|
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 ... |
1-628 |
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: 1276.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKD---QGELERQLLQ 77
Cdd:cd14920 43 MYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDhniPGELERQLLQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 78 ANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLL 157
Cdd:cd14920 123 ANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 158 LEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQK 237
Cdd:cd14920 203 LEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 238 VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDI 317
Cdd:cd14920 283 LCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDI 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 318 AGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECW 397
Cdd:cd14920 363 AGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECW 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 398 FPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWK 477
Cdd:cd14920 443 FPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWK 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 478 DVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLR 557
Cdd:cd14920 523 DVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLR 602
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30268331 558 CNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14920 603 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
1-628 |
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: 1269.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERQLLQANP 80
Cdd:cd14919 43 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 81 ILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEP 160
Cdd:cd14919 123 ILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 161 YNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSH 240
Cdd:cd14919 203 YNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSH 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 241 LLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGF 320
Cdd:cd14919 283 LLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGF 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 321 EIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPK 400
Cdd:cd14919 363 EIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPK 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 401 ATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVD 480
Cdd:cd14919 443 ATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVD 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 481 RIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNG 560
Cdd:cd14919 523 RIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNG 602
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30268331 561 VLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14919 603 VLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
1-628 |
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: 1246.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKD----QGELERQLL 76
Cdd:cd01377 43 KYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITGESGAGKTENTKKVIQYLASVAASSKKKKEsgkkKGTLEDQIL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 77 QANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDL 156
Cdd:cd01377 123 QANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 157 LLEPYNKYR-FLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAA 235
Cdd:cd01377 203 LLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 236 QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGIL 315
Cdd:cd01377 283 DKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 316 DIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPagPPGILALLDEE 395
Cdd:cd01377 362 DIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 396 CWFPKATDKSFVEKVMQEQGTHPK-FQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSE 474
Cdd:cd01377 440 CVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVAS 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 475 LWKDVDRiigldqvagmsETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLD 554
Cdd:cd01377 520 LFKDYEE-----------SGGGGGKKKKKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLH 588
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30268331 555 QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd01377 589 QLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
1-628 |
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: 1232.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQ-------GELER 73
Cdd:cd14932 43 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSFKTKKDQssialshGELEK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 74 QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLK 153
Cdd:cd14932 123 QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 154 TDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNT 233
Cdd:cd14932 203 SELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDT 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 234 AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIG 313
Cdd:cd14932 283 AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 314 ILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLD 393
Cdd:cd14932 363 ILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLD 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 394 EECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVS 473
Cdd:cd14932 443 EECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVS 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 474 ELWKDVDRIIGLDQVAGMSEtALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVL 553
Cdd:cd14932 523 ELWKDVDRIVGLDKVAGMGE-SLHGAFKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVL 601
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30268331 554 DQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14932 602 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
1-628 |
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: 1177.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQ-------GELER 73
Cdd:cd15896 43 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKTKKDQnslalshGELEK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 74 QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLK 153
Cdd:cd15896 123 QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 154 TDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNT 233
Cdd:cd15896 203 SELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNT 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 234 AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIG 313
Cdd:cd15896 283 AAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 314 ILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLD 393
Cdd:cd15896 363 ILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLD 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 394 EECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVS 473
Cdd:cd15896 443 EECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVS 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 474 ELWKDVDRIIGLDQVAGMSEtaLPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVL 553
Cdd:cd15896 523 ELWKDVDRIVGLDKVSGMSE--MPGAFKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVL 600
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30268331 554 DQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd15896 601 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
1-628 |
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: 1139.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQ---GELERQLLQ 77
Cdd:cd14921 43 MYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTsitGELEKQLLQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 78 ANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLL 157
Cdd:cd14921 123 ANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 158 LEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQK 237
Cdd:cd14921 203 LEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 238 VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDI 317
Cdd:cd14921 283 VCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDI 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 318 AGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECW 397
Cdd:cd14921 363 AGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECW 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 398 FPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWK 477
Cdd:cd14921 443 FPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWK 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 478 DVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLR 557
Cdd:cd14921 523 DVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLR 602
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30268331 558 CNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14921 603 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
2-628 |
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: 1070.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASShKSKKD-------------Q 68
Cdd:cd14911 44 YKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGESGAGKTENTKKVIQFLAYVAAS-KPKGSgavphpavnpavlI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 69 GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGA 148
Cdd:cd14911 123 GELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 149 GEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQAS 228
Cdd:cd14911 203 TPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQAT 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 229 MPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQG 308
Cdd:cd14911 283 LPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 309 ASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGI 388
Cdd:cd14911 363 ASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GI 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 389 LALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKpKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSS 468
Cdd:cd14911 440 MALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQ 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 469 DKFVSELWKDVDrIIGLDQVAgMSETALpGAfKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLD 548
Cdd:cd14911 519 DPFVVNIWKDAE-IVGMAQQA-LTDTQF-GA-RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKID 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 549 PHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14911 595 APLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
1-628 |
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: 1057.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQG---ELERQLLQ 77
Cdd:cd14930 43 MYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpgELERQLLQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 78 ANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLL 157
Cdd:cd14930 123 ANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 158 LEPYNKYRFLSNGHVTIPGQQdKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQK 237
Cdd:cd14930 203 LEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 238 VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDI 317
Cdd:cd14930 282 LCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 318 AGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECW 397
Cdd:cd14930 362 AGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECW 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 398 FPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWK 477
Cdd:cd14930 442 FPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWK 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 478 DVDRIIGLDQVAGMSETalPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLR 557
Cdd:cd14930 522 DVEGIVGLEQVSSLGDG--PPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLR 599
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30268331 558 CNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14930 600 CNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
1-628 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1020.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKdQGELERQLLQANP 80
Cdd:pfam00063 55 AYRGKRRGELPPHIFAIADEAYRSMLQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN-VGRLEEQILQSNP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 81 ILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEP 160
Cdd:pfam00063 134 ILEAFGNAKTVRNNNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTN 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 161 YNKYRFLSN-GHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVS 239
Cdd:pfam00063 214 PKDYHYLSQsGCYTIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 240 HLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAG 319
Cdd:pfam00063 294 SLLGIDSTELEKALCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 320 FEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWFP 399
Cdd:pfam00063 374 FEIFEKNSFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFP 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 400 KATDKSFVEKVMQEQGTHPKFQKPKQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDV 479
Cdd:pfam00063 451 KATDQTFLDKLYSTFSKHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDY 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 480 DRIIGLDQVagmsETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCN 559
Cdd:pfam00063 530 ETAESAAAN----ESGKSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCN 605
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30268331 560 GVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:pfam00063 606 GVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
1-640 |
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: 921.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKkdqGELERQLLQANP 80
Cdd:smart00242 62 KYRGKSRGELPPHVFAIADNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV---GSVEDQILESNP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 81 ILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEP 160
Cdd:smart00242 139 ILEAFGNAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 161 YNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNT-AAQKV 238
Cdd:smart00242 219 PEDYRYLNQGGcLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 239 SHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIA 318
Cdd:smart00242 299 AELLGVDPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIY 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 319 GFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECWF 398
Cdd:smart00242 378 GFEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEKK--PPGILSLLDEECRF 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 399 PKATDKSFVEKVMQEQGTHPKFQKPKQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD 478
Cdd:smart00242 455 PKGTDQTFLEKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 479 VdriigldqvagmsetalpGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRC 558
Cdd:smart00242 534 G------------------VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRY 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 559 NGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFRAGVLAHLEEE 638
Cdd:smart00242 596 LGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEEL 675
|
..
gi 30268331 639 RD 640
Cdd:smart00242 676 RE 677
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
1-628 |
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: 814.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRH-EMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKD--QGELERQLLQ 77
Cdd:cd00124 43 KYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILISGESGAGKTETTKLVLKYLAALSGSGSSKSSssASSIEQQILQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 78 ANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLL 157
Cdd:cd00124 123 SNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 158 LEPYNKYRFL-----SNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNT--DQASMP 230
Cdd:cd00124 203 LELLLSYYYLndylnSSGCDRIDGVDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 231 DNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQ-GA 309
Cdd:cd00124 283 DDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeST 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 310 SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGIL 389
Cdd:cd00124 363 SFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGIL 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 390 ALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSD 469
Cdd:cd00124 440 SLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 470 kfvselwkdvdriigldqvagmsetalpgafktrkgmfrtvgqlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDP 549
Cdd:cd00124 519 --------------------------------------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDP 554
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30268331 550 HLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd00124 555 ELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
2-1178 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 801.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSkkDQGELERQLLQANPI 81
Cdd:COG5022 123 YSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTV--EISSIEKQILATNPI 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 82 LEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPY 161
Cdd:COG5022 201 LEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNP 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 162 NKYRFLSNGHVT-IPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTAAQKVSH 240
Cdd:COG5022 281 KDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 241 LLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGaSFIGILDIAGF 320
Cdd:COG5022 360 LLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGF 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 321 EIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKpAGPPGILALLDEECWFPK 400
Cdd:COG5022 439 EIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPH 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 401 ATDKSFVEKVMQ--EQGTHPKFQKPKQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD 478
Cdd:COG5022 517 ATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDD 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 479 VDRIigldqvagmsetalpgafkTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRC 558
Cdd:COG5022 595 EENI-------------------ESKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRC 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 559 NGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS----IPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFRAGVLAH 634
Cdd:COG5022 656 CGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAA 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 635 LEEERDLKITDVIIGFQACCRGYLARKAFAKRQQQLTAMKVLQRNCAAYLKLRNWQWWRLFTKVKPLLQVSRQEEEMMAK 714
Cdd:COG5022 736 LEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSY 815
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 715 EEElvkVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLqaetelcAEAEELRAR-LTAKKQELEEIChdlEARVEEEEE 793
Cdd:COG5022 816 LAC---IIKLQKTIKREKKLRETEEVEFSLKAEVLIQKF-------GRSLKAKKRfSLLKKETIYLQS---AQRVELAER 882
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 794 RCQHLQAEKKKMQQniqeleeqleeeeSARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKKFDQLL- 872
Cdd:COG5022 883 QLQELKIDVKSISS-------------LKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIe 949
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 873 AEEKTISAKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKqfrtEMEDLMSSKDDVGKSVHELEKSKRAL 952
Cdd:COG5022 950 YVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKK----ELAELSKQYGALQESTKQLKELPVEV 1025
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 953 EQQVEEMKTQLEELEGELQATEDAKLR--LEVNLQAMKAQFErDLQGRDEQSEEKKKQL--------------VRQVREM 1016
Cdd:COG5022 1026 AELQSASKIISSESTELSILKPLQKLKglLLLENNQLQARYK-ALKLRRENSLLDDKQLyqlestenllktinVKDLEVT 1104
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1017 EAELEDERKQRSMAVAARKKLemdlkDLEAHIDSANK---NRDEAIKQLRKLQAQMKDCMRELDDTRA---------SRE 1084
Cdd:COG5022 1105 NRNLVKPANVLQFIVAQMIKL-----NLLQEISKFLSqlvNTLEPVFQKLSVLQLELDGLFWEANLEAlpspppfaaLSE 1179
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1085 EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRqaqqERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQ 1164
Cdd:COG5022 1180 KRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIF----SGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDTPAS 1255
|
1210
....*....|....
gi 30268331 1165 GNTELINDRLKKAN 1178
Cdd:COG5022 1256 MSNEKLLSLLNSID 1269
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
2-628 |
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: 725.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVAS---------SHKSKKDQGELE 72
Cdd:cd14927 44 YKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAIVAAlgdgpgkkaQFLATKTGGTLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 73 RQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHL 152
Cdd:cd14927 124 DQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPEL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 153 KTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMP 230
Cdd:cd14927 204 QDMLLVsmNPYD-YHFCSQGVTTVDNMDDGEELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEAD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 231 DNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGAS 310
Cdd:cd14927 283 GTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQF 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 311 FIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILA 390
Cdd:cd14927 362 FIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILS 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 391 LLDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKP---KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQ 466
Cdd:cd14927 439 ILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPrpdKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQK 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 467 SSDKFVSELWKDVdriigldqVAGMSETALPGAFKTRK---GMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKK 543
Cdd:cd14927 519 SQNKLLATLYENY--------VGSDSTEDPKSGVKEKRkkaASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKT 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 544 AGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK-GFMDGKQACVLMIKALELDSNLYRIGQ 622
Cdd:cd14927 591 PGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGH 670
|
....*.
gi 30268331 623 SKVFFR 628
Cdd:cd14927 671 TKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
2-628 |
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: 706.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASS-----HKSKKDQGELERQLL 76
Cdd:cd14913 44 YRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAATgdlakKKDSKMKGTLEDQII 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 77 QANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDL 156
Cdd:cd14913 124 SANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 157 LL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT- 233
Cdd:cd14913 204 LIttNPYD-YPFISQGEILVASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTe 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 234 AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIG 313
Cdd:cd14913 282 VADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 314 ILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLD 393
Cdd:cd14913 361 VLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILE 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 394 EECWFPKATDKSFVEKVM-QEQGTHPKFQKPKQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDK 470
Cdd:cd14913 438 EECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNR 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 471 FVSELWKDvdriigldqVAGMSETALPGAFKTRKG-MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDP 549
Cdd:cd14913 518 LLAHLYAT---------FATADADSGKKKVAKKKGsSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEH 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 550 HLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14913 589 SLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
1-628 |
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: 704.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKD-QGELERQLLQAN 79
Cdd:cd14934 43 MYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGESGAGKTENTKKVIQYFANIGGTGKQSSDgKGSLEDQIIQAN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 80 PILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE 159
Cdd:cd14934 123 PVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 160 PYNK-YRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKV 238
Cdd:cd14934 203 PNPKeYHWVSQGVTVVDNMDDGEELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 239 SHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIA 318
Cdd:cd14934 283 AHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 319 GFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGppgILALLDEECWF 398
Cdd:cd14934 362 GFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMG---IFSILEEQCVF 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 399 PKATDKSFVEKVMQEQ-GTHPKFQKPKQLKDK---ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSdkfvse 474
Cdd:cd14934 439 PKATDATFKAALYDNHlGKSSNFLKPKGGKGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS------ 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 475 lwkdvdriIGLDQVAGMSETALPGAFKTRKGM-FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVL 553
Cdd:cd14934 513 --------LGLLALLFKEEEAPAGSKKQKRGSsFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIM 584
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30268331 554 DQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14934 585 HQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
741-1312 |
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: 689.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 741 QLMAEKLQLQEQLQAETELCAEAEE----LRARLTAKKQELEEICHDLEArveeeeercqhLQAEKKKMQQNIQELEEQL 816
Cdd:pfam01576 493 QLEDERNSLQEQLEEEEEAKRNVERqlstLQAQLSDMKKKLEEDAGTLEA-----------LEEGKKRLQRELEALTQQL 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 817 EEEESARQKLqlekvttEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAGERDRAEAEAREK 896
Cdd:pfam01576 562 EEKAAAYDKL-------EKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREK 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 897 ETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDA 976
Cdd:pfam01576 635 ETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDA 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 977 KLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRD 1056
Cdd:pfam01576 715 KLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGRE 794
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1057 EAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSS 1136
Cdd:pfam01576 795 EAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGA 874
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1137 GKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKL 1216
Cdd:pfam01576 875 SGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKL 954
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1217 QEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQ 1296
Cdd:pfam01576 955 QEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQ 1034
|
570
....*....|....*.
gi 30268331 1297 LKRQLEEAEEEAQRAT 1312
Cdd:pfam01576 1035 LKRQLEEAEEEASRAN 1050
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
1-628 |
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: 688.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQ---GELERQLLQ 77
Cdd:cd14909 43 MYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGESGAGKTENTKKVIAYFATVGASKKTDEAAkskGSLEDQVVQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 78 ANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLL 157
Cdd:cd14909 123 TNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 158 L-EPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQ 236
Cdd:cd14909 203 LsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 237 KVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILD 316
Cdd:cd14909 283 RVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLD 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 317 IAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEEC 396
Cdd:cd14909 362 IAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEES 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 397 WFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLK---DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFV 472
Cdd:cd14909 439 MFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLL 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 473 SELWKDvdriiGLDQVAGMSETAlpGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLV 552
Cdd:cd14909 519 IEIFAD-----HAGQSGGGEQAK--GGRGKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLV 591
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30268331 553 LDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14909 592 MHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
2-628 |
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: 672.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERQLLQANPI 81
Cdd:cd14929 44 YKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGESGAGKTVNTKHIIQYFATIAAMIESKKKLGALEDQIMQANPV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 82 LEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEhlKTDLLLEPY 161
Cdd:cd14929 124 LEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 162 N--KYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVS 239
Cdd:cd14929 202 NpsDFHFCSCGAVAVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 240 HLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAG 319
Cdd:cd14929 282 FLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 320 FEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFP 399
Cdd:cd14929 361 FEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFP 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 400 KATDKSFVEKVMQEQ-GTHPKFQKPKQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELW 476
Cdd:cd14929 438 KATDLTFKTKLFDNHfGKSVHFQKPKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 477 KDvdriiglDQVAGmseTALPGAFKTRK--GMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLD 554
Cdd:cd14929 518 EN-------YISTD---SAIQFGEKKRKkgASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQ 587
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30268331 555 QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14929 588 QLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
2-628 |
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: 661.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVAS-SHKSKKDQ----GELERQLL 76
Cdd:cd14917 44 YRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAiGDRSKKDQtpgkGTLEDQII 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 77 QANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDL 156
Cdd:cd14917 124 QANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDML 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 157 LL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNTA 234
Cdd:cd14917 204 LItnNPYD-YAFISQGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 235 -AQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIG 313
Cdd:cd14917 282 eADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 314 ILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLD 393
Cdd:cd14917 361 VLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILE 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 394 EECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDK 470
Cdd:cd14917 438 EECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGKpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLK 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 471 FVSELWKDvdriigldqVAGMSETALPGAFKTRKG-MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDP 549
Cdd:cd14917 518 LLSNLFAN---------YAGADAPIEKGKGKAKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDN 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 550 HLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14917 589 PLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
2-628 |
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: 656.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKdqgELERQLLQANPI 81
Cdd:cd01380 45 YSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSGESGAGKTVSAKYAMRYFATVGGSSSGET---QVEEKVLASNPI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 82 LEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPY 161
Cdd:cd01380 122 MEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 162 NKYRFLSNG-HVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSH 240
Cdd:cd01380 202 EDFFYTNQGgSPVIDGVDDAAEFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 241 LLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGA-SFIGILDIAG 319
Cdd:cd01380 282 LLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 320 FEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEkpaGPPGILALLDEECWFP 399
Cdd:cd01380 362 FETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLP 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 400 KATDKSFVEKVMQEQGTHPK--FQKPKQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSsdkfvselwk 477
Cdd:cd01380 438 KGSDENWAQKLYNQHLKKPNkhFKKPRFSNTA--FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKAS---------- 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 478 dvdriigldqvagmsetalpgafKTRKgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLR 557
Cdd:cd01380 506 -----------------------KNRK---KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLR 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30268331 558 CNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd01380 560 ACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
2-628 |
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: 643.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVAS-SHKSKKD-----QGELERQL 75
Cdd:cd14916 44 YRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFASIAAiGDRSKKEnpnanKGTLEDQI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 76 LQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTD 155
Cdd:cd14916 124 IQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDM 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 156 LLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT 233
Cdd:cd14916 204 LLVtnNPYD-YAFVSQGEVSVASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGT 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 234 A-AQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFI 312
Cdd:cd14916 282 EdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFI 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 313 GILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALL 392
Cdd:cd14916 361 GVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSIL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 393 DEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSD 469
Cdd:cd14916 438 EEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVKGKqeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSL 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 470 KFVSELWKDVdriigldQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDP 549
Cdd:cd14916 518 KLMATLFSTY-------ASADTGDSGKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDN 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 550 HLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14916 591 PLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
2-628 |
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: 642.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKD-----QGELERQLL 76
Cdd:cd14918 44 YRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEesgkmQGTLEDQII 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 77 QANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDL 156
Cdd:cd14918 124 SANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEML 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 157 LL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT- 233
Cdd:cd14918 204 LIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTe 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 234 AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIG 313
Cdd:cd14918 282 VADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 314 ILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLD 393
Cdd:cd14918 361 VLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILE 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 394 EECWFPKATDKSFVEKVM-QEQGTHPKFQKPKQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDK 470
Cdd:cd14918 438 EECMFPKATDTSFKNKLYdQHLGKSANFQKPKVVKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMK 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 471 FVSELWKDVdriigldQVAGMSETALPGAfKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPH 550
Cdd:cd14918 518 TLASLFSTY-------ASAEADSGAKKGA-KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHE 589
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30268331 551 LVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14918 590 LVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
2-628 |
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: 641.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKD------QGELERQL 75
Cdd:cd14923 44 YRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEqqpgkmQGTLEDQI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 76 LQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLkTD 155
Cdd:cd14923 124 IQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-ID 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 156 LLLEPYNKYRF--LSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT 233
Cdd:cd14923 203 LLLISTNPFDFpfVSQGEVTVASIDDSEELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGT 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 234 -AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFI 312
Cdd:cd14923 282 eVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFI 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 313 GILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALL 392
Cdd:cd14923 361 GVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSIL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 393 DEECWFPKATDKSFVEKVM-QEQGTHPKFQKPKQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSD 469
Cdd:cd14923 438 EEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSL 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 470 KFVSELWKDVdriigLDQVAGMSETALPGAfKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDP 549
Cdd:cd14923 518 KLLSFLFSNY-----AGAEAGDSGGSKKGG-KKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDH 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 550 HLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14923 592 YLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
2-628 |
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: 636.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKD-------QGELERQ 74
Cdd:cd14912 44 YRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEeitsgkmQGTLEDQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 75 LLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKT 154
Cdd:cd14912 124 IISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 155 DLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDN 232
Cdd:cd14912 204 MLLIttNPYD-YPFVSQGEISVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 233 T-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASF 311
Cdd:cd14912 282 TeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYF 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 312 IGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILAL 391
Cdd:cd14912 361 IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSI 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 392 LDEECWFPKATDKSFVEKVM-QEQGTHPKFQKPKQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSS 468
Cdd:cd14912 438 LEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKVVKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSA 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 469 DKFVSELWKDVDRIIGLDQVAGMSETAlpgafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLD 548
Cdd:cd14912 518 MKTLAYLFSGAQTAEGASAGGGAKKGG-----KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAME 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 549 PHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFF 627
Cdd:cd14912 593 HELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFF 672
|
.
gi 30268331 628 R 628
Cdd:cd14912 673 K 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
2-628 |
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: 631.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKD-------QGELERQ 74
Cdd:cd14910 44 YRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEeatsgkmQGTLEDQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 75 LLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKT 154
Cdd:cd14910 124 IISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 155 DLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDN 232
Cdd:cd14910 204 MLLIttNPYD-YAFVSQGEITVPSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 233 T-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASF 311
Cdd:cd14910 282 TeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYF 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 312 IGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILAL 391
Cdd:cd14910 361 IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSI 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 392 LDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSS 468
Cdd:cd14910 438 LEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGKveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSS 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 469 DKFVSELWKDvdriigldqvAGMSETALPGAFK--TRKG-MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAG 545
Cdd:cd14910 518 MKTLALLFSG----------AAAAEAEEGGGKKggKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPG 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 546 KLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSK 624
Cdd:cd14910 588 AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTK 667
|
....
gi 30268331 625 VFFR 628
Cdd:cd14910 668 VFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
2-628 |
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: 629.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKskkdqgELERQLLQANPI 81
Cdd:cd14883 44 YFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGESGAGKTETTKLILQYLCAVTNNHS------WVEQQILEANTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 82 LEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGE--HLKTDLLLE 159
Cdd:cd14883 118 LEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 160 PYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKK-ERNTDQASMPDNTAAQK 237
Cdd:cd14883 198 EPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 238 VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGaSFIGILDI 317
Cdd:cd14883 278 VAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 318 AGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEECW 397
Cdd:cd14883 357 FGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECR 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 398 FPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWK 477
Cdd:cd14883 434 FPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFT 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 478 DVDrIIGLDQVAGMSETALPGAfKTRKGMfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLR 557
Cdd:cd14883 514 YPD-LLALTGLSISLGGDTTSR-GTSKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLR 590
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30268331 558 CNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14883 591 YAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
2-628 |
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: 622.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKD-------QGELERQ 74
Cdd:cd14915 44 YRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEeaasgkmQGTLEDQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 75 LLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKT 154
Cdd:cd14915 124 IISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 155 DLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDN 232
Cdd:cd14915 204 MLLIttNPYD-FAFVSQGEITVPSIDDQEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 233 T-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASF 311
Cdd:cd14915 282 TeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYF 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 312 IGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILAL 391
Cdd:cd14915 361 IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSI 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 392 LDEECWFPKATDKSFVEKVMQEQ-GTHPKFQKPKQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSS 468
Cdd:cd14915 438 LEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSG 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 469 DKFVSELWKDvdriiglDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLD 548
Cdd:cd14915 518 MKTLAFLFSG-------GQTAEAEGGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAME 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 549 PHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFF 627
Cdd:cd14915 591 HELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFF 670
|
.
gi 30268331 628 R 628
Cdd:cd14915 671 K 671
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
11-628 |
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: 604.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 11 PPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASshkskkDQGELERQLLQANPILEAFGNAKT 90
Cdd:cd01383 51 SPHVYAVADTAYREMMRDEINQSIIISGESGAGKTETAKIAMQYLAALGG------GSSGIENEILQTNPILEAFGNAKT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 91 VKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS-N 169
Cdd:cd01383 125 LRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 170 GHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDF 249
Cdd:cd01383 205 NCLTIDGVDDAKKFHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 250 TRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFE 329
Cdd:cd01383 285 MLALSTRKIQAGGDKIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 330 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEK 409
Cdd:cd01383 365 QLCINYANERLQQHFNRHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEKK--PLGLISLLDEESNFPKATDLTFANK 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 410 VMQEQGTHPKFQKPkqlKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLL----HQSSDKFVSELWKDVDRIigl 485
Cdd:cd01383 442 LKQHLKSNSCFKGE---RGGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLsscsCQLPQLFASKMLDASRKA--- 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 486 dqvagmsetALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGI 565
Cdd:cd01383 515 ---------LPLTKASGSDSQKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVV 585
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30268331 566 RICRQGFPNRVVFQEFRQRYEILTPNSIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd01383 586 RISRSGYPTRMTHQEFARRYGFLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
1-628 |
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: 603.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVasshkSKKDQGELER---QLLQ 77
Cdd:cd01378 43 SYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESGAGKTEASKRIMQYIAAV-----SGGSESEVERvkdMLLA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 78 ANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLL 157
Cdd:cd01378 118 SNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 158 LE-PYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTAAQ 236
Cdd:cd01378 198 LQrPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 237 KVSHLLGINVTDFTRGILTPRIKVG---RDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIG 313
Cdd:cd01378 277 FVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 314 ILDIAGFEIFDLNSFEQLCINYTNEKLQQLFnhTMFIL--EQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILAL 391
Cdd:cd01378 357 VLDIYGFEIFEKNSFEQFCINYVNEKLQQIF--IELTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEEK--PPGIFAI 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 392 LDEECWFP-KATDKSFVEKVMQEQGTHPKFQKPKQLKD--KADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSS 468
Cdd:cd01378 432 LDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHFElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSS 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 469 DKFVSELWKDVDRiigldqvagmsetalpgafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLD 548
Cdd:cd01378 512 NPFLRSLFPEGVD-------------------LDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFD 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 549 PHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd01378 573 EELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
1-628 |
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: 596.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASshKSKKDQGELERQLLQANP 80
Cdd:cd01384 44 QYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGESGAGKTETTKMLMQYLAYMGG--RAVTEGRSVEQQVLESNP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 81 ILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEP 160
Cdd:cd01384 122 LLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 161 YNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPD---NTAAQ 236
Cdd:cd01384 202 PKQFHYLNQSKcFELDGVDDAEEYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 237 KVSHLLGINVTDFTRGiLTPRIKVGRD-YVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL--DKTKRqgaSFIG 313
Cdd:cd01384 282 AAAELLMCDEKALEDA-LCKRVIVTPDgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIgqDPNSK---RLIG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 314 ILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKpaGPPGILALLD 393
Cdd:cd01384 358 VLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLD 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 394 EECWFPKATDKSFVEKVMQEQGTHPKFQKPKqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVS 473
Cdd:cd01384 435 EACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVA 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 474 ELWKDVDRiigldqvagmsetalPGAFKTRKgmFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVL 553
Cdd:cd01384 513 GLFPPLPR---------------EGTSSSSK--FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVL 575
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30268331 554 DQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNsIPKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 628
Cdd:cd01384 576 QQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPE-VLKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
1-628 |
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: 568.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSkkdqgeLERQLLQANP 80
Cdd:cd01381 43 LYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGESGAGKTESTKLILQYLAAISGQHSW------IEQQILEANP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 81 ILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEP 160
Cdd:cd01381 117 ILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 161 YNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKK--ERNTDQASMPDNTAAQK 237
Cdd:cd01381 197 ASDYYYLTQGNcLTCEGRDDAAEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLER 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 238 VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAS--FIGIL 315
Cdd:cd01381 277 AAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 316 DIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLI-EKPAgppGILALLDE 394
Cdd:cd01381 357 DIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPM---NIMSLIDE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 395 ECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFvse 474
Cdd:cd01381 433 ESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTS-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKF--- 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 475 lwkdVDRIIGLDQVAGMSetalpgafkTRKgmfR--TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLV 552
Cdd:cd01381 509 ----LKQLFNEDISMGSE---------TRK---KspTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELC 572
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30268331 553 LDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd01381 573 VRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
2-628 |
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: 557.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHkskkdQGELERQLLQANPI 81
Cdd:cd01382 45 YQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGESGAGKTESTKYILRYLTESWGSG-----AGPIEQRILEANPL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 82 LEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLlepy 161
Cdd:cd01382 120 LEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL---- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 162 nkyrflsnghvTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNT-------DQASMPDNTA 234
Cdd:cd01382 196 -----------KDPLLDDVGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 235 AqkvSHLLGINVTDF-----TRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKrqGA 309
Cdd:cd01382 265 A---AELLGLDQDELrvsltTRVMQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 310 SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGIL 389
Cdd:cd01382 340 YFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GIL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 390 ALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKP--------KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIA 461
Cdd:cd01382 417 DLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPrksklkihRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLE 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 462 TLLHQSSDKFVSELWKDVDRiigldqvagMSETALPgafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHE 541
Cdd:cd01382 497 SLICESKDKFIRSLFESSTN---------NNKDSKQ---KAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLK 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 542 KKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKgfMDGKQACVLMIKALELDSNLYRIG 621
Cdd:cd01382 565 MTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFG 642
|
....*..
gi 30268331 622 QSKVFFR 628
Cdd:cd01382 643 LTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
1-628 |
2.71e-171 |
|
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: 524.34 E-value: 2.71e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRheMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASShkskkdQGELERQLLQANP 80
Cdd:cd14872 45 MHKGPKE--MPPHTYNIADDAYRAMIVDAMNQSILISGESGAGKTEATKQCLSFFAEVAGS------TNGVEQRVLLANP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 81 ILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAgeHLKTDLLLEP 160
Cdd:cd14872 117 ILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGS 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 161 YNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQAS---MPDNTAAQ 236
Cdd:cd14872 195 SAAYGYLSLSGcIEVEGVDDVADFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 237 KVSHLLGINVTDFTRGILTPRIKV-GRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGIL 315
Cdd:cd14872 275 EVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 316 DIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEE 395
Cdd:cd14872 355 DIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKK--QPGLMLALDDQ 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 396 CWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSEL 475
Cdd:cd14872 432 VKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVL 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 476 WKDVDriigldqvagmsetalpGAFKTRKGmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQ 555
Cdd:cd14872 512 FPPSE-----------------GDQKTSKV---TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQ 571
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30268331 556 LRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILtPNSIPKGFM-DGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14872 572 LRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
1-628 |
2.14e-169 |
|
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: 520.08 E-value: 2.14e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVAsshksKKDQGELERQLLQANP 80
Cdd:cd01387 43 QYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGESGSGKTEATKLIMQYLAAVN-----QRRNNLVTEQILEATP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 81 ILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEP 160
Cdd:cd01387 118 LLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 161 YNKYRFLSNG-HVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQ---ASMPDNTAAQ 236
Cdd:cd01387 197 AEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 237 KVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASfIGILD 316
Cdd:cd01387 277 WVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLS-IAILD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 317 IAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEEC 396
Cdd:cd01387 356 IFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLISKK--PVGILHILDDEC 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 397 WFPKATDKSFVEKVMQEQGTHPKFQKPKQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELW 476
Cdd:cd01387 433 NFPQATDHSFLEKCHYHHALNELYSKPRM--PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLF 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 477 KdvdriigldQVAGMSETALP----GAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLV 552
Cdd:cd01387 511 S---------SHRAQTDKAPPrlgkGRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVV 581
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30268331 553 LDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGfMDGKQACVLMIKALELD-SNLYRIGQSKVFFR 628
Cdd:cd01387 582 MAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTpKDMYRLGATKVFLR 657
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
2-628 |
1.69e-168 |
|
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: 517.79 E-value: 1.69e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQ----DREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQ--------- 68
Cdd:cd14890 45 YHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQSIIISGESGAGKTEATKIIMQYLARITSGFAQGASGegeaaseai 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 69 ----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYL 144
Cdd:cd14890 125 eqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 145 LSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNT 224
Cdd:cd14890 205 LAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDT 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 225 DQASmpDNTAAQKVSH---LLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL 301
Cdd:cd14890 285 TVLE--DATTLQSLKLaaeLLGVNEDALEKALLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTI 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 302 DKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE- 380
Cdd:cd14890 363 SSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEg 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 381 KPAGPPGILALLDeECWFPKAT--DKSFVEKVMQEQGT-------------HPKFQKPKQLKDKaDFCIIHYAGKVDYKA 445
Cdd:cd14890 441 KVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHASFGRksgsggtrrgssqHPHFVHPKFDADK-QFGIKHYAGDVIYDA 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 446 DEWLMKNMDPLNDNIATLLHQSsdkfvselwkdvDRIIgldqvAGMSetalpgafktrkgmfrtVGQLYKEQLAKLMATL 525
Cdd:cd14890 519 SGFNEKNNETLNAEMKELIKQS------------RRSI-----REVS-----------------VGAQFRTQLQELMAKI 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 526 RNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSipkgfMDGKQACV 605
Cdd:cd14890 565 SLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVA 639
|
650 660
....*....|....*....|...
