEKTRRKLEGDS 1057
Cdd:PRK01156 239 SalnELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPvyknRNYINDYFKYKNDIENKKQILSNID 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1058 TDLSD------QIAELQAQIAE-LKMQlaKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKA 1130
Cdd:PRK01156 319 AEINKyhaiikKLSVLQKDYNDyIKKK--SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1131 EKQKRDLGEELEALKTELEDTLDSTAA-----QQELRSKREQEVNILK--KTLEEEAK-----TH--EAQIQEMRQKHSQ 1196
Cdd:PRK01156 397 LKIQEIDPDAIKKELNEINVKLQDISSkvsslNQRIRALRENLDELSRnmEMLNGQSVcpvcgTTlgEEKSNHIINHYNE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1197 AVEELAEQLEQTKR-VKANLEKAKQ---TLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELA 1272
Cdd:PRK01156 477 KKSRLEEKIREIEIeVKDIDEKIVDlkkRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1273 D-KVTKLQVELDNVTGLLSQSDSKS-SKLTKDFSALESQLQD----TQELLQEENRQKLSLSTKLKQVEDEKNSFREQ-- 1344
Cdd:PRK01156 557 SlKLEDLDSKRTSWLNALAVISLIDiETNRSRSNEIKKQLNDlesrLQEIEIGFPDDKSYIDKSIREIENEANNLNNKyn 636
|
490 500 510
....*....|....*....|....*....|.
gi 29436380 1345 -LEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:PRK01156 637 eIQENKILIEKLRGKIDNYKKQIAEIDSIIP 667
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1063-1158 |
1.44e-04 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 45.04 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1063 QIAELQAQIAELKMQLAKKEEELQAALARVEEEAAqknmalkkIRELESQISELQEDLESERASRNKAEKQkrDLGEELE 1142
Cdd:COG4223 1 EIAALEAAVAELPAQLTALEQRLAALEAAPAAAAA--------TAALEARLAALRAALAAAREAVAAAAAA--ALEARLA 70
|
90
....*....|....*.
gi 29436380 1143 ALKTELEDTLDSTAAQ 1158
Cdd:COG4223 71 ALEAKAAAPEAEAAAA 86
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
898-1288 |
1.64e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.98 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 898 EAEELRAR---LTAKKQ--ELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLeeeesarQKLQlekvtteak 972
Cdd:PRK04778 90 EAEELNDKfrfRKAKHEinEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLY-------RELR--------- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 973 lKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTnLTEE---EEKSKSLAKLKNKheamITDLEERLRREEKQRQELEkt 1049
Cdd:PRK04778 154 -KSLLANRFSFGPALDELEKQLENLEEEFSQFVE-LTESgdyVEAREILDQLEEE----LAALEQIMEEIPELLKELQ-- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1050 rrklegdsTDLSDQIAELQAQIAELKMQ--------LAKKEEELQAALARVEEEAAQKNM--ALKKIRELESQISELQED 1119
Cdd:PRK04778 226 --------TELPDQLQELKAGYRELVEEgyhldhldIEKEIQDLKEQIDENLALLEELDLdeAEEKNEEIQERIDQLYDI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1120 LESERASRNKAEKQKRDLGEELEALKTELEDTldstaaQQELRskREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVE 1199
Cdd:PRK04778 298 LEREVKARKYVEKNSDTLPDFLEHAKEQNKEL------KEEID--RVKQSYTLNESELESVRQLEKQLESLEKQYDEITE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1200 ELAEQLEQTKRVKANLEKAKQTL---ENERGELANEVKVLlqgkgdsehkrKKVEAQLQElqvkfnEGERVRTELADkvT 1276
Cdd:PRK04778 370 RIAEQEIAYSELQEELEEILKQLeeiEKEQEKLSEMLQGL-----------RKDELEARE------KLERYRNKLHE--I 430
|
410
....*....|..
gi 29436380 1277 KLQVELDNVTGL 1288
Cdd:PRK04778 431 KRYLEKSNLPGL 442
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
962-1133 |
1.87e-04 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 44.12 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 962 LQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEK 1041
Cdd:pfam15619 16 LQNELAELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1042 QRQELEKTRRKLEGDSTDLS-DQIAELQAQIAELKMQLAKKEEELQAALARVEEEAA----QKNMALKKIRELESQISEL 1116
Cdd:pfam15619 96 ELLRLRDQLKRLEKLSEDKNlAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKsfrrQLAAEKKKHKEAQEEVKIL 175
|
170
....*....|....*..
gi 29436380 1117 QEDLESERASRNKAEKQ 1133
Cdd:pfam15619 176 QEEIERLQQKLKEKERE 192
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1047-1277 |
1.91e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1047 EKTRRKLEGDSTDLSDQIAELQAQiaelKMQLAKKEEELQAALARVEEeaaqknmalkkirelesqiseLQEDLEseras 1126
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEEL----ERELEQKAEEAEALLKEAEK---------------------LKEELE----- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1127 rnkaeKQKRDLGEELEALKTELEDtldstAAQQELRSKREQEVNILKKTLEEEAKTHEA----QIQEMRQKHSQAVEELA 1202
Cdd:PRK00409 555 -----EKKEKLQEEEDKLLEEAEK-----EAQQAIKEAKKEADEIIKELRQLQKGGYASvkahELIEARKRLNKANEKKE 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1203 EQLEQTKRVKANLEKakqtlenerGElanEVKVL-LQGKGDSEHKRKKVEAQLQE----LQVKFNEGERVRTELADKVTK 1277
Cdd:PRK00409 625 KKKKKQKEKQEELKV---------GD---EVKYLsLGQKGEVLSIPDDKEAIVQAgimkMKVPLSDLEKIQKPKKKKKKK 692
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1184-1374 |
2.64e-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: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1184 EAQIQEMRQKHSQAVEELAEQLEQtkrVKANLEKAKQTLENERGElanevkvllQGKGDSEHKRKKVEAQLQELQVKFNE 1263
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPE---LRKELEEAEAALEEFRQK---------NGLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1264 gerVRTELADkvtkLQVELDNVTGLLSQSDSKSSKLTKD--FSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSF 1341
Cdd:COG3206 231 ---ARAELAE----AEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL 303
|
170 180 190
....*....|....*....|....*....|....
gi 29436380 1342 REQLEE-EEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:COG3206 304 RAQLQQeAQRILASLEAELEALQAREASLQAQLA 337
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1035-1167 |
2.75e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 44.72 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1035 RLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKkeeeLQAALARVEEEAAQKNMALKKIRELESQIS 1114
Cdd:pfam00529 76 RLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQ----AQIDLARRRVLAPIGGISRESLVTAGALVA 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 29436380 1115 ELQEDLESERASRNKAEKQKRDLGEELEAL--KTELEDTLDSTAAQQELRSKREQ 1167
Cdd:pfam00529 152 QAQANLLATVAQLDQIYVQITQSAAENQAEvrSELSGAQLQIAEAEAELKLAKLD 206
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1198-1331 |
2.93e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.57 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1198 VEELAEQLEQTKRVKANLEkakQTLENERGELANevkvllqgkgdSEHKRKKVEAQLqelqvkfNEGERVRTELADKVTK 1277
Cdd:PRK09039 62 IAELADLLSLERQGNQDLQ---DSVANLRASLSA-----------AEAERSRLQALL-------AELAGAGAAAEGRAGE 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29436380 1278 LQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELL-------QEENRQKLSLSTKL 1331
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALdasekrdRESQAKIADLGRRL 181
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
960-1258 |
3.11e-04 |
|
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.
Pssm-ID: 462752 [Multi-domain] Cd Length: 307 Bit Score: 44.57 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 960 QKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTN-------LTEEEEKSKS-LAKLKNKHEAMITD 1031
Cdd:pfam09311 12 QAIQEQEAETRDQVKKLQEMLRQANDQLEKTMKDKKELEDKMNQLSEEtsnqvstLAKRNQKSETlLDELQQAFSQAKRN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1032 LEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRE-LE 1110
Cdd:pfam09311 92 FQDQLAVLMDSREQVSDELVRLQKDNESLQGKHSLHVSLQQAEKFDMPDTVQELQELVLKYREELIEVRTAADHMEEkLK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1111 SQISELQEDLESERASRnkaEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQevniLKKTLEEEAKTHEaQIQEM 1190
Cdd:pfam09311 172 AEILFLKEQIQAEQCLK---ENLEETLQAEIENCKEEIASISSLKVELERIKAEKEQ----LENGLTEKIRQLE-DLQTT 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29436380 1191 rqkhsqaVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQ 1258
Cdd:pfam09311 244 -------KGSLETQLKKETNEKAAVEQLVFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIR 304
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1062-1279 |
3.20e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.57 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1062 DQIAELQAQIAELKMQLAkkeeelqaalarVEEEAAQknmalkkirELESQISELQEDLESerasrnkaekqkrdlgeeL 1141
Cdd:PRK09039 53 SALDRLNSQIAELADLLS------------LERQGNQ---------DLQDSVANLRASLSA------------------A 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1142 EALKTELEDTLDSTAAQQELRSKREQEvniLKKTLEEEAKTHEaqiQEMRQkhsqaVEELAEQLEQTKRVKANLEKAKQt 1221
Cdd:PRK09039 94 EAERSRLQALLAELAGAGAAAEGRAGE---LAQELDSEKQVSA---RALAQ-----VELLNQQIAALRRQLAALEAALD- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29436380 1222 lenergelanevkvllqgkgDSEHKRKKVEAQLQELqvkfneGERVRTELADKVTKLQ 1279
Cdd:PRK09039 162 --------------------ASEKRDRESQAKIADL------GRRLNVALAQRVQELN 193
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
876-1167 |
3.25e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 876 SQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEIC---HDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQL 952
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAekrDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 953 EEEESARQKLQLEKVTTEAKLKKLEEEQIILEdqncKLAKEKKLLEDRIAefTTNLTEEEEKskslaKLKNKheamITDL 1032
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSID----KLRKEIERLEWRQQ--TEVLSPEEEK-----ELVEK----IKEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1033 EERLRREEKQRQELEKTrRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEeaaqknmALKKIRELESQ 1112
Cdd:COG1340 146 EKELEKAKKALEKNEKL-KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADE-------LRKEADELHKE 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 29436380 1113 ISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLdSTAAQQELRSKREQ 1167
Cdd:COG1340 218 IVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALK-REKEKEELEEKAEE 271
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
974-1276 |
3.25e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 974 KKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKL 1053
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1054 EGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQ 1133
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1134 KRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVka 1213
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE-- 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29436380 1214 NLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVT 1276
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAA 306
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1050-1179 |
3.25e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1050 RRKLEGDSTdlSDQIAELQAQIAELKMQlakkeeelQAALARVEEEAAQKnmalkKIRELESQISELQEDLESERAsRNK 1129
Cdd:COG0542 401 RVRMEIDSK--PEELDELERRLEQLEIE--------KEALKKEQDEASFE-----RLAELRDELAELEEELEALKA-RWE 464
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 29436380 1130 AEKQkrdLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEE 1179
Cdd:COG0542 465 AEKE---LIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
882-1107 |
3.87e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 882 KLQLQEQLQAETELCAEAEELRARLTAKKQELEEIchDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQK 961
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEF--RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 962 LQLEKVTTEAKLKKLEEEQIILEdqnckLAKEKKLLEDRIAEFTTNLTEE--------EEKSKSLAKLKNKHEAMITDLE 1033
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNhpdvialrAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29436380 1034 ERLRREEKQRQELEKTRRKLEGDStdlsDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIR 1107
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
973-1207 |
3.94e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 973 LKKLEEEQII-LEDQNCKLAKEK--KLLEDRI-AEFTTN-LTEEEEKSKSLAKLKNKHEamITDLEERLRREEKQRQELE 1047
Cdd:PRK05771 22 LEALHELGVVhIEDLKEELSNERlrKLRSLLTkLSEALDkLRSYLPKLNPLREEKKKVS--VKSLEELIKDVEEELEKIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1048 KTRRKLEGDSTDLSDQIAELQAQIAELK--------MQLAKKEEELQAALARVEEEaaqknmalkKIRELESQISELQED 1119
Cdd:PRK05771 100 KEIKELEEEISELENEIKELEQEIERLEpwgnfdldLSLLLGFKYVSVFVGTVPED---------KLEELKLESDVENVE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1120 LESERASRN-----KAEKQKRDLGEELEALKTELEDTLDSTAAQQELrSKREQEVNILKKTLEEEakthEAQIQEMRQKH 1194
Cdd:PRK05771 171 YISTDKGYVyvvvvVLKELSDEVEEELKKLGFERLELEEEGTPSELI-REIKEELEEIEKERESL----LEELKELAKKY 245
|
250
....*....|...
