|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
100-770 |
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: 1267.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITG 179
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 180 ESGAGKTVNTKRVIQYFATIAALGSKKDqaqqSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKK----ESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGST 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 260 GKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFPMISQGEITVKSIDDVEEFIATDTA 339
Cdd:cd01377 157 GKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 340 IDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQ 419
Cdd:cd01377 237 FDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 420 TVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFV 499
Cdd:cd01377 317 NKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 500 LEQEEYKKEGIDWEFIDFGMDLAACIELIEKP-LGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFEKPKPgkGKAE 578
Cdd:cd01377 397 LEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKP--KKSE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 579 AHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEAdtgSKKGGKKKGGSFQTVSAVFREN 658
Cdd:cd01377 475 AHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGG---GGGKKKKKGGSFRTVSQLHKEQ 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 659 LGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASVIPEGQ 738
Cdd:cd01377 552 LNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGF 631
|
650 660 670
....*....|....*....|....*....|..
gi 1316056572 739 FiDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd01377 632 D-DGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-770 |
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: 1242.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITG 179
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 180 ESGAGKTVNTKRVIQYFATIAALGskkDQAQQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATG---DLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 260 GKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFPMISQGEITVKSIDDVEEFIATDTA 339
Cdd:cd14913 158 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 340 IDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQ 419
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 420 TVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFV 499
Cdd:cd14913 318 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 500 LEQEEYKKEGIDWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFEKPKPGKGKAEA 579
Cdd:cd14913 398 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 580 HFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEADTGSKKGGKKKGGSFQTVSAVFRENL 659
Cdd:cd14913 478 HFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 660 GKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASVIPEGQF 739
Cdd:cd14913 558 NKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQF 637
|
650 660 670
....*....|....*....|....*....|.
gi 1316056572 740 IDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14913 638 IDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-770 |
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: 1145.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITG 179
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 180 ESGAGKTVNTKRVIQYFATIAALGSKKDQAQqsSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQQ--PGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 260 GKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFPMISQGEITVKSIDDVEEFIATDTA 339
Cdd:cd14923 159 GKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 340 IDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQ 419
Cdd:cd14923 239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 420 TVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFV 499
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 500 LEQEEYKKEGIDWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFEKPKPGKGKAEA 579
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 580 HFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEADTG--SKKGGKKKGGSFQTVSAVFRE 657
Cdd:cd14923 479 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSggSKKGGKKKGSSFQTVSAVFRE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 658 NLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASVIPEG 737
Cdd:cd14923 559 NLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEG 638
|
650 660 670
....*....|....*....|....*....|...
gi 1316056572 738 QFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14923 639 QFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-770 |
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: 1143.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITG 179
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 180 ESGAGKTVNTKRVIQYFATIAALGSKKDQaQQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKE-EAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 260 GKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFPMISQGEITVKSIDDVEEFIATDTA 339
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 340 IDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQ 419
Cdd:cd14915 240 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 420 TVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFV 499
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 500 LEQEEYKKEGIDWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFEKPKPGKGKAEA 579
Cdd:cd14915 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 580 HFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEAD-TGSKKGGKKKGGSFQTVSAVFREN 658
Cdd:cd14915 480 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEgGGGKKGGKKKGSSFQTVSALFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 659 LGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASVIPEGQ 738
Cdd:cd14915 560 LNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 1316056572 739 FIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14915 640 FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-770 |
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: 1137.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITG 179
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 180 ESGAGKTVNTKRVIQYFATIAALGSKKDQaQQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKE-EATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 260 GKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFPMISQGEITVKSIDDVEEFIATDTA 339
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 340 IDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQ 419
Cdd:cd14910 240 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 420 TVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFV 499
Cdd:cd14910 320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 500 LEQEEYKKEGIDWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFEKPKPGKGKAEA 579
Cdd:cd14910 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 580 HFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEADT-GSKKGGKKKGGSFQTVSAVFREN 658
Cdd:cd14910 480 HFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEgGGKKGGKKKGSSFQTVSALFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 659 LGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASVIPEGQ 738
Cdd:cd14910 560 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 1316056572 739 FIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14910 640 FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
100-770 |
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: 1137.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITG 179
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 180 ESGAGKTVNTKRVIQYFATIAALGSKKdqaQQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKK---KEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 260 GKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFPMISQGEITVKSIDDVEEFIATDTA 339
Cdd:cd14918 158 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 340 IDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQ 419
Cdd:cd14918 238 IDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 420 TVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFV 499
Cdd:cd14918 318 TVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 500 LEQEEYKKEGIDWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFEKPKPGKGKAEA 579
Cdd:cd14918 398 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 580 HFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEADTGSKKGGKKKGGSFQTVSAVFRENL 659
Cdd:cd14918 478 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAKKKGSSFQTVSALFRENL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 660 GKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASVIPEGQF 739
Cdd:cd14918 558 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQF 637
|
650 660 670
....*....|....*....|....*....|.