gi 30268331 606 LMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14890 640 VLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
7-628 |
1.83e-164 |
|
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: 506.15 E-value: 1.83e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 7 RHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLayvasSHKSKKDQGELERQLLQANPILEAFG 86
Cdd:cd14897 50 RSQRPPHLFWIADQAYRRLLETGRNQCILVSGESGAGKTESTKYMIKHL-----MKLSPSDDSDLLDKIVQINPLLEAFG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 87 NAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRF 166
Cdd:cd14897 125 NASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 167 LSNGHVTIPGQQD-------KDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVS 239
Cdd:cd14897 205 LRDDNRNRPVFNDseeleyyRQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 240 HLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL----DKTKRQGASFIGIL 315
Cdd:cd14897 285 KLLGIDEVELTEALISNVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGIL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 316 DIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILALLDEE 395
Cdd:cd14897 365 DMSGFENFKINSFDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFKK--PLGILPLLDEE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 396 CWFPKATDKSFVEKVMQEQGTHPKFQKPKQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSEL 475
Cdd:cd14897 442 STFPQSTDSSLVQKLNKYCGESPRYVASPG--NRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDL 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 476 WKdvdriigldqvagmsetalpgafktrkgmfrtvgQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQ 555
Cdd:cd14897 520 FT----------------------------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQ 565
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30268331 556 LRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSiPKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 628
Cdd:cd14897 566 LLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
7-626 |
6.78e-164 |
|
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: 505.48 E-value: 6.78e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 7 RHEMPPHIYAITDTAYRSMMQDRE----DQSILCTGESGAGKTENTKKVIQYLAYVASshKSKKDQGELER-----QLLQ 77
Cdd:cd14901 55 ERKLPPHVYAVADKAFRAMLFASRgqkcDQSILVSGESGAGKTETTKIIMNYLASVSS--ATTHGQNATERenvrdRVLE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 78 ANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLL 157
Cdd:cd14901 133 SNPILEAFGNARTNRNNNSSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 158 LEPYNKYRFL--SNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVF-KKERNTDQASMPDNTA 234
Cdd:cd14901 213 LTHVEEYKYLnsSQCYDRRDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLAN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 235 AQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAS-FIG 313
Cdd:cd14901 293 VRAACDLLGLDMDVLEKTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIG 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 314 ILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIDLIEkpAGPPGIL 389
Cdd:cd14901 373 IVDIFGFEIFATNSLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLF 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 390 ALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSD 469
Cdd:cd14901 446 SLLDEQCLLPRGNDEKLANKYYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSN 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 470 KFVSElwkdvdriigldqvagmsetalpgafktrkgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDP 549
Cdd:cd14901 526 AFLSS----------------------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDA 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 550 HLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNL-----YRIGQSK 624
Cdd:cd14901 572 KRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIehlppFQVGKTK 651
|
..
gi 30268331 625 VF 626
Cdd:cd14901 652 VF 653
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
2-628 |
2.05e-163 |
|
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: 504.31 E-value: 2.05e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVAsshkskkdqGELE----RQLLQ 77
Cdd:cd14903 45 YLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVSGESGAGKTETTKILMNHLATIA---------GGLNdstiKKIIE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 78 ANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLsgAGEHLKTDLL 157
Cdd:cd14903 116 VNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 158 LEPYNKYRFL-SNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASM--PDNTA 234
Cdd:cd14903 194 LDSANECAYTgANKTIKIEGMSDRKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 235 AQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGI 314
Cdd:cd14903 274 AVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 315 LDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEkpaGPPGILALLDE 394
Cdd:cd14903 353 LDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLND 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 395 ECWFPKATDKSFVEKVMqeqGTHPKFQK----PKqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDK 470
Cdd:cd14903 429 EVMRPKGNEESFVSKLS---SIHKDEQDviefPR--TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKP 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 471 FVSELWKDvdrIIGLDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPH 550
Cdd:cd14903 504 FLRMLFKE---KVESPAAASTSLARGARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHL 580
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30268331 551 LVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSiPKGFMDGKQACVLMIKALELDS-NLYRIGQSKVFFR 628
Cdd:cd14903 581 MVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
1-628 |
4.76e-163 |
|
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: 504.60 E-value: 4.76e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVasshkSKKDQGE-LERQLLQAN 79
Cdd:cd01385 43 MYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESGSGKTESTNFLLHHLTAL-----SQKGYGSgVEQTILGAG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 80 PILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE 159
Cdd:cd01385 118 PVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 160 PYNKYRFL--SNGHvTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKER-NTDQASMPDNTAAQ 236
Cdd:cd01385 198 QPEDYHYLnqSDCY-TLEGEDEKYEFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 237 K-VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL----DKTKRQGASf 311
Cdd:cd01385 277 DiISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 312 IGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILAL 391
Cdd:cd01385 356 IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISKK--PTGLLCL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 392 LDEECWFPKATDKSFVEKVMQEQGTHPKFQKPkQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKF 471
Cdd:cd01385 433 LDEESNFPGATNQTLLAKFKQQHKDNKYYEKP-QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAF 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 472 VSELwkdvdriIGLDQVAGMSETALPGAFKT-----RKGMFR-----------------------------TVGQLYKEQ 517
Cdd:cd01385 511 VREL-------IGIDPVAVFRWAVLRAFFRAmaafrEAGRRRaqrtaghsltlhdrttksllhlhkkkkppSVSAQFQTS 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 518 LAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILtpnsIPKGF 597
Cdd:cd01385 584 LSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL 659
|
650 660 670
....*....|....*....|....*....|.
gi 30268331 598 MDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd01385 660 ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
11-628 |
1.45e-161 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 499.29 E-value: 1.45e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 11 PPHIYAITDTAYRSMMQDR----EDQSILCTGESGAGKTENTKKVIQYLA----YVASSHKSKKDQG---ELERQLLQAN 79
Cdd:cd14892 56 PPHVFSIAERAYRAMKGVGkgqgTPQSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANaheSIEECVLLSN 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 80 PILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE 159
Cdd:cd14892 136 LILEAFGNAKTIRNDNSSRFGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 160 PYNKYRFLSNGH-VTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFkkERNTDQ----ASMPDNTA 234
Cdd:cd14892 216 PAESFLFLNQGNcVEVDGVDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVN 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 235 AQKVSHLLGINVTDFTRGILTPRIKVGRDYV-QKAQTKEQADFAIEALAKATYERMFRWLVLRINKAldkTKRQG----- 308
Cdd:cd14892 294 VAKAAGLLGVDAAELMFKLVTQTTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINAC---HKQQTsgvtg 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 309 -------ASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEK 381
Cdd:cd14892 371 gaasptfSPFIGILDIFGFEIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQK 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 382 PagPPGILALLDEECWFP-KATDKSFVEKVMQEQ-GTHPKFQKPKQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDN 459
Cdd:cd14892 450 K--PLGLLPLLEEQMLLKrKTTDKQLLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDD 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 460 IATLLHQSSDkfvselwkdvdriigldqvagmsetalpgafktrkgmFRTvgqlykeQLAKLMATLRNTNPNFVRCIIPN 539
Cdd:cd14892 526 LRDLLRSSSK-------------------------------------FRT-------QLAELMEVLWSTTPSYIKCIKPN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 540 HEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS-IPKGFMDGKQACVLMIKALE-----L 613
Cdd:cd14892 562 NLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNKaGVAASPDACDATTARKKCEEivaraL 641
|
650
....*....|....*
gi 30268331 614 DSNLYRIGQSKVFFR 628
Cdd:cd14892 642 ERENFQLGRTKVFLR 656
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
11-590 |
2.55e-161 |
|
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: 499.22 E-value: 2.55e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 11 PPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQgeLERQLLQANPILEAFGNAKT 90
Cdd:cd14888 53 SPHVFSTASSAYQGMCNNKKSQTILISGESGAGKTESTKYVMKFLACAGSEDIKKRSL--VEAQVLESNPLLEAFGNART 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 91 VKNDNSSRFGKFIRINFD---------VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPY 161
Cdd:cd14888 131 LRNDNSSRFGKFIELQFSklkskrmsgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEEN 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 162 NKYRFLSN------------------------GHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIV 217
Cdd:cd14888 211 DEKLAKGAdakpisidmssfephlkfryltksSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNIL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 218 FKKERNTDQASMPDNTAAQ---KVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLV 294
Cdd:cd14888 291 FENNEACSEGAVVSASCTDdleKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVV 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 295 LRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQP 374
Cdd:cd14888 371 ERTNESIGYSKDNSLLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQD 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 375 CIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKqlKDKADFCIIHYAGKVDYKADEWLMKNMD 454
Cdd:cd14888 450 CVDLLQ--EKPLGIFCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKD 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 455 PLNDNIATLLHQSSDKFVSELWKD-VDRIIGLdqvagmsetalpgafKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFV 533
Cdd:cd14888 526 QLSVDAQEVIKNSKNPFISNLFSAyLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFI 590
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 30268331 534 RCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 590
Cdd:cd14888 591 RCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
2-628 |
1.12e-159 |
|
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: 494.31 E-value: 1.12e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSH---KSKKDQGELERQLLQA 78
Cdd:cd14873 45 YSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISGESGAGKTESTKLILKFLSVISQQSlelSLKEKTSCVEQAILES 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 79 NPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL 158
Cdd:cd14873 125 SPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 159 EPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKkerNTDQASMPDNTAAQK 237
Cdd:cd14873 205 STPENYHYLNqSGCVEDKTISDQESFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 238 VSHLLGINVTDFTRgILTPRIKVGR-DYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALdkTKRQGASFIGILD 316
Cdd:cd14873 282 SAELLGLDPTQLTD-ALTQRSMFLRgEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 317 IAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEEC 396
Cdd:cd14873 359 IFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEES 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 397 WFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELW 476
Cdd:cd14873 435 HFPQATDSTLLEKLHSQHANNHFYVKPRVAVN--NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 477 kdvdriiglDQVAGMSETALPGAFKTRKGmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQL 556
Cdd:cd14873 513 ---------EHVSSRNNQDTLKCGSKHRR--PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQL 581
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30268331 557 RCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKqaCVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14873 582 RYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
1-628 |
1.73e-159 |
|
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: 492.95 E-value: 1.73e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVasshkSKKDQGELERQLLQANP 80
Cdd:cd01379 43 LYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGESGAGKTESANLLVQQLTVL-----GKANNRTLEEKILQVNP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 81 ILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSG-AGEHLKTDLLLE 159
Cdd:cd01379 118 LMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 160 PYNKYRFLSNGHVTIPG----QQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFK---KERNTDQASM-PD 231
Cdd:cd01379 198 ENKPPRYLQNDGLTVQDivnnSGNREKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRiSN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 232 NTAAQKVSHLLGINVTDFtRGILTPRIKVGR-DYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL--DKTKRQG 308
Cdd:cd01379 278 PEALNNVAKLLGIEADEL-QEALTSHSVVTRgETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 309 ASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCID-LIEKPAgppG 387
Cdd:cd01379 357 PLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---G 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 388 ILALLDEECWFPKATDKSFVEKVMQEQGTHPkFQKPKqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQS 467
Cdd:cd01379 433 LLALLDEESRFPKATDQTLVEKFHNNIKSKY-YWRPK--SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSS 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 468 SDKFVSElwkdvdriigldqvagmsetalpgafktrkgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKL 547
Cdd:cd01379 510 ENPLVRQ----------------------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 548 DPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL--TPNSIPKGfmdGKQACVLMIKALELDSnlYRIGQSKV 625
Cdd:cd01379 556 DREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLafKWNEEVVA---NRENCRLILERLKLDN--WALGKTKV 630
|
...
gi 30268331 626 FFR 628
Cdd:cd01379 631 FLK 633
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
2-628 |
3.19e-145 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 456.29 E-value: 3.19e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMM----QDREDQSILCTGESGAGKTENTKKVIQYLAYVAsshkskKDQGELERQLLQ 77
Cdd:cd14889 44 YKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVISGESGAGKTESTKLLLRQIMELC------RGNSQLEQQILQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 78 ANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSG-AGEHLKTDL 156
Cdd:cd14889 118 VNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGiSAEDRENYG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 157 LLEPyNKYRFLSNGHvtipGQQD-----KDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKkerntdqasmPD 231
Cdd:cd14889 197 LLDP-GKYRYLNNGA----GCKRevqywKKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFE----------MD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 232 NTAAQKVSH-------------------LLG--INVTDFTRGiltprikvgrDYVQKAQTKEQADFAIEALAKATYERMF 290
Cdd:cd14889 262 DDEALKVENdsngwlkaaagqfgvseedLLKtlTCTVTFTRG----------EQIQRHHTKQQAEDARDSIAKVAYGRVF 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 291 RWLVLRINKALDKTKRQG--ASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDF 368
Cdd:cd14889 332 GWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 369 gLDLQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKadFCIIHYAGKVDYKADEW 448
Cdd:cd14889 412 -KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRSKSPK--FTVNHYAGKVTYNASGF 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 449 LMKNMDPLNDNIATLLHQSSDKFVSELWK-DVDRIIGLDQVAGMSETALPGAFKTRKgmfRTVGQLYKEQLAKLMATLRN 527
Cdd:cd14889 487 LEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLMPRAKLPQAGSDNFNSTRK---QSVGAQFKHSLGVLMEKMFA 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 528 TNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL--TPNsIPKgfmdGKQACV 605
Cdd:cd14889 564 ASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCL 638
|
650 660
....*....|....*....|...
gi 30268331 606 LMIKALELDSnlYRIGQSKVFFR 628
Cdd:cd14889 639 RILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
5-594 |
1.65e-143 |
|
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: 450.53 E-value: 1.65e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 5 KKRHEMPPHIYAITDTAYRSMMQ----DREDQSILCTGESGAGKTENTKKVIQYLAYV-----ASSHKSKKDQGELERQL 75
Cdd:cd14900 59 KGSDPMPPHIYQVAGEAYKAMMLglngVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlAASVSMGKSTSGIAAKV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 76 LQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEhlktd 155
Cdd:cd14900 139 LQTNILLESFGNARTLRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE----- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 156 lllepynkyrflsnghvtipGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTD-QASMPDNTA 234
Cdd:cd14900 214 --------------------AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 235 AQKV------SHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL---DKTK 305
Cdd:cd14900 274 PSSIwsrdaaATLLSVDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 306 RQGAS-FIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAG 384
Cdd:cd14900 354 SHGGLhFIGILDIFGFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QR 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 385 PPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDplndniatLL 464
Cdd:cd14900 431 PTGILSLIDEECVMPKGSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VL 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 465 HQSSdkfvselwkdVDriigldqvagmsetalpgafktrkgMFRTVGQlYKEQLAKLMATLRNTNPNFVRCIIPNHEKKA 544
Cdd:cd14900 503 HQEA----------VD-------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKA 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 30268331 545 GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIP 594
Cdd:cd14900 547 GIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
11-628 |
4.47e-143 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 449.88 E-value: 4.47e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 11 PPHIYAITDTAYRSMMQDRE---DQSILCTGESGAGKTENTKKVIQYL------------AYVASSHKSKKDQG-ELERQ 74
Cdd:cd14891 52 PPHPYAIAEMAYQQMCLGSGrmqNQSIVISGESGAGKTETSKIILRFLttravggkkasgQDIEQSSKKRKLSVtSLDER 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 75 LLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY-IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLK 153
Cdd:cd14891 132 LMDTNPILESFGNAKTLRNHNSSRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 154 TDLLLEPYNKYRFLS-NGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKK----ERNTDQAS 228
Cdd:cd14891 212 KELLLLSPEDFIYLNqSGCVSDDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIAS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 229 MPDNTAAQKVSHLLGINVTDFTRGILTPRIkVGRDYVQKAQ-TKEQADFAIEALAKATYERMFRWLVLRINKALDKtKRQ 307
Cdd:cd14891 292 ESDKEALATAAELLGVDEEALEKVITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPD 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 308 GASFIGILDIAGFEIFDL-NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPP 386
Cdd:cd14891 370 PLPYIGVLDIFGFESFETkNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPN 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 387 GILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQlKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLH 465
Cdd:cd14891 447 GILPLLDNEARNPNPSDAKLNETLHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLA 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 466 qSSDKFVselwkdvdriigldqvagmsetalpgafktrkgmfrtvgqlykEQLAKLMATLRNTNPNFVRCIIPNHEKKAG 545
Cdd:cd14891 526 -SSAKFS-------------------------------------------DQMQELVDTLEATRCNFIRCIKPNAAMKVG 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 546 KLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIK-ALELDSNLYRIGQSK 624
Cdd:cd14891 562 VFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTLTQAILwAFRVPSDAYRLGRTR 641
|
....
gi 30268331 625 VFFR 628
Cdd:cd14891 642 VFFR 645
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
9-591 |
3.14e-142 |
|
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: 448.71 E-value: 3.14e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 9 EMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYL--------------AYVASSHKSKKDQGELERQ 74
Cdd:cd14907 60 KEPPHIYAIAALAFKQLFENNKKQAIVISGESGAGKTENAKYAMKFLtqlsqqeqnseevlTLTSSIRATSKSTKSIEQK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 75 LLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLK 153
Cdd:cd14907 140 ILSCNPILEAFGNAKTVRNDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 154 TDL-LLEPYNKYRFLS---NGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQA-- 227
Cdd:cd14907 220 QQLgLKNQLSGDRYDYlkkSNCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSpc 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 228 SMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL------ 301
Cdd:cd14907 300 CVKNKETLQIIAKLLGIDEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdek 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 302 -DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDL 378
Cdd:cd14907 380 dQQLFQNKYLSIGLLDIFGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDL 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 379 IEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLND 458
Cdd:cd14907 459 LDKP--PIGIFNLLDDSCKLATGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQ 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 459 NIATLLHQSSDKFVSELWKDVDRiigldqvagmSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIP 538
Cdd:cd14907 536 SIINCIQNSKNRIISSIFSGEDG----------SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKP 605
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 30268331 539 NHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 591
Cdd:cd14907 606 NEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
1-628 |
6.24e-136 |
|
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: 431.29 E-value: 6.24e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQgelerQLLQANP 80
Cdd:cd14904 44 QYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVSGESGAGKTETTKIVMNHLASVAGGRKDKTIA-----KVIDVNP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 81 ILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEP 160
Cdd:cd14904 119 LLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 161 YNKYRFL--SNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFkKERNTDQASMPDNTAAQKV 238
Cdd:cd14904 199 NCQYQYLgdSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 239 SHLLGINVTDF-----TRGILT--PRIKVGRDYVQKAQTKeqadfaiEALAKATYERMFRWLVLRINKALDKTKRQGASF 311
Cdd:cd14904 278 AKMLGLPTTRIeealcNRSVVTrnESVTVPLAPVEAEENR-------DALAKAIYSKLFDWMVVKINAAISTDDDRIKGQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 312 IGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpaGPPGILAL 391
Cdd:cd14904 351 IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIAL 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 392 LDEECWFPKATDKSFVEKV---MQEQGTHPKFQKPKQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSS 468
Cdd:cd14904 427 MNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKV--KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSS 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 469 DKFVSELWKDVDriigldqvaGMSETALPGAFKTRKGMfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLD 548
Cdd:cd14904 505 LDLLTELFGSSE---------APSETKEGKSGKGTKAP-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFD 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 549 PHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGfmDGKQACVLMIKALELDSNL-YRIGQSKVFF 627
Cdd:cd14904 575 KRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIGRKSPLeYQIGKSLIYF 652
|
.
gi 30268331 628 R 628
Cdd:cd14904 653 K 653
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
6-611 |
1.79e-132 |
|
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: 424.30 E-value: 1.79e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 6 KRHEMPPHIYAITDTAYRSMMQ-DREDQSILCTGESGAGKTENTKKVIQYLAYV----ASSHKSKKDQGELERQLLQANP 80
Cdd:cd14902 57 QLSELPPHVFAIGGKAFGGLLKpERRNQSILVSGESGSGKTESTKFLMQFLTSVgrdqSSTEQEGSDAVEIGKRILQTNP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 81 ILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEP 160
Cdd:cd14902 137 ILESFGNAQTIRNDNSSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 161 YNKYRFLSNGHVT---IPGQQDKD--MFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKE-RNTDQASMPDNTA 234
Cdd:cd14902 217 GGKYELLNSYGPSfarKRAVADKYaqLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASR 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 235 AQ--KVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALD--------KT 304
Cdd:cd14902 297 FHlaKCAELMGVDVDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSD 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 305 KRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPag 384
Cdd:cd14902 377 EDEELATIGILDIFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDK-- 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 385 PPGILALLDEECWFPKATDKSFVEKVMQEQGThpkfqkpkqlkdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLL 464
Cdd:cd14902 454 SNGLFSLLDQECLMPKGSNQALSTKFYRYHGG------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDIL 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 465 HQSSDKFVSelwkdvdrIIGLDQVAGMSETALPGAFKTRKGMFRT--VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEK 542
Cdd:cd14902 522 SSSSNEVVV--------AIGADENRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVK 593
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30268331 543 KAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL-----TPNSIPK-GFMDGKQA--CVLMIKAL 611
Cdd:cd14902 594 KPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFkcflsTRDRAAKmNNHDLAQAlvTVLMDRVL 670
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
10-628 |
4.31e-130 |
|
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: 417.43 E-value: 4.31e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 10 MPPHIYAITDTAYRSMMQ-------DREDQSILCTGESGAGKTENTKKVIQYLAYVASSHK----SKKDQGELERQLLQA 78
Cdd:cd14895 52 LPPHVFSIAEGAYRSLRRrlhepgaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTatssSKRRRAISGSELLSA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 79 NPILEAFGNAKTVKNDNSSRFGKFIRINF-----DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLK 153
Cdd:cd14895 132 NPILESFGNARTLRNDNSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 154 TDLLLEPYN--KYRFLSNG--HVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTD---- 225
Cdd:cd14895 212 LELQLELLSaqEFQYISGGqcYQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeed 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 226 -----------QASMPDNTAAQK---VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFR 291
Cdd:cd14895 292 ngaasapcrlaSASPSSLTVQQHldiVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQ 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 292 WLVLRINKALDKTK----------RQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGI 361
Cdd:cd14895 372 FLVSKVNSASPQRQfalnpnkaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGI 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 362 EWNFIDFGLDlQPCIDLIEkpAGPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQKPKqlKDKAD--FCIIHYAG 439
Cdd:cd14895 452 KWNAVDYEDN-SVCLEMLE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAG 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 440 KVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETalpgafKTRKGMFRTV--GQLYKEQ 517
Cdd:cd14895 527 AVRYQAEGFCEKNKDQPNAELFSVLGKTSDAHLRELFEFFKASESAELSLGQPKL------RRRSSVLSSVgiGSQFKQQ 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 518 LAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGF 597
Cdd:cd14895 601 LASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDA 680
|
650 660 670
....*....|....*....|....*....|.
gi 30268331 598 MDGKQACVLMIKALELdsnlyriGQSKVFFR 628
Cdd:cd14895 681 TASALIETLKVDHAEL-------GKTRVFLR 704
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
12-628 |
2.32e-126 |
|
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: 406.60 E-value: 2.32e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 12 PHIYAITDTAYRSMMQD-REDQSILCTGESGAGKTENTKKVIQYLAYVASSHK-SKKDQGELER-----QLLQANPILEA 84
Cdd:cd14908 63 PHVFAIADRSYRQMMSEiRASQSILISGESGAGKTESTKIVMLYLTTLGNGEEgAPNEGEELGKlsimdRVLQSNPILEA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 85 FGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGE--------HLKTDL 156
Cdd:cd14908 143 FGNARTLRNDNSSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 157 LLEPYNKYRFLSNGHVTIPGQ-QDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTAA 235
Cdd:cd14908 223 GLQLPNEFHYTGQGGAPDLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGN 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 236 QK----VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGA-S 310
Cdd:cd14908 302 EKclarVAKLLGVDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrS 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 311 FIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPagPPGILA 390
Cdd:cd14908 382 SVGVLDIFGFECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQAK--KKGILT 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 391 LLDEECWFP-KATDKSFVEKVM--------QEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLM-KNMDPLNdni 460
Cdd:cd14908 459 MLDDECRLGiRGSDANYASRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP--- 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 461 atllhqssdkfvselwkdvdriigldqvagmsetalpgafKTRKGMFRTvGQLYKEQLAKLMATLRNTNPNFVRCIIPNH 540
Cdd:cd14908 536 ----------------------------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPND 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 541 EKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnSIPK----GFMDGKQACVLMIKALELDSN 616
Cdd:cd14908 575 AAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlsWSMERLDPQKLCVKKMCKDLV 653
|
650 660
....*....|....*....|....*....
gi 30268331 617 LYR-----------------IGQSKVFFR 628
Cdd:cd14908 654 KGVlspamvsmknipedtmqLGKSKVFMR 682
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
9-671 |
2.50e-126 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 410.96 E-value: 2.50e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 9 EMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQgeleRQLLQANPILEAFGNA 88
Cdd:PTZ00014 161 KLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQ----NAIMAANPVLEAFGNA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 89 KTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS 168
Cdd:PTZ00014 237 KTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYIN 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 169 NGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVF--KKERNTDQASM--PDNTAA-QKVSHLLG 243
Cdd:PTZ00014 317 PKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESLEVfNEACELLF 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 244 INVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsFIGILDIAGFEIF 323
Cdd:PTZ00014 397 LDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVF 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 324 DLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLI-EKPAgppGILALLDEECWFPKAT 402
Cdd:PTZ00014 476 KNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLcGKGK---SVLSILEDQCLAPGGT 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 403 DKSFVEKVMQEQGTHPKFQKPKQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRI 482
Cdd:PTZ00014 552 DEKFVSSCNTNLKNNPKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVE 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 483 IGldqvagmsetalpgafKTRKGMFrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVL 562
Cdd:PTZ00014 631 KG----------------KLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSIL 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 563 EGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR---AGVLAHLEEER 639
Cdd:PTZ00014 693 EALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREK 772
|
650 660 670
....*....|....*....|....*....|..
gi 30268331 640 DLKITDVIIGFQACCRGYLARKAFAKRQQQLT 671
Cdd:PTZ00014 773 LAAWEPLVSVLEALILKIKKKRKVRKNIKSLV 804
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
2-628 |
3.90e-125 |
|
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: 402.24 E-value: 3.90e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLayvaSSHKSKKDQGELeRQLLQANPI 81
Cdd:cd14896 44 YHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSGHSGSGKTEAAKKIVQFL----SSLYQDQTEDRL-RQPEDVLPI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 82 LEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPY 161
Cdd:cd14896 119 LESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 162 NKYRFLSNGHV-TIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQ--ASMPDNTAAQKV 238
Cdd:cd14896 198 ETYYYLNQGGAcRLQGKEDAQDFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 239 SHLLGINvTDFTRGILTPRIKV-GRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGA-SFIGILD 316
Cdd:cd14896 278 ARLLQVP-PERLEGAVTHRVTEtPYGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVD 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 317 IAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDfGLDLQPCIDLIEkpAGPPGILALLDEEC 396
Cdd:cd14896 357 AYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQT 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 397 WFPKATDKSFVEKVMQEQGTHPKFQKPKQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELW 476
Cdd:cd14896 434 WLSQATDHTFLQKCHYHHGDHPSYAKPQL--PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLF 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 477 KDVDRIIGLDQVAGmsetalpgafktrkgmfrTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQL 556
Cdd:cd14896 512 QEAEPQYGLGQGKP------------------TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQL 573
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30268331 557 RCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPkGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14896 574 RQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQE-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
9-626 |
1.10e-117 |
|
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: 382.03 E-value: 1.10e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 9 EMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQgeleRQLLQANPILEAFGNA 88
Cdd:cd14876 52 KLPPHVFYTARRALENLHGVNKSQTIIVSGESGAGKTEATKQIMRYFASAKSGNMDLRIQ----TAIMAANPVLEAFGNA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 89 KTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLs 168
Cdd:cd14876 128 KTIRNNNSSRFGRFMQLDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFL- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 169 NGHVT-IPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKErntDQASMPDntAA----------QK 237
Cdd:cd14876 207 NPKCLdVPGIDDVADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 238 VSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsFIGILDI 317
Cdd:cd14876 282 ACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDI 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 318 AGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGILALLDEECW 397
Cdd:cd14876 361 FGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 398 FPKATDKSFVEKVMQEQGTHPKFqKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWK 477
Cdd:cd14876 438 APGGSDEKFVSACVSKLKSNGKF-KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFE 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 478 DVDRIIGldqvagmsetalpgafKTRKGMFrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLR 557
Cdd:cd14876 517 GVVVEKG----------------KIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLH 578
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30268331 558 CNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVF 626
Cdd:cd14876 579 ALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
12-626 |
1.94e-116 |
|
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: 379.19 E-value: 1.94e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 12 PHIYAITDTAYRSMMQDRE--DQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGELER---QLLQANPILEAFG 86
Cdd:cd14880 56 PHIFTVGEQTYRNVKSLIEpvNQSIVVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERieqRILNSNPVMEAFG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 87 NAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRF 166
Cdd:cd14880 136 NACTLRNNNSSRFGKFIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSW 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 167 LSNGHVTIpgqqDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVS---HLLG 243
Cdd:cd14880 216 LPNPERNL----EEDCFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVRtsaLLLK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 244 INVTDFTRGILTPRIKVGRDYV--QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFE 321
Cdd:cd14880 292 LPEDHLLETLQIRTIRAGKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 322 IFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLDEECWFPKA 401
Cdd:cd14880 372 SFPENSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRP 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 402 TDKSFVEKVMQEQGTHPKFQKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDR 481
Cdd:cd14880 449 SSAAQLQTRIESALAGNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPE 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 482 IIGLDQVAGMSETALpgafktrkgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGV 561
Cdd:cd14880 529 EKTQEEPSGQSRAPV-----------LTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGL 597
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30268331 562 LEGIRICRQGFPNRVVFQEFRQRYEILTPN--SIPKGFMDGKQAcvlmikalELDSNLYRIGQSKVF 626
Cdd:cd14880 598 VETIHISAAGFPIRVSHQNFVERYKLLRRLrpHTSSGPHSPYPA--------KGLSEPVHCGRTKVF 656
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
9-624 |
3.21e-113 |
|
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: 372.00 E-value: 3.21e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 9 EMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKK-----DQGELERQLLQANPILE 83
Cdd:cd14906 53 SPIPHIYAVALRAYQSMVSEKKNQSIIISGESGSGKTEASKTILQYLINTSSSNQQQNnnnnnNNNSIEKDILTSNPILE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 84 AFGNAKTVKNDNSSRFGKFIRINFD-VNGYIVGANIETYLLEKSR-AIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEP- 160
Cdd:cd14906 133 AFGNSRTTKNHNSSRFGKFLKIEFRsSDGKIDGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNd 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 161 YNKYRFL--------------SNGHVTIPGQQDKD-MFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTD 225
Cdd:cd14906 213 PSKYRYLdarddvissfksqsSNKNSNHNNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 226 QAS--MPDNTAA-QKVSHLLGINVTDFTRGILTPRIKV-GRDYV-----QKAQTKEQADfaieALAKATYERMFRWLVLR 296
Cdd:cd14906 293 KYAyqKDKVTASlESVSKLLGYIESVFKQALLNRNLKAgGRGSVycrpmEVAQSEQTRD----ALSKSLYVRLFKYIVEK 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 297 INKALDKTKRQ----GAS------FIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI 366
Cdd:cd14906 369 INRKFNQNTQSndlaGGSnkknnlFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNS 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 367 DFgLDLQPCIDLIEKPAGppGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQkpKQLKDKADFCIIHYAGKVDYKAD 446
Cdd:cd14906 449 NF-IDNKECIELIEKKSD--GILSLLDDECIMPKGSEQSLLEKYNKQYHNTNQYY--QRTLAKGTLGIKHFAGDVTYQTD 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 447 EWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriigldqvagMSETALPGAFKTRKGMFRTVGQlYKEQLAKLMATLR 526
Cdd:cd14906 524 GWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ-------------QQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTIN 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 527 NTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVL 606
Cdd:cd14906 590 STSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQL 669
|
650
....*....|....*...
gi 30268331 607 MIKALELDSNLYRIGQSK 624
Cdd:cd14906 670 ILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
1-628 |
1.38e-111 |
|
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: 366.63 E-value: 1.38e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKkdqgeLERQLLQA-N 79
Cdd:cd01386 43 MFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRSGSGKTTNCRHILEYLVTAAGSVGGV-----LSVEKLNAaL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 80 PILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE 159
Cdd:cd01386 118 TVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLN 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 160 PYNKyrflSNGHVTIPGQQDKDM------FQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNT 233
Cdd:cd01386 198 QLAE----SNSFGIVPLQKPEDKqkaaaaFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 234 AAQKVSHLLGINVTDFTRGI------------LTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL 301
Cdd:cd01386 274 WAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 302 dKTKRQGASFIGILDIAGFEifdlN----------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLD 371
Cdd:cd01386 354 -SSSHHSTSSITIVDTPGFQ----NpahsgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELS 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 372 LQPCIDLIEKPAG------------PPGILALLDEECWFPKATDKSFVEKVMQEQG--THPKFQKPKQLKDKA-DFCIIH 436
Cdd:cd01386 429 PGALVALIDQAPQqalvrsdlrdedRRGLLWLLDEEALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGH 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 437 YAGK--VDYKADEWLMK-NMDPLNDNIATLLHQSSDKFvselwkdvdriigldqvagmsetalpgAFKTRKGMFRTVgql 513
Cdd:cd01386 509 LLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQKET---------------------------AAVKRKSPCLQI--- 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 514 yKEQLAKLMATLRNTNPNFVRCIIPNHE------KKAGKLDPHLVLD------QLRCNGVLEGIRICRQGFPNRVVFQEF 581
Cdd:cd01386 559 -KFQVDALIDTLRRTGLHFVHCLLPQHNagkderSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEF 637
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 30268331 582 RQRYEILTPNSIPKGF-----MDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd01386 638 RRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
8-628 |
2.75e-110 |
|
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: 362.59 E-value: 2.75e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 8 HEMPPHIYAITDTAYRSM-MQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERQ----LLQANPIL 82
Cdd:cd14875 52 RLLPPHIWQVAHKAFNAIfVQGLGNQSVVISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQRSIADKidenLKWSNPVM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 83 EAFGNAKTVKNDNSSRFGKFIRINFD-VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDL-LLEP 160
Cdd:cd14875 132 ESFGNARTVRNDNSSRFGKYIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKT 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 161 YNKYRFLSNGHVTI----PGQ--QDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNtDQASMPDNTA 234
Cdd:cd14875 212 AQDYKCLNGGNTFVrrgvDGKtlDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 235 AQKVSHLLGINVTDFTRGILtprIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALD-KTKRQGASFIG 313
Cdd:cd14875 291 FLTACRLLQLDPAKLRECFL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 314 ILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEkpAGPPGILALLD 393
Cdd:cd14875 368 LLDIFGFENFTRNSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLD 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 394 EECWFPKATDKSFVEKVMQE-QGTHPKFQKPKQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFV 472
Cdd:cd14875 445 EECNFKGGTTERFTTNLWDQwANKSPYFVLPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFI 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 473 SELwkdvdriigLDQVAGMSEtalpgafktRKgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLV 552
Cdd:cd14875 524 RTL---------LSTEKGLAR---------RK---QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLV 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 553 LDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGK--QACVLMI----KALELDSNLYRIGQSKVF 626
Cdd:cd14875 583 GSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLayyqRLYGWAKPNYAVGKTKVF 662
|
..