gi 29436380 1195 SQAVEELAEQLEQ 1207
Cdd:PRK05771 246 LEELLALYEYLEI 258
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1050-1297 |
4.20e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1050 RRKLEGDSTDLS----------DQIAELQAQIAELKMQL----------AKKEEELQA-ALARVEEEAAQKNMALKKIRE 1108
Cdd:PHA02562 152 RRKLVEDLLDISvlsemdklnkDKIRELNQQIQTLDMKIdhiqqqiktyNKNIEEQRKkNGENIARKQNKYDELVEEAKT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1109 LESQISELQEDL-------ESERASRNKAEKQKRDLGEELEALKTEL----EDTLDSTAAQQelrskREQEVNILKKtLE 1177
Cdd:PHA02562 232 IKAEIEELTDELlnlvmdiEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyeKGGVCPTCTQQ-----ISEGPDRITK-IK 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1178 EEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKAN---LEKAKQTLENERGELanevkvllqgkgdsehkrKKVEAQL 1254
Cdd:PHA02562 306 DKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELknkISTNKQSLITLVDKA------------------KKVKAAI 367
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 29436380 1255 QELQVKF----NEGERVRTELADKVTKLQ------VELDNVTGLLSQSDSKSS 1297
Cdd:PHA02562 368 EELQAEFvdnaEELAKLQDELDKIVKTKSelvkekYHRGIVTDLLKDSGIKAS 420
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
965-1278 |
4.76e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.47 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 965 EKVTTEAKLKKLEEEQIILeDQNCKLAKE--KKLLE--DRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREE 1040
Cdd:pfam02029 47 DSELKPSGQGGLDEEEAFL-DRTAKREERrqKRLQEalERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1041 KQRQELEKTRRKLEGDSTDLSDqiAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDL 1120
Cdd:pfam02029 126 GRYKEEETEIREKEYQENKWST--EVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1121 ESERASRNkaekqkrdlGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEE----EAKTHEAQIQEMRQKHSQ 1196
Cdd:pfam02029 204 HPEVKSQN---------GEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEElrrrRQEKESEEFEKLRQKQQE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1197 AVEELAEqleqtkrVKANLEKAKQTLENERgelanevkvllQGKGDSEHKRKKVEaqlQELQVKFNEG-ERVRTELADKV 1275
Cdd:pfam02029 275 AELELEE-------LKKKREERRKLLEEEE-----------QRRKQEEAERKLRE---EEEKRRMKEEiERRRAEAAEKR 333
|
...
gi 29436380 1276 TKL 1278
Cdd:pfam02029 334 QKL 336
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1075-1225 |
4.77e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.31 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1075 KMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDS 1154
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQ 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29436380 1155 TAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEmrqkhsQAVEELAEQL------EQTKRVKANLEKAKQTLENE 1225
Cdd:PRK12705 107 LEEREKALSARELELEELEKQLDNELYRVAGLTPE------QARKLLLKLLdaeleeEKAQRVKKIEEEADLEAERK 177
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1014-1200 |
4.89e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1014 KSKSLAKLKNKHEAMITDLEERLRREE--------KQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEEL 1085
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEaikkeallEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1086 QaalarveeeaaqknmalKKIRELESQISELQEDLESerasrnkAEKQKrdlgEELEALKTELEDTLDSTAAQQelrskR 1165
Cdd:PRK12704 106 E-----------------KREEELEKKEKELEQKQQE-------LEKKE----EELEELIEEQLQELERISGLT-----A 152
|
170 180 190
....*....|....*....|....*....|....*
gi 29436380 1166 EQEVNILKKTLEEEAKtHEAQIQeMRQKHSQAVEE 1200
Cdd:PRK12704 153 EEAKEILLEKVEEEAR-HEAAVL-IKEIEEEAKEE 185
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
958-1219 |
5.01e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.04 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 958 ARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLED-------------RIAEFTTN----LTEEEEKSKSLAK 1020
Cdd:TIGR01612 1556 AHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDiqlslenfenkflKISDIKKKindcLKETESIEKKISS 1635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1021 LK-NKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSdqiaELQAQIAELKMQLAKKEEELQAALARVEEEAAQK 1099
Cdd:TIGR01612 1636 FSiDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD----ELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIA 1711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1100 NMalkkiRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSkreqevNILkKTLEEE 1179
Cdd:TIGR01612 1712 NK-----EEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIA------GCL-ETVSKE 1779
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 29436380 1180 AKTHEaqiqEMRQKHSQAVEELAEQLEQTKRVKANLEKAK 1219
Cdd:TIGR01612 1780 PITYD----EIKNTRINAQNEFLKIIEIEKKSKSYLDDIE 1815
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
1032-1160 |
5.35e-04 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 44.07 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1032 LEERLRREEKQR--QELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQlakKEEELQAALARVEEEAAQKNMALKKIREL 1109
Cdd:PRK00247 288 AEQRAQYREKQKekKAFLWTLRRNRLRMIITPWRAPELHAENAEIKKT---RTAEKNEAKARKKEIAQKRRAAEREINRE 364
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 29436380 1110 ESQisELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQE 1160
Cdd:PRK00247 365 ARQ--ERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENEESKGSPPQV 413
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1027-1220 |
5.44e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.89 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1027 AMITDLEERLRREEKQ-RQELEKTRRKLEGDSTDLSDQIAE---LQAQIAELKMQLAKKEEELQAALARVEEEAAQKnmA 1102
Cdd:COG1842 12 ANINALLDKAEDPEKMlDQAIRDMEEDLVEARQALAQVIANqkrLERQLEELEAEAEKWEEKARLALEKGREDLARE--A 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1103 LKKIRELESQIselqEDLESE----RASRNKAEKQKRDLGEELEALKTELeDTLDSTAAQQELRSK-REQEVNILKKTLE 1177
Cdd:COG1842 90 LERKAELEAQA----EALEAQlaqlEEQVEKLKEALRQLESKLEELKAKK-DTLKARAKAAKAQEKvNEALSGIDSDDAT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29436380 1178 EEAKTHEAQIQEMRQKhSQAVEELA---------EQLEQTKRVKANLEKAKQ 1220
Cdd:COG1842 165 SALERMEEKIEEMEAR-AEAAAELAagdslddelAELEADSEVEDELAALKA 215
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1058-1135 |
5.44e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.56 E-value: 5.44e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29436380 1058 TDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKR 1135
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERK 215
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
865-1178 |
5.57e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 865 ENRLTEMETLQSQLMAEKLQLQEQLQAETELcAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKkkmqqn 944
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA------ 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 945 iqeleeqleeeesarQKLQLEKVTTEAKLKKLEEEqiiledqncklAKEKKlleDRIAEFTTNLTEEEEKSKSLAKLKNK 1024
Cdd:PRK02224 547 ---------------AELEAEAEEKREAAAEAEEE-----------AEEAR---EEVAELNSKLAELKERIESLERIRTL 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1025 HEAmITDLEERLRREEKQRQEL------------EKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAK---KEEELqaal 1089
Cdd:PRK02224 598 LAA-IADAEDEIERLREKREALaelnderrerlaEKRERKRELEAEFDEARIEEAREDKERAEEYLEQveeKLDEL---- 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1090 arveeeAAQKNMALKKIRELESQISELqEDLESERasrnkaeKQKRDLGEELEALKTELEdTLDSTAAqqELRSK-REQE 1168
Cdd:PRK02224 673 ------REERDDLQAEIGAVENELEEL-EELRERR-------EALENRVEALEALYDEAE-ELESMYG--DLRAElRQRN 735
|
330
....*....|
gi 29436380 1169 VNILKKTLEE 1178
Cdd:PRK02224 736 VETLERMLNE 745
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1002-1153 |
5.64e-04 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 44.08 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1002 AEFTTNLTE--EEEKSKSlAKLKNKHEAMITDLEERLRreeKQR-----------QELEKTRRKLEGDSTDLSDQIAELQ 1068
Cdd:pfam03148 203 EKFTQDNIEraEKERAAS-AQLRELIDSILEQTANDLR---AQAdavnfalrkriEETEDAKNKLEWQLKKTLQEIAELE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1069 AQIAELKMQLAKKEEELQAALARVEEEAAQKNMAL----------KKIRELESQISELQEDLESERASRNKAEKQKRDLG 1138
Cdd:pfam03148 279 KNIEALEKAIRDKEAPLKLAQTRLENRTYRPNVELcrdeaqyglvDEVKELEETIEALKQKLAEAEASLQALERTRLRLE 358
|
170
....*....|....*....