gi 1316056572 740 IDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14918 638 IDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-770 |
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: 1112.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITG 179
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 180 ESGAGKTVNTKRVIQYFATIAALGSKKDQaQQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKE-EITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 260 GKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFPMISQGEITVKSIDDVEEFIATDTA 339
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 340 IDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQ 419
Cdd:cd14912 240 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 420 TVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFV 499
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 500 LEQEEYKKEGIDWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFEKPKPGKGKAEA 579
Cdd:cd14912 400 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 580 HFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEADTG---SKKGGKKKGGSFQTVSAVFR 656
Cdd:cd14912 480 HFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAgggAKKGGKKKGSSFQTVSALFR 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 657 ENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASVIPE 736
Cdd:cd14912 560 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 639
|
650 660 670
....*....|....*....|....*....|....
gi 1316056572 737 GQFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14912 640 GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
102-770 |
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: 1107.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGES 181
Cdd:cd14927 3 VLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 182 GAGKTVNTKRVIQYFATIAALG-SKKDQAQQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14927 83 GAGKTVNTKRVIQYFAIVAALGdGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 261 KLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFPMISQGEITVKSIDDVEEFIATDTAI 340
Cdd:cd14927 163 KLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHAM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 341 DILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQT 420
Cdd:cd14927 243 DILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 421 VPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFVL 500
Cdd:cd14927 323 VEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFIL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 501 EQEEYKKEGIDWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFEKPKPGKG-KAEA 579
Cdd:cd14927 403 EQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKrKYEA 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 580 HFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEA---DTGSKKGGKKKGGSFQTVSAVFR 656
Cdd:cd14927 483 HFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDStedPKSGVKEKRKKAASFQTVSQLHK 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 657 ENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASVIPE 736
Cdd:cd14927 563 ENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPD 642
|
650 660 670
....*....|....*....|....*....|....
gi 1316056572 737 GQFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14927 643 DKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-770 |
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: 1070.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITG 179
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 180 ESGAGKTVNTKRVIQYFATIAALG--SKKDQaqqSSGKiqGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFG 257
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGdrSKKDQ---TPGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 258 TSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFPMISQGEITVKSIDDVEEFIATD 337
Cdd:cd14917 156 ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 338 TAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTK 417
Cdd:cd14917 236 NAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 418 GQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTM 497
Cdd:cd14917 316 GQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 498 FVLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFEKPKPGKGKA 577
Cdd:cd14917 396 FVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKP 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 578 EAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEADTGSKKGGKKKGGSFQTVSAVFRE 657
Cdd:cd14917 476 EAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 658 NLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASVIPEG 737
Cdd:cd14917 556 NLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEG 635
|
650 660 670
....*....|....*....|....*....|...
gi 1316056572 738 QFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14917 636 QFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-770 |
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: 1056.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITG 179
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 180 ESGAGKTVNTKRVIQYFATIAALGSKKDQAQQSSGKiqGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 260 GKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFPMISQGEITVKSIDDVEEFIATDTA 339
Cdd:cd14916 159 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 340 IDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQ 419
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 420 TVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFV 499
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 500 LEQEEYKKEGIDWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFEKPKPGKGKAEA 579
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 580 HFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEA-DTGSKKGGKKKGGSFQTVSAVFREN 658
Cdd:cd14916 479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTgDSGKGKGGKKKGSSFQTVSALHREN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 659 LGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASVIPEGQ 738
Cdd:cd14916 559 LNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQ 638
|
650 660 670
....*....|....*....|....*....|..
gi 1316056572 739 FIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14916 639 FIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
100-770 |
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: 1002.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITG 179
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 180 ESGAGKTVNTKRVIQYFATIAALGSKKdqaqqssgKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESK--------KKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 260 GKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKpELIDALLITTNPYDFPMISQGEITVKSIDDVEEFIATDTA 339
Cdd:cd14929 153 GMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 340 IDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQ 419
Cdd:cd14929 232 MDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 420 TVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFV 499
Cdd:cd14929 312 NIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 500 LEQEEYKKEGIDWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFEKPKPGKGKAEA 579
Cdd:cd14929 392 LEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 580 HFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEADTGSKKGGKKKGGSFQTVSAVFRENL 659
Cdd:cd14929 472 HFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQFGEKKRKKGASFQTVASLHKENL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 660 GKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASVIPEGQF 739
Cdd:cd14929 552 NKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKF 631
|
650 660 670
....*....|....*....|....*....|.