gi 30268331 627 FR 628
Cdd:cd14875 663 LR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
9-628 |
8.16e-104 |
|
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: 344.18 E-value: 8.16e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 9 EMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKkdqgeLERQLLQANPILEAFGNA 88
Cdd:cd14886 57 DLPPHSYAVAQSALNGLISDGISQSCIVSGESGAGKTETAKQLMNFFAYGHSTSSTD-----VQSLILGSNPLLESFGNA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 89 KTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS 168
Cdd:cd14886 132 KTLRNNNSSRFGKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 169 NGHV-TIPGQQDKDMFQETMEAMRIMgIPEEEQMGLLRVISGVLQLGNIVFKKERN--TDQASMPDNTAA-QKVSHLLGI 244
Cdd:cd14886 212 ASKCyDAPGIDDQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 245 NVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALdKTKRQGASFIGILDIAGFEIFD 324
Cdd:cd14886 291 ESSKAAQAIITKVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 325 LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIEKPAgpPGILALLDEECWFPKATDK 404
Cdd:cd14886 370 RNTYEQLLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPN--LSIFSFLEEQCLIQTGSSE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 405 SFVE---KVMQEQGTHPKfqKPKQLKdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDR 481
Cdd:cd14886 447 KFTSsckSKIKNNSFIPG--KGSQCN----FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPN 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 482 IIGLdqvagmsetalpgafktRKGMFrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGV 561
Cdd:cd14886 521 EDGN-----------------MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSI 581
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30268331 562 LEGIRICRQGFPNRVVFQEFRQRYEILT--PNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14886 582 FESIQTIHRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
12-585 |
2.29e-102 |
|
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: 342.46 E-value: 2.29e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 12 PHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLA------------YVASSHKSKKDQGELERQLLQAN 79
Cdd:cd14899 65 PHLFAVARAAYIDIVQNGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnnnltnSESISPPASPSRTTIEEQVLQSN 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 80 PILEAFGNAKTVKNDNSSRFGKFIRINF-DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSG-----AGEHLK 153
Cdd:cd14899 145 PILEAFGNARTVRNDNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQ 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 154 TDLLLEPYNKYRFLSNGHVTI--PGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVF-----KKERNT-- 224
Cdd:cd14899 225 VLALSGGPQSFRLLNQSLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfa 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 225 DQASMPDNTAA-----QKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINK 299
Cdd:cd14899 305 DEARVMSSTTGafdhfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNN 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 300 AL--------------DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNF 365
Cdd:cd14899 385 KLqrqasapwgadesdVDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSF 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 366 IDFGlDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKV---MQEQGTHPKFQKPKQLKDKADFCIIHYAGKVD 442
Cdd:cd14899 465 VDFP-NNRACLELFEHR--PIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVT 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 443 YKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiiglDQVAGMSETALPGAFKTRKGMFRT----VGQLYKEQL 518
Cdd:cd14899 542 YTIDGFLAKNKDSFCESAAQLLAGSSNPLIQALAAGSND----EDANGDSELDGFGGRTRRRAKSAIaavsVGTQFKIQL 617
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30268331 519 AKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 585
Cdd:cd14899 618 NELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
2-628 |
4.66e-95 |
|
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: 319.65 E-value: 4.66e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYlaYVASShkskKDQGELERQLLQANPI 81
Cdd:cd14937 40 YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGESGSGKTEASKLVIKY--YLSGV----KEDNEISNTLWDSNFI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 82 LEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPY 161
Cdd:cd14937 114 LEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 162 NKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQmGLLRVISGVLQLGNIVFK---KERNTDQASMPDNT--AAQ 236
Cdd:cd14937 194 NEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNMHDMKD-DLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVN 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 237 KVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKrQGASFIGILD 316
Cdd:cd14937 273 EISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 317 IAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIEkpaGPPGILALLDEEC 396
Cdd:cd14937 352 IFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLR---GKTSIISILEDSC 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 397 WFPKATDKSFVEKVMQEQGTHPKFQKPKQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELW 476
Cdd:cd14937 428 LGPVKNDESIVSVYTNKFSKHEKYASTKKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLY 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 477 KDVDriigldqvagMSETAlpgafkTRKGMfrtVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQL 556
Cdd:cd14937 507 EDVE----------VSESL------GRKNL---ITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQL 567
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30268331 557 RCNGVLEGIRIcRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQAcVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14937 568 FSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEK-VSMILQNTVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
12-628 |
3.77e-94 |
|
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: 319.67 E-value: 3.77e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 12 PHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGeLERQLLQANPILEAFGNAKTV 91
Cdd:cd14887 62 PHPFGLAEFAYCRLVRDRRSQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG-LEARLLQSGPVLEAFGNAHTV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 92 KNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLlepynkyrflsngh 171
Cdd:cd14887 141 LNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSS-------------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 172 vtiPGQQDKDMF--QETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTA--------AQKVSHL 241
Cdd:cd14887 207 ---AGEGDPESTdlRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 242 L-------GINVTDFTRGILT--------PRIKVGRDYV------------QKAQTKEQADFAIEALAKATYERMFRWLV 294
Cdd:cd14887 284 SevkclssGLKVTEASRKHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 295 LRINKALDKTKR-------------QGASFIGILDIAGFEIF---DLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQR 358
Cdd:cd14887 364 ARINAGLQRSAKpsesdsdedtpstTGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQ 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 359 EGIEWNFI--DFGLDLQPCIDLIEKPA---------------------GPPGILALLDE------ECWFPKATDKSFVEK 409
Cdd:cd14887 444 EGVFQNQDcsAFPFSFPLASTLTSSPSstspfsptpsfrsssafatspSLPSSLSSLSSslssspPVWEGRDNSDLFYEK 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 410 VMQEQGTHPKFQK--PKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLhQSSDKFVSElwkdvdriIGLDQ 487
Cdd:cd14887 524 LNKNIINSAKYKNitPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTRL--------VGSKK 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 488 VAGMSetalpgAFKTRKgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRI 567
Cdd:cd14887 595 NSGVR------AISSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRV 665
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30268331 568 CRQGFPNRVVFQEFRQRYEILTPNSIpKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 628
Cdd:cd14887 666 MADGFPCRLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
12-590 |
1.03e-91 |
|
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: 308.36 E-value: 1.03e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 12 PHIYAITDTAYRSMMQdREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSkkdqgeLERQLLQANPILEAFGNAKTV 91
Cdd:cd14898 51 PHVYDVAEASVQDLLV-HGNQTIVISGESGSGKTENAKLVIKYLVERTASTTS------IEKLITAANLILEAFGNAKTQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 92 KNDNSSRFGKFIRINFDvnGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDlllepYNKYRF-LSNG 170
Cdd:cd14898 124 LNDNSSRFGKRIKLKFD--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSStAGNK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 171 HVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLlrvisGVLQLGNIVFKKERNTDQASmpdNTAAQKVSHLLGINVTDFT 250
Cdd:cd14898 197 ESIVQLSEKYKMTCSAMKSLGIANFKSIEDCLL-----GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 251 RGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTkrqGASFIGILDIAGFEIFDLNSFEQ 330
Cdd:cd14898 269 ESLVKFSIQVKGETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 331 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKv 410
Cdd:cd14898 346 LCINWTNEKIQNDFIKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVK- 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 411 MQEQGTHpkfqkpkQLKDKADFCII--HYAGKVDYKADEWLMKNMDplndniatllhqssdkfvselwKDVDRIIGLDQV 488
Cdd:cd14898 421 IKKYLNG-------FINTKARDKIKvsHYAGDVEYDLRDFLDKNRE----------------------KGQLLIFKNLLI 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 489 AgmsetalpgafktRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRIC 568
Cdd:cd14898 472 N-------------DEGSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLS 538
|
570 580
....*....|....*....|..
gi 30268331 569 RQGFPNRVVFQEFRQRYEILTP 590
Cdd:cd14898 539 KQCFPQEIPKDRFEERYRILGI 560
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
11-627 |
2.15e-88 |
|
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: 301.01 E-value: 2.15e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 11 PPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVI-QYLAYVASSHKSKKdqgeLERQLLQANPILEAFGNAK 89
Cdd:cd14879 64 PPHAYDLAARAYLRMRRRSEDQAVVFLGETGSGKSESRRLLLrQLLRLSSHSKKGTK----LSSQISAAEFVLDSFGNAK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 90 TVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFL-- 167
Cdd:cd14879 140 TLTNPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLas 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 168 SNGHVT--IPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVF--KKERNTDQASMpDNTAA-QKVSHLL 242
Cdd:cd14879 220 YGCHPLplGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVAAFL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 243 GINVTDFtRGILTPRIK-VGRD----YVQKAQTKEQADfaieALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDI 317
Cdd:cd14879 299 GVSPEDL-ETSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDF 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 318 AGFEIFD---LNSFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIEKPAGppGIL 389
Cdd:cd14879 374 PGFQNRSstgGNSLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGKPG--GLL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 390 ALLDEEC-WFPKATDKSFVEKVMQEQGTHPKF---QKPKQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLndniatllh 465
Cdd:cd14879 446 GILDDQTrRMPKKTDEQMLEALRKRFGNHSSFiavGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVL--------- 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 466 qSSDkFVSelwkdvdriigldqvagmsetalpgafktrkgMFRTVGQLyKEQLAKLMATLRNTNPNFVRCIIPNHEKKAG 545
Cdd:cd14879 517 -SPD-FVN--------------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 546 KLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnsipkgFMDGKQACVLMIKALELDSNLYRIGQSKV 625
Cdd:cd14879 562 SFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKV 635
|
..
gi 30268331 626 FF 627
Cdd:cd14879 636 FL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
4-628 |
3.27e-82 |
|
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: 284.02 E-value: 3.27e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 4 GKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKkdqgeLERQLLQANPILE 83
Cdd:cd14878 49 GQLCSSLPPHLFSCAERAFHQLFQERRPQCFILSGERGSGKTEASKQIMKHLTCRASSSRTT-----FDSRFKHVNCILE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 84 AFGNAKTVKNDNSSRFGKFIRINF-DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYN 162
Cdd:cd14878 124 AFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLC 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 163 KYRFLSNGH----VTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKV 238
Cdd:cd14878 204 AHRYLNQTMredvSTAERSLNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 239 SHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL---DKTKRQGASFIGIL 315
Cdd:cd14878 284 AGMLQVSTDELASALTTDIQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGIL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 316 DIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCID-LIEKPAgppGILALLDE 394
Cdd:cd14878 364 DIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPS---GFLSLLDE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 395 ECWFPKATDKSFVEKV---MQEQGTHPKFQKPKQ------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLL 464
Cdd:cd14878 441 ESQMIWSVEPNLPKKLqslLESSNTNAVYSPMKDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVM 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 465 HQSSDKFVSELwkdvdriigldqvagmsetalpgaFKTRkgmFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKA 544
Cdd:cd14878 521 KTSENVVINHL------------------------FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLP 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 545 GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSI-PKGFMDGKQACVLMIKALELDSnlYRIGQS 623
Cdd:cd14878 574 DTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVR 651
|
....*
gi 30268331 624 KVFFR 628
Cdd:cd14878 652 KVFLK 656
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
32-614 |
3.47e-80 |
|
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: 277.38 E-value: 3.47e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 32 QSILCTGESGAGKTENTKKVIQYLAYVASshkskkdqGELE----RQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 107
Cdd:cd14881 69 QAIILSGTSGSGKTYASMLLLRQLFDVAG--------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 108 dVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYN--KYRFLSNGHVTIPGQQDKDMFQE 185
Cdd:cd14881 141 -TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAARFQA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 186 TMEAMRIMGIPeeeQMGLLRVISGVLQLGNIVFKkERNTDQASMPDNTAAQKVSHLLGINVTDFTRGiLTPRIK-VGRDY 264
Cdd:cd14881 220 WKACLGILGIP---FLDVVRVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRG-LTTRTHnARGQL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 265 VQKAQTKEQADFAIEALAKATYERMFRWLVLRINKaldkTKRQGAS--------FIGILDIAGFEIFDLNSFEQLCINYT 336
Cdd:cd14881 295 VKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCINLC 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 337 NEKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIEkpAGPPGILALLDEECwFPKATDKSFVEKVMQEQG 415
Cdd:cd14881 371 AETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHR 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 416 THPKFQKPKQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFvselwkdvdriigldqvagmseta 495
Cdd:cd14881 447 QNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF------------------------ 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 496 lpgAFKTRKGMFRTvgqlykeQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNR 575
Cdd:cd14881 502 ---GFATHTQDFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHR 571
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 30268331 576 VVFQEFRQRYEILTPNSIPKGFMDGKQAC--VLMIKALELD 614
Cdd:cd14881 572 MRFKAFNARYRLLAPFRLLRRVEEKALEDcaLILQFLEAQP 612
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
10-580 |
1.77e-73 |
|
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: 259.45 E-value: 1.77e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 10 MPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVasshKSKKDQGELERQLLQANPILEAFGNAK 89
Cdd:cd14884 60 PKAHIYDIANMAYKNMRGKLKRQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMTERIDKLIYINNILESMSNAT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 90 TVKNDNSSRFGKFIRINFD---------VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSG-AGEHLKTDLLLE 159
Cdd:cd14884 136 TIKNNNSSRCGRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 160 PYNKYRFLSN----------GHVTIPG----------QQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFK 219
Cdd:cd14884 216 NCGVYGLLNPdeshqkrsvkGTLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 220 kerntdqasmpdntaaqKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINK 299
Cdd:cd14884 296 -----------------AAAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINR 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 300 ALDKTKRQGA-----------SFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDF 368
Cdd:cd14884 359 NVLKCKEKDEsdnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVA 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 369 GlDLQPCIDLIEKpagppgILALLDE-----ECWFPKATDKSFV-----EKVMQEQGTH------PKFQK---PKQLKDK 429
Cdd:cd14884 439 P-SYSDTLIFIAK------IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVsygfvlNHDADgtaKKQNIKK 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 430 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSElwkdvdriigldqvagmsetalpGAFKTRKGMFRT 509
Cdd:cd14884 512 NIFFIRHYAGLVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLS 568
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30268331 510 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQE 580
Cdd:cd14884 569 VSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
13-593 |
2.54e-62 |
|
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: 225.52 E-value: 2.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 13 HIYAITDTAYRSMMQDRED-QSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKDQGELERqllqanpILEAFGNAKTV 91
Cdd:cd14874 45 HISGVAENALDRIKSMSSNaESIVFGGESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAIES-------VFKSFGCAKTL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 92 KNDNSSRFGKFIRINFDVNgYIVGANIE-TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNG 170
Cdd:cd14874 118 KNDEATRFGCSIDLLYKRN-VLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 171 HVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTD---QASMPDNTAAQK-VSHLLGINV 246
Cdd:cd14874 197 NSTENIQSDVNHFKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKwVAFLLEVDF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 247 TDFTRgILTPRIKVGrdyvqKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGAsfIGILDIAGFEIFDLN 326
Cdd:cd14874 277 DQLVN-FLLPKSEDG-----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNN 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 327 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNF-IDFGLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKS 405
Cdd:cd14874 349 GVEEFLINSVNERIENLFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLFKK--PYGLLPLLTDECKFPKGSHES 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 406 FVEKVMQEQGTHPKFQKPKQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigl 485
Cdd:cd14874 427 YLEHCNLNHTDRSSYGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY------ 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 486 dqvagmsetalpgAFKTRKgMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGI 565
Cdd:cd14874 500 -------------SSNTSD-MIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELL 565
|
570 580
....*....|....*....|....*...
gi 30268331 566 RICRQGFPNRVVFQEFRQRYEILTPNSI 593
Cdd:cd14874 566 SFRIKGYPVKISKTTFARQYRCLLPGDI 593
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
2-628 |
6.04e-62 |
|
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: 224.62 E-value: 6.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 2 YKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVAsshksKKDQGELERqLLQANPI 81
Cdd:cd14882 44 YRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGESYSGKTTNARLLIKHLCYLG-----DGNRGATGR-VESSIKA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 82 LEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSG--AGEHLKtDLLLE 159
Cdd:cd14882 118 ILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 160 PYNKYRFLSNGHVTIPG---------QQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKerNTDQASMP 230
Cdd:cd14882 197 AGRNYRYLRIPPEVPPSklkyrrddpEGNVERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 231 DNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKrqgAS 310
Cdd:cd14882 275 NTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 311 F-----IGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQpciDLIEKP 382
Cdd:cd14882 352 FgdkysISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVD---QLMTKP 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 383 AgppGILALLDEECwfPKATDKSFV-EKVMQEQGTHPKfqkpkqLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIA 461
Cdd:cd14882 429 D---GLFYIIDDAS--RSCQDQNYImDRIKEKHSQFVK------KHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMI 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 462 TLLHQSSDKFVSELWKDvdriiglDQVAGMsetalpgafKTRKGMFRTVGQlykEQLAKLMATLRNTNPNFVRCIIPNHE 541
Cdd:cd14882 498 ETMRSSLDESVKLMFTN-------SQVRNM---------RTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 542 KKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDgKQACVLMIKALELDSnlYRIG 621
Cdd:cd14882 559 YKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIG 635
|
....*..
gi 30268331 622 QSKVFFR 628
Cdd:cd14882 636 KTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
1-586 |
2.66e-61 |
|
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: 224.85 E-value: 2.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASS----HKSKKDQGELE---R 73
Cdd:cd14893 53 LYEKDTVNDAPPHVFALAQNALRCMQDAGEDQAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHpigQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 74 QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAgEH-- 151
Cdd:cd14893 133 QILHAFTILEAFGNAATRQNRNSSRFAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdp 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 152 -LKTDLLL-EPYNKYRFLSN-----GHVTIPGQQDKDMfqetMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVF------ 218
Cdd:cd14893 212 tLRDSLEMnKCVNEFVMLKQadplaTNFALDARDYRDL----MSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeg 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 219 -KKERNTDQASMPDNTA------AQ--KVSHLLGIN--VTD---FTRGILTpriKVGRDYVQ--KAQTKEQADFAIEALA 282
Cdd:cd14893 288 gKSVGGANSTTVSDAQScalkdpAQilLAAKLLEVEpvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 283 KATYERMFRWLVLRINKAL----DKTKR-------QGasfIGILDIAGFEIFD--LNSFEQLCINYTNEKLQQLF-NHTM 348
Cdd:cd14893 365 RSLYESLFNFLVETLNGILggifDRYEKsnivinsQG---VHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 349 FI----LEQEEYQREG--IEWNFIDFGLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVMQEQGTHPKFQK 422
Cdd:cd14893 442 AInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSR 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 423 PKQLKDKAD------------FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKfvselwkdVDRIIGLDQVA- 489
Cdd:cd14893 520 PNMGADTTNeylapskdwrllFIVQHHCGKVTYNGKGLSSKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAa 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 490 -----GMSETALPGAF--KTRKGMFR----------TVGQLYKEQLAKLMAtLRNTNPNFVRCIIPNHEKKAGKLDPHLV 552
Cdd:cd14893 592 assekAAKQTEERGSTssKFRKSASSaresknitdsAATDVYNQADALLHA-LNHTGKNFLVCIKPNETLEEGVFDSAYV 670
|
650 660 670
....*....|....*....|....*....|....
gi 30268331 553 LDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 586
Cdd:cd14893 671 MKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
6-581 |
5.55e-61 |
|
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: 222.66 E-value: 5.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 6 KRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASShKSKKdqgeLERQLLQANPILEAF 85
Cdd:cd14905 47 QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSGKSENTKIIIQYLLTTDLS-RSKY----LRDYILESGIILESF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 86 GNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYR 165
Cdd:cd14905 122 GHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYH 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 166 FLSN-GHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNtdQASMPDNTAAQKVSHLLGI 244
Cdd:cd14905 202 YLNQgGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 245 NVTDFTRGILTPRIKVGRDYVQKAqtkeqadfaiEALAKATYERMFRWLVLRINKALDKTkrQGASFIGILDIAGFEIFD 324
Cdd:cd14905 280 DSTKLENILISDRSMPVNEAVENR----------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQ 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 325 LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEW-NFIDFGlDLQPCIDLIEKpagppgILALLDEECWFPKATD 403
Cdd:cd14905 348 LNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 404 KSFVEKVMQEQGTHPKF-QKPKQlkdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFV---SELWKDV 479
Cdd:cd14905 421 QIFLEKLQNFLSRHHLFgKKPNK------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLfsrDGVFNIN 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 480 DRIIGLDQVAGMSETALPGAFKTRKGMFR------------------------------TVGQLYKeQLAKLMATLRNTN 529
Cdd:cd14905 495 ATVAELNQMFDAKNTAKKSPLSIVKVLLScgsnnpnnvnnpnnnsgggggggnsgggsgSGGSTYT-TYSSTNKAINNSN 573
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 30268331 530 PN--FVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFP----NRVVFQEF 581
Cdd:cd14905 574 CDfhFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
705-1301 |
8.98e-56 |
|
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: 212.34 E-value: 8.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 705 SRQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDL 784
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 785 EARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKK 864
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 865 QKKFDQLLAEEktisakyagerdraeaearEKETKALSLARALEEAMEQKAElERLNKQfrtemedlmsskddvGKSVHE 944
Cdd:pfam01576 161 ISEFTSNLAEE-------------------EEKAKSLSKLKNKHEAMISDLE-ERLKKE---------------EKGRQE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 945 LEKSKRALE-------QQVEEMKTQLEELEGELQATEDaklrlevNLQAMKAQFErDLQGRDEQSEEKKKQLVRQVREME 1017
Cdd:pfam01576 206 LEKAKRKLEgestdlqEQIAELQAQIAELRAQLAKKEE-------ELQAALARLE-EETAQKNNALKKIRELEAQISELQ 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1018 AELEDERKQRSMAVAARKKLEMDLK----DLEAHIDSANKNRDEAIKQLRKLqAQMKDCMREldDTRASREEILAQAKEN 1093
Cdd:pfam01576 278 EDLESERAARNKAEKQRRDLGEELEalktELEDTLDTTAAQQELRSKREQEV-TELKKALEE--ETRSHEAQLQEMRQKH 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1094 EKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDR 1173
Cdd:pfam01576 355 TQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEK 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1174 LKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEmEGTVKSKYKASITALEAKIAQLEEQLDNETKERQ 1253
Cdd:pfam01576 435 LSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKR 513
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 30268331 1254 AACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQL 1301
Cdd:pfam01576 514 NVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQL 561
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
15-626 |
3.53e-52 |
|
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: 196.98 E-value: 3.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 15 YAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKS------------------KKDQGELERQLL 76
Cdd:cd14938 58 YHVVHNALKNLNELKRNQSIIISGESGSGKSEIAKNIINFIAYQVKGSRRlptnlndqeednihneenTDYQFNMSEMLK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 77 QANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDL 156
Cdd:cd14938 138 HVNVVMEAFGNAKTVKNNNSSRFSKFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMY 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 157 LLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNI-----VFKKE---------- 221
Cdd:cd14938 217 FLKNIENYSMLNNEKGFEKFSDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkaFRKKSllmgknqcgq 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 222 -----------RNTDQASMPDNTAAQKV-SHLLGINVTDFTRGILTPRIkVGRDYVQKAQTKEQADFAIEALAKATYERM 289
Cdd:cd14938 297 ninyetilselENSEDIGLDENVKNLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEEL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 290 FRWLVLRINKALDKTKR--QGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFID 367
Cdd:cd14938 376 FNWIIYKINEKCTQLQNinINTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNS 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 368 FGLDLQPCIDLIEKPAgpPGILALLDEECWFPKATDKS-FVEKVMQEQGTHPKFQKPKQLK-DKADFCIIHYAGKVDYKA 445
Cdd:cd14938 456 ENIDNEPLYNLLVGPT--EGSLFSLLENVSTKTIFDKSnLHSSIIRKFSRNSKYIKKDDITgNKKTFVITHSCGDIIYNA 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 446 DEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFRTVGQ----LYKEQLAKL 521
Cdd:cd14938 534 ENFVEKNIDILTNRFIDMVKQSENEYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTEL 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 522 MATLRNTNPNFVRCIIPNHEKKA-GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPnsipkgfmDG 600
Cdd:cd14938 614 EKLQETTFCHFIVCMKPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DL 685
|
650 660
....*....|....*....|....*.
gi 30268331 601 KQACVLMIKALELDSNLYRIGQSKVF 626
Cdd:cd14938 686 KEKVEALIKSYQISNYEWMIGNNMIF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
1-112 |
3.80e-50 |
|
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: 174.84 E-value: 3.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1 MYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSHKSKKD----------QGE 70
Cdd:cd01363 22 FYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFNGINKGEtegwvylteiTVT 101
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 30268331 71 LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 112
Cdd:cd01363 102 LEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
44-569 |
1.11e-26 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 118.31 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 44 KTENTKKVIQYLAYVASSHKSKKdqgelERQLLQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVNGY---IVGANI 118
Cdd:cd14894 223 KLEHLEDEEQLRMYFKNPHAAKK-----LSIVLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 119 ETYLLEKSRAIRQA------KEERTFHIFYYLLSGAGEH-----LKTDLLLEPYN--KYRFLSNGHVTIPG--------Q 177
Cdd:cd14894 298 SPFLLEKSRVTSERgresgdQNELNFHILYAMVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwK 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 178 QDKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDN---TAAQKVSHLLGI-NVTDFTRGI 253
Cdd:cd14894 378 KDVERWQQVIDGLDELNVSPDEQKTIFKVLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERML 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 254 LTPRIKV--GRDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKAL-------DKTKRQ---------GASFIGIL 315
Cdd:cd14894 458 MTKSVSLqsTSETFEVTLEKGQVNHVRDTLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIV 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 316 DIAGFEIFDLNSFEQLCINYTNEKLqqlfnhtmfileqeeYQREGiewNFIDFGLDLQPCI-------DLIEKPAGPPGI 388
Cdd:cd14894 538 DVFGFEDLTHNSLDQLCINYLSEKL---------------YAREE---QVIAVAYSSRPHLtardsekDVLFIYEHPLGV 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 389 LALLDEECWFPKAT----------DKSFVEKVMQEQGThpKFQKPKQLKDKAD-----------FCIIHYAGKVDYKADE 447
Cdd:cd14894 600 FASLEELTILHQSEnmnaqqeekrNKLFVRNIYDRNSS--RLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDAND 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 448 WLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiIGLD-----QVAGMSETALPGAfKTRKGMFRTVGQLYKEQLAKLM 522
Cdd:cd14894 678 FVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQ-LGWSpntnrSMLGSAESRLSGT-KSFVGQFRSHVNVLTSQDDKNM 755
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 30268331 523 atlrntnPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICR 569
Cdd:cd14894 756 -------PFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
720-1301 |
4.12e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.40 E-value: 4.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 720 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEichdLEARVEEEEERCQHLQ 799
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE----LELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 800 AEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDdllvdldhqrqsacNLEKKQKKFDQLLAEEKTIS 879
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE--------------ELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 880 AKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEM 959
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 960 KTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQlvRQVREMEAELEDERKQRSMAVAARKKLEM 1039
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA--AARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1040 -------------DLKDLEAHIDSANKNRDEAIkqLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQ 1106
Cdd:COG1196 519 lrglagavavligVEAAYEAALEAALAAALQNI--VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGA 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1107 LQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINT 1186
Cdd:COG1196 597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1187 DLNLERSHAQKNENARQQLERQNKELKVKLQEmegtvkskykasitALEAKIAQLEEQLDNETKERQAACKQVRRTEKKL 1266
Cdd:COG1196 677 AEAELEELAERLAEEELELEEALLAEEEEERE--------------LAEAEEERLEEELEEEALEEQLEAEREELLEELL 742
|
570 580 590
....*....|....*....|....*....|....*
gi 30268331 1267 KDVLLQVDDERRNAEQYKDqADKASTRLKQLKRQL 1301
Cdd:COG1196 743 EEEELLEEEALEELPEPPD-LEELERELERLEREI 776
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1011-1301 |
1.77e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.00 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1011 RQVREMEAELEdeRKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAqmkdcmrELDDTRASREEILAQA 1090
Cdd:COG1196 213 ERYRELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1091 KENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELI 1170
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1171 NDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTvKSKYKASITALEAKIAQLEEQLDNETK 1250
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 30268331 1251 ERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQL 1301
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
720-1247 |
2.23e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.62 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 720 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEEL---RARLTAKKQELEEICHDLEARVEEEEERCQ 796
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 797 HLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEK 876
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 877 TISAKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLmsskddvgKSVHELEKSKRALEQQV 956
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL--------LEEAALLEAALAELLEE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 957 EEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKK 1036
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1037 LEmDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAER 1116
Cdd:COG1196 566 LK-AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1117 AKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQgnTELINDRLKKANLQIDQINTDLNLERSHAQ 1196
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE--LELEEALLAEEEEERELAEAEEERLEEELE 722
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 30268331 1197 KNENARQQLERQNKELKVKLQEMEGTVKSKY-----KASITALEAKIAQLEEQLDN 1247
Cdd:COG1196 723 EEALEEQLEAEREELLEELLEEEELLEEEALeelpePPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
942-1301 |
6.58e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.08 E-value: 6.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 942 VHELEKSKRALEQQVE------EMKTQLEELEGELQATEDAKLRLEvnlqamkaqfERDLQGRDEQSEEKKKQLVRQVRE 1015
Cdd:COG1196 195 LGELERQLEPLERQAEkaeryrELKEELKELEAELLLLKLRELEAE----------LEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1016 MEAELEDERKQrsmavaarkklemdLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEK 1095
Cdd:COG1196 265 LEAELEELRLE--------------LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1096 KLKSMEAEMIQLQEELAAAERAKRQAQQERDELAdeianssgkgalalEEKRRLEARIAQLEEELEEEQgntELINDRLK 1175
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAE--------------EALLEAEAELAEAEEELEELA---EELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1176 KANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTvkskyKASITALEAKIAQLEEQLDNETKERQAA 1255
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE-----EEALEEAAEEEAELEEEEEALLELLAEL 468
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 30268331 1256 CKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQL 1301
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
893-1279 |
8.50e-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: 8.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 893 AREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQA 972
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 973 TEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKkqlvrqvrEMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSAN 1052
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELA--------EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1053 KNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEI 1132
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1133 ANSSGKgaLALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQiDQINTDLNLERSHAQKNENAR----QQLERQ 1208
Cdd:TIGR02168 897 EELSEE--LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ-ERLSEEYSLTLEEAEALENKIeddeEEARRR 973
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30268331 1209 NKELKVKLQEMeGTVkskykaSITALEAkIAQLEEQLDNETKERqaacKQVRRTEKKLKDVLLQVDDERRN 1279
Cdd:TIGR02168 974 LKRLENKIKEL-GPV------NLAAIEE-YEELKERYDFLTAQK----EDLTEAKETLEEAIEEIDREARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
718-1301 |
2.72e-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: 91.27 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 718 LVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAE----ELRARLTAKKQELEEICHDLE---ARVEE 790
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELEsrleELEEQLETLRSKVAQLELQIAslnNEIER 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 791 EEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRqsacnLEKKQKKFDQ 870
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE-----LEEAEQALDA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 871 LLAEEKTISAKYAG-ERDRAEAEAREKETKALSLARA-LEEAMEQKAELERLNKQFRTEMED---------LMSSKDDVG 939
Cdd:TIGR02168 480 AERELAQLQARLDSlERLQENLEGFSEGVKALLKNQSgLSGILGVLSELISVDEGYEAAIEAalggrlqavVVENLNAAK 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 940 KSVHELEKS---KRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQ-------------------- 996
Cdd:TIGR02168 560 KAIAFLKQNelgRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvddldnalelak 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 997 ------------------------GRDEQS-------------EEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEM 1039
Cdd:TIGR02168 640 klrpgyrivtldgdlvrpggvitgGSAKTNssilerrreieelEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK 719
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1040 DLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKR 1119
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1120 QAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNE 1199
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1200 NARQQLERQNKELKVKLQEMEGTVKSKYKAsITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKD---VLLQVDDE 1276
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESK-RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeysLTLEEAEA 958
|
650 660
....*....|....*....|....*
gi 30268331 1277 rrNAEQYKDQADKASTRLKQLKRQL 1301
Cdd:TIGR02168 959 --LENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
741-1301 |
1.02e-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: 89.35 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 741 QLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEE 820
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 821 SARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAGERDRAEAEAREKETKA 900
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 901 LSLARALEEAMEQKAELERLNKQFRTEMEDLMSSK------------DDVGKSVHELEKSKRALEQQVEEMKTQLEELEG 968
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeeaelkelqaelEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 969 ELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQ--------LVRQVREMEAELE---------------DERK 1025
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQsglsgilgVLSELISVDEGYEaaieaalggrlqavvVENL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1026 QRSM-AVAARKK--------LEMD------------------------LKDLEAHIDSANK------------------- 1053
Cdd:TIGR02168 556 NAAKkAIAFLKQnelgrvtfLPLDsikgteiqgndreilkniegflgvAKDLVKFDPKLRKalsyllggvlvvddldnal 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1054 --------------------------------------NRDEAIKQLRKLQAQMKDCMRE----LDDTRASREEILAQAK 1091
Cdd:TIGR02168 636 elakklrpgyrivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKIAElekaLAELRKELEELEEELE 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1092 ENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELIN 1171
Cdd:TIGR02168 716 QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1172 DRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVK------SKYKASITALEAKIAQLEEQL 1245
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelsediESLAAEIEELEELIEELESEL 875
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 30268331 1246 DNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQL 1301
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
720-1300 |
6.82e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.12 E-value: 6.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 720 KVREKQLAAENRLTEMetlqSQLMAEKLQLQEQLQAETELCAEAeelrARLTAKKQELEEICHDLEARVEEEEERCQHLQ 799
Cdd:PTZ00121 1141 KAEEARKAEDAKRVEI----ARKAEDARKAEEARKAEDAKKAEA----ARKAEEVRKAEELRKAEDARKAEAARKAEEER 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 800 AEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEE--KT 877
Cdd:PTZ00121 1213 KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEkkKA 1292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 878 ISAKYAGERDRAEaEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSK---RALEQ 954
Cdd:PTZ00121 1293 DEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEekaEAAEK 1371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 955 QVEEMKTQLEEL-----------EGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSE-----EKKKQLVRQVREMEA 1018
Cdd:PTZ00121 1372 KKEEAKKKADAAkkkaeekkkadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKkadeaKKKAEEAKKADEAKK 1451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1019 ELEDERKQRSM---AVAARKKLEMDLKDLEAH-IDSANKNRDEAIK---QLRKLQAQMK--DCMRELDDTRASREEILAQ 1089
Cdd:PTZ00121 1452 KAEEAKKAEEAkkkAEEAKKADEAKKKAEEAKkADEAKKKAEEAKKkadEAKKAAEAKKkaDEAKKAEEAKKADEAKKAE 1531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1090 AKENEKKLKSME----AEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQG 1165
Cdd:PTZ00121 1532 EAKKADEAKKAEekkkADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1166 NTELINDRLKKANLQidqintdlNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQL 1245
Cdd:PTZ00121 1612 AKKAEEAKIKAEELK--------KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 30268331 1246 DNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQ 1300
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
862-1183 |
9.76e-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: 9.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 862 EKKQKKFDQLLAEEKTISAKYAGERDRAEA----EAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDD 937
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 938 VGKSVHELEKSKRALEQQVEEM--------KTQLEELEGELQATEDAklrlevnlQAMKAQFERDLQGRDEQSEEKKKQL 1009
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERS--------IAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1010 VRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQaqmkdcmRELDDTRASREEILAQ 1089
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR-------EKLEKLKREINELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1090 AKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEeqgntel 1169
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR------- 480
|
330
....*....|....