gi 29436380 1139 EELE----ALKTELEDTLD 1153
Cdd:pfam03148 359 EDIAvkanSLFIDREKCMG 377
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
867-1066 |
7.47e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 867 RLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEI---CHDLEARVEeeeercqHLQAEKKKMQQ 943
Cdd:COG1579 8 ALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLekeIKRLELEIE-------EVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 944 niqeleeqleeeesarqklQLEKVTTEAKLKKLEEEQIILEdqncklaKEKKLLEDRIAEFttnLTEEEEKSKSLAKLKN 1023
Cdd:COG1579 81 -------------------QLGNVRNNKEYEALQKEIESLK-------RRISDLEDEILEL---MERIEELEEELAELEA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 29436380 1024 KHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAE 1066
Cdd:COG1579 132 ELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
1016-1279 |
7.53e-04 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 42.99 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1016 KSLAKLKNKHEAMITDLEERLRREEKQRQELektRRKLEGDST--DLSDQIAELQAQIAELK---MQLAKKEEELQAALA 1090
Cdd:pfam13949 27 DDLPKLKQRNREILDEAEKLLDEEESEDEQL---RAKYGTRWTrpPSSELTATLRAEIRKYReilEQASESDSQVRSKFR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1091 RVEEeaaqknmalkKIRELESQISELQEDLESERASRNKAEKQK-----RDLGEELEALKTELEDTLdstaaqQELRSKR 1165
Cdd:pfam13949 104 EHEE----------DLELLSGPDEDLEAFLPSSRRAKNSPSVEEqvaklRELLNKLNELKREREQLL------KDLKEKA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1166 EQEvNILKKTLEEEAKTHEAQIQE-MRQKHSQAVEELAEQLEQTKRVKANLEKakqtlenergELANEVKVLLQGKGDSE 1244
Cdd:pfam13949 168 RND-DISPKLLLEKARLIAPNQEEqLFEEELEKYDPLQNRLEQNLHKQEELLK----------EITEANNEFLQDKRVDS 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 29436380 1245 HKRKKVEAQLQ----------ELQVKFNEGERVRTELADKVTKLQ 1279
Cdd:pfam13949 237 EKQRQREEALQklenaydkykELVSNLQEGLKFYNDLTEILEKLL 281
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
989-1203 |
8.07e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 42.43 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 989 KLAKEKKLLEDRIAEFTTNLTEEE--EKSKSLAKLKNKHEAMITDLEERlrreEKQRQELEKTRRKLEGDSTDLSDQIAE 1066
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDygDDLESVEALLKKHEALEAELAAH----EERVEALNELGEQLIEEGHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1067 LQAQIAELKMQLAKKEEELQAALarveEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKrdLGEELEALKT 1146
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRL----EEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEE--LLKKHKELEE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 29436380 1147 ELEdtldstAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAE 1203
Cdd:cd00176 154 ELE------AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEE 204
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1029-1363 |
8.99e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.69 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1029 ITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEeeaaqknmalKKIRE 1108
Cdd:pfam06160 88 LDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELE----------KQLAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1109 LESQISELQEdlESERASRNKAEKQKRDLGEELEALKTELED--TLDSTAaQQELRSKREQEVNILKKTLEE----EAKT 1182
Cdd:pfam06160 158 IEEEFSQFEE--LTESGDYLEAREVLEKLEEETDALEELMEDipPLYEEL-KTELPDQLEELKEGYREMEEEgyalEHLN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1183 HEAQIQEMRQKHSQAVEELAEQleQTKRVKANLEKAKQTLENERGELANEVKvllqGKGDSEHKRKKVEAQLQELQVKFN 1262
Cdd:pfam06160 235 VDKEIQQLEEQLEENLALLENL--ELDEAEEALEEIEERIDQLYDLLEKEVD----AKKYVEKNLPEIEDYLEHAEEQNK 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1263 EgervrteladkvtkLQVELDNV--TGLLSQSD-SKSSKLTKDFSALESQLQDTQELLQE--------ENRQKlSLSTKL 1331
Cdd:pfam06160 309 E--------------LKEELERVqqSYTLNENElERVRGLEKQLEELEKRYDEIVERLEEkevayselQEELE-EILEQL 373
|
330 340 350
....*....|....*....|....*....|....*.
gi 29436380 1332 KQVEDEKNSFREQLEE----EEEAKHNLEKQIATLH 1363
Cdd:pfam06160 374 EEIEEEQEEFKESLQSlrkdELEAREKLDEFKLELR 409
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
990-1312 |
9.30e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 43.51 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 990 LAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRRE------EKQRQELEKTRRKLEGDSTDLSDQ 1063
Cdd:pfam13166 87 LGEESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDEcwkkikRKKNSALSEALNGFKYEANFKSRL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1064 IAELQAQI---------AELKMQLAKKEEELQAALARVEEEAAQKnMALKKIRELESQISELQEDLESERASRNKAEKQK 1134
Cdd:pfam13166 167 LREIEKDNfnagvllsdEDRKAALATVFSDNKPEIAPLTFNVIDF-DALEKAEILIQKVIGKSSAIEELIKNPDLADWVE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1135 RDL-------------GEEL-EALKTELEDTLDSTAAQQ---------ELRSKREQEVNIL----------------KKT 1175
Cdd:pfam13166 246 QGLelhkahldtcpfcGQPLpAERKAALEAHFDDEFTEFqnrlqklieKVESAISSLLAQLpavsdlasllsafeldVED 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1176 LEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQtKRVKANLEKAKQTLE--NERGELANEVKVLLqgKGDSEHKRKKVEAQ 1253
Cdd:pfam13166 326 IESEAEVLNSQLDGLRRALEAKRKDPFKSIEL-DSVDAKIESINDLVAsiNELIAKHNEITDNF--EEEKNKAKKKLRLH 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1254 L-QELQVKFNEGERVRTELADKVTKLQVELDNVTgllsqsdSKSSKLTKDFSALESQLQD 1312
Cdd:pfam13166 403 LvEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLE-------AEIKKLREEIKELEAQLRD 455
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
856-1374 |
9.54e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 856 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEIchdLEARVEEEEERCQHLQ 935
Cdd:pfam02463 261 EKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK---EKKKAEKELKKEKEEI 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 936 AEKKKM----------QQNIQELEEQLEEEESARQKLQLEKVTTEAklKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFT 1005
Cdd:pfam02463 338 EELEKElkeleikreaEEEEEEELEKLQEKLEQLEEELLAKKKLES--ERLSSAAKLKEEELELKSEEEKEAQLLLELAR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1006 TNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELqaQIAELKMQLAKKEEEL 1085
Cdd:pfam02463 416 QLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET--QLVKLQEQLELLLSRQ 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1086 QAALARVEEEAAQKNMALKKIR-----------------------ELESQISELQEDLESERASRNKAEKQKRdLGEELE 1142
Cdd:pfam02463 494 KLEERSQKESKARSGLKVLLALikdgvggriisahgrlgdlgvavENYKVAISTAVIVEVSATADEVEERQKL-VRALTE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1143 ALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTL 1222
Cdd:pfam02463 573 LPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGV 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1223 ENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSKLTKD 1302
Cdd:pfam02463 653 SLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQD 732
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29436380 1303 FSALESQLQDTQELLQEENRQKLSLSTKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:pfam02463 733 KINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELR 804
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
872-1078 |
1.03e-03 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 43.40 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 872 ETLQSQLMAE-KLQLQEQLQAETELCAEAEELRARLTAK-KQELEEICHDLEARveeeeercqhLQAEKKKMQQNIQELE 949
Cdd:COG4487 17 ESLYADIVKQrRAEFEKELAERLADAAKREAALELAEAKaKAQLQEQVAEKDAE----------IAELRARLEAEERKKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 950 EQLEEEESARQK-LQLEKVTTEAKLKKLEEEQIiledqncKLAKEKKLLEDRIAEFTtnLTEEEEKSKSLAKLKNKheam 1028
Cdd:COG4487 87 LAVAEEKEKELAaLQEALAEKDAKLAELQAKEL-------ELLKKERELEDAKREAE--LTVEKERDEELDELKEK---- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29436380 1029 itdleerLRREEKQRQELEKTRRKLEGDST--DLSDQIAELQAQIAELKMQL 1078
Cdd:COG4487 154 -------LKKEEEEKQLAEKSLKVAEYEKQlkDMQEQIEELKRKKEQGSTQL 198
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
998-1192 |
1.16e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 42.32 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 998 EDRIAEFTTNLTEEEEKsksLAKLKNKHEAM---ITDLEERLRREE--------------KQRQELEKTRRKLEGDSTDL 1060
Cdd:pfam00261 14 EERLKEAMKKLEEAEKR---AEKAEAEVAALnrrIQLLEEELERTEerlaealekleeaeKAADESERGRKVLENRALKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1061 SDQIAELQAQIAELK----------MQLAKKEEELQAALARVEEEAAQKNMalkKIRELESQISELQEDLESERASRNKA 1130
Cdd:pfam00261 91 EEKMEILEAQLKEAKeiaeeadrkyEEVARKLVVVEGDLERAEERAELAES---KIVELEEELKVVGNNLKSLEASEEKA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29436380 1131 EKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQ 1192
Cdd:pfam00261 168 SEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQ 229
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
982-1110 |
1.33e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 41.09 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 982 ILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKsksLAKLKNKHEAMITDLEER--LRREEKQRQELEKTRRKLEGDSTD 1059
Cdd:PRK07352 47 ILEERREAILQALKEAEERLRQAAQALAEAQQK---LAQAQQEAERIRADAKARaeAIRAEIEKQAIEDMARLKQTAAAD 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 29436380 1060 LSDQ----IAELQAQIAElkMQLAKKEEELQAALarveEEAAQKNMALKKIRELE 1110
Cdd:PRK07352 124 LSAEqervIAQLRREAAE--LAIAKAESQLPGRL----DEDAQQRLIDRSIANLG 172
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
856-1185 |
1.34e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.30 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 856 KVREKQLAAENRLTEMETLQSQLMAEKLQlqEQLQAETELCAEAEELRARLTAKKQELeeichdleARVEEEEERCQHLQ 935
Cdd:PLN03229 440 KLKEQILKAKESSSKPSELALNEMIEKLK--KEIDLEYTEAVIAMGLQERLENLREEF--------SKANSQDQLMHPVL 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 936 AEK-KKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKlkkleeeqiILEDQNCKLAKEKKLLEDRIAEfTTNLTEEEEK 1014
Cdd:PLN03229 510 MEKiEKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAK---------ALSEKKSKAEKLKAEINKKFKE-VMDRPEIKEK 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1015 SKSL-AKLKNKHEAMITDLEERLRRE-EKQRQELEKTRRKLEgDSTDLsdQIAELQAQIAELKMQLAkkEEELQAALARV 1092
Cdd:PLN03229 580 MEALkAEVASSGASSGDELDDDLKEKvEKMKKEIELELAGVL-KSMGL--EVIGVTKKNKDTAEQTP--PPNLQEKIESL 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1093 EEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKrdlgeeLEALKTELEDTLDSTAAQQELRSKREQevniL 1172
Cdd:PLN03229 655 NEEINKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEKEK------IEALEQQIKQKIAEALNSSELKEKFEE----L 724
|
330
....*....|...