gi 1316056572 740 IDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14929 632 VSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
88-770 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 979.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 88 IEDMAMMTHLNEPCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFML 167
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 168 TDRENQSVLITGESGAGKTVNTKRVIQYFATIAAlgskkdqaqQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSR 247
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSG---------SGSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 248 FGKFIRIHFGTSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLItTNPYDFPMISQ-GEITVKS 326
Cdd:pfam00063 152 FGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TNPKDYHYLSQsGCYTIDG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 327 IDDVEEFIATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYP 406
Cdd:pfam00063 231 IDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 407 RVKVGNEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQ-ARAFFIGVLDIAGFEIFDFNSLEQLCINFT 485
Cdd:pfam00063 311 RIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 486 NEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFGmDLAACIELIE-KPLGIFSILEEECMFPKASDTTFKNKLIDQHlGKN 564
Cdd:pfam00063 391 NEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKH 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 565 RAFEKPKPGKgkaEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLY----AAHASAEADTGSKKG 640
Cdd:pfam00063 469 PHFQKPRLQG---ETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFpdyeTAESAAANESGKSTP 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 641 GKKKGGSFQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYG 720
Cdd:pfam00063 546 KRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQ 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1316056572 721 DFKQRYKVLNASVIPEGqFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:pfam00063 626 EFVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
81-782 |
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: 966.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 81 NPPKFDKIEDMAMMTHLNEPCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISD 160
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 161 NAYQFMLTDRENQSVLITGESGAGKTVNTKRVIQYFATIAalgskkdqaqqSSGKIQGSLEDQIVAANPLLEAYGNAKTV 240
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVS-----------GSNTEVGSVEDQILESNPILEAFGNAKTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 241 RNDNSSRFGKFIRIHFGTSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTnPYDFPMISQG 320
Cdd:smart00242 150 RNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 321 -EITVKSIDDVEEFIATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQA-EPDGTEVADKIAYLLGLNSAD 398
Cdd:smart00242 229 gCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 399 MLKALCYPRVKVGNEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLE 478
Cdd:smart00242 309 LEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 479 QLCINFTNEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFGmDLAACIELIE-KPLGIFSILEEECMFPKASDTTFKNKLi 557
Cdd:smart00242 389 QLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKL- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 558 DQHLGKNRAFEKPKPgkgKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEADTgs 637
Cdd:smart00242 467 NQHHKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGSK-- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 638 kkggkkkgGSFQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRI 717
Cdd:smart00242 542 --------KRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRL 613
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316056572 718 LYGDFKQRYKVLNASVIPEGQFiDNKKASEKLLGSIDVDHTQYKFGHTKVFFKAGLLGTLEEMRD 782
Cdd:smart00242 614 PFDEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-770 |
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: 951.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITG 179
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 180 ESGAGKTVNTKRVIQYFATIAAlGSKKDQAQQSsgkiQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGA-SKKTDEAAKS----KGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 260 GKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFPMISQGEITVKSIDDVEEFIATDTA 339
Cdd:cd14909 156 GKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 340 IDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQ 419
Cdd:cd14909 236 FDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 420 TVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFV 499
Cdd:cd14909 316 NVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 500 LEQEEYKKEGIDWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFEKPKPGK-GKAE 578
Cdd:cd14909 396 LEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 579 AHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEADTGSKKGGKKKG-GSFQTVSAVFRE 657
Cdd:cd14909 476 AHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKgGGFATVSSAYKE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 658 NLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASVIPEG 737
Cdd:cd14909 556 QLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGE 635
|
650 660 670
....*....|....*....|....*....|...
gi 1316056572 738 QfiDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14909 636 E--DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
102-770 |
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: 951.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGES 181
Cdd:cd14934 3 VLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 182 GAGKTVNTKRVIQYFATIAALGSkkdqaQQSSGKiqGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd14934 83 GAGKTENTKKVIQYFANIGGTGK-----QSSDGK--GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 262 LASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFPMISQGEITVKSIDDVEEFIATDTAID 341
Cdd:cd14934 156 LAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 342 ILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQTV 421
Cdd:cd14934 236 VLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 422 PQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFVLE 501
Cdd:cd14934 316 EQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 502 QEEYKKEGIDWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFEKPKPGKGK-AEAH 580
Cdd:cd14934 396 QEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 581 FSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSgNKLLCFLYAAHASAEADTgskkGGKKKGGSFQTVSAVFRENLG 660
Cdd:cd14934 476 FELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKS-SLGLLALLFKEEEAPAGS----KKQKRGSSFMTVSNFYREQLN 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 661 KLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASVIPEGqFI 740
Cdd:cd14934 551 KLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FV 629
|
650 660 670
....*....|....*....|....*....|
gi 1316056572 741 DNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14934 630 DNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
100-770 |
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: 812.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRI-EAPPHIFSISDNAYQFMLTDRENQSVLIT 178
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 179 GESGAGKTVNTKRVIQYFATIAALGSKKDQAQQSSgkiqgsLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGT 258
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSASS------IEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 259 SGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFPM----ISQGEITVKSIDDVEEFI 334