gi 30268331 1170 INDRLKKANLQIDQ 1183
Cdd:TIGR02169 481 VEKELSKLQRELAE 494
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
721-1284 |
2.95e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 84.35 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 721 VREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHD---LEARVEEEEERCQH 797
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSkrkLEEKIRELEERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 798 LQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSAcNLEKKQKKFDQLLAEEKT 877
Cdd:PRK03918 271 LKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 878 IsakyagERDRAEAEAReketkalslARALEEAMEQKAELERLNKQFRTEmedlmsSKDDVGKSVHELEKSKRALEQQVE 957
Cdd:PRK03918 350 L------EKRLEELEER---------HELYEEAKAKKEELERLKKRLTGL------TPEKLEKELEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 958 EMKTQLEELEGELQATEDAKLRLEvnlqamKAQFERDLQGRdEQSEEKKKQLvrqVREMEAELEDERKQRSMAVAARKKL 1037
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELK------KAKGKCPVCGR-ELTEEHRKEL---LEEYTAELKRIEKELKEIEEKERKL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1038 EMDLKDLEAHIdsankNRDEAIKQLRKLQAQMKDCMRELDDTRAsrEEILAQAKENEK----------KLKSMEAEMIQL 1107
Cdd:PRK03918 479 RKELRELEKVL-----KKESELIKLKELAEQLKELEEKLKKYNL--EELEKKAEEYEKlkekliklkgEIKSLKKELEKL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1108 QE---ELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQI 1184
Cdd:PRK03918 552 EElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1185 NTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKykaSITALEAKIAQLEEQLD------NETKERQAACKQ 1258
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSR---ELAGLRAELEELEKRREeikktlEKLKEELEEREK 708
|
570 580
....*....|....*....|....*.
gi 30268331 1259 VRRTEKKLKDVLLQVDDERRNAEQYK 1284
Cdd:PRK03918 709 AKKELEKLEKALERVEELREKVKKYK 734
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
882-1273 |
3.82e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 84.35 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 882 YAGERDRAEAEAREKEtkalSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKT 961
Cdd:TIGR02169 669 SRSEPAELQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 962 QLEELEGELQATEDAKLRLEVNLQAMKAQFErdlQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDL 1041
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLH---KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1042 KDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQA 1121
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1122 QQERDELADEIanssgkgalaleekRRLEARIAQLEEELEEEQGNTELInDRLKKANLQIDQINTDLNLERSHAQKNENA 1201
Cdd:TIGR02169 902 ERKIEELEAQI--------------EKKRKRLSELKAKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQRVEEE 966
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30268331 1202 RQQLERQNKelkVKLQEMEGTVKskykasitaleaKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQV 1273
Cdd:TIGR02169 967 IRALEPVNM---LAIQEYEEVLK------------RLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
729-1302 |
5.04e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.04 E-value: 5.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 729 ENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARltakkqelEEICHDLEARVEEEEERCQHLQAEKKKMQQN 808
Cdd:PTZ00121 1211 ERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNN--------EEIRKFEEARMAHFARRQAAIKAEEARKADE 1282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 809 IQELEEQLEEEeSARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKqkkfdqllAEEKTISAKYAGERDR 888
Cdd:PTZ00121 1283 LKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK--------AEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 889 AEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKsKRALEQQVEEMKTQLEELEG 968
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKK 1432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 969 ELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRsmAVAARKKLEMDLKDLEAhi 1048
Cdd:PTZ00121 1433 ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK--AEEAKKKADEAKKAAEA-- 1508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1049 dsaNKNRDEAIKQLRKLQAqmkDCMRELDDTRASREeilaqAKENEKKLKsmeAEMIQLQEELAAAERAKRQAQQERDEL 1128
Cdd:PTZ00121 1509 ---KKKADEAKKAEEAKKA---DEAKKAEEAKKADE-----AKKAEEKKK---ADELKKAEELKKAEEKKKAEEAKKAEE 1574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1129 ADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQidqintdlNLERSHAQKNENARQQLERQ 1208
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK--------KAEEEKKKVEQLKKKEAEEK 1646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1209 NKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQAD 1288
Cdd:PTZ00121 1647 KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
570 580
....*....|....*....|.
gi 30268331 1289 KASTRLKQLKRQ-------LE 1302
Cdd:PTZ00121 1727 ENKIKAEEAKKEaeedkkkAE 1747
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
992-1301 |
4.00e-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: 80.88 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 992 ERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKD 1071
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1072 CMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQ-QERDELADEIAnssgkgalalEEKRRLE 1150
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLE----------EEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1151 ARIAQLEEELEEEQGNTELINDrlKKANLQIDQINTDlnlershAQKNENARQQlerqnKELKVKLQEMEGTVKSKykas 1230
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEK--EIQELQEQRIDLK-------EQIKSIEKEI-----ENLNGKKEELEEELEEL---- 873
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30268331 1231 italEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQL 1301
Cdd:TIGR02169 874 ----EAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
685-1268 |
7.38e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.57 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 685 KLRNWQWWRLFTKVKPLLQVSRQEEEMMAKEEE---LVKVREKQLAAENRLTEMETLQSQLmaeKLQLQEQLQAEtELCA 761
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKadeLKKAEEKKKADEAKKAEEKKKADEA---KKKAEEAKKAD-EAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 762 EAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLE 841
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 842 EELDDLLVDLDHQRQSACNlEKKQKKFDQLLAEEKTISAKYAGERDRAEAEAREKEtKALSLARALEEAmeQKAELERLN 921
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK-KAEEAKKKAEEA--KKADEAKKK 1478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 922 KQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEvnlqAMKAQFERDLQGRDEQ 1001
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE----AKKAEEKKKADELKKA 1554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1002 SEEKKKQLVRQVREMEAELEDE----RKQRSMAVAARKKLEMDLKDLEAHI----DSANKNRDEAIK--QLRKLQAQMKd 1071
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKnmalRKAEEAKKAEEARIEEVMKLYEEEKkmkaEEAKKAEEAKIKaeELKKAEEEKK- 1633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1072 cmrELDDTRASREEilaQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEianssGKGALALEEKRRLEA 1151
Cdd:PTZ00121 1634 ---KVEQLKKKEAE---EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE-----KKAAEALKKEAEEAK 1702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1152 RIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDlnlERSHAQKNENARQQLERQNKELKVKlqemegtvKSKYKASI 1231
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE---AEEDKKKAEEAKKDEEEKKKIAHLK--------KEEEKKAE 1771
|
570 580 590
....*....|....*....|....*....|....*..
gi 30268331 1232 TALEAKIAQLEEQLDNETKERQAackQVRRTEKKLKD 1268
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDEKRRM---EVDKKIKDIFD 1805
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
721-1299 |
5.55e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.03 E-value: 5.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 721 VREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHdleaRVEEEEERCQHLQA 800
Cdd:PRK03918 146 SREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLR----EINEISSELPELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 801 EKKKMQqniqeleeqleeeesaRQKLQLEKVTTEaklkkleeelddllvdldhqrqsacnLEKKQKKFDQLLAEEKTISA 880
Cdd:PRK03918 222 ELEKLE----------------KEVKELEELKEE--------------------------IEELEKELESLEGSKRKLEE 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 881 KYAGERDRAEaEAREKETKALSLARALEEAMEQKAELERLNKqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQV---E 957
Cdd:PRK03918 260 KIRELEERIE-ELKKEIEELEEKVKELKELKEKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIkelE 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 958 EMKTQLEELEGELQATEDAKLRLEVNLQAmkaqFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKqrsmavaARKKL 1037
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHEL----YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK-------AKEEI 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1038 EMDLKDLEAHI---DSANKNRDEAIKQLRKLQAQMKDCMRELDDTRasREEILAqakENEKKLKSMEAEMIQLQEELAAA 1114
Cdd:PRK03918 404 EEEISKITARIgelKKEIKELKKAIEELKKAKGKCPVCGRELTEEH--RKELLE---EYTAELKRIEKELKEIEEKERKL 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1115 ERAKRQAQQERDELADEIANSSgkgalALEEKRRLEARIaQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSH 1194
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKE-----LAEQLKELEEKL-KKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1195 AQKNEnaRQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEqLDNETKERQAACKQVRRTEKKLKDVLLQVD 1274
Cdd:PRK03918 553 ELKKK--LAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEP-FYNEYLELKDAEKELEREEKELKKLEEELD 629
|
570 580
....*....|....*....|....*
gi 30268331 1275 DERRNAEQYKDQADKASTRLKQLKR 1299
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEK 654
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
799-1133 |
5.79e-14 |
|
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: 77.40 E-value: 5.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 799 QAEKK--KMQQNIQeleeqleeeesarqklQLEKVTTEAKLKKLEEelddllvdldhQRQSACNLEKKQKKfDQLLAEEK 876
Cdd:TIGR02168 176 ETERKleRTRENLD----------------RLEDILNELERQLKSL-----------ERQAEKAERYKELK-AELRELEL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 877 TISAK----YAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRAL 952
Cdd:TIGR02168 228 ALLVLrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 953 EQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEE------KKKQLVRQVREMEAELEDERKQ 1026
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEleeleaELEELESRLEELEEQLETLRSK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1027 RSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDcmRELDDTRASREEILAQAKENEKKLKSMEAEMIQ 1106
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEE 465
|
330 340
....*....|....*....|....*..
gi 30268331 1107 LQEELAAAERAKRQAQQERDELADEIA 1133
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLD 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
950-1301 |
9.35e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 76.65 E-value: 9.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 950 RALEQQVEEMKtQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSM 1029
Cdd:TIGR02169 170 RKKEKALEELE-EVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1030 AVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKL----QAQMKDCMRELDDTRASREEILA----QAKENEKKLKSME 1101
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeQLRVKEKIGELEAEIASLERSIAekerELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1102 AEMIQLQEELAAAERAKRQAQQERDELADEIANSSgkgalalEEKRRLEARIAQLEEELEEEQgntelinDRLKKANLQI 1181
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK-------EELEDLRAELEEVDKEFAETR-------DELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1182 DQINTDLN-LERSHAQKNENARQQLERQnkelkvklqemegtvkSKYKASITALEAKIAQLEEqldnetkERQAACKQVR 1260
Cdd:TIGR02169 395 EKLKREINeLKRELDRLQEELQRLSEEL----------------ADLNAAIAGIEAKINELEE-------EKEDKALEIK 451
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 30268331 1261 RTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQL 1301
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
733-1269 |
2.44e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 75.15 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 733 TEMETLQSQLMAEKLQLQEQLqaeTELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQniqel 812
Cdd:pfam15921 299 SQLEIIQEQARNQNSMYMRQL---SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQ----- 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 813 eeqleeeESARQKLQLEKVTTEaklkkleeelddllvdlDHQRQSACNLEKKQKK--FDQLLAEEKTIsakyagERDRAE 890
Cdd:pfam15921 371 -------ESGNLDDQLQKLLAD-----------------LHKREKELSLEKEQNKrlWDRDTGNSITI------DHLRRE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 891 AEAREKETKAL-SLARALEEAMEQKAELERLNKQFRTE--------MEDLMSSKDDVGKSVHELEKSKRALE---QQVEE 958
Cdd:pfam15921 421 LDDRNMEVQRLeALLKAMKSECQGQMERQMAAIQGKNEslekvsslTAQLESTKEMLRKVVEELTAKKMTLEsseRTVSD 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 959 MKTQLEELEGELQAT--EDAKLRLEVNLQAmkaqfeRDLQGRDEQSEekkkqlvrQVREMEAELEDERKQRSMAVAARKK 1036
Cdd:pfam15921 501 LTASLQEKERAIEATnaEITKLRSRVDLKL------QELQHLKNEGD--------HLRNVQTECEALKLQMAEKDKVIEI 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1037 LEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAER 1116
Cdd:pfam15921 567 LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLR 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1117 AKRQAQQERDELADEIANSSGKGALALEEKRRLEARIaqleeeleeeQGNTELINDRLKKANLQIDQINTDLNLERSHAQ 1196
Cdd:pfam15921 647 AVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF----------RNKSEEMETTTNKLKMQLKSAQSELEQTRNTLK 716
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30268331 1197 KNENArqqlerQNKELKVKLQeMEGTVKSKyKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDV 1269
Cdd:pfam15921 717 SMEGS------DGHAMKVAMG-MQKQITAK-RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTV 781
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
861-1301 |
7.61e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.41 E-value: 7.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 861 LEKKQKKFDQLLAEEKTISAKYAG-----------ERDRAEAEAREKETKALSLARALEeAMEQKAELERlnKQFRTEME 929
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGnggdrleqlerEIERLERELEERERRRARLEALLA-ALGLPLPASA--EEFAALRA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 930 DLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQ-------- 1001
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAElpfvgeli 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1002 ---SEEKKKQ--------------LV-----RQVRE------MEAELEDERKQRSMAVAARKKLE-------MDLKD--- 1043
Cdd:COG4913 468 evrPEEERWRgaiervlggfaltlLVppehyAAALRwvnrlhLRGRLVYERVRTGLPDPERPRLDpdslagkLDFKPhpf 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1044 ---LEAHIdsaNKNRD----EAIKQLRK------LQAQMKD--CMRELDDTRASREE-ILAQakENEKKLKSMEAEMIQL 1107
Cdd:COG4913 548 rawLEAEL---GRRFDyvcvDSPEELRRhpraitRAGQVKGngTRHEKDDRRRIRSRyVLGF--DNRAKLAALEAELAEL 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1108 QEELAAAERAKRQAQQERDeladeianssgkgalALEEKRRLEARIAQLEEELeeeqgntelinDRLKKANLQIDQintd 1187
Cdd:COG4913 623 EEELAEAEERLEALEAELD---------------ALQERREALQRLAEYSWDE-----------IDVASAEREIAE---- 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1188 LNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKAsITALEAKIAQLEEQLDNETKERQAACKQVR-----RT 1262
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGE-IGRLEKELEQAEEELDELQDRLEAAEDLARlelraLL 751
|
490 500 510
....*....|....*....|....*....|....*....
gi 30268331 1263 EKKLKDVLLQvDDERRNAEQYKDQADKASTRLKQLKRQL 1301
Cdd:COG4913 752 EERFAAALGD-AVERELRENLEERIDALRARLNRAEEEL 789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
899-1134 |
8.64e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.41 E-value: 8.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 899 KALSL-ARALeeAMEQkaeLERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRAlEQQVEEMKTQ---LEELEGELQATE 974
Cdd:COG4913 192 KALRLlHKTQ--SFKP---IGDLDDFVREYMLEEPDTFEAADALVEHFDDLERA-HEALEDAREQielLEPIRELAERYA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 975 DAKLRLEVN------LQAMKAQFERDL-QGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMD-LKDLEA 1046
Cdd:COG4913 266 AARERLAELeylraaLRLWFAQRRLELlEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLER 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1047 HIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEmiqLQEELAAAERAKRQAQQERD 1126
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA---LEEALAEAEAALRDLRRELR 422
|
....*...
gi 30268331 1127 ELADEIAN 1134
Cdd:COG4913 423 ELEAEIAS 430
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
865-1268 |
1.05e-12 |
|
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: 72.24 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 865 QKKFDQLLAEEKTISAKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHE 944
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 945 LEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKaqferdlqgrdeqseEKKKQLVRQVREMEAELEDER 1024
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK---------------ERAKKAGAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1025 KQRSMAVAARKKLEMDLKDLEAHIDsankNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEM 1104
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLA----QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1105 IQLQEELAAAERAKRQAQQERDELADEIANSSGKGA---LALEEKRrleariAQLEEELEEEQGNTELINDRLKKANLQI 1181
Cdd:pfam07888 254 EGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLAdasLALREGR------ARWAQERETLQQSAEADKDRIEKLSAEL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1182 DQINTDLNLERSHAQK-----------NENARQQLERQNKELKVKLQEMEGTvKSKYKASITALEAKIAQLEEQLDNET- 1249
Cdd:pfam07888 328 QRLEERLQEERMEREKlevelgrekdcNRVQLSESRRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVAd 406
|
410 420
....*....|....*....|
gi 30268331 1250 -KERQAACKQVRRTEKKLKD 1268
Cdd:pfam07888 407 aKWSEAALTSTERPDSPLSD 426
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
823-1175 |
1.34e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.79 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 823 RQKLQLEKVTTEaklkkleeelddllvdldhqRQSACNLEKKQKKFDQLLAE-EKTISAKYAGERDRAEAEaREKEtKAL 901
Cdd:TIGR02169 200 LERLRREREKAE--------------------RYQALLKEKREYEGYELLKEkEALERQKEAIERQLASLE-EELE-KLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 902 SLARALEEAMEQKAE-LERLNKQFRTEMEDLMSSkddVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRL 980
Cdd:TIGR02169 258 EEISELEKRLEEIEQlLEELNKKIKDLGEEEQLR---VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 981 EVNLQAMKAQFErDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIK 1060
Cdd:TIGR02169 335 LAEIEELEREIE-EERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1061 QLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSgkga 1140
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ---- 489
|
330 340 350
....*....|....*....|....*....|....*
gi 30268331 1141 lalEEKRRLEARIAQLEEELEEEQGNTELINDRLK 1175
Cdd:TIGR02169 490 ---RELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
854-1312 |
1.36e-12 |
|
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: 72.78 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 854 QRQSACNLEKKQKKfDQLLAEEKTISAK----YAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEME 929
Cdd:TIGR02168 206 ERQAEKAERYKELK-AELRELELALLVLrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 930 DLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEE----- 1004
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEleele 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1005 -KKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQ-----AQMKDCMRELDD 1078
Cdd:TIGR02168 365 aELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkleeAELKELQAELEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1079 TRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSG--KGALALEEKRRLEARIAQL 1156
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsEGVKALLKNQSGLSGILGV 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1157 EEELEEEQGNTEL-----INDRL-----KKANLQIDQINTDLNLER-----------SHAQKNENARQQLERQN------ 1209
Cdd:TIGR02168 525 LSELISVDEGYEAaieaaLGGRLqavvvENLNAAKKAIAFLKQNELgrvtflpldsiKGTEIQGNDREILKNIEgflgva 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1210 -------KELKVKLQEMEGTV------------KSKY----------------------------------KASITALEA 1236
Cdd:TIGR02168 605 kdlvkfdPKLRKALSYLLGGVlvvddldnalelAKKLrpgyrivtldgdlvrpggvitggsaktnssilerRREIEELEE 684
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30268331 1237 KIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRAT 1312
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
900-1143 |
1.85e-12 |
|
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: 70.56 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 900 ALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLR 979
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 980 LEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAvAARKKLEMDLKDLEAHIDSANKNRDEAI 1059
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA-PARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1060 KQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKG 1139
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
....
gi 30268331 1140 ALAL 1143
Cdd:COG4942 254 KLPW 257
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
723-1038 |
2.60e-12 |
|
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: 71.63 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 723 EKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEK 802
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 803 KKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKY 882
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 883 AGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQ 962
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 963 LEELEGELQATEDaKLRLEVNLQAMKA-QFERDLQGRDEQSEEKKKQLVRQVREM---------EAELEDER-----KQR 1027
Cdd:TIGR02168 931 LEGLEVRIDNLQE-RLSEEYSLTLEEAeALENKIEDDEEEARRRLKRLENKIKELgpvnlaaieEYEELKERydfltAQK 1009
|
330
....*....|.
gi 30268331 1028 SMAVAARKKLE 1038
Cdd:TIGR02168 1010 EDLTEAKETLE 1020
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
862-1311 |
3.07e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.71 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 862 EKKQKKFDQLLAEEktisAKYAGERDRAEAEAREKETKALSLARALEEA----MEQKAELERLNKQFRTEMEDLMSSKDD 937
Cdd:PTZ00121 1119 EAKKKAEDARKAEE----ARKAEDARKAEEARKAEDAKRVEIARKAEDArkaeEARKAEDAKKAEAARKAEEVRKAEELR 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 938 VGKSVHELEKSKRALE-QQVEEMKTQLEELEGE-LQATEDAKLRLEvnlQAMKAQFERDLQGRDEQSEEKKKQLVRQVRE 1015
Cdd:PTZ00121 1195 KAEDARKAEAARKAEEeRKAEEARKAEDAKKAEaVKKAEEAKKDAE---EAKKAEEERNNEEIRKFEEARMAHFARRQAA 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1016 MEAEleDERKQRSMAVAARKKLEMDLKDLEA--HIDSANKNRDEAIK--QLRKLQAQMKDCMRELDD--------TRASR 1083
Cdd:PTZ00121 1272 IKAE--EARKADELKKAEEKKKADEAKKAEEkkKADEAKKKAEEAKKadEAKKKAEEAKKKADAAKKkaeeakkaAEAAK 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1084 EEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDelADEIANSSGKGALALEEKRRLEAriAQLEEELEEE 1163
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK--ADEAKKKAEEDKKKADELKKAAA--AKKKADEAKK 1425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1164 QGNTELINDRLKKANLQIDQINtDLNLERSHAQKNENARQQLERQNK--ELKVKLQEMEGTVKSKYKASIT---ALEAKI 1238
Cdd:PTZ00121 1426 KAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEAKKADEAKKKAEEAkkkADEAKK 1504
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30268331 1239 AQLEEQLDNETKERQAACK--QVRRTEKKLKDVLLQVDDERRNAEQYK--DQADKASTRLK--QLKRQLEEAEEEAQRA 1311
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKadEAKKAEEAKKADEAKKAEEKKKADELKkaEELKKAEEKKKaeEAKKAEEDKNMALRKA 1583
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
722-1092 |
3.93e-12 |
|
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: 71.24 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 722 REKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEIC---HDLEARVEEEEERCQHL 798
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqiSALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 799 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDdllvdldhQRQSACNLEKKQkkFDQLLAEEKTI 878
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE--------QLKEELKALREA--LDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 879 SAKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQVEE 958
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA----EIEELEELIEELESELEALLNERASLEEALAL 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 959 MKTQLEELEGELQATEDAKLRLEVNLQAMKAQFErDLQGRDEQSEEKKKQLVRQVREM-EAELEDERKQRSMAVAARKKL 1037
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLA-QLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEA 970
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30268331 1038 EMDLKDLEAHIDS---ANKNRDEAIKQLRK----LQAQMKDCMRELDDTRASREEILAQAKE 1092
Cdd:TIGR02168 971 RRRLKRLENKIKElgpVNLAAIEEYEELKErydfLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
861-1155 |
6.85e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.48 E-value: 6.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 861 LEKKQKKFDQLLAEEKTISAKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRT-EMEDLMSSKDDVG 939
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQ 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 940 KSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFE------RDLQGRDEQSEEKKKQLVRQV 1013
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKsiekeiENLNGKKEELEEELEELEAAL 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1014 REMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKdcmrELDDTRASREEIlaqaKEN 1093
Cdd:TIGR02169 878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEI----PEE 949
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30268331 1094 EKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQ 1155
Cdd:TIGR02169 950 ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
722-1121 |
1.03e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.71 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 722 REKQLAAENRLTEMETLQSQLMAEKlqlqeqlqaeTELCAEAEELRARLTAKKQELEEICHDLEArveeeeercqhLQAE 801
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSEL----------RRIENRLDELSQELSDASRKIGEIEKEIEQ-----------LEQE 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 802 KKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKlkkleeelddllvdldhqrqsacnLEKKQKKFDQLLAEEKTISAK 881
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEAR------------------------IEELEEDLHKLEEALNDLEAR 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 882 YAGER--------DRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALE 953
Cdd:TIGR02169 788 LSHSRipeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 954 QQVEEMKTQLEELEGELQatedaklrlevnlqamkaqferDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAA 1033
Cdd:TIGR02169 868 EELEELEAALRDLESRLG----------------------DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1034 RKKLEMDLKDLEAHIdSANKNRDEAIKQLRKLQAQMKDCMRELDD-----TRASR--EEILAQAKENEKKLKSMEAEMIQ 1106
Cdd:TIGR02169 926 LEALEEELSEIEDPK-GEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnMLAIQeyEEVLKRLDELKEKRAKLEEERKA 1004
|
410
....*....|....*
gi 30268331 1107 LQEELAAAERAKRQA 1121
Cdd:TIGR02169 1005 ILERIEEYEKKKREV 1019
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
882-1243 |
1.50e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.30 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 882 YAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKT 961
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 962 QLEELEGELQATEDAKLRLEVNLQAMKA-QFERDLQG--RDEQSEEKKKqlvrQVREMEAELEDERKQRSmAVAARKKLE 1038
Cdd:PRK02224 427 REAELEATLRTARERVEEAEALLEAGKCpECGQPVEGspHVETIEEDRE----RVEELEAELEDLEEEVE-EVEERLERA 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1039 MDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAK 1118
Cdd:PRK02224 502 EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1119 RQAQQERDELADeIANSSGKGALALEEKRRLEARIAQLEEEleeeqgNTELiNDRLKKANLQIDQINTDLNLERSHAQKN 1198
Cdd:PRK02224 582 AELKERIESLER-IRTLLAAIADAEDEIERLREKREALAEL------NDER-RERLAEKRERKRELEAEFDEARIEEARE 653
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 30268331 1199 EnaRQQLERQNKELKVKLQEMEGTvKSKYKASITALEAKIAQLEE 1243
Cdd:PRK02224 654 D--KERAEEYLEQVEEKLDELREE-RDDLQAEIGAVENELEELEE 695
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
892-1301 |
5.43e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.40 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 892 EAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQ 971
Cdd:PRK03918 145 ESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 972 ATEDAKLRLE---VNLQAMKAQfERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKdLEAHI 1048
Cdd:PRK03918 225 KLEKEVKELEelkEEIEELEKE-LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1049 DSANKNRDEAIKQLRKLQAQMKDCMRELDDtrasREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAK---------- 1118
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKE----LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKakkeelerlk 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1119 -RQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTElindRLKKA-------NLQIDQINTDLNL 1190
Cdd:PRK03918 379 kRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE----ELKKAkgkcpvcGRELTEEHRKELL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1191 ERSHAQ--KNENARQQLERQNKELKVKLQEMEGTVKSkykasitalEAKIAQLEEQLDnetkerqaackQVRRTEKKLKD 1268
Cdd:PRK03918 455 EEYTAElkRIEKELKEIEEKERKLRKELRELEKVLKK---------ESELIKLKELAE-----------QLKELEEKLKK 514
|
410 420 430
....*....|....*....|....*....|....
gi 30268331 1269 VLLQ-VDDERRNAEQYKDQADKASTRLKQLKRQL 1301
Cdd:PRK03918 515 YNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
942-1288 |
6.16e-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: 67.39 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 942 VHELEKSKRALEQQVE------EMKTQLEELEGELQAtedakLRLEvnlqamkaqferDLQGRDEQSEEKKKQLVRQVRE 1015
Cdd:TIGR02168 195 LNELERQLKSLERQAEkaerykELKAELRELELALLV-----LRLE------------ELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1016 MEAELederkqrsmavaarKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEK 1095
Cdd:TIGR02168 258 LTAEL--------------QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1096 KLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANssgkgalALEEKRRLEARIAQLEEELEEEqgnteliNDRLK 1175
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEE-------LEAELEELESRLEELEEQLETL-------RSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1176 KANLQIDQINTDLnlershaqknENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAA 1255
Cdd:TIGR02168 390 QLELQIASLNNEI----------ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459
|
330 340 350
....*....|....*....|....*....|...
gi 30268331 1256 CKQVRRTEKKLKDVLLQVDDERRNAEQYKDQAD 1288
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLD 492
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
883-1300 |
8.72e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.33 E-value: 8.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 883 AGERDRAEAEAREKETKALslARALEEAMEQKAELERLNKQFRTEMEDLmsskdDVGKSVHELEKSKRALEQQVEEMKTQ 962
Cdd:COG4717 75 ELEEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 963 LEELEG---ELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEM 1039
Cdd:COG4717 148 LEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1040 DLKDLEA-HIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILA-------------QAKENEKKLKSMEAEMI 1105
Cdd:COG4717 228 ELEQLENeLEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallfLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1106 QLQEELAAAERAKRQAQQERDELADEIANSSGKGAL-ALEEKRRLEARIAQLEEELEEEQGNTELindrlkKANLQIDQI 1184
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLdRIEELQELLREAEELEEELQLEELEQEI------AALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1185 NTDLNLERSHAQKNEnaRQQLERQNKELKVKLQEMEGTVKSKYKA-SITALEAKIAQLEEQLDNETKERQAACKQVRRTE 1263
Cdd:COG4717 382 EDEEELRAALEQAEE--YQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELREELAELE 459
|
410 420 430
....*....|....*....|....*....|....*..
gi 30268331 1264 KKLKDvlLQVDDERRNAEQykdQADKASTRLKQLKRQ 1300
Cdd:COG4717 460 AELEQ--LEEDGELAELLQ---ELEELKAELRELAEE 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
703-1121 |
3.40e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 703 QVSRQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAEtELCAEAEELRARLTAKKQELEEICH 782
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL-PLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 783 DLEARvEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESAR----------QKLQLEKVTTEAKLKKLEEELDDLLVDLD 852
Cdd:COG4717 154 RLEEL-RELEEELEELEAELAELQEELEELLEQLSLATEEElqdlaeeleeLQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 853 HQRQSACNLEKKQKKFDQLLAEEKTISAKYAGERDRAEAEAREKETKALSLA----------RALEEAMEQKAELERLNK 922
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGllallflllaREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 923 QFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQ--ATEDAKLRLEVNLQAMKAQFERDLQGRDE 1000
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEAGVEDEEELRAALE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1001 QSEEKKkQLVRQVREMEAELEDERK--QRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCM--REL 1076
Cdd:COG4717 393 QAEEYQ-ELKEELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEedGEL 471
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 30268331 1077 DDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQA 1121
Cdd:COG4717 472 AELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPP 516
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1055-1311 |
4.02e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1055 RDEAIKQLRKLQAQM---KDCMRELDdtraSREEILAQAKENEKKLKSMEAEMIQLQEELAAAERakRQAQQERDELADE 1131
Cdd:COG1196 174 KEEAERKLEATEENLerlEDILGELE----RQLEPLERQAEKAERYRELKEELKELEAELLLLKL--RELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1132 IANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERshaQKNENARQQLERQNKE 1211
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE---ERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1212 LKVKLQEMEGTvkskyKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKAS 1291
Cdd:COG1196 325 LAELEEELEEL-----EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
250 260
....*....|....*....|
gi 30268331 1292 TRLKQLKRQLEEAEEEAQRA 1311
Cdd:COG1196 400 AQLEELEEAEEALLERLERL 419
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
853-1300 |
7.09e-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: 63.70 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 853 HQRQSACNLEKKQK-------KFDQLLAEEKTISAKYAGE---------RDRAEAEAREKETKALSLARaLEEAmeqKAE 916
Cdd:pfam12128 270 DETLIASRQEERQEtsaelnqLLRTLDDQWKEKRDELNGElsaadaavaKDRSELEALEDQHGAFLDAD-IETA---AAD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 917 LERLNkQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQV-EEMKTQLEELEGELQATEDAKLRLevnlqamKAQFERDL 995
Cdd:pfam12128 346 QEQLP-SWQSELENLEERLKALTGKHQDVTAKYNRRRSKIkEQNNRDIAGIKDKLAKIREARDRQ-------LAVAEDDL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 996 QGRDEQSEEKKKQLVRQVREMEAELE---DERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQaqmkdc 1072
Cdd:pfam12128 418 QALESELREQLEAGKLEFNEEEYRLKsrlGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQ------ 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1073 mRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAE-------------------RAKRQAQQERDELADEIA 1133
Cdd:pfam12128 492 -SELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAgtllhflrkeapdweqsigKVISPELLHRTDLDPEVW 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1134 NSSGKGALAL----------------EEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQK 1197
Cdd:pfam12128 571 DGSVGGELNLygvkldlkridvpewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKN 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1198 NENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLdNETKERQAACKQVRRTEKKLKdvLLQVDDER 1277
Cdd:pfam12128 651 ARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKH-QAWLEEQKEQKREARTEKQAY--WQVVEGAL 727
|
490 500
....*....|....*....|....*...
gi 30268331 1278 RNAEQYKDQA-----DKASTRLKQLKRQ 1300
Cdd:pfam12128 728 DAQLALLKAAiaarrSGAKAELKALETW 755
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1075-1322 |
1.76e-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: 61.32 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1075 ELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIA 1154
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1155 QLEeeleeeqgntELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKsKYKASITAL 1234
Cdd:COG4942 101 AQK----------EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-ELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1235 EAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRATPP 1314
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
....*...
gi 30268331 1315 AGNCSASW 1322
Cdd:COG4942 250 ALKGKLPW 257
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
957-1300 |
2.61e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 957 EEMKTQLEELEGELQATEDAKLRLEVN-LQAMKAQFERDLqgrdEQSEEKKKQLVRQVREMEAELEDERKQRsmavAARK 1035
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERLNgLESELAELDEEI----ERYEEQREQARETRDEADEVLEEHEERR----EELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1036 KLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAE 1115
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1116 RAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHA 1195
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1196 QKNENARQQLERQNKELKVKLQEMEGTVK---------------------------SKYKASITALEAKIAQLEEQLDnE 1248
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEeaealleagkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVE-E 493
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 30268331 1249 TKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQ 1300
Cdd:PRK02224 494 VEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER 545
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1003-1282 |
4.27e-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: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1003 EEKKKQLVRQVREMEAELEDerkqrsmAVAARKKLEMDLKDLEAhidsanknRDEAIKQLRKLQAQMKDcMRELDDTRAS 1082
Cdd:COG4913 609 RAKLAALEAELAELEEELAE-------AEERLEALEAELDALQE--------RREALQRLAEYSWDEID-VASAEREIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1083 REEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANssgkgalALEEKRRLEARIAQLEEELEE 1162
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ-------AEEELDELQDRLEAAEDLARL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1163 EQgnTELINDRLKKANLQidqintdlNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLE 1242
Cdd:COG4913 746 EL--RALLEERFAAALGD--------AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP 815
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 30268331 1243 E------QLDNE---TKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQ 1282
Cdd:COG4913 816 EylalldRLEEDglpEYEERFKELLNENSIEFVADLLSKLRRAIREIKE 864
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
860-1128 |
7.47e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 7.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 860 NLEKKQKKFDQLLAEEKTIsAKYAGERDRAEAEAREKETKALSLARALEEAMEQK------AELERLNKQfrteMEDLMS 933
Cdd:COG4913 608 NRAKLAALEAELAELEEEL-AEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaeREIAELEAE----LERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 934 SKDDVgksvhelekskRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQV 1013
Cdd:COG4913 683 SSDDL-----------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1014 REMEAELEDERKQRSMAvaarkklemdlKDLEAHIDSANKNRDEAIKQLRKLQAQMK----DCMRELDDTRASREEILA- 1088
Cdd:COG4913 752 EERFAAALGDAVERELR-----------ENLEERIDALRARLNRAEEELERAMRAFNrewpAETADLDADLESLPEYLAl 820
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 30268331 1089 ------------QAKENEKKLKSMEAEMIQLQEELaaaERAKRQAQQERDEL 1128
Cdd:COG4913 821 ldrleedglpeyEERFKELLNENSIEFVADLLSKL---RRAIREIKERIDPL 869
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1050-1323 |
9.60e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.07 E-value: 9.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1050 SANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELA 1129
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1130 DEIANSSGKGAL--ALeekrrLEAriaqleeeleeeQGNTELInDRLKKANLQIDQINTDLNLERSHAQKNENARQQLER 1207
Cdd:COG3883 93 RALYRSGGSVSYldVL-----LGS------------ESFSDFL-DRLSALSKIADADADLLEELKADKAELEAKKAELEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1208 QNKELKVKLQEMEgTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQA 1287
Cdd:COG3883 155 KLAELEALKAELE-AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 30268331 1288 DKASTRLKQLKRQLEEAEEEAQRATPPAGNCSASWR 1323
Cdd:COG3883 234 AAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAA 269
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
727-1152 |
1.09e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 727 AAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEA----------RVEEEEERCQ 796
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAEterereelaeEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 797 HLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKKfdqllAEEK 876
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE-----LREE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 877 tiSAKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQV 956
Cdd:PRK02224 365 --AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 957 EEMKT----------------------------QLEELEGELQATEDAKLRLE------VNLQAMKAQFERDLQGRD--- 999
Cdd:PRK02224 443 EEAEAlleagkcpecgqpvegsphvetieedreRVEELEAELEDLEEEVEEVEerleraEDLVEAEDRIERLEERREdle 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1000 ----------EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIdSANKNRDEAIKQLRKLQAQM 1069
Cdd:PRK02224 523 eliaerretiEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL-AELKERIESLERIRTLLAAI 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1070 KDCMRELDDTRASREEILAQAKENEKKLKSM------------EAEMIQLQEELAAAERAKRQAQQERDELA---DEIAN 1134
Cdd:PRK02224 602 ADAEDEIERLREKREALAELNDERRERLAEKrerkreleaefdEARIEEAREDKERAEEYLEQVEEKLDELReerDDLQA 681
|
490
....*....|....*...