gi 29436380 1173 KKTLEEEAKTHEA 1185
Cdd:PLN03229 725 EAELAAARETAAE 737
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
1044-1242 |
1.36e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 42.38 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1044 QELEKTRRKLEGDSTDLSDQiaELQAQIAELkmqlakkeEELQAALARVEEEAAQKNMALKKIRE------LESQISELQ 1117
Cdd:pfam15294 70 SQAEKWHLKLQADISELENR--ELLEQIAEF--------EEREFTSSNKKPNFELNKPKLEPLNEgggsalLHMEIERLK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1118 EDLESERASRNKAEKQKRDLGEELEALKTELEDTLDsTAAQQELRSKREQEVNilkkTLEEEAKTHEAQIQEMRQKHSQA 1197
Cdd:pfam15294 140 EENEKLKERLKTLESQATQALDEKSKLEKALKDLQK-EQGAKKDVKSNLKEIS----DLEEKMAALKSDLEKTLNASTAL 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 29436380 1198 VEELAEQLEQTK----RVKANLEKAKQTLENERGELA--NEVKVLLQGKGD 1242
Cdd:pfam15294 215 QKSLEEDLASTKhellKVQEQLEMAEKELEKKFQQTAayRNMKEMLTKKNE 265
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
899-1166 |
1.48e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 42.71 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 899 AEELRARLTAKKQELEeichdlearveeeEERCQHLQAEKKKMqqniqeleeqleeeeSARQKLQLEKVTTEAKLKKLEE 978
Cdd:pfam05701 182 VEELTIELIATKESLE-------------SAHAAHLEAEEHRI---------------GAALAREQDKLNWEKELKQAEE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 979 EQIILEDQ-------NCKLAKEKKLLEDRIAEFTTNLteeEEKSKSLAKLKNKHEAMITDLEERLrreEKQRQELEKTRR 1051
Cdd:pfam05701 234 ELQRLNQQllsakdlKSKLETASALLLDLKAELAAYM---ESKLKEEADGEGNEKKTSTSIQAAL---ASAKKELEEVKA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1052 KLEgdstDLSDQIAELQAQIAELKMQLAKKEEELqAALARVEeeaaqkNMALKKIRELESQISELQEDLESERASRNKAE 1131
Cdd:pfam05701 308 NIE----KAKDEVNCLRVAAASLRSELEKEKAEL-ASLRQRE------GMASIAVSSLEAELNRTKSEIALVQAKEKEAR 376
|
250 260 270
....*....|....*....|....*....|....*.
gi 29436380 1132 KQKRDLGEELEALKTELEDT-LDSTAAQQELRSKRE 1166
Cdd:pfam05701 377 EKMVELPKQLQQAAQEAEEAkSLAQAAREELRKAKE 412
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
854-1170 |
1.55e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 854 LVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELrarltakkqeLEEichDLEARVEEEEERCQH 933
Cdd:COG3096 838 LAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLL----------ADE---TLADRLEELREELDA 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 934 LQAEKKKMQQNIQELEEQLEEEESARQK-LQLEKVttEAKLKKLEEEQiiledqncKLAKEKKLLEDRIAEFTTNLTEEE 1012
Cdd:COG3096 905 AQEAQAFIQQHGKALAQLEPLVAVLQSDpEQFEQL--QADYLQAKEQQ--------RRLKQQIFALSEVVQRRPHFSYED 974
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1013 EkskslAKLKNKHEAMITDLEERLRREEKQRqelEKTRRKLEGDSTDLSDQIAELQAqiaeLKMQLAKKEEELQAALARV 1092
Cdd:COG3096 975 A-----VGLLGENSDLNEKLRARLEQAEEAR---REAREQLRQAQAQYSQYNQVLAS----LKSSRDAKQQTLQELEQEL 1042
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1093 EE---EAAQKNMALKKIRElesqiSELQEDLESERASRNKAEKQKRDLGEELEALKTELedtldsTAAQQELRSKREQEV 1169
Cdd:COG3096 1043 EElgvQADAEAEERARIRR-----DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRL------RKAERDYKQEREQVV 1111
|
.
gi 29436380 1170 N 1170
Cdd:COG3096 1112 Q 1112
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
958-1210 |
1.83e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.21 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 958 ARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLAKEKKLLEDriaefttnltEEEEKSKSLAKLKNKHEAMITDLEERLR 1037
Cdd:pfam13868 72 KRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE----------DQAEAEEKLEKQRQLREEIDEFNEEQAE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1038 REEKQRQELEKTRRKLEgdstdlsdqiaelqaqiaelkMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQ 1117
Cdd:pfam13868 142 WKELEKEEEREEDERIL---------------------EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1118 EDLESERASRNKAEKQKRDLGEELEALKTELEdtldstaAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQA 1197
Cdd:pfam13868 201 AERDELRAKLYQEEQERKERQKEREEAEKKAR-------QRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAED 273
|
250
....*....|...
gi 29436380 1198 VEELAEQLEQTKR 1210
Cdd:pfam13868 274 EEIEQEEAEKRRM 286
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
1060-1225 |
1.85e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 41.65 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1060 LSDQIAELQAQIAELKMQ---LAKKEEELQA---------ALARVEEE--AAQKNMALKKIRELESQISELQEDLESERA 1125
Cdd:pfam17078 8 LHDQIDALTKTNLQLTVQsqnLLSKLEIAQQkeskflenlASLKHENDnlSSMLNRKERRLKDLEDQLSELKNSYEELTE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1126 SRNKAEKQKRDLGEELEALKTELE------DTLdsTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVE 1199
Cdd:pfam17078 88 SNKQLKKRLENSSASETTLEAELErlqiqyDAL--VDSQNEYKDHYQQEINTLQESLEDLKLENEKQLENYQQRISSNDK 165
|
170 180
....*....|....*....|....*.
gi 29436380 1200 ELAEQLEQTKRVKANLEKAKQTLENE 1225
Cdd:pfam17078 166 DIDTKLDSYNNKFKNLDNIYVNKNNK 191
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
957-1219 |
1.92e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 957 SARQKL--QLEKVTTEAKLKKLEEEQI-ILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKlknKHEAMITDLE 1033
Cdd:PHA02562 150 PARRKLveDLLDISVLSEMDKLNKDKIrELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA---RKQNKYDELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1034 ERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLA--KKEEE--------------LQAALARVEEEAA 1097
Cdd:PHA02562 227 EEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfQKVIKmyekggvcptctqqISEGPDRITKIKD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1098 QKNMALKKIRELESQISELQEdLESErasRNKAEKQKRDLGEELEALKTELedtldstaaqqelrskreqevnilkKTLE 1177
Cdd:PHA02562 307 KLKELQHSLEKLDTAIDELEE-IMDE---FNEQSKKLLELKNKISTNKQSL-------------------------ITLV 357
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 29436380 1178 EEAKTHEAQIQEM---RQKHSQAVEELAEQLEQTKRVKANLEKAK 1219
Cdd:PHA02562 358 DKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1071-1206 |
2.01e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 42.74 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1071 IAELKMQLAKKEEELQAALARVEEEAAQknmalkkIRELESQISELQEDLESERASRNKAEKQ-------KRDLGEELEA 1143
Cdd:pfam05911 690 FEQLKSEKENLEVELASCTENLESTKSQ-------LQESEQLIAELRSELASLKESNSLAETQlkcmaesYEDLETRLTE 762
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29436380 1144 LKTELEdtldstaaqqELRSKREQevniLKKTLEEEAKTHEAQIQEMRqkhsqaveELAEQLE 1206
Cdd:pfam05911 763 LEAELN----------ELRQKFEA----LEVELEEEKNCHEELEAKCL--------ELQEQLE 803
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
984-1089 |
2.04e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 42.34 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 984 EDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRklegdstdlsdQ 1063
Cdd:smart00435 276 EKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEKKKK-----------Q 344
|
90 100
....*....|....*....|....*.