Cdd:cd00124 155 TGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDDAEEFQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 335 ATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREE--QAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGN 412
Cdd:cd00124 235 ELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 413 EMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAF--FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 490
Cdd:cd00124 315 ETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEStsFIGILDIFGFENFEVNSFEQLCINYANEKLQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 491 QFFNHTMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFEK 569
Cdd:cd00124 395 QFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 570 PKpgkgKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKsgnkllcflyaahasaeadtgskkggkkkggsfq 649
Cdd:cd00124 474 KR----KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS---------------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 650 tvSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL 729
Cdd:cd00124 516 --GSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRIL 593
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1316056572 730 NASvIPEGQFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd00124 594 APG-ATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
50-1116 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 810.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 50 CKLIKKDGSKVTVETDGGKTLTVKEDDIhprNPPKFDKIEDMAMMTHLNEPCVLYNLKDRFASWMIYTYSGLFCVVVNPY 129
Cdd:COG5022 33 KGKVTEEGKKEDGESVSVKKKVLGNDRI---KLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 130 KWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGESGAGKTVNTKRVIQYFATIAAlgskkdqa 209
Cdd:COG5022 110 RDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTS-------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 210 qqSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGKLASADIETYLLEKSRVTFQLSAERSYHI 289
Cdd:COG5022 182 --SSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 290 FYQLMTAhKPELIDALLITTNPYDFPMISQGE-ITVKSIDDVEEFIATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKF 368
Cdd:COG5022 260 FYQLLAG-DPEELKKLLLLQNPKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEF 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 369 KqKQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRIN 448
Cdd:COG5022 339 K-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRIN 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 449 EMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFgMDLAACIELI 528
Cdd:COG5022 418 KSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY-FDNQPCIDLI 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 529 EK--PLGIFSILEEECMFPKASDTTFKNKLIDQ-HLGKNRAFEKPKPGKGKaeahFSLVHYAGTVDYNITGWLDKNKDPL 605
Cdd:COG5022 497 EKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVKHYAGDVEYDVEGFLDKNKDPL 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 606 NESVVQLYQKSGNKLLcflyaahasaeADTGSKKGGKKKGGSFQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTP 685
Cdd:COG5022 573 NDDLLELLKASTNEFV-----------STLFDDEENIESKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSP 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 686 GLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASVIPEGQFI---DNKKASEKLLGSIDVDHTQYKF 762
Cdd:COG5022 642 WTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDTKNAVKSILEELVIDSSKYQI 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 763 GHTKVFFKAGLLGTLEEMRDEKLASLVTMTQALCRGYVMRKEFVKMMERRDAIYTVQYNVRSFMNVKNWPWMNLYFKIKP 842
Cdd:COG5022 722 GNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQP 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 843 LLKSAETEKElqnMKEnYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLS---DAEERCEGLIKSKIQL 919
Cdd:COG5022 802 LLSLLGSRKE---YRS-YLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKkrfSLLKKETIYLQSAQRV 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 920 EAKLKETTERLEDEEEINaELTAKKRKLEDECSELKKDID-----DLELTLAKVEKEKHATEN-KVKNLTEEMATQDEAI 993
Cdd:COG5022 878 ELAERQLQELKIDVKSIS-SLKLVNLELESEIIELKKSLSsdlieNLEFKTELIARLKKLLNNiDLEEGPSIEYVKLPEL 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 994 AKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQekklRMDLERAKRKLEgdlklaqesIMDL 1073
Cdd:COG5022 957 NKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQ----YGALQESTKQLK---------ELPV 1023
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*..
gi 1316056572 1074 ENDKQQSDEKIKKKDFEISQLLSKIEDEQSL----GAQLQKKIKELQ 1116
Cdd:COG5022 1024 EVAELQSASKIISSESTELSILKPLQKLKGLllleNNQLQARYKALK 1070
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
101-770 |
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: 783.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 101 CVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGE 180
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 181 SGAGKTVNTKRVIQYFATIAALGSKKDQA----QQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHF 256
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAASKPKGSGAvphpAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 257 GTSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELiDALLITTNPYDFPMISQGEITVKSIDDVEEFIAT 336
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQ-REKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 337 DTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAE-PDGTeVADKIAYLLGLNSADMLKALCYPRVKVGNEMV 415
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 416 TKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLD-TKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 494
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 495 HTMFVLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQHLgknrafEKPKPGK 574
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 575 G--KAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYA----AHASAEADTGSKKGGKKKGGSF 648
Cdd:cd14911 474 TdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKdaeiVGMAQQALTDTQFGARTRKGMF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 649 QTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKV 728
Cdd:cd14911 554 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1316056572 729 LNASVIPEGqFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14911 634 LTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-770 |
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: 750.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGES 181
Cdd:cd14920 3 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 182 GAGKTVNTKRVIQYFATIAAlgskkDQAQQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd14920 83 GAGKTENTKKVIQYLAHVAS-----SHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 262 LASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPEL-IDALLITTNPYDFpmISQGEITVKSIDDVEEFIATDTAI 340
Cdd:cd14920 158 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFNNYRF--LSNGYIPIPGQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 341 DILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAE-PDGTeVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQ 419
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 420 TVPQVNNAVSALCKSVYEKMFLWMVIRINEMLD-TKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMF 498
Cdd:cd14920 315 TKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 499 VLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKASDTTFKNKLIdQHLGKNRAFEKPKPGKG 575
Cdd:cd14920 395 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 576 KAEahFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLY--------AAHASAEADTGSKKGGKKKGGS 647