gi 30268331 1135 SSGKGALALEEKRRLEAR 1152
Cdd:PRK02224 682 EIGAVENELEELEELRER 699
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
940-1302 |
1.38e-08 |
|
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: 59.26 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 940 KSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFErDLQGRDEQSEEKKKQLVRQVREMEAE 1019
Cdd:TIGR04523 218 SQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS-EKQKELEQNNKKIKELEKQLNQLKSE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1020 LEDERKQRSMAVAarKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKS 1099
Cdd:TIGR04523 297 ISDLNNQKEQDWN--KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1100 MEAE--------------------MIQLQEELAAAERAK-RQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEE 1158
Cdd:TIGR04523 375 LKKEnqsykqeiknlesqindlesKIQNQEKLNQQKDEQiKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1159 ELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKS------KYKASIT 1232
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSlkekieKLESEKK 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1233 ALEAKIAQLEEQL--DNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLK--------------Q 1296
Cdd:TIGR04523 535 EKESKISDLEDELnkDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKdlikeieekekkisS 614
|
....*.
gi 30268331 1297 LKRQLE 1302
Cdd:TIGR04523 615 LEKELE 620
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
885-1126 |
1.63e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 57.61 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 885 ERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLE 964
Cdd:COG1340 16 KIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 965 ELEGELQATEDAKLRLEvNLQAMKAQFERDLQGRDeQSEEKKKQLVRQVREMEAELEDERKQRsmavaarkKLEMDLKDL 1044
Cdd:COG1340 96 ELRKELAELNKAGGSID-KLRKEIERLEWRQQTEV-LSPEEEKELVEKIKELEKELEKAKKAL--------EKNEKLKEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1045 EAHIDSANKNRDEAIKQLRKLQ-------AQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEEL------ 1111
Cdd:COG1340 166 RAELKELRKEAEEIHKKIKELAeeaqelhEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELrelrke 245
|
250 260
....*....|....*....|...
gi 30268331 1112 --------AAAERAKRQAQQERD 1126
Cdd:COG1340 246 lkklrkkqRALKREKEKEELEEK 268
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
944-1142 |
1.84e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 944 ELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQ---FERDLQGRDEQSEEKKKQLVRQVREME--- 1017
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidkLQAEIAEAEAEIEERREELGERARALYrsg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1018 ---------------AELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRAS 1082
Cdd:COG3883 100 gsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1083 REEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALA 1142
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
949-1273 |
2.37e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 949 KRALEQQVEEMKTQLEELegelqATEDAKLRLEVN-LQAMKAQFERDLQGR-----DEQSEEKKKQLVRQVREMEAELED 1022
Cdd:PRK04863 781 RAAREKRIEQLRAEREEL-----AERYATLSFDVQkLQRLHQAFSRFIGSHlavafEADPEAELRQLNRRRVELERALAD 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1023 ----ERKQRSMAVAARKKLEMdlkdLEAHIDSANKNRDEA-IKQLRKLQAQMKDCmreLDDTR--ASREEILAQAKENEK 1095
Cdd:PRK04863 856 hesqEQQQRSQLEQAKEGLSA----LNRLLPRLNLLADETlADRVEEIREQLDEA---EEAKRfvQQHGNALAQLEPIVS 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1096 KLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANssgKGALALEEKRRLEAriaqleeeleEEQGNTELINDRLK 1175
Cdd:PRK04863 929 VLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQR---RAHFSYEDAAEMLA----------KNSDLNEKLRQRLE 995
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1176 KANLQIDQINTDLNLERS-HAQKNE------NARQQLERQNKELKVKLQEM-----EG------TVKSKYKASITALEAK 1237
Cdd:PRK04863 996 QAEQERTRAREQLRQAQAqLAQYNQvlaslkSSYDAKRQMLQELKQELQDLgvpadSGaeerarARRDELHARLSANRSR 1075
|
330 340 350
....*....|....*....|....*....|....*.
gi 30268331 1238 IAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQV 1273
Cdd:PRK04863 1076 RNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
701-1019 |
2.70e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 701 LLQVSRQEEEMMAKEEELVKVREKQLA-AENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEE 779
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 780 ICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSAC 859
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 860 NLEKKQKKFDQLLAEEKTISAKYAGERDRAEAEAREKETKALSLARALEEAMEQ-----------KAELERLNKQFRTEM 928
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKlaqlelrleglEVRIDNLQERLSEEY 949
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 929 EDLMsskDDVGKSVHELEKSKRALEQQVEEMKTQLEELEgelqatedaklrlEVNLQAM---KAQFER--DLQGRDEQSE 1003
Cdd:TIGR02168 950 SLTL---EEAEALENKIEDDEEEARRRLKRLENKIKELG-------------PVNLAAIeeyEELKERydFLTAQKEDLT 1013
|
330
....*....|....*.
gi 30268331 1004 EKKKQLVRQVREMEAE 1019
Cdd:TIGR02168 1014 EAKETLEEAIEEIDRE 1029
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
912-1301 |
2.82e-08 |
|
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: 58.49 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 912 EQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQF 991
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 992 ER---------DLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQL 1062
Cdd:TIGR04523 211 QKnkslesqisELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1063 RKLQAQ------------MKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELAD 1130
Cdd:TIGR04523 291 NQLKSEisdlnnqkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1131 EIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNK 1210
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1211 ELKVKLQEMEGTVK------SKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYK 1284
Cdd:TIGR04523 451 VKELIIKNLDNTREsletqlKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
410
....*....|....*..
gi 30268331 1285 DQADKASTRLKQLKRQL 1301
Cdd:TIGR04523 531 SEKKEKESKISDLEDEL 547
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1000-1226 |
3.22e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1000 EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDT 1079
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1080 RASREEILAQAkenEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEE 1159
Cdd:COG4942 103 KEELAELLRAL---YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30268331 1160 LEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSK 1226
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
865-1300 |
3.68e-08 |
|
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: 58.21 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 865 QKKFDQLLaEEKTISAKYAGERDRAEAEAREKET-----KALSLARALEEAMEQKAELERLNKQFRTEMEDLmssKDDVG 939
Cdd:pfam15921 73 KEHIERVL-EEYSHQVKDLQRRLNESNELHEKQKfylrqSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL---RNQLQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 940 KSVHELEKSKRALEQQVEEMKTQLEEL-------EGELQATEDAKLRLE---------------VNLQAMKAQFERDLQG 997
Cdd:pfam15921 149 NTVHELEAAKCLKEDMLEDSNTQIEQLrkmmlshEGVLQEIRSILVDFEeasgkkiyehdsmstMHFRSLGSAISKILRE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 998 RDEQSEEKKKQLVRQVREMEA-ELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDC---- 1072
Cdd:pfam15921 229 LDTEISYLKGRIFPVEDQLEAlKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIqeqa 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1073 -------MRELDDTRAS----REEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIanssgKGAL 1141
Cdd:pfam15921 309 rnqnsmyMRQLSDLESTvsqlRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL-----QKLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1142 ALEEKRRLEARI--AQLEEELEEEQGNTELIND---RLKKANLQIDQINTDLNLERSHAQKnenarqQLERQNKELKVKL 1216
Cdd:pfam15921 384 ADLHKREKELSLekEQNKRLWDRDTGNSITIDHlrrELDDRNMEVQRLEALLKAMKSECQG------QMERQMAAIQGKN 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1217 QEMEgtvkskykaSITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLkQ 1296
Cdd:pfam15921 458 ESLE---------KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV-D 527
|
....
gi 30268331 1297 LKRQ 1300
Cdd:pfam15921 528 LKLQ 531
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
697-1290 |
3.75e-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: 58.06 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 697 KVKPLLQVSRQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLM-------AEKLQLQEQLQAETELCAEAEELRAR 769
Cdd:TIGR00618 281 ETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLmkraahvKQQSSIEEQRRLLQTLHSQEIHIRDA 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 770 LTAKKQELEEICHDLEARveeeeercQHLqaekKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLV 849
Cdd:TIGR00618 361 HEVATSIREISCQQHTLT--------QHI----HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAH 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 850 DLDHQRQSACNLEKKQKKFDQLLAEEK--TISAKYAGERDRAEAE---------AREKETKALSLARALEEameqkAELE 918
Cdd:TIGR00618 429 AKKQQELQQRYAELCAAAITCTAQCEKleKIHLQESAQSLKEREQqlqtkeqihLQETRKKAVVLARLLEL-----QEEP 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 919 RLNKQFRTEMEDLMSSKDDVGKSVHELEkskrALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGR 998
Cdd:TIGR00618 504 CPLCGSCIHPNPARQDIDNPGPLTRRMQ----RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 999 DEQSEEK---KKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCM-R 1074
Cdd:TIGR00618 580 NRSKEDIpnlQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQeR 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1075 ELDDTRASREEILAQAKENEKKLKSMEAEMIQL---QEELAAAERAKRQAQQ---ERDELADEIANSSGKGALALEEKRR 1148
Cdd:TIGR00618 660 VREHALSIRVLPKELLASRQLALQKMQSEKEQLtywKEMLAQCQTLLRELEThieEYDREFNEIENASSSLGSDLAARED 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1149 LEARIAQLEEELEEEQGNtELINDRLKKANLQIDQINTDLNLERShAQKNENARQQLERQNKELKVKLQEMEGTVKSkYK 1228
Cdd:TIGR00618 740 ALNQSLKELMHQARTVLK-ARTEAHFNNNEEVTAALQTGAELSHL-AAEIQFFNRLREEDTHLLKTLEAEIGQEIPS-DE 816
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30268331 1229 ASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKA 1290
Cdd:TIGR00618 817 DILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
859-1297 |
4.12e-08 |
|
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: 57.81 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 859 CNLEKkqkkfdQLLAEEKTISAKYAGERDRAEAEAREKETKALSLARALEEaMEQKAELERLNKQFR--TEMEDLMSSKD 936
Cdd:pfam05483 157 CNLLK------ETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEE-LRVQAENARLEMHFKlkEDHEKIQHLEE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 937 DVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEvnlQAMKAQferdlqgrdeqsEEKKKQLVRQVREM 1016
Cdd:pfam05483 230 EYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE---EKTKLQ------------DENLKELIEKKDHL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1017 EAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKE---- 1092
Cdd:pfam05483 295 TKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrlek 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1093 NEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDEL--------------------ADEIANSSGKGALALEEKRR---- 1148
Cdd:pfam05483 375 NEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELkkilaedeklldekkqfekiAEELKGKEQELIFLLQAREKeihd 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1149 LEARI-----AQLEEELEEEQGNTELINDRLKKANL------------QIDQINTDLNLE-RSHAQKNENARQQLERQNK 1210
Cdd:pfam05483 455 LEIQLtaiktSEEHYLKEVEDLKTELEKEKLKNIELtahcdklllenkELTQEASDMTLElKKHQEDIINCKKQEERMLK 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1211 ELKvKLQEMEG-------TVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQY 1283
Cdd:pfam05483 535 QIE-NLEEKEMnlrdeleSVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEEL 613
|
490
....*....|....*...
gi 30268331 1284 KDQ----ADKASTRLKQL 1297
Cdd:pfam05483 614 HQEnkalKKKGSAENKQL 631
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
986-1153 |
5.32e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 55.32 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 986 AMKAQFER--DLQGRD---EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIK 1060
Cdd:COG1579 1 AMPEDLRAllDLQELDselDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1061 QLRKLQA--QMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANssgK 1138
Cdd:COG1579 81 QLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA---E 157
|
170
....*....|....*
gi 30268331 1139 GALALEEKRRLEARI 1153
Cdd:COG1579 158 LEELEAEREELAAKI 172
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1074-1298 |
5.69e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1074 RELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEE--LAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEA 1151
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1152 RIAQLEEELEEEQGNTELINDRLkkanlQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASI 1231
Cdd:COG3206 248 QLGSGPDALPELLQSPVIQQLRA-----QLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30268331 1232 TALEAKIAQLEEQLDNETKERQaackQVRRTEKKLKDvlLQvdderRNAEQYKDQADKASTRLKQLK 1298
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLA----ELPELEAELRR--LE-----REVEVARELYESLLQRLEEAR 378
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
865-1311 |
6.30e-08 |
|
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: 57.36 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 865 QKKFDQLLAEEKTISAKyagERDRAEAEAREKETKALSLARALEEAMEQKAELERlnKQFRTEMEDLMSSKDDVGKSVHE 944
Cdd:TIGR00606 172 KQKFDEIFSATRYIKAL---ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIR--DQITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 945 LEKSKRALeQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDER 1024
Cdd:TIGR00606 247 LDPLKNRL-KEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1025 KQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLK----SM 1100
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVierqED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1101 EAEMI-QLQEELAAAERAKrqaQQERDELADEIansSGKGALALEEKRRLEARIAQLEEELEEEQgNTELINDRLkkanL 1179
Cdd:TIGR00606 406 EAKTAaQLCADLQSKERLK---QEQADEIRDEK---KGLGRTIELKKEILEKKQEELKFVIKELQ-QLEGSSDRI----L 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1180 QIDQINTDLNLERSHAQKNENARQQLERQnkelkVKLQEMEGTVKSKYKASITALEAKIAQLE--EQLDNETKERQAACK 1257
Cdd:TIGR00606 475 ELDQELRKAERELSKAEKNSLTETLKKEV-----KSLQNEKADLDRKLRKLDQEMEQLNHHTTtrTQMEMLTKDKMDKDE 549
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 30268331 1258 QVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRA 1311
Cdd:TIGR00606 550 QIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASL 603
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
730-1131 |
6.80e-08 |
|
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: 57.04 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 730 NRLTEMETLQSQLMAEKLQLQEQLQAET---ELCAEAEELRARLTAKKQELeeicHDLEARVEEEEERCQHLQAEKKKMQ 806
Cdd:pfam05483 402 NKEVELEELKKILAEDEKLLDEKKQFEKiaeELKGKEQELIFLLQAREKEI----HDLEIQLTAIKTSEEHYLKEVEDLK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 807 QNIQELEEQLEEEESARQKLQLE--KVTTEAKLKKLEEElddllvdldhQRQSACNLEKKQKkfDQLLAEEKTISAKYAG 884
Cdd:pfam05483 478 TELEKEKLKNIELTAHCDKLLLEnkELTQEASDMTLELK----------KHQEDIINCKKQE--ERMLKQIENLEEKEMN 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 885 ERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLE 964
Cdd:pfam05483 546 LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 965 ELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKK---KQLVRQVREMEAELEDERK-QRSMAVAARKKLEMD 1040
Cdd:pfam05483 626 AENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKiseEKLLEEVEKAKAIADEAVKlQKEIDKRCQHKIAEM 705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1041 LKDLEAHIDSANKNRDEAIKQLrklqAQMKDCMRELDDTRASREEILAQAKENEKKLKSmeaemiQLQEELAAAERAKRQ 1120
Cdd:pfam05483 706 VALMEKHKHQYDKIIEERDSEL----GLYKNKEQEQSSAKAALEIELSNIKAELLSLKK------QLEIEKEEKEKLKME 775
|
410
....*....|.
gi 30268331 1121 AQQERDELADE 1131
Cdd:pfam05483 776 AKENTAILKDK 786
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
861-1301 |
9.84e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.83 E-value: 9.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 861 LEKKQKKFDQL---LAEEKTISAKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDD 937
Cdd:PRK01156 192 LKSSNLELENIkkqIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 938 VGKSVHELEKSKR-----------------ALEQQVEEMKTQLEELEGELQATEDAKLRLEVnLQAMKAQFERDLQGRDE 1000
Cdd:PRK01156 272 NNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKKQILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDD 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1001 ---------QSEEKKKQLVRQVREMEAELEDERKQR------------------SMAVAARKKLEMDLKDLEAHIDSANK 1053
Cdd:PRK01156 351 lnnqileleGYEMDYNSYLKSIESLKKKIEEYSKNIermsafiseilkiqeidpDAIKKELNEINVKLQDISSKVSSLNQ 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1054 NRDEAIKQLRKLQAQMKD---------CMRELDDTRASReeilaQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQE 1124
Cdd:PRK01156 431 RIRALRENLDELSRNMEMlngqsvcpvCGTTLGEEKSNH-----IINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1125 RDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQI-DQINTDLNleRSHAQKN----E 1199
Cdd:PRK01156 506 KEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDlDSKRTSWL--NALAVISlidiE 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1200 NARQQLERQNKELK---VKLQEMEGT---VKSKYKASITALEAKIAQLEEQLdNETKERQAACKQVRRTEKKLKDVLLQV 1273
Cdd:PRK01156 584 TNRSRSNEIKKQLNdleSRLQEIEIGfpdDKSYIDKSIREIENEANNLNNKY-NEIQENKILIEKLRGKIDNYKKQIAEI 662
|
490 500
....*....|....*....|....*...
gi 30268331 1274 DDERRNAEQYKDQADKASTRLKQLKRQL 1301
Cdd:PRK01156 663 DSIIPDLKEITSRINDIEDNLKKSRKAL 690
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
944-1301 |
9.91e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 944 ELEKSKRALE----QQVEEMKTQLEELEGELQATEDAKLRLevnlqamkaqfeRDLQGRDEQSEEKKKQLVRQVREMEAE 1019
Cdd:COG4717 50 RLEKEADELFkpqgRKPELNLKELKELEEELKEAEEKEEEY------------AELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1020 LE--DERKQRSMAVAARKKLEMDLKDLEAHIDSAnknrDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAK-ENEKK 1096
Cdd:COG4717 118 LEklEKLLQLLPLYQELEALEAELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1097 LKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEAR-----IAQLEEELEEEQGNTELIN 1171
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliAAALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1172 DRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKY------KASITALEAKIAQLEEQL 1245
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlppdlsPEELLELLDRIEELQELL 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 30268331 1246 DNETKERQAACKQVRRTEKK--LKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQL 1301
Cdd:COG4717 354 REAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQL 411
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
865-1175 |
1.04e-07 |
|
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: 55.84 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 865 QKKFDQLLAEEKTISAKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLN---KQFRTEMEDLMSSKDDVGKS 941
Cdd:pfam19220 54 EALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRielRDKTAQAEALERQLAAETEQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 942 VHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFER------DLQGRDEQSEEKKKQLVRQVRE 1015
Cdd:pfam19220 134 NRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEqaaelaELTRRLAELETQLDATRARLRA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1016 MEAELEDERKQRSMAVAA-----------RKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMkdcmRELDdtRASRE 1084
Cdd:pfam19220 214 LEGQLAAEQAERERAEAQleeaveahraeRASLRMKLEALTARAAATEQLLAEARNQLRDRDEAI----RAAE--RRLKE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1085 EILAQAKEnEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQ 1164
Cdd:pfam19220 288 ASIERDTL-ERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVER 366
|
330
....*....|.
gi 30268331 1165 GNTELINDRLK 1175
Cdd:pfam19220 367 AALEQANRRLK 377
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
854-1232 |
1.16e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.29 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 854 QRQSACNLEKKQKKFDQLLAEEKtisakyageRDRAEAEAREKETKalslaRALEEAME-QKAELERlNKQFRTEMEDLM 932
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERL---------RQEKEEKAREVERR-----RKLEEAEKaRQAEMDR-QAAIYAEQERMA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 933 SSKDdvgksvHELEKSkraleqQVEEMKTQLEELEGELQATEDAKLRlevnlQAMKAQFERdlqgrdeqseEKKKQLVRQ 1012
Cdd:pfam17380 344 MERE------RELERI------RQEERKRELERIRQEEIAMEISRMR-----ELERLQMER----------QQKNERVRQ 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1013 vremeaELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKE 1092
Cdd:pfam17380 397 ------ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1093 NEKKLKSmeaemiqlqeELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRR-LEARIAQLEEELEEEQGNTELIN 1171
Cdd:pfam17380 471 ERKRKKL----------ELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKlLEKEMEERQKAIYEEERRREAEE 540
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1172 DRLKKANL----QIDQINTDLNLERSHAQKNENARQQLeRQNKELKVKLQEMEG-----TVKSKYKASIT 1232
Cdd:pfam17380 541 ERRKQQEMeerrRIQEQMRKATEERSRLEAMEREREMM-RQIVESEKARAEYEAttpitTIKPIYRPRIS 609
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
944-1155 |
1.43e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 944 ELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQfERDLQGRDEQSEEKKKQLVRQVREMEAELEDE 1023
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1024 RKQ-RSMAVAARKKLEMDLKDLEAHIDSANknrdEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEA 1102
Cdd:COG4942 103 KEElAELLRALYRLGRQPPLALLLSPEDFL----DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 30268331 1103 EMIQLQEELAAAERAKRQAQQERDELAdeianssgkgalalEEKRRLEARIAQ 1155
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLE--------------KELAELAAELAE 217
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
720-1301 |
1.58e-07 |
|
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: 56.13 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 720 KVREKQLAAENRLTEMETLQSQLMAEKLQ-LQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHL 798
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQaKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 799 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTI 878
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 879 SAKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDlmsskddvGKSVHELEKSKRALEQQVEE 958
Cdd:pfam02463 337 IEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSS--------AAKLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 959 MKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLE 1038
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1039 MDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAK 1118
Cdd:pfam02463 489 LLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1119 RqaqqERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKN 1198
Cdd:pfam02463 569 A----LTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1199 ENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQvdDERR 1278
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE--AEEL 722
|
570 580
....*....|....*....|...
gi 30268331 1279 NAEQYKDQADKASTRLKQLKRQL 1301
Cdd:pfam02463 723 LADRVQEAQDKINEELKLLKQKI 745
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
799-1309 |
1.72e-07 |
|
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: 56.13 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 799 QAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTI 878
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 879 SAKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEE 958
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 959 MKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDE-------QSEEKKKQLVRQVREMEAELEDERKQRSMAV 1031
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEllakkklESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1032 AARK--------------KLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKD-----------------CMRELDDTR 1080
Cdd:pfam02463 413 LARQledllkeekkeeleILEEEEESIELKQGKLTEEKEELEKQELKLLKDELElkksedllketqlvklqEQLELLLSR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1081 ASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDEL---ADEIANSSGKGALALEEKRRLEARIAQLE 1157
Cdd:pfam02463 493 QKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENykvAISTAVIVEVSATADEVEERQKLVRALTE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1158 EELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAK 1237
Cdd:pfam02463 573 LPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGV 652
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30268331 1238 IAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQ 1309
Cdd:pfam02463 653 SLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA 724
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
944-1120 |
1.89e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.78 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 944 ELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDlqgrdeqseEKKKQLVRQVREMEA---EL 1020
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---------EEQLGNVRNNKEYEAlqkEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1021 EDERKQRSmavaarkklemdlkDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSM 1100
Cdd:COG1579 99 ESLKRRIS--------------DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
170 180
....*....|....*....|..
gi 30268331 1101 EAEMI-QLQEELAAA-ERAKRQ 1120
Cdd:COG1579 165 REELAaKIPPELLALyERIRKR 186
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
860-1297 |
1.95e-07 |
|
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: 55.80 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 860 NLEKKQKKFDQLLAE-----EKTISAKYAGERDRAEAEAREKEtkalslaraLEEAMEQKAELERLNKQFRTEMEDLMSS 934
Cdd:TIGR04523 233 NIEKKQQEINEKTTEisntqTQLNQLKDEQNKIKKQLSEKQKE---------LEQNNKKIKELEKQLNQLKSEISDLNNQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 935 KD-DVGKSVHElekskraleqQVEEMKTQLEELEGELQATEDAKLRLEVNLqamkAQFERDLQGRDEQSEEKKKQLvrqv 1013
Cdd:TIGR04523 304 KEqDWNKELKS----------ELKNQEKKLEEIQNQISQNNKIISQLNEQI----SQLKKELTNSESENSEKQREL---- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1014 REMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSA---NKNRDEAIKQL----RKLQAQMKDCMRELDDTRASREEI 1086
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQeklNQQKDEQIKKLqqekELLEKEIERLKETIIKNNSEIKDL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1087 LAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGN 1166
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1167 TELINDRLKKANLQIDQINTDLNlershAQKNENARQQLERQNKELKVKLQEMEGTVKSkYKASITALEAKIAQLEEQLD 1246
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELN-----KDDFELKKENLEKEIDEKNKEIEELKQTQKS-LKKKQEEKQELIDQKEKEKK 599
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 30268331 1247 NETKERQAACKQVRRTEKKLKDvllqVDDERRNAEQYKDQADKASTRLKQL 1297
Cdd:TIGR04523 600 DLIKEIEEKEKKISSLEKELEK----AKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
718-1216 |
2.52e-07 |
|
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: 55.50 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 718 LVKVREKqlaaENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTakkQELEEICHDLEARVEEEEERCQH 797
Cdd:pfam05483 246 LIQITEK----ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLT---KELEDIKMSLQRSMSTQKALEED 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 798 LQAEKKKMQQNIQELEEQLEEEESARQKLQLekVTTEAklkkleeelddllvdldhqRQSACNLEK----KQKKFDQLLA 873
Cdd:pfam05483 319 LQIATKTICQLTEEKEAQMEELNKAKAAHSF--VVTEF-------------------EATTCSLEEllrtEQQRLEKNED 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 874 EEKTISAKYAGERDRAEAEAREKETKALSLaRALEEAMEQKAELERLNKQFRTEMEDLMSSKDDV-------GKSVHELE 946
Cdd:pfam05483 378 QLKIITMELQKKSSELEEMTKFKNNKEVEL-EELKKILAEDEKLLDEKKQFEKIAEELKGKEQELifllqarEKEIHDLE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 947 -------KSKRALEQQVEEMKTQLEELE---GELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREM 1016
Cdd:pfam05483 457 iqltaikTSEEHYLKEVEDLKTELEKEKlknIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQI 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1017 EAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASRE------EILAQA 1090
Cdd:pfam05483 537 ENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEnknkniEELHQE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1091 KENEKKLKSMEAEMIQLQE-ELAAAERAKRQAQQERDELAD------EIANSSGKGALALEEKRRL---EARIAQLEEEL 1160
Cdd:pfam05483 617 NKALKKKGSAENKQLNAYEiKVNKLELELASAKQKFEEIIDnyqkeiEDKKISEEKLLEEVEKAKAiadEAVKLQKEIDK 696
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1161 EEEQGNTELINdRLKKANLQIDQI----NTDLNLERSHAQKNENARQQLERQNKELKVKL 1216
Cdd:pfam05483 697 RCQHKIAEMVA-LMEKHKHQYDKIieerDSELGLYKNKEQEQSSAKAALEIELSNIKAEL 755
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
868-1301 |
2.83e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 868 FDQLLAEEKTISAK-YAgerdRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDD--------- 937
Cdd:PRK04863 259 FKHLITESTNYVAAdYM----RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDleqdyqaas 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 938 ---------------VGKSVHELEKSKRALEQQ---VEEMKTQLEELEGELQATEDAKLRLEVNL----QAMKAQFERDL 995
Cdd:PRK04863 335 dhlnlvqtalrqqekIERYQADLEELEERLEEQnevVEEADEQQEENEARAEAAEEEVDELKSQLadyqQALDVQQTRAI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 996 QGRDE-QSEEKKKQL-------VRQVREMEAELEDERKQrsmAVAARKKLEMDLKDLEAhidsANKNRDEAIKQLRKLQA 1067
Cdd:PRK04863 415 QYQQAvQALERAKQLcglpdltADNAEDWLEEFQAKEQE---ATEELLSLEQKLSVAQA----AHSQFEQAYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1068 QMkdcmrelddtraSREEILAQAKENEKKLKSMEAEMIQLQE---ELAAAERAKRQaQQERDELADEIANSSGKGALALE 1144
Cdd:PRK04863 488 EV------------SRSEAWDVARELLRRLREQRHLAEQLQQlrmRLSELEQRLRQ-QQRAERLLAEFCKRLGKNLDDED 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1145 EKRRLEARIAQLEEeleeeqgntelindrlkkanlqidqintDLNLERSHAQKNenaRQQLERQNKELKVKLQEMEgtvk 1224
Cdd:PRK04863 555 ELEQLQEELEARLE----------------------------SLSESVSEARER---RMALRQQLEQLQARIQRLA---- 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1225 SKYKASITALEAkIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKAS-------TRLKQL 1297
Cdd:PRK04863 600 ARAPAWLAAQDA-LARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSqpggsedPRLNAL 678
|
....
gi 30268331 1298 KRQL 1301
Cdd:PRK04863 679 AERF 682
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
729-1132 |
7.08e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 729 ENRLTEMETLQSQLMAEKLQLQEQLQAETE---LCAEAEELRARLTAK-KQELEEICHDLEARVEEEEERCQHLQAEKKK 804
Cdd:PRK03918 337 EERLEELKKKLKELEKRLEELEERHELYEEakaKKEELERLKKRLTGLtPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 805 MQQNIQELEEQLEEEESARQK---------------------LQLEKVTTE-AKLKKLEEELddllvdldhqRQSACNLE 862
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAKGKcpvcgrelteehrkelleeytAELKRIEKElKEIEEKERKL----------RKELRELE 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 863 KKQKKFDQLLAEEKTISAKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRtEMEDLMSSKDDVGKSV 942
Cdd:PRK03918 487 KVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKL 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 943 HELEKSKRALEQQVEEMK-TQLEELEGELQATE----------DAKLRLEVNLQAMKaqferDLQGRDEQSEEKKKQLVR 1011
Cdd:PRK03918 566 DELEEELAELLKELEELGfESVEELEERLKELEpfyneylelkDAEKELEREEKELK-----KLEEELDKAFEELAETEK 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1012 QVREMEAELEDERKQRSMAVAARK-----KLEMDLKDLEAHIDSANKNRDEAIKQLRKLQaqmkdcmRELDDTRASREEI 1086
Cdd:PRK03918 641 RLEELRKELEELEKKYSEEEYEELreeylELSRELAGLRAELEELEKRREEIKKTLEKLK-------EELEEREKAKKEL 713
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 30268331 1087 laqakeneKKLKSMEAEMIQLQEELAAAE-RAKRQAQQERDELADEI 1132
Cdd:PRK03918 714 --------EKLEKALERVEELREKVKKYKaLLKERALSKVGEIASEI 752
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
863-1211 |
1.17e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 863 KKQKKFDQLLAEEKTISAKYAGERDRAEA-EAREKETKAL--SLARALEEAMEQKAELERLNKQF----RTEMEDLMSSK 935
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEElEERLEELRELeeELEELEAELAELQEELEELLEQLslatEEELQDLAEEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 936 DDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQ------- 1008
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlfl 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1009 ------LVRQVREMEAELEDERKQRSMAVAARKKLE-MDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRA 1081
Cdd:COG4717 282 vlgllaLLFLLLAREKASLGKEAEELQALPALEELEeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1082 SREeILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSG--KGALALEEKRRLEARIAQLEEE 1159
Cdd:COG4717 362 ELQ-LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGelEELLEALDEEELEEELEELEEE 440
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 30268331 1160 LEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKnENARQQLERQNKE 1211
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEEDGELAELLQEL-EELKAELRELAEE 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
911-1298 |
1.57e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.72 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 911 MEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELegelqatedakLRLEVNLQAMKAQ 990
Cdd:TIGR04523 92 KKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEI-----------KKKEKELEKLNNK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 991 FeRDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMA----------VAARKKLEMDLKDLEAHIDSANKNRDEAIK 1060
Cdd:TIGR04523 161 Y-NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLelllsnlkkkIQKNKSLESQISELKKQNNQLKDNIEKKQQ 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1061 QLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEEL----AAAERAKRQAQQERD-ELADEIANS 1135
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLnqlkSEISDLNNQKEQDWNkELKSELKNQ 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1136 SgkgalalEEKRRLEARIAQleeeleeeqgNTELINdrlkKANLQIDQINTDLNLERShaqKNENARQQLERQNKELKVK 1215
Cdd:TIGR04523 320 E-------KKLEEIQNQISQ----------NNKIIS----QLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEKL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1216 LQEmegtvKSKYKASITALEAKIAQLEEQLDNETKERQaackqvrrtekklkdvllQVDDERRNAEQYKDQADKASTRLK 1295
Cdd:TIGR04523 376 KKE-----NQSYKQEIKNLESQINDLESKIQNQEKLNQ------------------QKDEQIKKLQQEKELLEKEIERLK 432
|
...
gi 30268331 1296 QLK 1298
Cdd:TIGR04523 433 ETI 435
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
954-1298 |
2.31e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 51.95 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 954 QQVEEMKTQ-LEELEGELQATEDAKLRLEvnlqamKAQFErdlqgrdEQSEEKKKQLVR-QVREME------------AE 1019
Cdd:pfam05701 59 EAAEAAKAQvLEELESTKRLIEELKLNLE------RAQTE-------EAQAKQDSELAKlRVEEMEqgiadeasvaakAQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1020 LEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKqlrklqaqmkdcmrelddtRAsrEEILAQAKENEKKLKS 1099
Cdd:pfam05701 126 LEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIK-------------------RA--EEAVSASKEIEKTVEE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1100 MEAEMIQLQEELAAA-------------------------ERAKRQAQQERDELADEIANS-------SGKGALALEEKR 1147
Cdd:pfam05701 185 LTIELIATKESLESAhaahleaeehrigaalareqdklnwEKELKQAEEELQRLNQQLLSAkdlksklETASALLLDLKA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1148 RLEARIAQLEEELEEEQGNTELINDRLKKA-----------NLQIDQINTDLNLERSHAqknENARQQLERQNKELkVKL 1216
Cdd:pfam05701 265 ELAAYMESKLKEEADGEGNEKKTSTSIQAAlasakkeleevKANIEKAKDEVNCLRVAA---ASLRSELEKEKAEL-ASL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1217 QEMEGtvkskyKASITaleakIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQ 1296
Cdd:pfam05701 341 RQREG------MASIA-----VSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRK 409
|
..