gi 29436380 1064 IAELQAQIAELKMQLAKKEEELQAAL 1089
Cdd:smart00435 345 IERLEERIEKLEVQATDKEENKTVAL 370
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1083-1190 |
2.45e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 41.98 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1083 EELQAALARVEEEAAqknmaLKKIRELESQISELQEDLESERASRNKAEKQ----KRDlGEELEALKteledtldstaaq 1158
Cdd:PRK05431 12 EAVKEALAKRGFPLD-----VDELLELDEERRELQTELEELQAERNALSKEigqaKRK-GEDAEALI------------- 72
|
90 100 110
....*....|....*....|....*....|....*
gi 29436380 1159 qelrskreQEVNILK---KTLEEEAKTHEAQIQEM 1190
Cdd:PRK05431 73 --------AEVKELKeeiKALEAELDELEAELEEL 99
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
854-1150 |
2.52e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 854 LVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQH 933
Cdd:COG4372 68 LEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 934 LQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTE-AKLKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEE 1012
Cdd:COG4372 148 REEELKELEEQLESLQEELAALEQELQALSEAEAEQAlDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1013 EKSKSLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARV 1092
Cdd:COG4372 228 EAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 29436380 1093 EEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELED 1150
Cdd:COG4372 308 SLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
872-1345 |
2.75e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 42.24 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 872 ETLQSQLMAEKLQLQEQLQAEteLCA-EAEELRARLTA--KKQELEEICHDLEArveeeeercqhLQAEKKKMQQNIQEL 948
Cdd:pfam15818 52 ETLAKQHKEAMAVFKKQLQMK--MCAlEEEKGKYQLATeiKEKEIEGLKETLKA-----------LQVSKYSLQKKVSEM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 949 EeqleeeesarQKLQLEKVTTEAKLKKLEEeqiiLEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKLKNKHEAM 1028
Cdd:pfam15818 119 E----------QKLQLHLLAKEDHHKQLNE----IEKYYATITGQFGLVKENHGKLEQNVQEAIQLNKRLSALNKKQESE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1029 ITDLEERLRREekqrqelektrrklegdSTDLSDQIAELQAQIAELKMQLAKKEEELQaalarveeeaaqknmalkkire 1108
Cdd:pfam15818 185 ICSLKKELKKV-----------------TSDLIKSKVTCQYKMGEENINLTIKEQKFQ---------------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1109 lesqisELQEDLESERASRNKaekqkrdLGEELEALKTELEDTLDSTAAQQELRSKREQEVNilkkTLEEEAKTHEAQIQ 1188
Cdd:pfam15818 226 ------ELQERLNMELELNKK-------INEEITHIQEEKQDIIISFQHMQQLLQQQTQANT----EMEAELKALKENNQ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1189 EMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLlqgkGDSEHKRKKVEAQLQELQVKFneGERVR 1268
Cdd:pfam15818 289 TLERDNELQREKVKENEEKFLNLQNEHEKALGTWKKHVEELNGEINEI----KNELSSLKETHIKLQEHYNKL--CNQKK 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29436380 1269 TELADKVTKLQvELDNVTGLLSQSDSKSSKLTKDFSALESqlqdtqellQEENRQKLSLSTKLKQVEDEKNSFREQL 1345
Cdd:pfam15818 363 FEEDKKFQNVP-EVNNENSEMSTEKSENLIIQKYNSEQEI---------REENTKSFCSDTEYRETEKKKGPPVEEI 429
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1216-1364 |
2.76e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1216 EKAKQTLenerGELANEVKVLLQGkgdSEHKRKKVEAQLQELQVKFNEGERVRTELADKVTKLQVELDNvtgLLSQSDSK 1295
Cdd:PRK00409 505 EEAKKLI----GEDKEKLNELIAS---LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDK---LLEEAEKE 574
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29436380 1296 SSKLTKdfSALESQLQDTQELLQEENRQKLSLstKLKQVEDEKNSFREQLEEEEEAKHNLEKQIATLHA 1364
Cdd:PRK00409 575 AQQAIK--EAKKEADEIIKELRQLQKGGYASV--KAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
1056-1133 |
2.81e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 41.47 E-value: 2.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29436380 1056 DSTDLSDQIAELQAQIAELKMQLakkeEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQ 1133
Cdd:COG0845 55 DPPDLQAALAQAQAQLAAAQAQL----ELAKAELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARAN 128
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
872-1143 |
2.89e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 42.23 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 872 ETLQSQLMAEKLQLQEqlqAETELCAEAEELRARLTAKKQELEEICHDLEARveeeeERCQHLQAEKKKMqqniqeleeq 951
Cdd:PLN03188 1043 ESPEKKLEQERLRWTE---AESKWISLAEELRTELDASRALAEKQKHELDTE-----KRCAEELKEAMQM---------- 1104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 952 lEEEESARqklQLEKVTteaklkKLEEEQIILedqnckLAKEKKLLEDriaefttnlTEEEEKSKSLAKLKNKHEAMITD 1031
Cdd:PLN03188 1105 -AMEGHAR---MLEQYA------DLEEKHIQL------LARHRRIQEG---------IDDVKKAAARAGVRGAESKFINA 1159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1032 LEERLRREEKQRqelEKTRRKLEGDSTDLSDQI---AELQAQIAELKMQLAKKEEELQAALAR---VEEEAAQKNMALKK 1105
Cdd:PLN03188 1160 LAAEISALKVER---EKERRYLRDENKSLQAQLrdtAEAVQAAGELLVRLKEAEEALTVAQKRamdAEQEAAEAYKQIDK 1236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 29436380 1106 I-RELESQISELQEDL-------ESERASRNKAEKQKRDLGEELEA 1143
Cdd:PLN03188 1237 LkRKHENEISTLNQLVaesrlpkEAIRPACNDDCMAKYDAGEPLSE 1282
|
|
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
1062-1150 |
2.95e-03 |
|
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.
Pssm-ID: 197361 [Multi-domain] Cd Length: 87 Bit Score: 38.10 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1062 DQIAELQAQIAELKMQLAKKEEELQaalaRVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEEL 1141
Cdd:cd09803 1 GEIDELAARLQEAEEALALKQEDID----ELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQL 76
|
....*....
gi 29436380 1142 EALKTELED 1150
Cdd:cd09803 77 EYLQRENQE 85
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1047-1241 |
3.01e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 41.93 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1047 EKTRRKLEgDSTDLSDQIA----ELQAQ-IAELKMQLAKKEEELQAALARVEEEAAQknmalKKIRELESQiselQEDLE 1121
Cdd:PTZ00491 643 ERTRDSLQ-KSVQLAIEITtksqEAAARhQAELLEQEARGRLERQKMHDKAKAEEQR-----TKLLELQAE----SAAVE 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1122 SERASRNKAEKqkrdlgeELEALKTELEDTLDstaaQQELRSKREQevnILKKT-LEEEAKTHEAQIQEMRQKHSQAVE- 1199
Cdd:PTZ00491 713 SSGQSRAEALA-------EAEARLIEAEAEVE----QAELRAKALR---IEAEAeLEKLRKRQELELEYEQAQNELEIAk 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 29436380 1200 --ELAEqLEQTK--RVKANLekAKQTLEnergELAN---EVKV-LLQGKG 1241
Cdd:PTZ00491 779 akELAD-IEATKfeRIVEAL--GRETLI----AIARagpELQAkLLGGLG 821
|
|
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
1183-1344 |
3.10e-03 |
|
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.
Pssm-ID: 462869 [Multi-domain] Cd Length: 303 Bit Score: 41.22 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1183 HEAQIQEMRqkhsqavEELAEQLEQTKrvKANLEKAKqtLENERGELANEVKVLlqgKGDSEhkrkKVEAQLQELQVKFN 1262
Cdd:pfam09738 84 DEGSLRDIK-------HELKEVEEKYR--KAMISNAQ--LDNEKSNLMYQVDLL---KDKLE----EMEESLAELQRELR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1263 EGERVRTELADKVTKLQVELDNVTGLLSQSDSKSSK--------LTKDFSALESQLQDTQELLQEENRQKL------SLS 1328
Cdd:pfam09738 146 EKNKELERLKRNLRRLQFQLAELKEQLKQRDELIEKhglvivpdENTNGEEENSPADAKRALVSVEAAEVLesagegSLD 225
|
170
....*....|....*.
gi 29436380 1329 TKLKQVEDEKNSFREQ 1344
Cdd:pfam09738 226 VRLKKLADEKEELLDE 241
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
1059-1151 |
3.47e-03 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 40.34 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1059 DLSDQIAEL----------QAQIAEL---KMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERA 1125
Cdd:pfam05266 72 SLMESFAELekhgfdvkapQSRINKLlslKDRQTKLLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKE 151
|
90 100
....*....|....*....|....*.
gi 29436380 1126 SRNKAEKQKRDLGEELEALKTELEDT 1151
Cdd:pfam05266 152 KKEAADKEIARLKSEAEKLEQEIQDV 177
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
1018-1122 |
3.67e-03 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 39.95 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1018 LAKLKNKHeamiTDLEERLRREEKQRQELEKTRRKLEgdstdlsDQIAELQAQIAELkmqlakkeeELQAALARVEEEAA 1097
Cdd:pfam05266 97 LLSLKDRQ----TKLLEELKKLEKKIAEEESEKRKLE-------EEIDELEKKILEL---------ERQLALAKEKKEAA 156
|
90 100
....*....|....*....|....*
gi 29436380 1098 QknmalKKIRELESQISELQEDLES 1122
Cdd:pfam05266 157 D-----KEIARLKSEAEKLEQEIQD 176
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1018-1372 |
3.84e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.38 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1018 LAKLKNKHeaMITDLEERLRREEKQRQELekTRRKLegdsTDLSDQIAELQAQIAELKMQLAKKE-EELQAALARVEEEA 1096
Cdd:pfam06160 31 LSKVKKLN--LTGETQEKFEEWRKKWDDI--VTKSL----PDIEELLFEAEELNDKYRFKKAKKAlDEIEELLDDIEEDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1097 AQKNMALKKIRELESQIS-ELQEDLESERASRNKAEKQKRDLGEELEALKT---ELEDTLDS----TAAQQELRSKREQE 1168
Cdd:pfam06160 103 KQILEELDELLESEEKNReEVEELKDKYRELRKTLLANRFSYGPAIDELEKqlaEIEEEFSQfeelTESGDYLEAREVLE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1169 vnilkkTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENErgELANEVKVLlqgkgdsEHKRK 1248
Cdd:pfam06160 183 ------KLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALEHL--NVDKEIQQL-------EEQLE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1249 KVEAQLQELQVKfnegervrtELADKVTKLQVELDNVTGLLSQ-------SDSKSSKLTKDFSALESQLQDTQELLQEen 1321
Cdd:pfam06160 248 ENLALLENLELD---------EAEEALEEIEERIDQLYDLLEKevdakkyVEKNLPEIEDYLEHAEEQNKELKEELER-- 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 29436380 1322 rqkLSLSTKLKqvEDEKNSFREqleeeeeakhnLEKQIATLHAQVADMKKK 1372
Cdd:pfam06160 317 ---VQQSYTLN--ENELERVRG-----------LEKQLEELEKRYDEIVER 351
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1131-1219 |
3.90e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1131 EKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEvnilKKTLEEEAKTHEAQIQEMRQKHS--QAVEELAEQLEQT 1208
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQE----LVALEGLAAELEEKQQELEAQLEqlQEKAAETSQERKQ 216
|
90
....*....|.
gi 29436380 1209 KRVKANLEKAK 1219
Cdd:PRK11448 217 KRKEITDQAAK 227
|
|
| AIP3 |
smart00806 |
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ... |
974-1250 |
3.98e-03 |
|
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in Saccharomyces cerevisiae that was previously identified as an actin-interacting protein. Actin-interacting protein 3 (Aip3p) localizes at the cell cortex where cytoskeleton assembly must be achieved to execute polarized cell growth, and deletion of AIP3 causes gross defects in cell and cytoskeletal polarity. Aip3p localization is mediated by the secretory pathway, mutations in early- or late-acting components of the secretory apparatus lead to Aip3p mislocalization.