Cdd:cd14920 474 KAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdvdrivgLDQVTGMTETAFGSAYKTKKGM 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 648 FQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 727
Cdd:cd14920 552 FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1316056572 728 VLNASVIPEGqFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14920 632 ILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
102-770 |
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: 701.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGES 181
Cdd:cd14932 3 VLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 182 GAGKTVNTKRVIQYFATIA-ALGSKKDQAqqSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14932 83 GAGKTENTKKVIQYLAYVAsSFKTKKDQS--SIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 261 KLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITT-NPYDFpmISQGEITVKSIDDVEEFIATDTA 339
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDySKYRF--LSNGNVTIPGQQDKELFAETMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 340 IDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAE-PDGTeVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKG 418
Cdd:cd14932 239 FRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 419 QTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLD-TKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTM 497
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 498 FVLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKASDTTFKNKLIdQHLGKNRAFEKPKpgK 574
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPK--K 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 575 GKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLY-------AAHASAEADTGSKKGGKKKGGS 647
Cdd:cd14932 475 LKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWkdvdrivGLDKVAGMGESLHGAFKTRKGM 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 648 FQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 727
Cdd:cd14932 555 FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 634
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1316056572 728 VLNASVIPEGqFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14932 635 ILTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-770 |
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: 674.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFA-SWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLIT 178
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 179 GESGAGKTVNTKRVIQYFATIAALGSKKDQaqqssgkiqgsLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGT 258
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGGSSSGETQ-----------VEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 259 SGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTA-HKPELiDALLITTNPYDFPMISQGEITVKSIDDVEEFIATD 337
Cdd:cd01380 150 NYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAaSLPEL-KELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 338 TAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEqAEPDGTEVADKIAY-LLGLNSADMLKALCYPRVKVGNEMVT 416
Cdd:cd01380 229 KALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDS-ASISPDDEHLQIACeLLGIDESQLAKWLCKRKIVTRSEVIV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 417 KGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAF--FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 494
Cdd:cd01380 308 KPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhsFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 495 HTMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRA-FEKPKPG 573
Cdd:cd01380 388 QHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKhFKKPRFS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 574 KGKaeahFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLlcflyaahasaeadtgskkggkkkggsfQTVSA 653
Cdd:cd01380 467 NTA----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK----------------------------KTVGS 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 654 VFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASv 733
Cdd:cd01380 515 QFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPS- 593
|
650 660 670
....*....|....*....|....*....|....*..
gi 1316056572 734 iPEGQFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd01380 594 -KEWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
102-770 |
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: 674.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGES 181
Cdd:cd14921 3 VLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 182 GAGKTVNTKRVIQYFATIAAlgSKKDQAQQSsgkIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd14921 83 GAGKTENTKKVIQYLAVVAS--SHKGKKDTS---ITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 262 LASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITT-NPYDFpmISQGEITVKSIDDVEEFIATDTAI 340
Cdd:cd14921 158 IVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGfNNYTF--LSNGFVPIPAAQDDEMFQETLEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 341 DILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAE-PDGTeVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQ 419
Cdd:cd14921 236 SIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 420 TVPQVNNAVSALCKSVYEKMFLWMVIRINEMLD-TKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMF 498
Cdd:cd14921 315 TKEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 499 VLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKASDTTFKNKLIdQHLGKNRAFEKPKPGKG 575
Cdd:cd14921 395 ILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLC-TEQGNHPKFQKPKQLKD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 576 KAEahFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYA--------AHASAEADTGSKKGGKKKGGS 647
Cdd:cd14921 474 KTE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKdvdrivglDQMAKMTESSLPSASKTKKGM 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 648 FQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 727
Cdd:cd14921 552 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1316056572 728 VLNASVIPEGqFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14921 632 ILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-770 |
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: 653.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGES 181
Cdd:cd14919 3 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 182 GAGKTVNTKRVIQYFATIAalgskkdqAQQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd14919 83 GAGKTENTKKVIQYLAHVA--------SSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 262 LASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPEL-IDALLITTNPYDFpmISQGEITVKSIDDVEEFIATDTAI 340
Cdd:cd14919 155 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLkTDLLLEPYNKYRF--LSNGHVTIPGQQDKDMFQETMEAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 341 DILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAE-PDGTeVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQ 419
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 420 TVPQVNNAVSALCKSVYEKMFLWMVIRINEMLD-TKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMF 498
Cdd:cd14919 312 TKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 499 VLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKASDTTFKNKLIdQHLGKNRAFEKPKPGKG 575
Cdd:cd14919 392 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVV-QEQGTHPKFQKPKQLKD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 576 KAEahFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYA--------AHASAEADTGSKKGGKKKGGS 647
Cdd:cd14919 471 KAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriiglDQVAGMSETALPGAFKTRKGM 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 648 FQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 727