gi 30268331 1297 LK 1298
Cdd:pfam05701 410 AK 411
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
720-1139 |
2.74e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 720 KVREKQLAAENRLTEMETLQSqlmAEKLQLQEQLQAETELCAEAEELRARLTAKKQE----LEEICHDLEARVEEEEERC 795
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKK---ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEeakkADEAKKAEEKKKADELKKA 1554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 796 QHLQA--EKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKkQKKFDQLLA 873
Cdd:PTZ00121 1555 EELKKaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE-LKKAEEEKK 1633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 874 EEKTISAKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKqfrtEMEDLMSSKDDVGKSVHELEKSKRaLE 953
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK----AEEDEKKAAEALKKEAEEAKKAEE-LK 1708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 954 QQVEEMKTQLEELEgelQATEDAKLRLEvnlQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAa 1033
Cdd:PTZ00121 1709 KKEAEEKKKAEELK---KAEEENKIKAE---EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI- 1781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1034 rkKLEMDLKDLEAHIDSANKNRD-----EAIKQLRKLQAQMKDCMRELDDTRA-----SREEILAQAKENEK-------- 1095
Cdd:PTZ00121 1782 --EEELDEEDEKRRMEVDKKIKDifdnfANIIEGGKEGNLVINDSKEMEDSAIkevadSKNMQLEEADAFEKhkfnknne 1859
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 30268331 1096 ------KLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKG 1139
Cdd:PTZ00121 1860 ngedgnKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAG 1909
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
853-1127 |
2.81e-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: 51.43 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 853 HQRQSACNLEKKQKKFDQL---LAEEKTisakyAGERDRAEAEAREKETKALSLARAlEEAMEQKAELERLNkqfrteme 929
Cdd:pfam07888 91 QSREKHEELEEKYKELSASseeLSEEKD-----ALLAQRAAHEARIRELEEDIKTLT-QRVLERETELERMK-------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 930 dlmsskddvgksvhelEKSKRALEQQVEEmKTQLEELEGELQATEDAKLRLEVNLQAMK-AQFERD-----LQGRDEQSE 1003
Cdd:pfam07888 157 ----------------ERAKKAGAQRKEE-EAERKQLQAKLQQTEEELRSLSKEFQELRnSLAQRDtqvlqLQDTITTLT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1004 EKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMdlkdLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTR-AS 1082
Cdd:pfam07888 220 QKLTTAHRKEAENEALLEELRSLQERLNASERKVEG----LGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASlAL 295
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 30268331 1083 REEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDE 1127
Cdd:pfam07888 296 REGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERME 340
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
949-1284 |
3.31e-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: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 949 KRALEQQVEEMKTQLEELegelqATEDAKLRLEVN-LQAMKAQFERDLQGR-----DEQSEEKKKQLVRQVREMEAELED 1022
Cdd:COG3096 780 RAAREKRLEELRAERDEL-----AEQYAKASFDVQkLQRLHQAFSQFVGGHlavafAPDPEAELAALRQRRSELERELAQ 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1023 ----ERKQRSMAVAARKKLEMdlkdLEAHIDSANKNRDEAikqlrkLQAQMKDCMRELDDTRASREEI------LAQAKE 1092
Cdd:COG3096 855 hraqEQQLRQQLDQLKEQLQL----LNKLLPQANLLADET------LADRLEELREELDAAQEAQAFIqqhgkaLAQLEP 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1093 NEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAN----SSGKGALALEEKR----RLEARIAQLEEELEEEq 1164
Cdd:COG3096 925 LVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRrphfSYEDAVGLLGENSdlneKLRARLEQAEEARREA- 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1165 gnteliNDRLKKANLQIDQINTDL-NLERSHAQKNENArQQLERQNKELKVKL-QEMEGTV---KSKYKASITALEAKIA 1239
Cdd:COG3096 1004 ------REQLRQAQAQYSQYNQVLaSLKSSRDAKQQTL-QELEQELEELGVQAdAEAEERArirRDELHEELSQNRSRRS 1076
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 30268331 1240 QLEEQLDNETKERQAACKQVRRTEKKLKdvllqvdDERRNAEQYK 1284
Cdd:COG3096 1077 QLEKQLTRCEAEMDSLQKRLRKAERDYK-------QEREQVVQAK 1114
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
897-1327 |
3.37e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 897 ETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKddvgksVHELEKSKRALEQQVEEMKTQLEELEGELQATEDA 976
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE------LEELRAELARLEAELERLEARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 977 klRLEVNLQAmKAQFERDLQGRDEQSEEKK---KQLVRQVREMEAELEDERKQrsmAVAARKKLEMDLKDLEAHIDSANK 1053
Cdd:COG4913 332 --IRGNGGDR-LEQLEREIERLERELEERErrrARLEALLAALGLPLPASAEE---FAALRAEAAALLEALEEELEALEE 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1054 NRDEAIKQLRKLQAQMKDCMRELDDTRAS-----------REEILAQAKENEKKLKSMeAEMIQLQEELA----AAERAK 1118
Cdd:COG4913 406 ALAEAEAALRDLRRELRELEAEIASLERRksniparllalRDALAEALGLDEAELPFV-GELIEVRPEEErwrgAIERVL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1119 R-----------------------------QAQQERDELADEIANSSGKGALA--LEEK-----RRLEARIAQLEE---- 1158
Cdd:COG4913 485 GgfaltllvppehyaaalrwvnrlhlrgrlVYERVRTGLPDPERPRLDPDSLAgkLDFKphpfrAWLEAELGRRFDyvcv 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1159 --ELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHA--QKNENARQQLERQNKELKVKLQEMEGTVKsKYKASITAL 1234
Cdd:COG4913 565 dsPEELRRHPRAITRAGQVKGNGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLE-ALEAELDAL 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1235 EAKIAQLE--EQLDNETKERQAACKQVRRTEKKLKDVLL----------QVDDERRNAEQYKDQADKASTRLKQLKRQLE 1302
Cdd:COG4913 644 QERREALQrlAEYSWDEIDVASAEREIAELEAELERLDAssddlaaleeQLEELEAELEELEEELDELKGEIGRLEKELE 723
|
490 500
....*....|....*....|....*
gi 30268331 1303 EAEEEAQRATPPAGNCSASWRTPLR 1327
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELR 748
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
722-1300 |
4.07e-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: 51.51 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 722 REKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEichDLEARVEEEEERCQHLQAE 801
Cdd:pfam02463 211 EYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLA---QVLKENKEEEKEKKLQEEE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 802 KKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAK 881
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 882 YAGERDRAEAEAREKETKALSLARALEEAMEQKAELER----LNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVE 957
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKeaqlLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLT 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 958 EMKTQLEELEGELQATEDAKLRLEVNLQamKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSM-------- 1029
Cdd:pfam02463 448 EEKEELEKQELKLLKDELELKKSEDLLK--ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKdgvggrii 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1030 -AVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKlksmeaemIQLQ 1108
Cdd:pfam02463 526 sAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKS--------IAVL 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1109 EELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDL 1188
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1189 NLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLK- 1267
Cdd:pfam02463 678 IQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRl 757
|
570 580 590
....*....|....*....|....*....|...
gi 30268331 1268 DVLLQVDDERRNAEQYKDQADKASTRLKQLKRQ 1300
Cdd:pfam02463 758 KKEEKEEEKSELSLKEKELAEEREKTEKLKVEE 790
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1040-1134 |
4.49e-06 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 50.84 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1040 DLKDLEAHIDS-----ANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEI---LAQAKENEKKLKSMEAEMIQLQEEL 1111
Cdd:PRK05431 3 DIKLIRENPEAvkealAKRGFPLDVDELLELDEERRELQTELEELQAERNALskeIGQAKRKGEDAEALIAEVKELKEEI 82
|
90 100
....*....|....*....|...
gi 30268331 1112 AAAERAKRQAQQERDELADEIAN 1134
Cdd:PRK05431 83 KALEAELDELEAELEELLLRIPN 105
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
944-1128 |
4.66e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 944 ELEKSKRALEQQVEEMKTQLEELEGELQA----------TEDAKLRLE--VNLQAMKAQFERDLQGRDEQSEEKKKQLVR 1011
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlSEEAKLLLQqlSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1012 QVREMEAELEDE-----RKQRSMAVAARKKLEM-------DLKDLEAHIDSANKNRDEAIKQ-LRKLQAQMkdcmRELDD 1078
Cdd:COG3206 252 GPDALPELLQSPviqqlRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRiLASLEAEL----EALQA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 30268331 1079 TRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDEL 1128
Cdd:COG3206 328 REASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
749-1301 |
4.82e-06 |
|
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: 51.27 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 749 LQEQLQAETELCAEAE-ELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQL-----EEEESA 822
Cdd:pfam15921 90 LQRRLNESNELHEKQKfYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKclkedMLEDSN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 823 RQKLQLEK-------VTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAGE----RDRAEA 891
Cdd:pfam15921 170 TQIEQLRKmmlshegVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRifpvEDQLEA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 892 EAREKETKALSLARALEEAMEQ--------------------------KAELERLNKQFRTEMEDLMSSKDDVGKSV--- 942
Cdd:pfam15921 250 LKSESQNKIELLLQQHQDRIEQliseheveitgltekassarsqansiQSQLEIIQEQARNQNSMYMRQLSDLESTVsql 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 943 -HELEKSKRALEQQVEEMKTQLEELEGELQA--TEDAKLRLEV-NLQAMKAQFERDLQGRDEQSEEKKKQLVR------- 1011
Cdd:pfam15921 330 rSELREAKRMYEDKIEELEKQLVLANSELTEarTERDQFSQESgNLDDQLQKLLADLHKREKELSLEKEQNKRlwdrdtg 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1012 ---QVREMEAELEDerkqRSMAVaarKKLEMDLKDLEAHID-------SANKNRDEAIKQLRKLQAQmkdcmreLDDTRA 1081
Cdd:pfam15921 410 nsiTIDHLRRELDD----RNMEV---QRLEALLKAMKSECQgqmerqmAAIQGKNESLEKVSSLTAQ-------LESTKE 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1082 SREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIanssgkgALALEEKRRLEARIAQLEEELE 1161
Cdd:pfam15921 476 MLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV-------DLKLQELQHLKNEGDHLRNVQT 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1162 EEQGNTELINDRLKKANLQIDQINTDLNLERSH---AQKNENARQQLERQNKELKVKLQEMEgTVKSKYKASITALEAKI 1238
Cdd:pfam15921 549 ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHgrtAGAMQVEKAQLEKEINDRRLELQEFK-ILKDKKDAKIRELEARV 627
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30268331 1239 AQLEEQ---LDNETKERQAACKQVRRTEKKLKDVLLQVDDERRN-AEQY-------KDQADKASTRLKQLKRQL 1301
Cdd:pfam15921 628 SDLELEkvkLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSlSEDYevlkrnfRNKSEEMETTTNKLKMQL 701
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
727-979 |
4.89e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 727 AAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELeeicHDLEARVEEEEERCQHLQAEKKKMQ 806
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI----RALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 807 QNIqeleeqleeeesARQKLQLEKVTTEAKLKKLEEELDDLLvdldhQRQSACNLEKKQKKFDQLLAEEKTISAKYAGER 886
Cdd:COG4942 97 AEL------------EAQKEELAELLRALYRLGRQPPLALLL-----SPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 887 DRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEEL 966
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
250
....*....|...
gi 30268331 967 EGELQATEDAKLR 979
Cdd:COG4942 240 AERTPAAGFAALK 252
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
899-1079 |
5.20e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.01 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 899 KALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSkddvgksvhELEKSKRALEQQVEEMKTQLEELEGELQATEDAKL 978
Cdd:COG2433 374 RGLSIEEALEELIEKELPEEEPEAEREKEHEERELT---------EEEEEIRRLEEQVERLEAEVEELEAELEEKDERIE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 979 RLEvnlqaMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKqrsmavaARKKLEMDLKDLEAHIDSANKNRDEA 1058
Cdd:COG2433 445 RLE-----RELSEARSEERREIRKDREISRLDREIERLERELEEERE-------RIEELKRKLERLKELWKLEHSGELVP 512
|
170 180
....*....|....*....|.
gi 30268331 1059 IKQLRKLQaqmKDCMRELDDT 1079
Cdd:COG2433 513 VKVVEKFT---KEAIRRLEEE 530
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1000-1155 |
5.78e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.67 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1000 EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDS--------ANKNRD----EAIKQLRKLQA 1067
Cdd:COG1842 19 DKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKweekarlaLEKGREdlarEALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1068 QMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLqeelaaaeRAKRQAQQERDELADEIANSSGKGALALEEkr 1147
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTL--------KARAKAAKAQEKVNEALSGIDSDDATSALE-- 168
|
....*...
gi 30268331 1148 RLEARIAQ 1155
Cdd:COG1842 169 RMEEKIEE 176
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
872-1027 |
6.39e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 872 LAEEKTISAKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEM-----------EDLMSSKDDVGK 940
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELqklekrllqkeENLDRKLELLEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 941 SVHELEKSKRALEQQVEEMKTQLEELEgELQATEDAKLRLEVNLQAMKAQfERDLQGRDEQSEEKKKQLVRQVrEMEAEL 1020
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELE-ELIEEQLQELERISGLTAEEAK-EILLEKVEEEARHEAAVLIKEI-EEEAKE 184
|
....*..
gi 30268331 1021 EDERKQR 1027
Cdd:PRK12704 185 EADKKAK 191
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
890-1301 |
9.14e-06 |
|
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: 49.85 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 890 EAEAREKETKALSLARALEE--AMEQKAELERLNKQFRTEMEDLMSSK-DDVGKSVHELE---------KSKRAL---EQ 954
Cdd:pfam06160 14 ELEERKNELMNLPVQEELSKvkKLNLTGETQEKFEEWRKKWDDIVTKSlPDIEELLFEAEelndkyrfkKAKKALdeiEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 955 QVEEMKTQLEELEGELQA--TEDAKLRLEVN-LQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELE--DERKQRSM 1029
Cdd:pfam06160 94 LLDDIEEDIKQILEELDEllESEEKNREEVEeLKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSqfEELTESGD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1030 AVAARK---KLEMDLKDLEAHIDS-------ANKNRDEAIKQLRKLQAQMK---------DCMRELDDTRASREEILAQA 1090
Cdd:pfam06160 174 YLEAREvleKLEEETDALEELMEDipplyeeLKTELPDQLEELKEGYREMEeegyalehlNVDKEIQQLEEQLEENLALL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1091 KEN-----EKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANssgkgalALEEKRRLEARIaqleeeleeeqg 1165
Cdd:pfam06160 254 ENLeldeaEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEH-------AEEQNKELKEEL------------ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1166 ntelinDRLKkanlQIDQINTDlnlERSHAQKNENARQQLERQNKELKVKLQEMEGT---VKSKYK---ASITALEAKIA 1239
Cdd:pfam06160 315 ------ERVQ----QSYTLNEN---ELERVRGLEKQLEELEKRYDEIVERLEEKEVAyseLQEELEeilEQLEEIEEEQE 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30268331 1240 QLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVddERRN----AEQYKDQADKASTRLKQLKRQL 1301
Cdd:pfam06160 382 EFKESLQSLRKDELEAREKLDEFKLELREIKRLV--EKSNlpglPESYLDYFFDVSDEIEDLADEL 445
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1058-1301 |
9.62e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 9.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1058 AIKQLRKLQAQMKDCMreLDDTRAsrEEILAQAKENEKKLKSMEAEMIQLQEELAAAERAkRQAQQERDELADEIAnssg 1137
Cdd:COG4913 202 SFKPIGDLDDFVREYM--LEEPDT--FEAADALVEHFDDLERAHEALEDAREQIELLEPI-RELAERYAAARERLA---- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1138 kgalaleEKRRLEARIaqleeeleeeqgntelindRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQ 1217
Cdd:COG4913 273 -------ELEYLRAAL-------------------RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1218 EMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRR-------TEKKLKDVLLQVDDERRNAEQ----YKDQ 1286
Cdd:COG4913 327 ELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAlglplpaSAEEFAALRAEAAALLEALEEeleaLEEA 406
|
250
....*....|....*
gi 30268331 1287 ADKASTRLKQLKRQL 1301
Cdd:COG4913 407 LAEAEAALRDLRREL 421
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
862-1243 |
1.01e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 862 EKKQKKFDQL---LAEEKTISAKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDV 938
Cdd:PRK01156 342 IKKKSRYDDLnnqILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDI 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 939 GKSVHELEKSKRALEQQVEEMKTQLEELEGE------------------LQATEDAKLRLEVNLQamkaQFERDLQGRDE 1000
Cdd:PRK01156 422 SSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttlgeeksnhiINHYNEKKSRLEEKIR----EIEIEVKDIDE 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1001 QSEEKKKQLVRQVREMEAELEDERKQRSmavAARKKLEmDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRE----- 1075
Cdd:PRK01156 498 KIVDLKKRKEYLESEEINKSINEYNKIE---SARADLE-DIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTswlna 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1076 --------LDDTRASREEILAQAKENEKKLKSMEAEMiqlqeelaaaERAKRQAQQERDELADEIANSSGKGALALEEKR 1147
Cdd:PRK01156 574 lavislidIETNRSRSNEIKKQLNDLESRLQEIEIGF----------PDDKSYIDKSIREIENEANNLNNKYNEIQENKI 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1148 RLEaRIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKY 1227
Cdd:PRK01156 644 LIE-KLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDIN 722
|
410
....*....|....*...
gi 30268331 1228 K--ASITALEAKIAQLEE 1243
Cdd:PRK01156 723 EtlESMKKIKKAIGDLKR 740
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
889-1137 |
1.06e-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: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 889 AEAEAREKETKALSLARALEEAmeqKAELERLNKQfrteMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEG 968
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAA---QAELDALQAE----LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 969 EL-------QATEDAKLRLEVNLQA-------MKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQrsmAVAAR 1034
Cdd:COG3883 87 ELgeraralYRSGGSVSYLDVLLGSesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1035 KKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAA 1114
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
250 260
....*....|....*....|...
gi 30268331 1115 ERAKRQAQQERDELADEIANSSG 1137
Cdd:COG3883 244 ASAAGAGAAGAAGAAAGSAGAAG 266
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
741-1218 |
1.12e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.97 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 741 QLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQniqeleeQLEEEE 820
Cdd:TIGR00618 167 ELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE-------ALQQTQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 821 SARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSAcNLEKKQKKFDQL-----LAEEKTISAKYAGERDRAEAEARE 895
Cdd:TIGR00618 240 QSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEA-VLEETQERINRArkaapLAAHIKAVTQIEQQAQRIHTELQS 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 896 KETKALSLARALEEAMEQKAELERLNKQFRT--EMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQ-- 971
Cdd:TIGR00618 319 KMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQsl 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 972 ATEDAKLRLEVNLQAMKAQFERDLQGrdeqseekkkQLVRQVREMEAELEDERKQRsmavAARKKLEMDLKDLEAHIDSA 1051
Cdd:TIGR00618 399 CKELDILQREQATIDTRTSAFRDLQG----------QLAHAKKQQELQQRYAELCA----AAITCTAQCEKLEKIHLQES 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1052 NKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLqEELAAAERAKRQAQQERDELADE 1131
Cdd:TIGR00618 465 AQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDI-DNPGPLTRRMQRGEQTYAQLETS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1132 IANSSGKGALALEEKRRLEariAQLEEELEEEQGNTELINdRLKKanlQIDQINTDLNLERSHAQKNENARQQLERQNKE 1211
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLK---EQMQEIQQSFSILTQCDN-RSKE---DIPNLQNITVRLQDLTEKLSEAEDMLACEQHA 616
|
....*..
gi 30268331 1212 LKVKLQE 1218
Cdd:TIGR00618 617 LLRKLQP 623
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
959-1148 |
1.44e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 959 MKTQLEELEgELQATEDAKLRLEVNLQAMKAQFERdlqgrdeqSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLE 1038
Cdd:COG1579 2 MPEDLRALL-DLQELDSELDRLEHRLKELPAELAE--------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1039 MDLKDLEAHIDSANKNRD-EAI-KQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAER 1116
Cdd:COG1579 73 ARIKKYEEQLGNVRNNKEyEALqKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA 152
|
170 180 190
....*....|....*....|....*....|..
gi 30268331 1117 AKRQAQQERDELADEIANSSGKGALALEEKRR 1148
Cdd:COG1579 153 ELEAELEELEAEREELAAKIPPELLALYERIR 184
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
902-1009 |
1.46e-05 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 46.54 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 902 SLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLE 981
Cdd:pfam11559 42 ELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLK 121
|
90 100
....*....|....*....|....*...
gi 30268331 982 VNLQAMKAQFERDLQGRDEQSEEKKKQL 1009
Cdd:pfam11559 122 NALQQIKTQFAHEVKKRDREIEKLKERL 149
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
914-1310 |
1.46e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.73 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 914 KAELERLNKQFRTEMEDLMSSKDDvGKSVHEleKSKRALEQQVEEMKTQLEELEGELQATEdaklrlevnlqamkaqfer 993
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNE-SNELHE--KQKFYLRQSVIDLQTKLQEMQMERDAMA------------------- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 994 DLQGRDEQSEEK-KKQLVRQVREMEAElederkqrsmavaarKKLEMDLKdleahidsanKNRDEAIKQLRKLQAQMKDC 1072
Cdd:pfam15921 131 DIRRRESQSQEDlRNQLQNTVHELEAA---------------KCLKEDML----------EDSNTQIEQLRKMMLSHEGV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1073 MREL-----DDTRASREEILAQAKENEKKLKSMEAEMIQLQEEL-AAAERAKRQAQQERDELADEIANSSGKGALALEEK 1146
Cdd:pfam15921 186 LQEIrsilvDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELdTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1147 R-RLEARIAQLEEELEeeqGNTElindRLKKANLQIDQINTDLnlershaqknENARQQLERQNKELKVKLQEMEGTV-- 1223
Cdd:pfam15921 266 QdRIEQLISEHEVEIT---GLTE----KASSARSQANSIQSQL----------EIIQEQARNQNSMYMRQLSDLESTVsq 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1224 -KSKYKASITALEAKIAQLEEQL---DNETKERQAACKQVRRTEKKLKDVL--LQVDDERR------NAEQYK---DQAD 1288
Cdd:pfam15921 329 lRSELREAKRMYEDKIEELEKQLvlaNSELTEARTERDQFSQESGNLDDQLqkLLADLHKRekelslEKEQNKrlwDRDT 408
|
410 420
....*....|....*....|..
gi 30268331 1289 KASTRLKQLKRQLEEAEEEAQR 1310
Cdd:pfam15921 409 GNSITIDHLRRELDDRNMEVQR 430
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
865-1086 |
1.47e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 49.26 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 865 QKKFDQLLAEEKTISAKYAGER-DRAEAEAREKE----TKALSLARALEEAMEQK--AELERLNKQFrtemEDLMSSKDD 937
Cdd:pfam05667 278 AELLSSFSGSSTTDTGLTKGSRfTHTEKLQFTNEapaaTSSPPTKVETEEELQQQreEELEELQEQL----EDLESSIQE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 938 VGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRL---EVNLQAMKAQFE---RDLQGRDEQSEEKKKQLV- 1010
Cdd:pfam05667 354 LEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLpdaEENIAKLQALVDasaQRLVELAGQWEKHRVPLIe 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1011 --RQVREMEAELEDERKQ------------RSMAVAARKKLEMdLKDLEAHIDSANK--NRD-------EAIKQLRKlqa 1067
Cdd:pfam05667 434 eyRALKEAKSNKEDESQRkleeikelrekiKEVAEEAKQKEEL-YKQLVAEYERLPKdvSRSaytrrilEIVKNIKK--- 509
|
250
....*....|....*....
gi 30268331 1068 QMKDCMRELDDTRASREEI 1086
Cdd:pfam05667 510 QKEEITKILSDTKSLQKEI 528
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
861-1020 |
1.55e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 861 LEKKQKKFDQLLAEEKTISAKYA---GERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKD- 936
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAeleDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 937 -DVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVRE 1015
Cdd:COG1579 92 eALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
....*
gi 30268331 1016 MEAEL 1020
Cdd:COG1579 172 IPPEL 176
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1085-1267 |
2.22e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1085 EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIanssgkgalaleekRRLEARIAQleeeleeeq 1164
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEI--------------KRLELEIEE--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1165 gntelINDRLKKANLQIDQINTdlNLERSHAQKNEnarQQLERQNKELKVKLQEMEGTVKSKyKASITALEAKIAQLEEQ 1244
Cdd:COG1579 71 -----VEARIKKYEEQLGNVRN--NKEYEALQKEI---ESLKRRISDLEDEILELMERIEEL-EEELAELEAELAELEAE 139
|
170 180
....*....|....*....|...
gi 30268331 1245 LDNETKERQAACKQVRRTEKKLK 1267
Cdd:COG1579 140 LEEKKAELDEELAELEAELEELE 162
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
514-538 |
2.86e-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: 2.86e-05
10 20
....*....|....*....|....*
gi 30268331 514 YKEQLAKLMATLRNTNPNFVRCIIP 538
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
729-1097 |
3.04e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.35 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 729 ENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQN 808
Cdd:pfam07888 79 ESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 809 IQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKKFDQLLAeektisakyAGERDR 888
Cdd:pfam07888 159 AKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT---------TAHRKE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 889 AEAEAREKETKALslaRALEEAMEQKAELerlnkqFRTEMEDLMSSKDdvgKSVHELEKSKraleQQVEEMKTQLEELeg 968
Cdd:pfam07888 230 AENEALLEELRSL---QERLNASERKVEG------LGEELSSMAAQRD---RTQAELHQAR----LQAAQLTLQLADA-- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 969 ELQATEDaklrlevnlQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQrsmavaaRKKLEMDLKDLEahi 1048
Cdd:pfam07888 292 SLALREG---------RARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERME-------REKLEVELGREK--- 352
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 30268331 1049 DSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKL 1097
Cdd:pfam07888 353 DCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1042-1290 |
3.42e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1042 KDLEAHIDSANKNRDeaikqlrkLQAQMKDCMRELDDTRASREEILAQAKENEkklksmeaemiQLQEELAAAERAKRQA 1121
Cdd:PRK11281 39 ADVQAQLDALNKQKL--------LEAEDKLVQQDLEQTLALLDKIDRQKEETE-----------QLKQQLAQAPAKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1122 QQERDELADEiANSSGKGALALEEKRRLEARIAQleeeleeeqgntelINDRLKKANLQIDQINTDL-----NLERSHAQ 1196
Cdd:PRK11281 100 QAELEALKDD-NDEETRETLSTLSLRQLESRLAQ--------------TLDQLQNAQNDLAEYNSQLvslqtQPERAQAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1197 KNENAR--QQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNET-------KERQAACKQVRRTEKKLK 1267
Cdd:PRK11281 165 LYANSQrlQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTqlqdllqKQRDYLTARIQRLEHQLQ 244
|
250 260
....*....|....*....|...
gi 30268331 1268 dvLLQVDDERRNAEQYKDQADKA 1290
Cdd:PRK11281 245 --LLQEAINSKRLTLSEKTVQEA 265
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
905-1310 |
3.84e-05 |
|
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: 48.20 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 905 RALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQvEEMKTQLEELEGELQATEdAKLRLEVNL 984
Cdd:pfam05557 190 KNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE-EKYREEAATLELEKEKLE-QELQSWVKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 985 QAMKAQFER---DLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRsmavaarKKLEMDLKDLEAHIDSANKNRDEAIKQ 1061
Cdd:pfam05557 268 AQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR-------RELEQELAQYLKKIEDLNKKLKRHKAL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1062 LRKLQAQMKDCMRELDDTRA---SREEILAQAKENEKKLKSME--AEMIQLQEELAAAERAkrqaqqeRDELADEIANSS 1136
Cdd:pfam05557 341 VRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEeaEDMTQKMQAHNEEMEA-------QLSVAEEELGGY 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1137 GKGALALEekRRLEARIAQLEEELeeeQGNTELINDRLKKANlqidqinTDLNLERshaqknenarQQLERQNKELKVKL 1216
Cdd:pfam05557 414 KQQAQTLE--RELQALRQQESLAD---PSYSKEEVDSLRRKL-------ETLELER----------QRLREQKNELEMEL 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1217 --QEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDderRNAEQYKDQADKastRL 1294
Cdd:pfam05557 472 erRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVL---RLPETTSTMNFK---EV 545
|
410
....*....|....*.
gi 30268331 1295 KQLKRQLEEAEEEAQR 1310
Cdd:pfam05557 546 LDLRKELESAELKNQR 561
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1007-1254 |
4.26e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1007 KQLVRQVREMEAELEDERKQRSMavaarkklemdLKDLEAHIDSANKNRDEAikqlrklqAQMKDCMRELDDTRASREEI 1086
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIEL-----------LEPIRELAERYAAARERL--------AELEYLRAALRLWFAQRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1087 LAQAKenekkLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGkgalaleekrrleARIAQLEEELEEEQGN 1166
Cdd:COG4913 292 LLEAE-----LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG-------------DRLEQLEREIERLERE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1167 TELINDRLKKANLQIDQINTDLNLErshaqknenaRQQLERQNKELKVKLQEMEgTVKSKYKASITALEAKIAQLEEQLD 1246
Cdd:COG4913 354 LEERERRRARLEALLAALGLPLPAS----------AEEFAALRAEAAALLEALE-EELEALEEALAEAEAALRDLRRELR 422
|
....*...
gi 30268331 1247 NETKERQA 1254
Cdd:COG4913 423 ELEAEIAS 430
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
999-1300 |
4.30e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 999 DEQSEEKKKQLVRQVREMEAELEDERKQRSmavaARKKLEMDLKDLEAHIDSANKNRDEAikqLRKLQAQMKDCMRELDD 1078
Cdd:PTZ00121 1090 DEATEEAFGKAEEAKKTETGKAEEARKAEE----AKKKAEDARKAEEARKAEDARKAEEA---RKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1079 TRasREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANssgkgALALEEKRRLEA-RIAQLE 1157
Cdd:PTZ00121 1163 AR--KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEE-----ARKAEDAKKAEAvKKAEEA 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1158 EELEEEQGNTEliNDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGT--VKSKYKASITALE 1235
Cdd:PTZ00121 1236 KKDAEEAKKAE--EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAeeKKKADEAKKKAEE 1313
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30268331 1236 AKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVllqvddERRNAEQYKDQADKASTRLKQLKRQ 1300
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEA------AKAEAEAAADEAEAAEEKAEAAEKK 1372
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
720-1152 |
4.37e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.30 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 720 KVREKQlaaENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEArveeeeercqHLQ 799
Cdd:pfam12128 475 RAREEQ---EAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLH----------FLR 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 800 AEKKKMQQNIQELEEQLEEEesaRQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACN--LEKKQKKFDQLLAEEKT 877
Cdd:pfam12128 542 KEAPDWEQSIGKVISPELLH---RTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEeeLRERLDKAEEALQSARE 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 878 ISAKYAGERDRAEAEArEKETKALSLAR-ALEEAMEqkaELERLNKQFRTEM----EDLMSSKDDVGKSVHELEKSKRAL 952
Cdd:pfam12128 619 KQAAAEEQLVQANGEL-EKASREETFARtALKNARL---DLRRLFDEKQSEKdkknKALAERKDSANERLNSLEAQLKQL 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 953 EQQVEEMKTQ---------------LEELEGELQATED----AKLRLEVN----LQAMKAQFERDLQGRDeQSEEKKKQL 1009
Cdd:pfam12128 695 DKKHQAWLEEqkeqkreartekqayWQVVEGALDAQLAllkaAIAARRSGakaeLKALETWYKRDLASLG-VDPDVIAKL 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1010 VRQVREMEAELEDERKQRSMAV-------------------------AARKKLEMDLKDLEAHIDSANKNRDEAIKQLRK 1064
Cdd:pfam12128 774 KREIRTLERKIERIAVRRQEVLryfdwyqetwlqrrprlatqlsnieRAISELQQQLARLIADTKLRRAKLEMERKASEK 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1065 LQAQMKDCMRELDDtRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALE 1144
Cdd:pfam12128 854 QQVRLSENLRGLRC-EMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETW 932
|
....*...
gi 30268331 1145 EKRRLEAR 1152
Cdd:pfam12128 933 ESLREEDH 940
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
737-1152 |
5.22e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 737 TLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLeARVEEEEErcqhlQAEK-KKMQQNIQELEEQ 815
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHL-NLVQTALR-----QQEKiERYQADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 816 LEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKKFDQ---LLAEEKT------ISAKYAGER 886
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQavqALERAKQlcglpdLTADNAEDW 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 887 dRAEAEAREKE--TKALSLARAL---EEAMEQKAELERLNKQFRTEMEdlMSSKDDVGKSVHELEKSKRALEQQVEEMKT 961
Cdd:PRK04863 444 -LEEFQAKEQEatEELLSLEQKLsvaQAAHSQFEQAYQLVRKIAGEVS--RSEAWDVARELLRRLREQRHLAEQLQQLRM 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 962 QLEELEGElqatedakLRLEVNLQAMKAQFERDLqGRDEQSEEKKKQLvrqVREMEAELEDERKQRSMAVAARKKLEMDL 1041
Cdd:PRK04863 521 RLSELEQR--------LRQQQRAERLLAEFCKRL-GKNLDDEDELEQL---QEELEARLESLSESVSEARERRMALRQQL 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1042 KDLEAHidsanknrdeaIKQLRKLQAQmkdcMRELDDTRASREEILAQAKENEkklKSMEAEMIQLQEELAAAERAKRQA 1121
Cdd:PRK04863 589 EQLQAR-----------IQRLAARAPA----WLAAQDALARLREQSGEEFEDS---QDVTEYMQQLLERERELTVERDEL 650
|
410 420 430
....*....|....*....|....*....|.
gi 30268331 1122 QQERDELADEIANSSGKGALALEEKRRLEAR 1152
Cdd:PRK04863 651 AARKQALDEEIERLSQPGGSEDPRLNALAER 681
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1053-1311 |
5.42e-05 |
|
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: 47.74 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1053 KNRDEAIKQLRKLQ---AQMKDCMRELD------DTRASREEILA--QAKENEKKLKSMEAEMIQLQEELAAAERAKRQA 1121
Cdd:TIGR02168 172 ERRKETERKLERTRenlDRLEDILNELErqlkslERQAEKAERYKelKAELRELELALLVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1122 QQERDELADEIANSSGKGALALEEKRRLEARIAQLeeeleeeQGNTELINDRLKKANLQIDQINtdlnlershaqkneNA 1201
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEEL-------QKELYALANEISRLEQQKQILR--------------ER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1202 RQQLERQNKELKVKLQEMEgtvkskykASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAE 1281
Cdd:TIGR02168 311 LANLERQLEELEAQLEELE--------SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
250 260 270
....*....|....*....|....*....|
gi 30268331 1282 QYKDQADKASTRLKQLKRQLEEAEEEAQRA 1311
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERL 412
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
720-1033 |
7.00e-05 |
|
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: 46.98 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 720 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQaetELCAEAEELRARLTAKKQELEeichDLEARVEEEEERCQHLQ 799
Cdd:pfam19220 66 KLRRELAGLTRRLSAAEGELEELVARLAKLEAALR---EAEAAKEELRIELRDKTAQAE----ALERQLAAETEQNRALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 800 AEKK----KMQQNIQELEEQLEEEESARQKLQLekvTTEAKLKKLEEELDDLLVDLDHQRQSAcNLEKKQKKFDQLLAEE 875
Cdd:pfam19220 139 EENKalreEAQAAEKALQRAEGELATARERLAL---LEQENRRLQALSEEQAAELAELTRRLA-ELETQLDATRARLRAL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 876 KTISAKYAGERDRAEAEAREK----ETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRA 951
Cdd:pfam19220 215 EGQLAAEQAERERAEAQLEEAveahRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDT 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 952 LEQQVEEMKTQLEELEGELQATEDAKLRLEVN-------LQAMKAQFER------DLQGRDEQS----EEKKKQLVRQVR 1014
Cdd:pfam19220 295 LERRLAGLEADLERRTQQFQEMQRARAELEERaemltkaLAAKDAALERaeeriaSLSDRIAELtkrfEVERAALEQANR 374
|
330
....*....|....*....