Pssm-ID: 214826 [Multi-domain] Cd Length: 426 Bit Score: 41.19 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 974 KKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSlaklknkHEAMITDLEERLRREEKQRQELEKTRRKL 1053
Cdd:smart00806 92 NELDEVKQALESQREAIQRLKERQQNSAANIARPAASPSPVLAS-------SSSAISLANNPDKLNKEQRAELKSLQREL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1054 EGDSTDLSDQIAELQAQIAELKMQLAK-KEEELQAALA--RVEEEAAQKNMA------LKKIRELESQISELQEDLeSER 1124
Cdd:smart00806 165 AVLRQTHNSFFTEIKESIKDILEKIDKfKSSSLSASGSsnRAYVESSKKKLSedsdslLTKVDDLQDIIEALRKDV-AQR 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1125 ASRnKAEKQKRDLGEELEALKTELEDtldstaaqqeLRSKREQEVNILKKTLEEEAkthEAQIQEMRQKHSQavEELAEQ 1204
Cdd:smart00806 244 GVR-PSKKQLETVQKELETARKELKK----------MEEYIDIEKPIWKKIWEAEL---DKVCEEQQFLTLQ--EDLIAD 307
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 29436380 1205 LeqtkrvKANLEKAKQTLENerGELANEvkvlLQGKGDSEHKRKKV 1250
Cdd:smart00806 308 L------KEDLEKAEETFDL--VEQCCE----EQEKGPSKNRNKPV 341
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1010-1219 |
4.00e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 41.50 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1010 EEEEKSKSLAK--LKNKHEAMITDLEErlrreekQRQELEKTRRKLEGDSTDLSDQ--IAELQAQIAELKMQLAKK---- 1081
Cdd:PRK07735 13 EAARRAKEEARkrLVAKHGAEISKLEE-------ENREKEKALPKNDDMTIEEAKRraAAAAKAKAAALAKQKREGteev 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1082 -EEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDstaaqqe 1160
Cdd:PRK07735 86 tEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEE------- 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29436380 1161 lrskrEQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAK 1219
Cdd:PRK07735 159 -----ETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAK 212
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1058-1229 |
4.20e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 39.53 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1058 TDLSDQIAELQAQIAELKMQLakkeEELQAALARVEEEAAQKNMAlkKIRELESQISELQEDLESERASRNKAEKQKRDL 1137
Cdd:pfam08614 10 NRLLDRTALLEAENAKLQSEP----ESVLPSTSSSKLSKASPQSA--SIQSLEQLLAQLREELAELYRSRGELAQRLVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1138 GEELEALKTELEdtldstAAQQELRSKREQevnilKKTLEEEAKTHEAQIQEMRQKHSQAVEELA---EQLEQtkrvkan 1214
Cdd:pfam08614 84 NEELQELEKKLR------EDERRLAALEAE-----RAQLEEKLKDREEELREKRKLNQDLQDELValqLQLNM------- 145
|
170
....*....|....*
gi 29436380 1215 LEKAKQTLENERGEL 1229
Cdd:pfam08614 146 AEEKLRKLEKENREL 160
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
900-1144 |
4.30e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 900 EELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQ-QNIQELEEQLEEEESARQKLQLEKVT-TEAKLKKLE 977
Cdd:PRK01156 468 NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLEsEEINKSINEYNKIESARADLEDIKIKiNELKDKHDK 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 978 EEQII-------LEDQNCKLAKEKKLLEDR-IAEFTTNLTEEEEKSKSLAKL--------------KNKHEAMITDLEER 1035
Cdd:PRK01156 548 YEEIKnrykslkLEDLDSKRTSWLNALAVIsLIDIETNRSRSNEIKKQLNDLesrlqeieigfpddKSYIDKSIREIENE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1036 LRREEKQRQELEKTRR---KLEGDSTDLSDQIA----------ELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMA 1102
Cdd:PRK01156 628 ANNLNNKYNEIQENKIlieKLRGKIDNYKKQIAeidsiipdlkEITSRINDIEDNLKKSRKALDDAKANRARLESTIEIL 707
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 29436380 1103 LKKIRELESQISELQEDLESERasrnKAEKQKRDLGEELEAL 1144
Cdd:PRK01156 708 RTRINELSDRINDINETLESMK----KIKKAIGDLKRLREAF 745
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
938-1323 |
4.64e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.38 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 938 KKKMQQNIQELEEQLEEEESARQKLQLEKVT-------TEAKLKKLEEEQIILEDQncKLAKEKKLLED--------RIA 1002
Cdd:pfam06160 5 RKKIYKEIDELEERKNELMNLPVQEELSKVKklnltgeTQEKFEEWRKKWDDIVTK--SLPDIEELLFEaeelndkyRFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1003 EFTTNLTEEEEKsksLAKLKNKHEAMITDLEERLRREEKQRQELE-------KTRRKLEGDSTDLSDQIAELQAQIAELK 1075
Cdd:pfam06160 83 KAKKALDEIEEL---LDDIEEDIKQILEELDELLESEEKNREEVEelkdkyrELRKTLLANRFSYGPAIDELEKQLAEIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1076 MQLAKKEEE------LQAA--LARVEEEAAQKNMALKKI--------RELESQISELQE---DLESE--RASRNKAEKQK 1134
Cdd:pfam06160 160 EEFSQFEELtesgdyLEARevLEKLEEETDALEELMEDIpplyeelkTELPDQLEELKEgyrEMEEEgyALEHLNVDKEI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1135 RDLGEELEALKTELEdTLDSTAAQQELRsKREQEVNILKKTLEEEAKTH---EAQIQEMRQKHSQAVEELAEQLEQTKRV 1211
Cdd:pfam06160 240 QQLEEQLEENLALLE-NLELDEAEEALE-EIEERIDQLYDLLEKEVDAKkyvEKNLPEIEDYLEHAEEQNKELKEELERV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1212 KANLEKAKQTLENERGeLANEVKVLlqgkgdsehkrkkvEAQLQELQVKFNEGERVRTELADKVTKLQVELDNVTGLLSQ 1291
Cdd:pfam06160 318 QQSYTLNENELERVRG-LEKQLEEL--------------EKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEE 382
|
410 420 430
....*....|....*....|....*....|..
gi 29436380 1292 SDSKSSKLTKDFSALESQLQDTQELLQEENRQ 1323
Cdd:pfam06160 383 FKESLQSLRKDELEAREKLDEFKLELREIKRL 414
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
864-1088 |
4.69e-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: 40.47 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 864 AENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLT---AKKQeleeichDLEARVEEEEERCQHLQAEKKK 940
Cdd:pfam06008 21 LENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATqtlAKAQ-------QVNAESERTLGHAKELAEAIKN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 941 MQQNIQELEEQ-----LEEEESARQKLQLEKVTTEAKLKKLEEEQIILEDQNCKLakEKKLLEDRIAEFTTNLTEEEEKS 1015
Cdd:pfam06008 94 LIDNIKEINEKvatlgENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEA--ELKAAQDLLSRIQTWFQSPQEEN 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29436380 1016 KSLAK----LKNKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAA 1088
Cdd:pfam06008 172 KALANalrdSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKTARDSLDAA 248
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1108-1345 |
4.73e-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: 40.90 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1108 ELESQISELQEdlESERASRNKAEKQK--RDL--GEELEALKTELEDTLDSTAAQQELRSKREQEVNilkktLEEEAKTH 1183
Cdd:pfam09787 1 NLESAKQELAD--YKQKAARILQSKEKliASLkeGSGVEGLDSSTALTLELEELRQERDLLREEIQK-----LRGQIQQL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1184 EAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQgkgdsEHKRKKVEAQLQeLQVKFNE 1263
Cdd:pfam09787 74 RTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEE-----ELRRSKATLQSR-IKDREAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1264 GERVRTELADKvtklqveldnvtgllSQSDSKSSKLtkdfsalESQL-QDTQELLQEEnrqklslsTKLKQVEDEKNSFR 1342
Cdd:pfam09787 148 IEKLRNQLTSK---------------SQSSSSQSEL-------ENRLhQLTETLIQKQ--------TMLEALSTEKNSLV 197
|
...