Cdd:cd14919 549 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 628
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1316056572 728 VLNASVIPEGqFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14919 629 ILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
102-770 |
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: 650.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGES 181
Cdd:cd15896 3 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 182 GAGKTVNTKRVIQYFATIAAlGSKKDQAQQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd15896 83 GAGKTENTKKVIQYLAHVAS-SHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 262 LASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITT-NPYDFpmISQGEITVKSIDDVEEFIATDTAI 340
Cdd:cd15896 162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENyNNYRF--LSNGNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 341 DILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAE-PDGTeVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQ 419
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASmPDNT-AAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 420 TVPQVNNAVSALCKSVYEKMFLWMVIRINEMLD-TKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMF 498
Cdd:cd15896 319 TQEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 499 VLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKASDTTFKNKLIdQHLGKNRAFEKPKpgKG 575
Cdd:cd15896 399 ILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVL-QEQGTHPKFFKPK--KL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 576 KAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLY------AAHASAEADTGSKKGGKKKGGSFQ 649
Cdd:cd15896 476 KDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWkdvdriVGLDKVSGMSEMPGAFKTRKGMFR 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 650 TVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL 729
Cdd:cd15896 556 TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 635
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1316056572 730 NASVIPEGqFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd15896 636 TPNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
102-770 |
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: 630.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGES 181
Cdd:cd14930 3 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 182 GAGKTVNTKRVIQYFATIAAlgSKKDQAQQSsgkIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd14930 83 GAGKTENTKKVIQYLAHVAS--SPKGRKEPG---VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 262 LASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPEL-IDALLITTNPYDF----PMISQGEitvksidDVEEFIAT 336
Cdd:cd14930 158 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLkADLLLEPCSHYRFltngPSSSPGQ-------ERELFQET 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 337 DTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAE-PDGTeVADKIAYLLGLNSADMLKALCYPRVKVGNEMV 415
Cdd:cd14930 231 LESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 416 TKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLD-TKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 494
Cdd:cd14930 310 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 495 HTMFVLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKASDTTFKNKlIDQHLGKNRAFEKPK 571
Cdd:cd14930 390 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEK-VAQEQGGHPKFQRPR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 572 PGKGKAEahFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYA--------AHASAEADTgsKKGGKK 643
Cdd:cd14930 469 HLRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegivglEQVSSLGDG--PPGGRP 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 644 KGGSFQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFK 723
Cdd:cd14930 545 RRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFR 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1316056572 724 QRYKVLNASVIPEGqFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14930 625 QRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-770 |
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: 618.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRgkKRIEAPPHIFSISDNAYQFMLTDRENQSVLITG 179
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 180 ESGAGKTVNTKRVIQYfatIAALGSkkdqaqQSSGkiqgsLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd01383 79 ESGAGKTETAKIAMQY---LAALGG------GSSG-----IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 260 GKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTnPYDFPMISQGE-ITVKSIDDVEEFIATDT 338
Cdd:cd01383 145 GKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQSNcLTIDGVDDAKKFHELKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 339 AIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKG 418
Cdd:cd01383 224 ALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 419 QTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQAR-AFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTM 497
Cdd:cd01383 304 LTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRtGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 498 FVLEQEEYKKEGIDWEFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKASDTTFKNKLiDQHLGKNRAFekpkpgKGK 576
Cdd:cd01383 384 FKLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 577 AEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEADTGSKKGGKKKGGSFQTVSAVFR 656
Cdd:cd01383 456 RGGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASRKALPLTKASGSDSQKQSVATKFK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 657 ENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLnasvIPE 736
Cdd:cd01383 536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFL----LPE 611
|
650 660 670
....*....|....*....|....*....|....*.
gi 1316056572 737 GQFIDNKKASEK--LLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd01383 612 DVSASQDPLSTSvaILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
102-770 |
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: 611.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGES 181
Cdd:cd01381 3 ILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 182 GAGKTVNTKRVIQYFATIaalgskkdqaqqsSGKiQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd01381 83 GAGKTESTKLILQYLAAI-------------SGQ-HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 262 LASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTnPYDFPMISQGE-ITVKSIDDVEEFIATDTAI 340
Cdd:cd01381 149 IEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGD-ASDYYYLTQGNcLTCEGRDDAAEFADIRSAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 341 DILGFTADEKFNIYKLTGAVMHHGNMKFKQKQRE--EQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKG 418
Cdd:cd01381 228 KVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 419 QTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFF---IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 495
Cdd:cd01381 308 LSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 496 TMFVLEQEEYKKEGIDWEFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKASDTTFKNKLIDQHlGKNRAFEKPkpgK 574
Cdd:cd01381 388 HIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP---K 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 575 GKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEADTGSKKggkkkggsfQTVSAV 654
Cdd:cd01381 463 SDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKS---------PTLSSQ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 655 FRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLnASVI 734
Cdd:cd01381 534 FRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVL-VPGI 612
|
650 660 670
....*....|....*....|....*....|....*.