gi 30268331 1015 EMEAELEDERKQRSMAVAA 1033
Cdd:pfam19220 375 RLKEELQRERAERALAQGA 393
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
820-1102 |
7.25e-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: 47.43 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 820 ESARQklqlekvtTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAGERDRAEAEAREKETK 899
Cdd:pfam17380 322 EKARQ--------AEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNER 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 900 ALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKsvhelEKSKRALEQQVEEM-KTQLEELEGELQAtedAKL 978
Cdd:pfam17380 394 VRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ-----REVRRLEEERAREMeRVRLEEQERQQQV---ERL 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 979 RL-EVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVRE-MEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRD 1056
Cdd:pfam17380 466 RQqEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEErKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQ 545
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 30268331 1057 EAIKQLRKLQAQMKDCMRELD--DTRASREEILAQAKENEKKLKSMEA 1102
Cdd:pfam17380 546 QEMEERRRIQEQMRKATEERSrlEAMEREREMMRQIVESEKARAEYEA 593
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
854-1267 |
8.29e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 854 QRQSACNLEKKQKKFDQLLAeektISAKYAGERDRAEAEAREKETKALSLARaleEAMEQKAELERLNKQFRTEMEDLMS 933
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEMLG----LAPGRQSIIDLKEKEIPELRNKLQKVNR---DIQRLKNDIEEQETLLGTIMPEEES 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 934 SKD---DVGksvhelekSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERD-----LQGRDEQSEEK 1005
Cdd:TIGR00606 784 AKVcltDVT--------IMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDtvvskIELNRKLIQDQ 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1006 KKQlVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMrelddtraSREE 1085
Cdd:TIGR00606 856 QEQ-IQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ--------QEKE 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1086 ILAQAKENEKKLKSMEAEMI--QLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIaQLEEELEEE 1163
Cdd:TIGR00606 927 ELISSKETSNKKAQDKVNDIkeKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKI-NEDMRLMRQ 1005
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1164 QGNTELINDRLKKANLQIDQINTDLnlershaqknenarQQLERQNKELKVKLQEMEgtvkskykasITALEAKIAQLEE 1243
Cdd:TIGR00606 1006 DIDTQKIQERWLQDNLTLRKRENEL--------------KEVEEELKQHLKEMGQMQ----------VLQMKQEHQKLEE 1061
|
410 420
....*....|....*....|....
gi 30268331 1244 QLDNETKERQAACKQVRRTEKKLK 1267
Cdd:TIGR00606 1062 NIDLIKRNHVLALGRQKGYEKEIK 1085
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
718-1311 |
8.58e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 718 LVKVREKQL-AAENRLTEMETLQSQLMaeklQLQEQLQAETELCAEAEELRARLTAKK--------QELEEICHDLEARV 788
Cdd:TIGR00606 239 IVKSYENELdPLKNRLKEIEHNLSKIM----KLDNEIKALKSRKKQMEKDNSELELKMekvfqgtdEQLNDLYHNHQRTV 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 789 EEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLE-KVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKK 867
Cdd:TIGR00606 315 REKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQaDRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 868 FDQLLAEEKTISAKYAGERdraEAEAREKETKAlslARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELE- 946
Cdd:TIGR00606 395 FHTLVIERQEDEAKTAAQL---CADLQSKERLK---QEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEg 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 947 KSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEE----------------KKKQLV 1010
Cdd:TIGR00606 469 SSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQlnhhtttrtqmemltkDKMDKD 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1011 RQVREMEAELEDE----------RKQRSMAVAARKK----LEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMREL 1076
Cdd:TIGR00606 549 EQIRKIKSRHSDEltsllgyfpnKKQLEDWLHSKSKeinqTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1077 DDTRASRE-----EILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQ--------QERDELADEIANSSGKGALAL 1143
Cdd:TIGR00606 629 FDVCGSQDeesdlERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCcpvcqrvfQTEAELQEFISDLQSKLRLAP 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1144 EEKRRLEARIAQLEEELEE-------EQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNEnarQQLERQNKELK-VK 1215
Cdd:TIGR00606 709 DKLKSTESELKKKEKRRDEmlglapgRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE---TLLGTIMPEEEsAK 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1216 LQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKER--QAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTR 1293
Cdd:TIGR00606 786 VCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRtvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK 865
|
650
....*....|....*...
gi 30268331 1294 LKQLKRQLEEAEEEAQRA 1311
Cdd:TIGR00606 866 TNELKSEKLQIGTNLQRR 883
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1040-1134 |
9.35e-05 |
|
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 46.54 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1040 DLKDLEAHIDS-----ANKNRDEAIKQLRKLQAQMKDCMRELDDTRASR----EEIlAQAKENEKKLKSMEAEMIQLQEE 1110
Cdd:COG0172 3 DIKLIRENPEAvkealAKRGFDLDVDELLELDEERRELQTEVEELRAERnalsKEI-GKAKKKGEEAEALIAEVKELKEE 81
|
90 100
....*....|....*....|....
gi 30268331 1111 LAAAERAKRQAQQERDELADEIAN 1134
Cdd:COG0172 82 IKELEEELKELEEELDELLLSIPN 105
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
721-1013 |
9.69e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 721 VREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETElcaEAEELRARL--------TAKKQELEEICHDLEARVEEEE 792
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE---ALNDLEARLshsripeiQAELSKLEEEVSRIEARLREIE 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 793 ERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKKFDQLL 872
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 873 AEEKTisakyagERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSkDDVGKSVHELEKSKRAL 952
Cdd:TIGR02169 899 RELER-------KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQRVEEEIRAL 970
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30268331 953 E-------QQVEEMKTQLEELEGELqatedAKLRLEvnlqamkaqfERDLQGRDEQSEEKKKQLVRQV 1013
Cdd:TIGR02169 971 EpvnmlaiQEYEEVLKRLDELKEKR-----AKLEEE----------RKAILERIEEYEKKKREVFMEA 1023
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1010-1299 |
1.01e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1010 VRQVREMEAELEDERKQRSMAVAA----RKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREE 1085
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEElkekRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1086 ILAQAKENEKKLKSMEAEMiqlqEELAAAERAKRQAQQERDELADEIANSSgkgaLALEEKRRLEARIAQLEEELEEEQg 1165
Cdd:COG1340 83 LNEKLNELREELDELRKEL----AELNKAGGSIDKLRKEIERLEWRQQTEV----LSPEEEKELVEKIKELEKELEKAK- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1166 ntelindRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKsKYKASITALEAKIAQLEEQL 1245
Cdd:COG1340 154 -------KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAD-ELRKEADELHKEIVEAQEKA 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 30268331 1246 DNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQyKDQADKASTRLKQLKR 1299
Cdd:COG1340 226 DELHEEIIELQKELRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEKLKK 278
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
949-1121 |
1.07e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 949 KRALEQQVEEMKTQ----LEELEGELQATEDAKLrLEVN--LQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEAELED 1022
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1023 ERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLqAQMkdcmrelddtraSREEILAQAKEN-EKKLKSME 1101
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI-SGL------------TAEEAKEILLEKvEEEARHEA 171
|
170 180
....*....|....*....|
gi 30268331 1102 AEMIQLQEELAAAErAKRQA 1121
Cdd:PRK12704 172 AVLIKEIEEEAKEE-ADKKA 190
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1025-1285 |
1.12e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1025 KQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEM 1104
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1105 IQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRL--KKANLQID 1182
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1183 QINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRT 1262
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260
....*....|....*....|...
gi 30268331 1263 EKKLKDVLLQVDDERRNAEQYKD 1285
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAAL 293
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
886-1151 |
1.43e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 886 RDRAEAEAREKETKALSLARALEEAMEQkaeLERLNKQFRTEMEDLMS-SKDDVGKSVHELEKSKRALEQQVEEMKTQLE 964
Cdd:PRK05771 34 EDLKEELSNERLRKLRSLLTKLSEALDK---LRSYLPKLNPLREEKKKvSVKSLEELIKDVEEELEKIEKEIKELEEEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 965 ELEGELQATEDAKLRLEVnLQAMKAQFERDLQGR---------DEQSEEKKKQLVRQVremEAELEDERKQRSMAVAArk 1035
Cdd:PRK05771 111 ELENEIKELEQEIERLEP-WGNFDLDLSLLLGFKyvsvfvgtvPEDKLEELKLESDVE---NVEYISTDKGYVYVVVV-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1036 klemdlkdleahidSANKNRDEAIKQLRKLQAQMKdcmrELDDTRASREEIlaqaKENEKKLKSMEAEMIQLQEELAAae 1115
Cdd:PRK05771 185 --------------VLKELSDEVEEELKKLGFERL----ELEEEGTPSELI----REIKEELEEIEKERESLLEELKE-- 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 30268331 1116 rakrqaqqERDELADEIANSSGkgaLALEEKRRLEA 1151
Cdd:PRK05771 241 --------LAKKYLEELLALYE---YLEIELERAEA 265
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
720-1301 |
1.44e-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: 46.50 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 720 KVREKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEIchdLEARVEEEEERCQHLQ 799
Cdd:pfam02463 261 EKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK---EKKKAEKELKKEKEEI 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 800 AEKKKM----------QQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDH--QRQSACNLEKKQKK 867
Cdd:pfam02463 338 EELEKElkeleikreaEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSeeEKEAQLLLELARQL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 868 FDQLLAEEKTISAKYAGERDRAEAEAR-------EKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGK 940
Cdd:pfam02463 418 EDLLKEEKKEELEILEEEEESIELKQGklteekeELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 941 SVH------ELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLqamKAQFERDLQGRDEQSEEKKKQLVRQVR 1014
Cdd:pfam02463 498 RSQkeskarSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIST---AVIVEVSATADEVEERQKLVRALTELP 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1015 EMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENE 1094
Cdd:pfam02463 575 LGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSL 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1095 KKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNTEL----I 1170
Cdd:pfam02463 655 EEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEaqdkI 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1171 NDRLKKANLQIDQINTDLNLERSHAQKNENARQQL--------ERQNKELKVKLQEMEGTVKSKYKASITALEAKiAQLE 1242
Cdd:pfam02463 735 NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELslkekelaEEREKTEKLKVEEEKEEKLKAQEEELRALEEE-LKEE 813
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 30268331 1243 EQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQL 1301
Cdd:pfam02463 814 AELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQEL 872
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
861-1140 |
1.70e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 46.00 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 861 LEKKQKKFDQllaeEKTISAKYAGERDRAEAeAREKETKALSLARALEEAMEQKaeLERLNKQFRTEMED---LMSSKDD 937
Cdd:PLN03229 464 IEKLKKEIDL----EYTEAVIAMGLQERLEN-LREEFSKANSQDQLMHPVLMEK--IEKLKDEFNKRLSRapnYLSLKYK 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 938 VGKsVHELEKSKRALEQqveemKTQLEELEGEL-QATEDAKLRLEV--NLQAMKAQFERD-LQGRDEQSEEKKKQLVRQV 1013
Cdd:PLN03229 537 LDM-LNEFSRAKALSEK-----KSKAEKLKAEInKKFKEVMDRPEIkeKMEALKAEVASSgASSGDELDDDLKEKVEKMK 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1014 REMEAELEDERKQRSMAVAARKKLEMDLK------DLEAHIDSANKNRDEAIKQLRKlQAQMKDCMREL--DDTRASREE 1085
Cdd:PLN03229 611 KEIELELAGVLKSMGLEVIGVTKKNKDTAeqtpppNLQEKIESLNEEINKKIERVIR-SSDLKSKIELLklEVAKASKTP 689
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 30268331 1086 ILAQAkeneKKLKSMEAemiQLQEELAAAERAKrQAQQERDELADEIANSSGKGA 1140
Cdd:PLN03229 690 DVTEK----EKIEALEQ---QIKQKIAEALNSS-ELKEKFEELEAELAAARETAA 736
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1033-1300 |
1.76e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1033 ARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELa 1112
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1113 aaeRAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQleeeLEEEQGNTELINDRLKKANLQIDQINTDLNlER 1192
Cdd:COG1340 81 ---DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIER----LEWRQQTEVLSPEEEKELVEKIKELEKELE-KA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1193 SHAQKNENARQQLERQNKELKVKLQEMEGTVKsKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQ 1272
Cdd:COG1340 153 KKALEKNEKLKELRAELKELRKEAEEIHKKIK-ELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEE 231
|
250 260
....*....|....*....|....*...
gi 30268331 1273 VDDERRNAEQYKDQADKASTRLKQLKRQ 1300
Cdd:COG1340 232 IIELQKELRELRKELKKLRKKQRALKRE 259
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1074-1294 |
2.13e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1074 RELDDTRASREEILAQAKENEKK-----LKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKgalaLEEKRR 1148
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEEKdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER----REELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1149 LEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLN-------LERSHAQKNENARQQLERQNKELKVKLQEmEG 1221
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDdllaeagLDDADAEAVEARREELEDRDEELRDRLEE-CR 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30268331 1222 TVKSKYKASITALEAKIAQLEEQldNETKERQAAckqvrRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRL 1294
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEER--AEELREEAA-----ELESELEEAREAVEDRREEIEELEEEIEELRERF 400
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
888-1296 |
2.14e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 888 RAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDD------------------------VGKSVH 943
Cdd:COG3096 275 RHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDleqdyqaasdhlnlvqtalrqqekIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 944 ELEKSKRALEQQ---VEEMKTQLEELEGELQATEDAKLRLEVNL----QAMKAQFERDLQGRDE-QSEEKKKQL------ 1009
Cdd:COG3096 355 DLEELTERLEEQeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyqQALDVQQTRAIQYQQAvQALEKARALcglpdl 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1010 -VRQVREMEAELEDERKQRSMAV-AARKKLEMDlkdleahiDSANKNRDEAIKQLRKLQAQMkdcmrELDDTRASREEIL 1087
Cdd:COG3096 435 tPENAEDYLAAFRAKEQQATEEVlELEQKLSVA--------DAARRQFEKAYELVCKIAGEV-----ERSQAWQTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1088 AQAKEnekkLKSMEAEMIQLQEELAAAERAKRQaQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNt 1167
Cdd:COG3096 502 RRYRS----QQALAQRLQQLRAQLAELEQRLRQ-QQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAE- 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1168 elindrlkkanlQIDQintdlnlershaqknenaRQQLERQNKELKVKLQEMEgtvkSKYKASITALEAkIAQLEEQLDN 1247
Cdd:COG3096 576 ------------AVEQ------------------RSELRQQLEQLRARIKELA----ARAPAWLAAQDA-LERLREQSGE 620
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 30268331 1248 ETKERQAACKQVRRTEKKLKdvllQVDDERRNAEQYKDQADKASTRLKQ 1296
Cdd:COG3096 621 ALADSQEVTAAMQQLLERER----EATVERDELAARKQALESQIERLSQ 665
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
912-1060 |
2.93e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 45.44 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 912 EQKAELERLNKQfrtEMEDLMSSKDDVgksVHELEKSKRALEQ---QVEEMKTQLEELEGELQATEDAKLRLEVNLQAMK 988
Cdd:pfam05911 677 DLKTEENKRLKE---EFEQLKSEKENL---EVELASCTENLEStksQLQESEQLIAELRSELASLKESNSLAETQLKCMA 750
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30268331 989 AQFErDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIK 1060
Cdd:pfam05911 751 ESYE-DLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKKESSNCDADQEDKK 821
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
854-1064 |
3.13e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 854 QRQSACNLEKKQKKFDQLLAEEKTISAkyagERDRAEAEareketkalslarALEEAMEQKAELERLNKqFRTEMEDLMS 933
Cdd:PHA02562 208 RKKNGENIARKQNKYDELVEEAKTIKA----EIEELTDE-------------LLNLVMDIEDPSAALNK-LNTAAAKIKS 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 934 SKDDVGKSVHELEKS------KRALEQQ---VEEMKTQLEELEGELQATEDAklrlevnlqamkaqferdlQGRDEQSEE 1004
Cdd:PHA02562 270 KIEQFQKVIKMYEKGgvcptcTQQISEGpdrITKIKDKLKELQHSLEKLDTA-------------------IDELEEIMD 330
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1005 KKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAhidsANKNRDEAIKQLRK 1064
Cdd:PHA02562 331 EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA----EFVDNAEELAKLQD 386
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
899-1140 |
3.62e-04 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 44.98 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 899 KALSLAR-ALEEAMEQKA---ELERLNKQFRTEMEDLMsskddvgksvhelekskRALEQQVEEMKTQLEELEGELQATE 974
Cdd:pfam13779 489 RRLRAAQeRLSEALERGAsdeEIAKLMQELREALDDYM-----------------QALAEQAQQNPQDLQQPDDPNAQEM 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 975 DAKlrlevNLQAMKAQFERDLQ-GRDEQSEekkkQLVRQVREMEAELEDERKQRSMAVAARKKLEMdLKDLEAHIDSANK 1053
Cdd:pfam13779 552 TQQ-----DLQRMLDRIEELARsGRRAEAQ----QMLSQLQQMLENLQAGQPQQQQQQGQSEMQQA-MDELGDLLREQQQ 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1054 NRDEAIKQLRKLQAQmkdcmrelDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQ--QERDELADE 1131
Cdd:pfam13779 622 LLDETFRQLQQQGGQ--------QQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEALGDLAERQQAlrRRLEELQDE 693
|
....*....
gi 30268331 1132 IANSSGKGA 1140
Cdd:pfam13779 694 LKELGGKEP 702
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1000-1136 |
3.70e-04 |
|
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: 43.51 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1000 EQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRD------------EAIKQLRKLQA 1067
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQaaltkgneelarEALAEKKSLEK 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30268331 1068 QMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAeRAKRQAQQERDELADEIANSS 1136
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAA-KAQEAVQTSLGSLSTSSATDS 165
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
944-1129 |
4.61e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.07 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 944 ELEKSKRALEQQVEEMKTQLEELEGELQATEDAKlrlevnlQAMKAqferdlqgrDEQSEEKKKQlvrqVREMEAELEDE 1023
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK-------QAEQA---------AKQAEEKQKQ----AEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1024 RKQRSMAVAARKKLEmdlkdleahiDSANKNRDEAIKqlrKLQAQMKdcmRELDDTRASREEILAQAKENEKKLKSMEAE 1103
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180
....*....|....*....|....*.
gi 30268331 1104 MIQLQEELAAAERAKRQAQQERDELA 1129
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAA 221
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
993-1312 |
4.97e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 993 RDLQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDC 1072
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1073 MRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSsgkgalALEEKRRLEAR 1152
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ------ALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1153 IAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASIT 1232
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1233 ALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRAT 1312
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDND 354
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1010-1316 |
5.07e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.83 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1010 VRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDtrASREEILAQ 1089
Cdd:pfam12128 236 IMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRD--ELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1090 akenEKKLKSMEAEMIQLQEELAAAERA---KRQAQQER-DELADEIANSSGKGALALEEKRRLEARIaQLEEELEEEQG 1165
Cdd:pfam12128 314 ----DAAVAKDRSELEALEDQHGAFLDAdieTAAADQEQlPSWQSELENLEERLKALTGKHQDVTAKY-NRRRSKIKEQN 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1166 NTEL--INDRLKKanlQIDQINTDLNLERSHAQKNENA-RQQLERQNKELKvklqEMEGTVKSKYKASITALEAKIAQLE 1242
Cdd:pfam12128 389 NRDIagIKDKLAK---IREARDRQLAVAEDDLQALESElREQLEAGKLEFN----EEEYRLKSRLGELKLRLNQATATPE 461
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30268331 1243 EQLDNETKerQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADK----ASTRLKQLKRQLeeaEEEAQRATPPAG 1316
Cdd:pfam12128 462 LLLQLENF--DERIERAREEQEAANAEVERLQSELRQARKRRDQASEalrqASRRLEERQSAL---DELELQLFPQAG 534
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
884-1124 |
5.61e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 884 GERDRAEAEAREKETKALSLARALEEAMEQkaeLERLNKQFRT-EMEDLMSSKDDVGKSVHELEKSKRALEQ------QV 956
Cdd:COG3096 846 SELERELAQHRAQEQQLRQQLDQLKEQLQL---LNKLLPQANLlADETLADRLEELREELDAAQEAQAFIQQhgkalaQL 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 957 EEMKT-------QLEELEGELQATEDAKLRLEVNLQAMKAQFER-------DLQGRDEQSEEKKKQLVRQVREMEAELed 1022
Cdd:COG3096 923 EPLVAvlqsdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRrphfsyeDAVGLLGENSDLNEKLRARLEQAEEAR-- 1000
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1023 eRKQRSMAVAARKKLEmdlkDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDT-----RASREEILAQAKEN---- 1093
Cdd:COG3096 1001 -REAREQLRQAQAQYS----QYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEaeeraRIRRDELHEELSQNrsrr 1075
|
250 260 270
....*....|....*....|....*....|....
gi 30268331 1094 ---EKKLKSMEAEMIQLQEELAAAERAKRQAQQE 1124
Cdd:COG3096 1076 sqlEKQLTRCEAEMDSLQKRLRKAERDYKQEREQ 1109
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
661-1111 |
6.50e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 661 KAFAKRQQQLTAMKVLQRNCAAY-----LKLRNWQWWRLFTKVKPLLQVSRQEEEMMAKEEELVKVREKQLaaeNRLTEM 735
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCAAAITctaqcEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARL---LELQEE 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 736 ETL---QSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQEL 812
Cdd:TIGR00618 503 PCPlcgSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRS 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 813 EEQLEEEESARQKLQLEkVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAGE---RDRA 889
Cdd:TIGR00618 583 KEDIPNLQNITVRLQDL-TEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTltqERVR 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 890 EAEAREKETKALSLARALEEAMEQKAELERLN------KQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQL 963
Cdd:TIGR00618 662 EHALSIRVLPKELLASRQLALQKMQSEKEQLTywkemlAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAL 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 964 EELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEaelEDERKQRSMAVAARKKLEMDLKD 1043
Cdd:TIGR00618 742 NQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLRE---EDTHLLKTLEAEIGQEIPSDEDI 818
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30268331 1044 LEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELddtrasreEILAQAKENEKKLKSMEAEMIQLQEEL 1111
Cdd:TIGR00618 819 LNLQCETLVQEEEQFLSRLEEKSATLGEITHQL--------LKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
701-1287 |
8.45e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 701 LLQVSRQEEEMMAKEEELVKVREKQLAAENRLTEMETLQSQLMAEKLQLQ---EQLQAETELCAEAEELRARLTAKKQEL 777
Cdd:TIGR00618 347 LQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQslcKELDILQREQATIDTRTSAFRDLQGQL 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 778 EEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQS 857
Cdd:TIGR00618 427 AHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 858 ACNLEKKQKKFDQLLAEEKTISAKYAGERDRAEAEAREKETKAlSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDD 937
Cdd:TIGR00618 507 CGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH-QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 938 VGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQamKAQFERDLQGRD--------EQSEEKKKQL 1009
Cdd:TIGR00618 586 IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH--LQQCSQELALKLtalhalqlTLTQERVREH 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1010 VRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQ 1089
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ 743
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1090 A-KENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQGNT- 1167
Cdd:TIGR00618 744 SlKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQc 823
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1168 ELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKvKLQEMEGTVKSKYKASITALEAKIAQLEEQLDn 1247
Cdd:TIGR00618 824 ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQA-KIIQLSDKLNGINQIKIQFDGDALIKFLHEIT- 901
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 30268331 1248 etkerqaACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQA 1287
Cdd:TIGR00618 902 -------LYANVRLANQSEGRFHGRYADSHVNARKYQGLA 934
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
873-1129 |
8.53e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.05 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 873 AEEKTISAKYAGERDRAEAEAREKETK--ALSLARALEEAMEQ-----KAELERLNKQFRTEMED-LMSSKDDVGKSVHE 944
Cdd:NF041483 522 AEETLERTRAEAERLRAEAEEQAEEVRaaAERAARELREETERaiaarQAEAAEELTRLHTEAEErLTAAEEALADARAE 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 945 LEKSKRALEQQVEEMKTQLEELEGELQA---TEDAKLRLEVNLQAMKAQFERD---LQGRDEQSEEKKKQlvrqvrEMEA 1018
Cdd:NF041483 602 AERIRREAAEETERLRTEAAERIRTLQAqaeQEAERLRTEAAADASAARAEGEnvaVRLRSEAAAEAERL------KSEA 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1019 ELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKdcmRELDDTRASREEILAQAKeneKKLK 1098
Cdd:NF041483 676 QESADRVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEAD---QERERAREQSEELLASAR---KRVE 749
|
250 260 270
....*....|....*....|....*....|....*....
gi 30268331 1099 SMEAEMIQLQEE--------LAAAErakRQAQQERDELA 1129
Cdd:NF041483 750 EAQAEAQRLVEEadrratelVSAAE---QTAQQVRDSVA 785
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1101-1268 |
9.79e-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: 42.80 E-value: 9.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1101 EAEMIQLQEELAAAERAKRQAQQERDELadeianssgkgalaleekRRLEARIAQLEEELEEEQGNTELINDRLKKANLQ 1180
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDRL------------------QALESELAISRQDYDGATAQLRAAQAAVKAAQAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1181 IDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSK---YKASITALEAKIAQLEEQLDNETKERQAACK 1257
Cdd:pfam00529 119 LAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLdqiYVQITQSAAENQAEVRSELSGAQLQIAEAEA 198
|
170
....*....|.
gi 30268331 1258 QVRRTEKKLKD 1268
Cdd:pfam00529 199 ELKLAKLDLER 209
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1054-1207 |
1.11e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1054 NRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKEnekKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIA 1133
Cdd:PRK09039 50 GKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRA---SLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELD 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30268331 1134 NSSGKGALALEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLNLerSHAQKNenarQQLER 1207
Cdd:PRK09039 127 SEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNV--ALAQRV----QELNR 194
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
860-1152 |
1.20e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 860 NLEKKQKKFDQLLAEEKTISAKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFrtemEDLMSSKDDVG 939
Cdd:PRK04778 120 DIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQF----VELTESGDYVE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 940 KSVH--ELEKSKRALEQQVEEMKTQLEELEGEL--QATEdaklrLEVNLQAMKAQ--------FERDLQGRDEQSEEKKK 1007
Cdd:PRK04778 196 AREIldQLEEELAALEQIMEEIPELLKELQTELpdQLQE-----LKAGYRELVEEgyhldhldIEKEIQDLKEQIDENLA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1008 QLVR-QVREMEAELED-ERKQRSM------AVAARKKLEMDLKDLEAHIDSANKNRDEAI-------------------- 1059
Cdd:PRK04778 271 LLEElDLDEAEEKNEEiQERIDQLydilerEVKARKYVEKNSDTLPDFLEHAKEQNKELKeeidrvkqsytlneselesv 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1060 ----KQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANS 1135
Cdd:PRK04778 351 rqleKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEI 430
|
330
....*....|....*..
gi 30268331 1136 sgkgalaleeKRRLEAR 1152
Cdd:PRK04778 431 ----------KRYLEKS 437
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
887-1241 |
1.23e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.50 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 887 DRAEAEAREKETKalslaraLEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHE---------LEKSKRALEQqVE 957
Cdd:TIGR01612 1297 DENISDIREKSLK-------IIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEianiynilkLNKIKKIIDE-VK 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 958 EMKTQLEE----LEGELQATED--AKLRLEVNLQAMKAQFERDLQGRD-EQSEEKKKQLVRQVREMEA------------ 1018
Cdd:TIGR01612 1369 EYTKEIEEnnknIKDELDKSEKliKKIKDDINLEECKSKIESTLDDKDiDECIKKIKELKNHILSEESnidtyfknaden 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1019 -----------ELEDERKQRSMAVA---ARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQA------QMKDCMREL-- 1076
Cdd:TIGR01612 1449 nenvlllfkniEMADNKSQHILKIKkdnATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKnkelfeQYKKDVTELln 1528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1077 -----------DDTRASREEILAQAKE-----------NEKKLKSMEAEMIQLQEELAAAERAKRQA---QQERDELAD- 1130
Cdd:TIGR01612 1529 kysalaiknkfAKTKKDSEIIIKEIKDahkkfileaekSEQKIKEIKKEKFRIEDDAAKNDKSNKAAidiQLSLENFENk 1608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1131 --EIANSSGKGALALEEKRRLEARIAQLE--EELEEEQGNTELIN------DRLKKANLQIDQINTDLNLERSHAQKNEN 1200
Cdd:TIGR01612 1609 flKISDIKKKINDCLKETESIEKKISSFSidSQDTELKENGDNLNslqeflESLKDQKKNIEDKKKELDELDSEIEKIEI 1688
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 30268331 1201 ARQQlERQNKELKV--KLQEMEGTVKSKYKASITALEAKIAQL 1241
Cdd:TIGR01612 1689 DVDQ-HKKNYEIGIieKIKEIAIANKEEIESIKELIEPTIENL 1730
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
960-1255 |
1.32e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.01 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 960 KTQLEELEGELQATEDAKLRLEvnlqAMKAQFERDLQGRdeqsEEKKKQLVRQVRemeAELEDERkQRSMAVAARKKLEM 1039
Cdd:PRK05035 435 KAEIRAIEQEKKKAEEAKARFE----ARQARLEREKAAR----EARHKKAAEARA---AKDKDAV-AAALARVKAKKAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1040 DLKDLEAHIDSANKNRDEAIKQLRKLQAqmkdcmrelddtRASREEILAQAKENEKKLKsmeaemIQlqeelAAAERAK- 1118
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQA------------RARQAEKQAAAAADPKKAA------VA-----AAIARAKa 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1119 RQAQQERDELADEIANSSGKGALAlEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIdqintdlnlershaqkn 1198
Cdd:PRK05035 560 KKAAQQAANAEAEEEVDPKKAAVA-AAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAI----------------- 621
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1199 enARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLEEQLDNET---KERQAA 1255
Cdd:PRK05035 622 --ARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEeaeDPKKAA 679
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
925-1149 |
1.34e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 925 RTEMEDLMSSKddVGKSVHELEKSK-RALEQQVEEMKTQLEELEGELQATEDaklrLEVNLQAMKAQFERDLQGRDEQSE 1003
Cdd:PHA02562 153 RKLVEDLLDIS--VLSEMDKLNKDKiRELNQQIQTLDMKIDHIQQQIKTYNK----NIEEQRKKNGENIARKQNKYDELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1004 EKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANK----------------NRDEAIKQLRKLQA 1067
Cdd:PHA02562 227 EEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1068 QMKDC---MRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALE 1144
Cdd:PHA02562 307 KLKELqhsLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQD 386
|
....*
gi 30268331 1145 EKRRL 1149
Cdd:PHA02562 387 ELDKI 391
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
917-1301 |
1.37e-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: 42.97 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 917 LERLNKqfrtEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGElqatedaKLRLEVNLQAMKAQFERDlq 996
Cdd:pfam15964 302 IERLTK----ERDDLMSALVSVRSSLAEAQQRESSAYEQVKQAVQMTEEANFE-------KTKALIQCEQLKSELERQ-- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 997 gRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMkdCMREL 1076
Cdd:pfam15964 369 -KERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQL--ASQEM 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1077 DDTRASREeilAQAKENEKKLKSMEAEM------IQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLE 1150
Cdd:pfam15964 446 DVTKVCGE---MRYQLNQTKMKKDEAEKehreyrTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLT 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1151 ARIAQLEEELEEEQGNTELI----NDRLKKANLQIDQINTDLN--LERSHAQ--KNENARQQLERQNKELKVKLQEMEGT 1222
Cdd:pfam15964 523 ELLGESEHQLHLTRLEKESIqqsfSNEAKAQALQAQQREQELTqkMQQMEAQhdKTVNEQYSLLTSQNTFIAKLKEECCT 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1223 VKSKYKASITALEAKIAQLE----------EQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADKAST 1292
Cdd:pfam15964 603 LAKKLEEITQKSRSEVEQLSqekeylqdrlEKLQKRNEELEEQCVQHGRMHERMKQRLRQLDKHCQATAQQLVQLLSKQN 682
|
....*....
gi 30268331 1293 RLKQLKRQL 1301
Cdd:pfam15964 683 QLFKERQNL 691
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
704-1299 |
1.47e-03 |
|
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: 42.82 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 704 VSRQEEEMMAKEEELVKVREKQLAAENRLTemetlqsqlmAEKLQLQEQLQAETELCAEAEELRARLTAKkqelEEICHD 783
Cdd:pfam07111 68 ISRQLQELRRLEEEVRLLRETSLQQKMRLE----------AQAMELDALAVAEKAGQAEAEGLRAALAGA----EMVRKN 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 784 LEARVEEEEERCQHLQAEK-KKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQrqsacnLE 862
Cdd:pfam07111 134 LEEGSQRELEEIQRLHQEQlSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQ------LS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 863 KKQKKFDQLLAEEKTISaKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLmsskddvgksV 942
Cdd:pfam07111 208 KTQEELEAQVTLVESLR-KYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSL----------T 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 943 HELEKSKRALEQQVEEMKTQLEELEGELQAT----EDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVRE--- 1015
Cdd:pfam07111 277 HMLALQEEELTRKIQPSDSLEPEFPKKCRSLlnrwREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEqai 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1016 MEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEK 1095
Cdd:pfam07111 357 LQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSN 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1096 KLkSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKR----------RLEARIAQLEEELEEEQG 1165
Cdd:pfam07111 437 RL-SYAVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLReernrldaelQLSAHLIQQEVGRAREQG 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1166 NTEliNDRLKKANLQIDQ---------INTDLNLERSHAQKNE------NARQQLERQNKELKVKLQEMEGTVKskykas 1230
Cdd:pfam07111 516 EAE--RQQLSEVAQQLEQelqraqeslASVGQQLEVARQGQQEsteeaaSLRQELTQQQEIYGQALQEKVAEVE------ 587
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1231 iTALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQVDDERR-NAEQYKDQADKASTRLKQLKR 1299
Cdd:pfam07111 588 -TRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRlQDEARKEEGQRLARRVQELER 656
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
747-1133 |
1.55e-03 |
|
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: 43.04 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 747 LQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKL 826
Cdd:pfam02463 625 VEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 827 QLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNLEKKQKKFDQLLAEEKTISAKYAGERDRAEAEAREKETKALSLARA 906
Cdd:pfam02463 705 EQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 907 LEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQA 986
Cdd:pfam02463 785 KLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEIT 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 987 MKAQFERDLQGRDEQSEEK---KKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIdsaNKNRDEAIKQLR 1063
Cdd:pfam02463 865 KEELLQELLLKEEELEEQKlkdELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEI---LLKYEEEPEELL 941
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30268331 1064 KLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSME-AEMIQLQEELAAAERAKRQAQQERDELADEIA 1133
Cdd:pfam02463 942 LEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAiEEFEEKEERYNKDELEKERLEEEKKKLIRAII 1012
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
886-1062 |
1.63e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 886 RDRAEAEAREKETKALSLARALEEAmeqkAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTqLEE 965
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEA----ALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK-LDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 966 LEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVrqVREMEAELEDERKQRSMAVAARKKLEMDLKDLE 1045
Cdd:PRK12705 103 LENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLL--LKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
170
....*....|....*..