gi 29436380 1343 EQL 1345
Cdd:pfam09787 198 LQL 200
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
919-1279 |
4.82e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.17 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 919 DLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQ----------------KLQLEKVTTE----------AK 972
Cdd:pfam05701 25 DWKAHRIQTVERRKLVELELEKVQEEIPEYKKQSEAAEAAKAqvleelestkrlieelKLNLERAQTEeaqakqdselAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 973 LKKLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKsksLAKLKNKHEAMITDLEERLRREEKQRQELEKTRRK 1052
Cdd:pfam05701 105 LRVEEMEQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEE---LESLRKEYASLVSERDIAIKRAEEAVSASKEIEKT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1053 LEGDSTDL--------SDQIAELQAQIAELKMQLAKKEEEL--QAALARVEEEAAQKNMALKKIRELESQI---SELQED 1119
Cdd:pfam05701 182 VEELTIELiatkesleSAHAAHLEAEEHRIGAALAREQDKLnwEKELKQAEEELQRLNQQLLSAKDLKSKLetaSALLLD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1120 LESERASR-NKAEKQKRDLGEELEALKTELEDTLDSTAAQ-QELRSKREQ---EVNILK---KTLEEEAKTHEAQIQEMR 1191
Cdd:pfam05701 262 LKAELAAYmESKLKEEADGEGNEKKTSTSIQAALASAKKElEEVKANIEKakdEVNCLRvaaASLRSELEKEKAELASLR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1192 QKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTEL 1271
Cdd:pfam05701 342 QREGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAA 421
|
....*...
gi 29436380 1272 ADKVTKLQ 1279
Cdd:pfam05701 422 STVESRLE 429
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1037-1220 |
5.12e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.95 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1037 RREEKQRQELEKTRrklegdSTDLSDQIAELQAQIAEL-KMQLAKKEEELQAALARVEEEAAQKN--MALKKIRELESQI 1113
Cdd:PRK09510 75 KRAEEQRKKKEQQQ------AEELQQKQAAEQERLKQLeKERLAAQEQKKQAEEAAKQAALKQKQaeEAAAKAAAAAKAK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1114 SELQEDLESERASRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQ---ELRSKREQEVNilKKTLEEEAKTHEAQIQEM 1190
Cdd:PRK09510 149 AEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKaaaEAKKKAEAEAK--KKAAAEAKKKAAAEAKAA 226
|
170 180 190
....*....|....*....|....*....|
gi 29436380 1191 RQKHSQAVEELAEQLEQTKRVKANLEKAKQ 1220
Cdd:PRK09510 227 AAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1065-1159 |
5.13e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 39.43 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1065 AELQAQIAELKMQLAKKEEELQAALARVEEEAAqkNMALKKIRELESQISELQEDLESERASRNKAEKQKRDlgEELEAL 1144
Cdd:COG2825 46 KKLEKEFKKRQAELQKLEKELQALQEKLQKEAA--TLSEEERQKKERELQKKQQELQRKQQEAQQDLQKRQQ--ELLQPI 121
|
90
....*....|....*
gi 29436380 1145 KTELEDTLDSTAAQQ 1159
Cdd:COG2825 122 LEKIQKAIKEVAKEE 136
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1116-1285 |
5.35e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1116 LQEDLESERASRNKAEKQKRDLG-EELEALKTELEDTLDST----AAQQELRSKREQEVNI--LKKTLEEEAKTHEAQIQ 1188
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEeeyaELQEELEELEEELEELeaELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1189 --EMRQKHSQAVEELA------EQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKR-KKVEAQLQELQV 1259
Cdd:COG4717 127 llPLYQELEALEAELAelperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQ 206
|
170 180
....*....|....*....|....*.
gi 29436380 1260 KFNEGERVRTELADKVTKLQVELDNV 1285
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQL 232
|
|
| DUF445 |
pfam04286 |
Protein of unknown function (DUF445); Predicted to be a membrane protein. |
994-1230 |
5.52e-03 |
|
Protein of unknown function (DUF445); Predicted to be a membrane protein.
Pssm-ID: 427840 [Multi-domain] Cd Length: 368 Bit Score: 40.69 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 994 KKLLEDRIAEFttNLTEEEEKSKSLAKLKNKHEAMITDLeerlrreekqrqeLEKTRRKLEGDstdlsdqiaELQAQIAE 1073
Cdd:pfam04286 110 KKALRRRLEEI--DLAPLLGKLLELLLAEGRHQALLDDL-------------LDRLRDWLRSE---------EGKQRIAE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1074 LKMQLAKKEEELQAALARVeeeaaqKNMALkkiRELESQISELQEDLESE------RASRNKAEK--QKRDLGEELEALK 1145
Cdd:pfam04286 166 MIDEFLEEWGPLVALLGGI------AEMIL---RALSSLLDEVQADPDHPlrlafdRAVRELITDllNDPELRAEVEELK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1146 telEDTLDSTAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEE---LAEQLEqtKRVKANLEKAkqtL 1222
Cdd:pfam04286 237 ---QKLLADPAVQDYVKALWESLRSLLLDDLSDPDSALRRRISELLAEFGERLAEdpeLRDKLN--EHLEDAAVGL---L 308
|
....*...
gi 29436380 1223 ENERGELA 1230
Cdd:pfam04286 309 PRYRLEIG 316
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
884-1327 |
5.53e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 41.04 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 884 QLQEQLQAETELCAEAEELRARLTAKKQELEE-----ICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESA 958
Cdd:pfam15964 71 QLKALLQQQTKKENELSPRRRKLSPSRTSEDEssslpTVHDLVPIINDQSQYIHHLEAEVKFCKEELSEMKQRVQVVVLE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 959 RQKLQ--LEKVTTEAKLKkleeEQIILED----QNCKLAKEK-KLLEDRIAEFTTNLtEEEEKSKSLAKLKNKHEAMitd 1031
Cdd:pfam15964 151 NEKLQqeLKSQTQEETLR----EQTLLDSsgnmQNSWCTPEDsRVHQTSKRPASHNL-AERLKSATTGEDEKWRLEL--- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1032 leERLRREEKQRQELektrrkLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAA---------LARVEEEA----AQ 1098
Cdd:pfam15964 223 --EKLKLLYEAKTEV------LESQVKSLRKDLAESQKTCEDLKERLKHKESLVAAStssrvgglcLKCAQHEAvlaqTH 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1099 KNMALKKIRELESQISELQEDLESERASRNKAEKQKRDLGEEL-EALKTELEDTLDSTAAQ---QELRSKREQEVNILKK 1174
Cdd:pfam15964 295 TNVHMQTIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQVkQAVQMTEEANFEKTKALiqcEQLKSELERQKERLEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1175 TLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEA-- 1252
Cdd:pfam15964 375 ELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGem 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1253 --QLQELQVKFNEGERVRTELADK-----------VTKLQVELDNVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQE 1319
Cdd:pfam15964 455 ryQLNQTKMKKDEAEKEHREYRTKtgrqleikdqeIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHL 534
|
....*...
gi 29436380 1320 ENRQKLSL 1327
Cdd:pfam15964 535 TRLEKESI 542
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1009-1219 |
5.95e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.09 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1009 TEEEEKSKS-LAKLKnkHEAMitdlEERLRREEKQRQElektRRKlegdstdlsdQIAELQAqiaelkmqlAKKEEELQA 1087
Cdd:PRK05035 440 AIEQEKKKAeEAKAR--FEAR----QARLEREKAAREA----RHK----------KAAEARA---------AKDKDAVAA 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1088 ALARVEEEAAQKNMALKKIRELESQISELQEDLESERASRnKAEKQKRDLGEELEALKTELEDTLDST----AAQQELRS 1163
Cdd:PRK05035 491 ALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQA-RARQAEKQAAAAADPKKAAVAAAIARAkakkAAQQAANA 569
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29436380 1164 KREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAK 1219
Cdd:PRK05035 570 EAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAK 625
|
|
| CCDC90-like |
pfam07798 |
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil ... |
1095-1209 |
6.16e-03 |
|
Coiled-coil domain-containing protein 90-like; This entry includes coiled-coil domain-containing proteins 90 (CCDC90) and related proteins. CCDC90A is a key regulator of the mitochondrial calcium uniporter (MCU) and hence was renamed MCUR1. A study in mammals and in yeast homolog fmp32 has reported that MCUR1 is a cytochrome c oxidase assembly factor and that it has an indirect role as a regulator of MCU, however, subsequent publications confirmed the function of MCUR1 as a regulator of MCU. The role of CCDC90B proteins is still not known.
Pssm-ID: 462268 [Multi-domain] Cd Length: 175 Bit Score: 39.03 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1095 EAAQKNMALKKIRELESQ-----ISELQEDLESER-----ASRNKAEKQKRDLgeelEALKTELEDTLDSTAAQQELrsk 1164
Cdd:pfam07798 36 ENVSKDLVTKEDLENETYlqkadLAELRSELQILEksefaALRSENEKLRREL----EKLKQRLREEITKLKADVRL--- 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 29436380 1165 reqEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTK 1209
Cdd:pfam07798 109 ---DLNLEKGRIREELKAQELKIQETNNKIDTEIANLRTQIESVK 150
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
968-1192 |
6.69e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 39.94 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 968 TTEAKLKKLEEEqiiLEDQNCKLAKEKKLLEDRIAEFTTNLTEEEEKSKSLAKL-----KNKHEAMITDLEERLRREEKQ 1042
Cdd:pfam15397 6 TSLEELKKHEDF---LTKLNLELIKAIQDTEDSTALKVRKLLQQYEKFGTIISIleysnKKQLQQAKAELQEWEEKEESK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1043 ----RQELEKTRRKLEGDSTDL--------------SDQIAELQAQIAELKMQLAKKEEELqaalarveeeaaqKNMALK 1104
Cdd:pfam15397 83 lnklEQQLEQLNAKIQKTQEELnflstykdkeypvkAVQIANLVRQLQQLKDSQQDELDEL-------------EEMRRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1105 KIRELESQISELQEDLEserasRNKAEKQKRDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNILKKtleeEAKTHE 1184
Cdd:pfam15397 150 VLESLSRKIQKKKEKIL-----SSLAEKTLSPYQESLLQKTRDNQVMLKEIEQFREFIDELEEEIPKLKA----EVQQLQ 220
|
....*...
gi 29436380 1185 AQIQEMRQ 1192
Cdd:pfam15397 221 AQRQEPRE 228
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
975-1150 |
6.78e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 40.88 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 975 KLEEEQIILEDQNCKLAKEKKLLEDRIAEFTTNLTEEE-----EKSKSLAKLKNKHE-AMITDLEERlrrEEKQRQELEk 1048
Cdd:COG5192 525 KSSESDLVVQDEPEDFFDVSKVANESISSNHEKLMESEfeelkKKWSSLAQLKSRFQkDATLDSIEG---EEELIQDDE- 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1049 trrklEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEaaqKNMALKKIRELESQIsELQEDLESERASRN 1128
Cdd:COG5192 601 -----KGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETE---REENARKKEELRGNF-ELEERGDPEKKDVD 671
|
170 180
....*....|....*....|..