gi 1316056572 735 PEGQFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd01381 613 PPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
105-770 |
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: 604.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 105 NLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGESGAG 184
Cdd:cd01378 6 NLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESGAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 185 KTVNTKRVIQYfatIAALGSKkdqaqqSSGKIQGsLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGKLAS 264
Cdd:cd01378 86 KTEASKRIMQY---IAAVSGG------SESEVER-VKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 265 ADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFPMISQGEITVKSIDDVEEFIATDTAIDILG 344
Cdd:cd01378 156 GHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 345 FTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDgTEVADKIAYLLGLNSADMLKALCYPRVKVGNEM---VTKGQTV 421
Cdd:cd01378 236 FTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 422 PQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARA-FFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFnhTMFVL 500
Cdd:cd01378 315 EQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIF--IELTL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 501 --EQEEYKKEGIDWEFIDFgMDLAACIELIE-KPLGIFSILEEECMFP-KASDTTFKNKLiDQHLGKNRAFEKPKPGKGK 576
Cdd:cd01378 393 kaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHFEL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 577 AEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLL--CFLYAahasAEADTGSKKGgkkkggsfqTVSAV 654
Cdd:cd01378 471 RRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLrsLFPEG----VDLDSKKRPP---------TAGTK 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 655 FRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASVI 734
Cdd:cd01378 538 FKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTW 617
|
650 660 670
....*....|....*....|....*....|....*.
gi 1316056572 735 PEGQFIDnKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd01378 618 PAWDGTW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
102-770 |
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: 585.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGES 181
Cdd:cd14883 3 INTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 182 GAGKTVNTKRVIQYfatIAALGSKKDQAQQssgkiqgsledQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd14883 83 GAGKTETTKLILQY---LCAVTNNHSWVEQ-----------QILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 262 LASADIETYLLEKSRVTFQLSAERSYHIFYQLMT--AHKPELiDALLITTNPYDFPMISQ-GEITVKSIDDVEEFIATDT 338
Cdd:cd14883 149 IKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAgaKHSKEL-KEKLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 339 AIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAE-PDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTK 417
Cdd:cd14883 228 AMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 418 GQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTM 497
Cdd:cd14883 308 PLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 498 FVLEQEEYKKEGIDWEFIDFgMDLAACIELIEK-PLGIFSILEEECMFPKASDTTFKNKLIDQHlGKNRAFEKPKPGKGK 576
Cdd:cd14883 388 FKLEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPDRRRWK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 577 AEahFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLL--CFLYAAHASAEADTGSKKGGKKKGGSFQ---TV 651
Cdd:cd14883 466 TE--FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVkeLFTYPDLLALTGLSISLGGDTTSRGTSKgkpTV 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 652 SAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNa 731
Cdd:cd14883 544 GDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLD- 622
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1316056572 732 sviPEGQFIDNKKASE---KLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14883 623 ---PRARSADHKETCGavrALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
100-770 |
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: 563.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLP-VYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLIT 178
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 179 GESGAGKTVNTKRVIQYfatIAALGSKKDQAQQSsgkiqgsLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGT 258
Cdd:cd01384 81 GESGAGKTETTKMLMQY---LAYMGGRAVTEGRS-------VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 259 SGKLASADIETYLLEKSRVTfQLSA-ERSYHIFYQLMTAHKPELIDALLITTnPYDFPMISQGE-ITVKSIDDVEEFIAT 336
Cdd:cd01384 151 AGRISGAAIRTYLLERSRVV-QVSDpERNYHCFYQLCAGAPPEDREKYKLKD-PKQFHYLNQSKcFELDGVDDAEEYRAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 337 DTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKqkqreEQAEPDGTEVADK--------IAYLLGLNSADMLKALCYPRV 408
Cdd:cd01384 229 RRAMDVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEksefhlkaAAELLMCDEKALEDALCKRVI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 409 KVGNEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEK 488
Cdd:cd01384 304 VTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 489 LQQFFNHTMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKASDTTFKNKLIDQhLGKNRAF 567
Cdd:cd01384 384 LQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 568 EKPKpgkgKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEAdtgskkggkKKGGS 647
Cdd:cd01384 462 SKPK----LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGT---------SSSSK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 648 FQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 727
Cdd:cd01384 529 FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFG 608
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1316056572 728 VLnASVIPEGQFiDNKKASEKLLGSIDVDhtQYKFGHTKVFFK 770
Cdd:cd01384 609 LL-APEVLKGSD-DEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
103-770 |
1.81e-168 |
|
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: 529.13 E-value: 1.81e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 103 LYNLKDRFASWMIYTYSGLFCVVVNPYKWLP-VYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGES 181
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 182 GAGKTVNTKRVIQYFAtiaalgskkdqaqQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd01382 84 GAGKTESTKYILRYLT-------------ESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 262 LASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLittnpydfpmisqgeiTVKSIDDVEEFIATDTAID 341
Cdd:cd01382 151 VVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 342 ILGFTADEKFNIYKLTGAVMHHGNMKFkqkqrEEQAEPD--GTEVADK-------IAYLLGLNSADMLKALCYpRVKVGN 412
Cdd:cd01382 215 KIGLSDEEKLDIFRVVAAVLHLGNIEF-----EENGSDSggGCNVKPKseqsleyAAELLGLDQDELRVSLTT-RVMQTT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 413 EMVTKGQ--TVP----QVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQArAFFIGVLDIAGFEIFDFNSLEQLCINFTN 486
Cdd:cd01382 289 RGGAKGTviKVPlkveEANNARDALAKAIYSKLFDHIVNRINQCIPFETS-SYFIGVLDIAGFEYFEVNSFEQFCINYCN 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 487 EKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNR 565