gi 30268331 1046 AHIDSANKNRDEAIKQL 1062
Cdd:PRK12705 181 ILAQAMQRIASETASDL 197
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
995-1301 |
1.67e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 995 LQGRDEQSEEKKKQLVRqvrEMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMR 1074
Cdd:pfam07888 32 LQNRLEECLQERAELLQ---AQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1075 ELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELAAAE--------RAKRQAQQERDELADEiANSSGKGALALEEK 1146
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLEREtelermkeRAKKAGAQRKEEEAER-KQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1147 RRLEARIAQLEEELEEEQGNTELINDrlkkanlQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGtVKSK 1226
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQD-------TITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG-LGEE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1227 YKASITALEAKIAQLEE------QLDNETKERQAACKQVRRTEKKLKDVLLQvdderrNAEQYKDQADKASTRLKQLKRQ 1300
Cdd:pfam07888 260 LSSMAAQRDRTQAELHQarlqaaQLTLQLADASLALREGRARWAQERETLQQ------SAEADKDRIEKLSAELQRLEER 333
|
.
gi 30268331 1301 L 1301
Cdd:pfam07888 334 L 334
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1099-1295 |
1.70e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1099 SMEAEMIQLqEELAAAERAKRQAQQERDELADEIANssgkgalALEEKRRLEARIAQleeeleeeqgntelINDRLKKAN 1178
Cdd:COG1579 1 AMPEDLRAL-LDLQELDSELDRLEHRLKELPAELAE-------LEDELAALEARLEA--------------AKTELEDLE 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1179 LQIDQINTDLNLERSHAQKNEnARQQLERQNKELKVKLQEMEGTvkskyKASITALEAKIAQLEEQLDNETKERQAACKQ 1258
Cdd:COG1579 59 KEIKRLELEIEEVEARIKKYE-EQLGNVRNNKEYEALQKEIESL-----KRRISDLEDEILELMERIEELEEELAELEAE 132
|
170 180 190
....*....|....*....|....*....|....*..
gi 30268331 1259 VRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLK 1295
Cdd:COG1579 133 LAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
938-1133 |
1.74e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.35 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 938 VGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFErDLQGRDEQS-----EEKKKQLVRQ 1012
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAE-KWEEKARLAlekgrEDLAREALER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1013 VREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLR--KLQAQMKDCMRELDDTRASREeiLAQA 1090
Cdd:COG1842 93 KAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKaaKAQEKVNEALSGIDSDDATSA--LERM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 30268331 1091 KEnekKLKSMEAEMiQLQEELAAAERAKRQ--AQQERDELADEIA 1133
Cdd:COG1842 171 EE---KIEEMEARA-EAAAELAAGDSLDDElaELEADSEVEDELA 211
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1041-1299 |
2.00e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1041 LKDLEAHIDSANKNRDEAIKQLRKLQAQMKD-------CMRELDDTRASREEIlaqakenEKKLKSMEAEMIQLQeelaa 1113
Cdd:PRK11637 49 LKSIQQDIAAKEKSVRQQQQQRASLLAQLKKqeeaisqASRKLRETQNTLNQL-------NKQIDELNASIAKLE----- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1114 aeraKRQAQQERDeLADEIANSSGKG---ALAL----EEKRRLEaRIaqleeeleeeQGNTELINDRLKKANLQIDQINT 1186
Cdd:PRK11637 117 ----QQQAAQERL-LAAQLDAAFRQGehtGLQLilsgEESQRGE-RI----------LAYFGYLNQARQETIAELKQTRE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1187 DLNLERSHAQKNENARQQLERQNKELKVKLQEmegtVKSKYKASITALEAKIAQLEEQLdnetkerqaacKQVRRTEKKL 1266
Cdd:PRK11637 181 ELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQ----ARNERKKTLTGLESSLQKDQQQL-----------SELRANESRL 245
|
250 260 270
....*....|....*....|....*....|....
gi 30268331 1267 KDVLLQVDDE-RRNAEQYKDQADKASTRLKQLKR 1299
Cdd:PRK11637 246 RDSIARAEREaKARAEREAREAARVRDKQKQAKR 279
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
944-1146 |
2.25e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 944 ELEKSKRALEQQVEEMKTQLEELEG-ELQATEDAKLRLEVNLQAmkaqferdlqgrdeQSEEkkkqLVRQVREMEAEL-E 1021
Cdd:COG0497 176 ELRADEAERARELDLLRFQLEELEAaALQPGEEEELEEERRRLS--------------NAEK----LREALQEALEALsG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1022 DERKQRSMAVAARKKLEmDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDD---------------TRASR--- 1083
Cdd:COG0497 238 GEGGALDLLGQALRALE-RLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFdperleeveerlallRRLARkyg 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30268331 1084 ---EEILAQAKENEKKLKSMEAemiqLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEK 1146
Cdd:COG0497 317 vtvEELLAYAEELRAELAELEN----SDERLEELEAELAEAEAELLEAAEKLSAARKKAAKKLEKA 378
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1084-1228 |
2.37e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1084 EEILAQAKEN--EKKLK------SMEAEMIQLQEELAAAERAKRQAQQERDELADEIAnssgkgalALEEKRRLEARIAQ 1155
Cdd:PRK00409 501 ENIIEEAKKLigEDKEKlneliaSLEELERELEQKAEEAEALLKEAEKLKEELEEKKE--------KLQEEEDKLLEEAE 572
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30268331 1156 LEeeleeeqgntelINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQnKELKVKLQEMEGTVKSKYK 1228
Cdd:PRK00409 573 KE------------AQQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEAR-KRLNKANEKKEKKKKKQKE 632
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
948-1143 |
2.62e-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: 41.67 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 948 SKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLqgrdEQSEEkkkqlvrQVREMEAELEDERkqr 1027
Cdd:pfam09787 41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEA----ESSRE-------QLQELEEQLATER--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1028 smavAARKKLEMDLKDLEAHIDSankNRDEAIKQLRKLQAQMKDCMRELDDTRA---SREEILAQAKENEKKLKSMEAEM 1104
Cdd:pfam09787 107 ----SARREAEAELERLQEELRY---LEEELRRSKATLQSRIKDREAEIEKLRNqltSKSQSSSSQSELENRLHQLTETL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 30268331 1105 IQLQEELAA--AERAKRQAQQERDELADEIANSSGKGALAL 1143
Cdd:pfam09787 180 IQKQTMLEAlsTEKNSLVLQLERMEQQIKELQGEGSNGTSI 220
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
929-1289 |
2.80e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 929 EDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQAT---EDAKlRLEVNLQAMKAQFERDLQGRDEQseek 1005
Cdd:TIGR01612 1118 DDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAisnDDPE-EIEKKIENIVTKIDKKKNIYDEI---- 1192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1006 kKQLVRQVREMEAELEDERKQRSMAVAARKKLEmdlKDLEAHIDSANKNRDEAIKQLRKLqaqmkdcMRELDDTRASREE 1085
Cdd:TIGR01612 1193 -KKLLNEIAEIEKDKTSLEEVKGINLSYGKNLG---KLFLEKIDEEKKKSEHMIKAMEAY-------IEDLDEIKEKSPE 1261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1086 ILAQAKENEKKLKSMEAEMIQLQEelaaaERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEEEQG 1165
Cdd:TIGR01612 1262 IENEMGIEMDIKAEMETFNISHDD-----DKDHHIISKKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQK 1336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1166 NTELINDRLKK-AN----LQIDQINTDLNLERSHAQKnenarqqLERQNKELKVKLQEMEGTVKsKYKASITALEAKiAQ 1240
Cdd:TIGR01612 1337 HNSDINLYLNEiANiyniLKLNKIKKIIDEVKEYTKE-------IEENNKNIKDELDKSEKLIK-KIKDDINLEECK-SK 1407
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 30268331 1241 LEEQLDNetkerqaacKQVRRTEKKLKDVLLQVDDERRNAEQYKDQADK 1289
Cdd:TIGR01612 1408 IESTLDD---------KDIDECIKKIKELKNHILSEESNIDTYFKNADE 1447
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
885-1026 |
3.03e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 42.13 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 885 ERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTE-----MEDLMSSKDDVGKSVHE-LEKSKRALEQQVEE 958
Cdd:NF012221 1607 QRDAILEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRNPfagglLDRVQEQLDDAKKISGKqLADAKQRHVDNQQK 1686
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30268331 959 MKTQLEELEGELQATEDAKLRLEVNLQAMKAQFER-----DLQGRDEQSEEKKKQLVRQvremEAELEDERKQ 1026
Cdd:NF012221 1687 VKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKrkddaLAKQNEAQQAESDANAAAN----DAQSRGEQDA 1755
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
864-1033 |
3.16e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 864 KQKKFDQLLAEEKTISAKYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVH 943
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 944 ELEKSKRALEQQVEEMKTQLEELEGELQatEDAKLRLEVNLQAMKAQFERDLqgrdeqsEEKKKQLVRQVREmEAELEDE 1023
Cdd:PRK12705 106 QLEEREKALSARELELEELEKQLDNELY--RVAGLTPEQARKLLLKLLDAEL-------EEEKAQRVKKIEE-EADLEAE 175
|
170
....*....|
gi 30268331 1024 RKQRSMAVAA 1033
Cdd:PRK12705 176 RKAQNILAQA 185
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
728-1111 |
3.26e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 728 AENRLTEMETLQSQLMAEKLQLQEQLQAETelcaeAEELRARLTAKKQELEEICHDL---EARVEEEEERCQHLQAEKKK 804
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNNQKEQDW-----NKELKSELKNQEKKLEEIQNQIsqnNKIISQLNEQISQLKKELTN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 805 MQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNLE----KKQKKFDQLLAEEKTISA 880
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDeqikKLQQEKELLEKEIERLKE 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 881 ---KYAGERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVE 957
Cdd:TIGR04523 434 tiiKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 958 EMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDlqgrdeQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKL 1037
Cdd:TIGR04523 514 DLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD------DFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEK 587
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30268331 1038 EMDLKDLEahidsanKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEEL 1111
Cdd:TIGR04523 588 QELIDQKE-------KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1091-1300 |
3.29e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1091 KENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERD-----ELADEIANSSGKGALALEEKRRLEaRIAQLEEeleeeqg 1165
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEkarqaEMDRQAAIYAEQERMAMERERELE-RIRQEER------- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1166 ntelindrlKKANLQIDQINTDLNLERSHaqknENARQQLERQNKELKVKlQEMEGTVKSKYkasitaleakiaqLEEQL 1245
Cdd:pfam17380 359 ---------KRELERIRQEEIAMEISRMR----ELERLQMERQQKNERVR-QELEAARKVKI-------------LEEER 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 30268331 1246 DNETKERQAACKQVRRTEKKLKDVLLQVDDERRNAEQYKdqadkasTRLKQLKRQ 1300
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMER-------VRLEEQERQ 459
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
944-1130 |
3.35e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 41.16 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 944 ELEKSKRALEQQVEEMKTQLEelegelQATED-AKLRLEVNLQAMKAQF------------ERDLQGRDEQSEEKKKQLV 1010
Cdd:pfam04849 91 SLLKQNSVLTERNEALEEQLG------SAREEiLQLRHELSKKDDLLQIysndaeesetesSCSTPLRRNESFSSLHGCV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1011 ------RQVREMEaelEDERKQRSMAvaarKKLEMDLKDLEAHidsANKNRDEAIKQLRKLQAQMKDCMREL----DDTR 1080
Cdd:pfam04849 165 qldalqEKLRGLE---EENLKLRSEA----SHLKTETDTYEEK---EQQLMSDCVEQLSEANQQMAELSEELarkmEENL 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 30268331 1081 ASREEI---LAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELAD 1130
Cdd:pfam04849 235 RQQEEItslLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQD 287
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
761-1278 |
3.62e-03 |
|
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: 41.65 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 761 AEAEELRARLTAKKQELE--EICH-----DLEARVEEEEERCQHLQAEKKKMQQNIQELEEQLEEEESARQKlQLEKVtt 833
Cdd:pfam05557 2 AELIESKARLSQLQNEKKqmELEHkrariELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALRE-QAELN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 834 eaklkkleeelddllvdldhqrqsacnlekkqkkfdQLLAEEKTISAKYAGERDRAEAEARE-KETKALSLARALEEAME 912
Cdd:pfam05557 79 ------------------------------------RLKKKYLEALNKKLNEKESQLADAREvISCLKNELSELRRQIQR 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 913 QKAELERLNkqfrTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKT---QLEELEGELQATEDAKLRLEvnlqAMKA 989
Cdd:pfam05557 123 AELELQSTN----SELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQSQEQDSEIVK----NSKS 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 990 QFERdlqgrdeqseekkkqlvrqVREMEAELE---DERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIK---QLR 1063
Cdd:pfam05557 195 ELAR-------------------IPELEKELErlrEHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATlelEKE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1064 KLQAQMKDCMRELDDTRASreeiLAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKgalAL 1143
Cdd:pfam05557 256 KLEQELQSWVKLAQDTGLN----LRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKK---IE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1144 EEKRRLEARIAQLEEELEEEQGNTELINdrLKKANLqiDQINTDLNLERSHAQKNENAR------QQLERQNKELKVKLQ 1217
Cdd:pfam05557 329 DLNKKLKRHKALVRRLQRRVLLLTKERD--GYRAIL--ESYDKELTMSNYSPQLLERIEeaedmtQKMQAHNEEMEAQLS 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30268331 1218 EMEGTVKSkYKASITALEAKIAQLEEQldNETKERQAACKQVRRTEKKLKDVLLQVDDERR 1278
Cdd:pfam05557 405 VAEEELGG-YKQQAQTLERELQALRQQ--ESLADPSYSKEEVDSLRRKLETLELERQRLRE 462
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
889-1155 |
3.69e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.47 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 889 AEAEAREKETKALSLARALEEA----MEQKaELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLE 964
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEArqarLERE-KAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 965 ElegelqatedaklrlevNLQAMKAQFERDLQGRDEQSEEKkkqlvrqvremEAELEDERKQRSMAVAAR---KKLEMDL 1041
Cdd:PRK05035 515 D-----------------NSAVIAAREARKAQARARQAEKQ-----------AAAAADPKKAAVAAAIARakaKKAAQQA 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1042 KDLEAHIDSANK----NRDEAIKQLRKLQAQMKD-----CMRELDDTRASREEILAQAKENEKKLKSMEAEMIQLQEELA 1112
Cdd:PRK05035 567 ANAEAEEEVDPKkaavAAAIARAKAKKAAQQAASaepeeQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKA 646
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 30268331 1113 AAE----RAK-RQAQQERDELADEIANSSGKGALAlEEKRRLEARIAQ 1155
Cdd:PRK05035 647 AVAaaiaRAKaRKAAQQQANAEPEEAEDPKKAAVA-AAIARAKAKKAA 693
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
935-1070 |
3.75e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 935 KDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVR 1014
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEAD 587
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 30268331 1015 EMEAELEDERKQRSMAVAARkklemDLKDLEAHIDSANKNRDEAIKQLRKLQAQMK 1070
Cdd:PRK00409 588 EIIKELRQLQKGGYASVKAH-----ELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1017-1155 |
3.80e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.87 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1017 EAELEDERKQRSMAVAARKKLEMDLKDLEA---HIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTR--ASREEILAQAK 1091
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDRLQAlesELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQidLARRRVLAPIG 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30268331 1092 E-NEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIAnssgkgALALEEKRRLEARIAQ 1155
Cdd:pfam00529 137 GiSRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQ------AEVRSELSGAQLQIAE 195
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
875-1025 |
4.06e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.64 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 875 EKTISAKYAGERDRAEAEAREKETKAL-SLARALEEAMEQ------------KAELERLNKQFRTEM----------EDL 931
Cdd:cd16269 96 MEQLEEKKEEFCKQNEEASSKRCQALLqELSAPLEEKISQgsysvpggyqlyLEDREKLVEKYRQVPrkgvkaeevlQEF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 932 MSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDL-QGRDEQSEEKKKQLV 1010
Cdd:cd16269 176 LQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLrQLKEKMEEERENLLK 255
|
170
....*....|....*
gi 30268331 1011 RQVREMEAELEDERK 1025
Cdd:cd16269 256 EQERALESKLKEQEA 270
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1032-1236 |
4.07e-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: 40.82 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1032 AARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQ--AKENEKKLKSMEAEMIQLQE 1109
Cdd:cd22656 114 EAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDegGAIARKEIKDLQKELEKLNE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1110 ELAAaerakrQAQQERDELADEIANssgkgalaLEEKRRLEARIAQLeeeleeeqgntelindrLKKANLQIDQINTDLN 1189
Cdd:cd22656 194 EYAA------KLKAKIDELKALIAD--------DEAKLAAALRLIAD-----------------LTAADTDLDNLLALIG 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 30268331 1190 LERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEA 1236
Cdd:cd22656 243 PAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAILAKLELEKA 289
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
724-1296 |
4.74e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 724 KQLAAENRLTEMETLQSQLMAEKlqlQEQLQAETELCAEAEELRARLTAKKQELE---EICHDLEARVEEEEERcqhlQA 800
Cdd:TIGR00606 183 RYIKALETLRQVRQTQGQKVQEH---QMELKYLKQYKEKACEIRDQITSKEAQLEssrEIVKSYENELDPLKNR----LK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 801 EKKKMQQNIQELEEQLEEEESARQKLQLEKVTTEAKLKKLEEELDDLLVDLDHQRQSACNlEKKQKKFDQLLAEEKTISA 880
Cdd:TIGR00606 256 EIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVR-EKERELVDCQRELEKLNKE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 881 KYAGERDRAEAEAREKEtkaLSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVG--KSVHELEKskralEQQVEE 958
Cdd:TIGR00606 335 RRLLNQEKTELLVEQGR---LQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERqiKNFHTLVI-----ERQEDE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 959 MKTqLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEaelederkQRSMAVAARKKLE 1038
Cdd:TIGR00606 407 AKT-AAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ--------QLEGSSDRILELD 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1039 MDLKDLEAHIDSANKNrdEAIKQLRKLQAQMKDCMRELDDTRASREEILAQAKENEKKLKSMEAemiQLQEELAAAERAK 1118
Cdd:TIGR00606 478 QELRKAERELSKAEKN--SLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEM---LTKDKMDKDEQIR 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1119 RQAQQERDELADEIANSSGKGALA------LEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQINTDLnler 1192
Cdd:TIGR00606 553 KIKSRHSDELTSLLGYFPNKKQLEdwlhskSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL---- 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1193 SHAQKNENARQQLERQNKELKvklqemegtVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTEKKLKDVLLQ 1272
Cdd:TIGR00606 629 FDVCGSQDEESDLERLKEEIE---------KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISD 699
|
570 580
....*....|....*....|....
gi 30268331 1273 VDDERRNAEQYKDQADKASTRLKQ 1296
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKKEK 723
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1032-1133 |
4.94e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1032 AARKKLEMD-----LKDLEAHIDSANKNRDEAIK--------QLRKLQAQMKDCMRELDDTRA---SREEILAQAKENEK 1095
Cdd:COG0542 399 AARVRMEIDskpeeLDELERRLEQLEIEKEALKKeqdeasfeRLAELRDELAELEEELEALKArweAEKELIEEIQELKE 478
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 30268331 1096 KLKSMEAEMIQLQEELAAAERAKRQAQQ-ERDEL-ADEIA 1133
Cdd:COG0542 479 ELEQRYGKIPELEKELAELEEELAELAPlLREEVtEEDIA 518
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1078-1300 |
4.94e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 41.36 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1078 DTRASREEILAQAKENEKKLKSMEAEMIQLQEElAAAERAKRQAQQERDELADEIANSSGKgaLALEEKRRLEAriaQLE 1157
Cdd:NF012221 1532 DNVVATSESSQQADAVSKHAKQDDAAQNALADK-ERAEADRQRLEQEKQQQLAAISGSQSQ--LESTDQNALET---NGQ 1605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1158 EELEEEQGNTELINDRLKKANLQIDQINTDLNlershaQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAK 1237
Cdd:NF012221 1606 AQRDAILEESRAVTKELTTLAQGLDALDSQAT------YAGESGDQWRNPFAGGLLDRVQEQLDDAKKISGKQLADAKQR 1679
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30268331 1238 IAQLEEQLDNETKERQAAckqVRRTEKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLKRQ 1300
Cdd:NF012221 1680 HVDNQQKVKDAVAKSEAG---VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESD 1739
|
|
| COG5638 |
COG5638 |
Uncharacterized conserved protein [Function unknown]; |
957-1213 |
5.05e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 227925 [Multi-domain] Cd Length: 622 Bit Score: 41.31 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 957 EEMKTQLEELEGELQA-TEDAKLRLEVNLQAMKAQFERDLQGRDE-QSEEKKKQLVRQVREMEAELEDERKQRSMAvAAR 1034
Cdd:COG5638 379 SKMQKLFSEKEIDFGLnSELVDMSDDGENGEMEDTFTSHLPASNEsESDDKLETTIEKLDRKLRERQENRKERQLK-KTK 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1035 KKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEILAQ--AKENEKKLKSMEAEMIQLQEELA 1112
Cdd:COG5638 458 DDSDVDLKDKKESINKKNKKGKHAIERTAASKEELELIKADDEDDEQLDHFDMKSilKAEKFKKNRKLKKKASNLEEGFV 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1113 AAERAKR-QAQQERDELADEIANSSGKGalaleekrrleariaqleeeleeEQGNTELINDRLKKANLQIDQINTDLNLE 1191
Cdd:COG5638 538 FDPKDPRfVAIFEDHNFAIDPTHPEFKK-----------------------TGGMKKIMDEKRKRLKNNIEQTQDGKPEL 594
|
250 260
....*....|....*....|....
gi 30268331 1192 RSHAQKNE--NARQQLERQNKELK 1213
Cdd:COG5638 595 KIKKRKAEkgDQRQELDRIVKSIK 618
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
846-1255 |
5.35e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.05 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 846 DLLVDLDHQRQSACNLEKKQKKFDQLLaeEKTISAKYAGERDRAEAEAREKETKALS---LARALEEAMEQKAELERLNK 922
Cdd:COG5278 97 SLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKALMdeiRARLLLLALALAALLLAAAA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 923 QFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQS 1002
Cdd:COG5278 175 LLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1003 EEKKKQLVRQVREMEAELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRAS 1082
Cdd:COG5278 255 AALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALA 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1083 REEILAQAKENEKKLKSMEAEMIQLQEELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQLEEELEE 1162
Cdd:COG5278 335 TALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAA 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1163 EQGNTELINDRLKKANLQIDQINTDLNLERSHAQKNENARQQLERQNKELKVKLQEMEGTVKSKYKASITALEAKIAQLE 1242
Cdd:COG5278 415 AASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALA 494
|
410
....*....|...
gi 30268331 1243 EQLDNETKERQAA 1255
Cdd:COG5278 495 AAAALSLALALAA 507
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1109-1311 |
5.57e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1109 EELAAAERAKRQAQQERDELADEIanssgkgalalEEKRRLEARIAQLeeeleeeQGNTELINDRLKKANLQIDqintdl 1188
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQ-----------EELEELEEELEEL-------EAELEELREELEKLEKLLQ------ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1189 nlershAQKNENARQQLERQNKELKVKLQEMEgtvksKYKASITALEAKIAQLEEQLDNETKERQAACKQVR-RTEKKLK 1267
Cdd:COG4717 127 ------LLPLYQELEALEAELAELPERLEELE-----ERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQ 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 30268331 1268 DVLLQVDDERRNAEQYKDQADKASTRLKQLKRQLEEAEEEAQRA 1311
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1032-1210 |
6.00e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1032 AARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQMKDCMRELDDTRASREEilaqakenEKKLKSMEAEMIQLQEEL 1111
Cdd:PRK11281 73 DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLRQL--------ESRLAQTLDQLQNAQNDL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1112 AAA-----------ERAKRQ---AQQERDELADEIANSS-GKGALALEEKRRLEARI----AQLEEELEEEQGNTELI-- 1170
Cdd:PRK11281 145 AEYnsqlvslqtqpERAQAAlyaNSQRLQQIRNLLKGGKvGGKALRPSQRVLLQAEQallnAQNDLQRKSLEGNTQLQdl 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 30268331 1171 -NDRLKKANLQIDQINTDLNL------ERSHAQKNENARQQLERQNK 1210
Cdd:PRK11281 225 lQKQRDYLTARIQRLEHQLQLlqeainSKRLTLSEKTVQEAQSQDEA 271
|
|
| PDCD7 |
pfam16021 |
Programmed cell death protein 7; |
907-1132 |
6.51e-03 |
|
Programmed cell death protein 7;
Pssm-ID: 464979 [Multi-domain] Cd Length: 305 Bit Score: 40.09 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 907 LEEAMEQKAELERLNKQFRTEMEDLMSSKDDvgksvhelEKSKRALEQQVEEMKTQLEElegELQATEDAKLR--LEVNL 984
Cdd:pfam16021 3 LSELRQALYSAARLVSRLETLCLELRENVED--------DSVWSESYSRAAELKHELQE---KLLLLEDPELLesLKRKL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 985 QAMKAQFERDLQGRDEQSEEKKKQLVRQVrEMEAELeDERKQRSMAVAARKKLEMDLKDLEAHIDSA-NKNRDEAIKQLR 1063
Cdd:pfam16021 72 ERRQKKRLRRKRRKEERKEEKKEEQERRA-EREAKI-DKWRRKQIQEVEEKKRERELKLAADAVLSEvRKKQADAKRMLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1064 KLQAQMKdcMRELDDTRASREEILAQAKENE--------------KKLKSMEAE-------MIQLQEELAAAERAKRQAQ 1122
Cdd:pfam16021 150 ILRSLEK--LRKLRKEAARRKGIKPESECDEafeshleklrsvwkKRTEEYSAEekalkvmLEGEQEEERKRRREKRQKK 227
|
250
....*....|
gi 30268331 1123 QERDELADEI 1132
Cdd:pfam16021 228 EREEFLQKKW 237
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1045-1146 |
6.88e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 38.19 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1045 EAHIDSANKNRDEAIKQLRKLQAQMKDcmrelddTRASREEILAQAKENEKKLKsmEAEMIQLQEELAA-AERAKRQAQQ 1123
Cdd:cd06503 36 AESLEEAEKAKEEAEELLAEYEEKLAE-------ARAEAQEIIEEARKEAEKIK--EEILAEAKEEAERiLEQAKAEIEQ 106
|
90 100
....*....|....*....|...
gi 30268331 1124 ERDELADEIANSSGKGALALEEK 1146
Cdd:cd06503 107 EKEKALAELRKEVADLAVEAAEK 129
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1088-1279 |
7.29e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.45 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1088 AQAKENEKKLKSmeaemiqLQEELAAAERAKRQAQQERDELadeianssgkgalaLEEKRRLEARIAQLEEELEEEQgnt 1167
Cdd:PRK11637 40 AHASDNRDQLKS-------IQQDIAAKEKSVRQQQQQRASL--------------LAQLKKQEEAISQASRKLRETQ--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1168 elinDRLKKANLQIDQINTDLN-LERSHAQKNENARQQLE---RQNK----ELKVKLQEME---------GTVKSKYKAS 1230
Cdd:PRK11637 96 ----NTLNQLNKQIDELNASIAkLEQQQAAQERLLAAQLDaafRQGEhtglQLILSGEESQrgerilayfGYLNQARQET 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 30268331 1231 ITALEAKIAQLEEQlDNETKERQAACKQVRRTEKKLKDVLLQVDDERRN 1279
Cdd:PRK11637 172 IAELKQTREELAAQ-KAELEEKQSQQKTLLYEQQAQQQKLEQARNERKK 219
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
912-1124 |
8.34e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.44 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 912 EQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRALEQQVEEMKTQLEELEGELQaTEDAKLRLEVNL-QAMKAQ 990
Cdd:pfam05622 290 ENKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQ-EQGSKAEDSSLLkQKLEEH 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 991 FErdlQGRDEQSEEKKKQLVRQVREMEAELEDERKQRSMAVAARKKlEMDLKDLEAHIDSANKNRDEAIKQLRKLQAQmk 1070
Cdd:pfam05622 369 LE---KLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRKK-DEDMKAMEERYKKYVEKAKSVIKTLDPKQNP-- 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 30268331 1071 dcmrelddtrASREEILA---QAKENEKKLKSMEAEMiqlqeelaaaERAKRQAQQE 1124
Cdd:pfam05622 443 ----------ASPPEIQAlknQLLEKDKKIEHLERDF----------EKSKLQREQE 479
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1028-1298 |
8.68e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1028 SMAVAARKKLEMDLKDLE--AHIDSANKNRdeaikqLRKLQAQMKDCMRELDDTrasreeilaqakenEKKLKSMEaEMI 1105
Cdd:PHA02562 146 QLSAPARRKLVEDLLDISvlSEMDKLNKDK------IRELNQQIQTLDMKIDHI--------------QQQIKTYN-KNI 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1106 QLQEELAAAERAKRQAQQerDELADEIANSSgkgalalEEKRRLEARIAQLEEELEEEQGNTELINDRLKKANLQIDQIN 1185
Cdd:PHA02562 205 EEQRKKNGENIARKQNKY--DELVEEAKTIK-------AEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQ 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1186 TDLNLERSHaQKNENARQQLERQNK---ELKVKLQEMEGtvkskykaSITALEAKIAQLEEQLDnetkerqaackQVRRT 1262
Cdd:PHA02562 276 KVIKMYEKG-GVCPTCTQQISEGPDritKIKDKLKELQH--------SLEKLDTAIDELEEIMD-----------EFNEQ 335
|
250 260 270
....*....|....*....|....*....|....*.
gi 30268331 1263 EKKLKDVLLQVDDERRNAEQYKDQADKASTRLKQLK 1298
Cdd:PHA02562 336 SKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQ 371
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
945-1310 |
8.85e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 40.38 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 945 LEKSK----RALEQQVEEMKTQLEELEGELQATEDAKLRLEVN--LQAMKAQFERDLQGRDEQSEEKKKQLVRQVREMEA 1018
Cdd:NF033838 78 LDKRKhtqnVALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKkeLDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKD 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1019 ELEDERkqRSMAVAARKKLEMDLKDLEAHIDSAnknrdeaikQLRKLQAQMKDcmrelddtrASREEILAQAKEnekKLK 1098
Cdd:NF033838 158 QKEEDR--RNYPTNTYKTLELEIAESDVEVKKA---------ELELVKEEAKE---------PRDEEKIKQAKA---KVE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1099 SMEAEMIQLQE----ELAAAERAKRQAQQERDELADEIANSSGKGALALEEKRRLEARIAQ-LEEELEEEQGNTELINDR 1173
Cdd:NF033838 215 SKKAEATRLEKiktdREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATpDKKENDAKSSDSSVGEET 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1174 LKKANLQIDQINTDLNLERSHAQKNENARQQLERQN------KELKVKLQEMEGTVKskykasitalEAKIAQLEEqldn 1247
Cdd:NF033838 295 LPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNyptntyKTLELEIAESDVKVK----------EAELELVKE---- 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30268331 1248 ETKERqaackqvrRTEKKLKDVLLQVddERRNAEqykdqadkaSTRLKQLKRQLEEAEEEAQR 1310
Cdd:NF033838 361 EAKEP--------RNEEKIKQAKAKV--ESKKAE---------ATRLEKIKTDRKKAEEEAKR 404
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
862-1124 |
8.99e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 39.79 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 862 EKKQKKFDQLLAEEKTISA--KYAGERDR----AEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMS-- 933
Cdd:pfam15905 66 QKNLKESKDQKELEKEIRAlvQERGEQDKrlqaLEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAkf 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 934 SKDDVGKSVH----ELEKSKRALEQQVEEMKTQLEELEGELQATEDaklrlevNLQAMK---AQFERDLQGRDEQSEEKK 1006
Cdd:pfam15905 146 SEDGTQKKMSslsmELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQK-------NLEHSKgkvAQLEEKLVSTEKEKIEEK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1007 KQLVRQVREMEaELEDERKQRSMAVAARKKLEMDLKDLEAHIDSANKNRDEAIKQLRKlqaQMKDCMRELDDTRASREEI 1086
Cdd:pfam15905 219 SETEKLLEYIT-ELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSK---QIKDLNEKCKLLESEKEEL 294
|
250 260 270
....*....|....*....|....*....|....*...
gi 30268331 1087 LAQAKENEKKLKsmeAEMIQLQEELAAAERAKRQAQQE 1124
Cdd:pfam15905 295 LREYEEKEQTLN---AELEELKEKLTLEEQEHQKLQQK 329
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
1184-1282 |
9.18e-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: 38.79 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 1184 INTDLNLERSHAQKnENARQQLERQNKElkvklqemEGTVKSKYKASITALEAKIAQLEEQLDNETKERQAACKQVRRTE 1263
Cdd:pfam05266 94 INKLLSLKDRQTKL-LEELKKLEKKIAE--------EESEKRKLEEEIDELEKKILELERQLALAKEKKEAADKEIARLK 164
|
90
....*....|....*....
gi 30268331 1264 KKLKDvllqVDDERRNAEQ 1282
Cdd:pfam05266 165 SEAEK----LEQEIQDVEL 179
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
722-1071 |
9.81e-03 |
|
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: 40.34 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 722 REKQLAAENRLTEMETLQSQLMAEKLQLQEQLQAETELCAEAEELRARLTAKKQELEEICHDLEArveeeeercqhLQAE 801
Cdd:pfam02463 697 RQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEE-----------KEEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 802 KKKMQQNIQELEEQLEEEESARQKLQLEKVTTEaklkkLEEELDDLLVDLDHQrqsacnlEKKQKKFDQLLAEEKTISAK 881
Cdd:pfam02463 766 KSELSLKEKELAEEREKTEKLKVEEEKEEKLKA-----QEEELRALEEELKEE-------AELLEEEQLLIEQEEKIKEE 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 882 YAgERDRAEAEAREKETKALSLARALEEAMEQKAELERLNKQFRTEMEDLMSSKDDVGKSVHELEKSKRAL-EQQVEEMK 960
Cdd:pfam02463 834 EL-EELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEeESQKLNLL 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30268331 961 TQLEELEGELQATEDAKLRLEVNLQAMKAQFERDLQGRDEQSEEKKKQLVRQvreMEAELEDERKQRSMAVAARKKLEMD 1040
Cdd:pfam02463 913 EEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKR---LLLAKEELGKVNLMAIEEFEEKEER 989
|
330 340 350
....*....|....*....|....*....|.
gi 30268331 1041 LKDLEAHIDSANKNRDEAIKQLRKLQAQMKD 1071
Cdd:pfam02463 990 YNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| |