gi 29436380 1129 KAEKQKRDLGEELEALKTELED 1150
Cdd:COG5192 672 WYTEEKRKIEEQLKINRSEFET 693
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1134-1257 |
7.50e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1134 KRDLGEELEALKTELEDTLDstAAQQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKA 1213
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 29436380 1214 NLEKAKQTLENERGELANEVKVLLQGKGDSEHKRKKVEAQLQEL 1257
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1039-1344 |
7.50e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1039 EEKQRQELEKTRrklEGDSTDLSDQIAELQAQIAELkmqlakkeEELQAALARVEEEAAQKNMALKKIRELESQISELQE 1118
Cdd:PRK10929 25 EKQITQELEQAK---AAKTPAQAEIVEALQSALNWL--------EERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1119 DLESERASRNKAE-------------KQKRDLGEELEALKtELEDTLdSTAAQQELRSKR-----EQEVNILKKTLEEEA 1180
Cdd:PRK10929 94 EPRSVPPNMSTDAleqeilqvssqllEKSRQAQQEQDRAR-EISDSL-SQLPQQQTEARRqlneiERRLQTLGTPNTPLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1181 KTHEAQIQEMRQKHSQAVEELaeQLEQtkrVKANlekAKQTLENERGELAnevkvllqgkgdsEHKRKKVEAQLQELQVK 1260
Cdd:PRK10929 172 QAQLTALQAESAALKALVDEL--ELAQ---LSAN---NRQELARLRSELA-------------KKRSQQLDAYLQALRNQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1261 FNEGERVRTELADKVTKLQVEldnVTGLLSQSDSKSSKLTKDFSALESQLQDTQELLQEENRQKLSlstKLKQVEDEKNS 1340
Cdd:PRK10929 231 LNSQRQREAERALESTELLAE---QSGDLPKSIVAQFKINRELSQALNQQAQRMDLIASQQRQAAS---QTLQVRQALNT 304
|
....
gi 29436380 1341 FREQ 1344
Cdd:PRK10929 305 LREQ 308
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
881-1235 |
7.64e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 40.40 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 881 EKLQLQEQL-QAETELcaeaEELRARLTAKKqeleeichDLEARVEEEEERCQHLQAE-----KKKMQQNIQELEEQLEE 954
Cdd:pfam05701 220 DKLNWEKELkQAEEEL----QRLNQQLLSAK--------DLKSKLETASALLLDLKAElaaymESKLKEEADGEGNEKKT 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 955 EESARQKLQLEKvtteaklKKLEEEQIILEdqncKLAKEKKLLedRIAEFTTNLTEEEEKSkSLAKLKNKhEAM----IT 1030
Cdd:pfam05701 288 STSIQAALASAK-------KELEEVKANIE----KAKDEVNCL--RVAAASLRSELEKEKA-ELASLRQR-EGMasiaVS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1031 DLEERLRReekQRQELEKTRRKLEGDSTDLSDQIAELQ--AQIAELKMQLAKKEEElqaALARVEEEAAQKNMALKKIre 1108
Cdd:pfam05701 353 SLEAELNR---TKSEIALVQAKEKEAREKMVELPKQLQqaAQEAEEAKSLAQAARE---ELRKAKEEAEQAKAAASTV-- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1109 lESQISELQEDLESERASRNKAEKQKRDLGE-ELEALKTELEDTLDS---TAAQQELRSKREQEVnilkktlEEEAKTHE 1184
Cdd:pfam05701 425 -ESRLEAVLKEIEAAKASEKLALAAIKALQEsESSAESTNQEDSPRGvtlSLEEYYELSKRAHEA-------EELANKRV 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 29436380 1185 A----QIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAkqtleNERGELANEVKV 1235
Cdd:pfam05701 497 AeavsQIEEAKESELRSLEKLEEVNREMEERKEALKIA-----LEKAEKAKEGKL 546
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1023-1228 |
8.74e-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: 39.70 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1023 NKHEAMITDLEERLRREEKQRQELEKTRRKLEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMA 1102
Cdd:pfam06008 15 YKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1103 LKKIRELESQISEL---QEDLESERASRNKAEKQK-------RDLGEELEALKTELEDTLDSTAAQQELRSKREQEVNIL 1172
Cdd:pfam06008 95 IDNIKEINEKVATLgenDFALPSSDLSRMLAEAQRmlgeirsRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKAL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29436380 1173 KKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENERGE 1228
Cdd:pfam06008 175 ANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQ 230
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
875-1345 |
8.79e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 875 QSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELeeichdlearveeeeercQHLQAEKKKMQQNIqeleeqlee 954
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQL------------------AQAPAKLRQAQAEL--------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 955 eesarQKLQLEKVTTEAK-LKKLEEEQiiledqncklakekklLEDRIAEFTTNLTEEEEK----SKSLAKLKNKHEAMI 1029
Cdd:PRK11281 104 -----EALKDDNDEETREtLSTLSLRQ----------------LESRLAQTLDQLQNAQNDlaeyNSQLVSLQTQPERAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1030 TDLEERLRREEKQRQELEKTRrklEGDSTDLSDQIAELQAQIAELKMQLAKKEEELQAALARVEEEAAQKNMALKKIREL 1109
Cdd:PRK11281 163 AALYANSQRLQQIRNLLKGGK---VGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1110 ESQISELQEDLESERasRNKAEKQkrdlgeelealKTELEDTLDSTAAQQELRSKREQEVNilkktleeeaktheaqiQE 1189
Cdd:PRK11281 240 EHQLQLLQEAINSKR--LTLSEKT-----------VQEAQSQDEAARIQANPLVAQELEIN-----------------LQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1190 MRQKHSQAVEELAEQLEQTKRVKANLEKAKQTLENergeLANEVKVlLQGkgdSEHKRKKVEAQLQEL-QVKFNEGervr 1268
Cdd:PRK11281 290 LSQRLLKATEKLNTLTQQNLRVKNWLDRLTQSERN----IKEQISV-LKG---SLLLSRILYQQQQALpSADLIEG---- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1269 teLADKVTKLQVELDNVT---GLLSQSDSKSSKLTKDFS---------ALESQLQDTQELLQEENRQ---KLSLSTKL-- 1331
Cdd:PRK11281 358 --LADRIADLRLEQFEINqqrDALFQPDAYIDKLEAGHKsevtdevrdALLQLLDERRELLDQLNKQlnnQLNLAINLql 435
|
490
....*....|....*.
gi 29436380 1332 --KQVEDEKNSFREQL 1345
Cdd:PRK11281 436 nqQQLLSVSDSLQSTL 451
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1063-1281 |
8.87e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.05 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1063 QIAELQAQIAELKMQlAKKEEELQAALARVEEEAAQKNMALKKIRELESQISELQEDLESERasrnkaekqkrdlgEELE 1142
Cdd:cd22656 95 EILELIDDLADATDD-EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQ--------------TALE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1143 ALKTELEDTLDstaaqQELRSKREQEVNILKKTLEEEAKTHEAQIQEMRQKHSQAVEELAEQLEQTKRVKANLEKAKQTL 1222
Cdd:cd22656 160 TLEKALKDLLT-----DEGGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDL 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29436380 1223 ENERGELANEVKVL--LQGKGDSehkrkkVEAQLQELQVKFNEGErvRTELADKVTKLQVE 1281
Cdd:cd22656 235 DNLLALIGPAIPALekLQGAWQA------IATDLDSLKDLLEDDI--SKIPAAILAKLELE 287
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1158-1374 |
9.39e-03 |
|
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: 40.54 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1158 QQELRSKREQEvniLKKTLEEEAKThEAQIQEMRQKHSQAVEE---LAEQLE-------QTKRVKANLEKAKQTLENERG 1227
Cdd:pfam01576 3 QEEEMQAKEEE---LQKVKERQQKA-ESELKELEKKHQQLCEEknaLQEQLQaetelcaEAEEMRARLAARKQELEEILH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1228 ELANEVKVLLQGKGDSEHKRKKVEAQLQELQVKFNEGERVRTELadkvtklqvELDNVTgllsqSDSKSSKLTKDFsale 1307
Cdd:pfam01576 79 ELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKL---------QLEKVT-----TEAKIKKLEEDI---- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29436380 1308 sqlqdtqeLLQEENRQKLSLSTKLkqVEDEKNSFREQLEEEEEAKHNLEKQIATLHAQVADMKKKKK 1374
Cdd:pfam01576 141 --------LLLEDQNSKLSKERKL--LEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLK 197
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1074-1258 |
9.64e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.62 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1074 LKMQLAKKEEELQAALARVEEEAAQKNMALKKIRELESqisELQEDLEserasrnkaekqkrdlgeELEALKTELE--DT 1151
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKD---ALEEELR------------------QLKQLEDELEdcDP 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1152 LDSTAAQQELrSKREQEVNILKKTLEEeaktheaqIQEMRQKHSQAVEELAEQleqtkrvkanlekaKQTLENergELAN 1231
Cdd:smart00787 204 TELDRAKEKL-KKLLQEIMIKVKKLEE--------LEEELQELESKIEDLTNK--------------KSELNT---EIAE 257
|
170 180
....*....|....*....|....*..
gi 29436380 1232 EVKVLLQGKGDSEHKRKKVEAQLQELQ 1258
Cdd:smart00787 258 AEKKLEQCRGFTFKEIEKLKEQLKLLQ 284
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1019-1092 |
9.81e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 40.05 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29436380 1019 AKLKNKHEAMITD----LEERLRREEKQRQELEKTRRKL----------EGDSTDLSDQIAELQAQIAELKMQLAKKEEE 1084
Cdd:PRK05431 16 EALAKRGFPLDVDelleLDEERRELQTELEELQAERNALskeigqakrkGEDAEALIAEVKELKEEIKALEAELDELEAE 95
|
....*...
gi 29436380 1085 LQAALARV 1092
Cdd:PRK05431 96 LEELLLRI 103
|
|
| |