Cdd:cd01382 368 EKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNHFR 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 566 aFEKPKPGKGKA-------EAhFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEADTgsk 638
Cdd:cd01382 447 -LSIPRKSKLKIhrnlrddEG-FLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDS--- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 639 kGGKKKGGSFQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRIL 718
Cdd:cd01382 522 -KQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTS 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1316056572 719 YGDFKQRYKvlnaSVIPEG-QFIDNK---KASEKLLGSIDVDhtqYKFGHTKVFFK 770
Cdd:cd01382 601 FHDLYNMYK----KYLPPKlARLDPRlfcKALFKALGLNEND---FKFGLTKVFFR 649
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
100-770 |
6.86e-166 |
|
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: 522.72 E-value: 6.86e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLP-VYDAVVVAGYRgKKRIEAPPHIFSISDNAYQFMLTDRENQSVLIT 178
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 179 GESGAGKTVNTKRVIQYFATIAALGSKKdqaqqssgkiQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHF-- 256
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKK----------RSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsk 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 257 -------GTSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLIT-TNPYDFPMISQGEITV---- 324
Cdd:cd14888 150 lkskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEeNDEKLAKGADAKPISIdmss 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 325 -----------KS-------IDDVEEFIATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQA---EPDGTE 383
Cdd:cd14888 230 fephlkfryltKSschelpdVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 384 VADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARA-FFIG 462
Cdd:cd14888 310 DLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSlLFCG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 463 VLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFGmDLAACIELI-EKPLGIFSILEEE 541
Cdd:cd14888 390 VLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 542 CMFPKASDTTFKNKLIDQHLGKNRaFEKPKpgkgKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLL 621
Cdd:cd14888 469 CFVPGGKDQGLCNKLCQKHKGHKR-FDVVK----TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFI 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 622 CFLYAAHASAEADtgskkgGKKKGGSFQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNG 701
Cdd:cd14888 544 SNLFSAYLRRGTD------GNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGG 617
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316056572 702 VLEGIRICRKGFPSRILYGDFKQRYKVLnasvipegqfidnkkasekLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14888 618 VLQAVQVSRAGYPVRLSHAEFYNDYRIL-------------------LNGEGKKQLSIWAVGKTLCFFK 667
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
850-1927 |
4.54e-165 |
|
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: 534.75 E-value: 4.54e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 850 EKELQNMKENYEKMQSDLttalakkKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAKLKETTER 929
Cdd:pfam01576 11 EEELQKVKERQQKAESEL-------KELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 930 LEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQ 1009
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1010 TLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDEKIKKKDF 1089
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1090 EISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNK 1169
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1170 KREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEAVAKAKGNL 1249
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1250 EKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKA 1329
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1330 KNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYETDAiQRTEELEEAKKKLAQRLQEAEESIE 1409
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1410 AVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMK 1489
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1490 NSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQLEL 1569
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1570 NQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRN 1649
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1650 VQGQLKDAQLHLDDAVRGQEDMKEQVAMVERRNGLMVAEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLN 1729
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1730 TKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLAM 1809
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1810 KGGKKQLQKLEQRVRELETEVEGEQKRGADAVKGVRKYERRVKELTYQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEA 1889
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 1316056572 1890 EEQANSHMSRLRKVQHEMEEAQERADIAESQVNKLRAK 1927
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
100-770 |
3.03e-162 |
|
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: 512.01 E-value: 3.03e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITG 179
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 180 ESGAGKTVNTKRVIQYFATIAalGSkkdqaqqssgkiQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVA--GS------------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 260 GKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELiDALLITTNPYDFpmISQGE-ITVKSIDDVEEFIATDT 338
Cdd:cd14872 147 GRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPAS-RGGWGSSAAYGY--LSLSGcIEVEGVDDVADFEEVVL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 339 AIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGT---EVADKIAYLLGLNSADMLKALCYPRVKVGNEMV 415
Cdd:cd14872 224 AMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVanrDVLKEVATLLGVDAATLEEALTSRLMEIKGCDP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 416 TKGQTVP-QVNNAVSALCKSVYEKMFLWMVIRINE-MLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 493
Cdd:cd14872 304 TRIPLTPaQATDACDALAKAAYSRLFDWLVKKINEsMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 494 NHTMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIEK-PLGIFSILEEECMFPKASDTTFKNKlIDQHLGKNRAFEkpKP 572
Cdd:cd14872 384 NQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIA-ANQTHAAKSTFV--YA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 573 GKGKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAhasAEADTGSKKGgkkkggsfqTVS 652
Cdd:cd14872 460 EVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPP---SEGDQKTSKV---------TLG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 653 AVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 732
Cdd:cd14872 528 GQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKT 607
|
650 660 670
....*....|....*....|....*....|....*...
gi 1316056572 733 vIPEGQFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14872 608 -IAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
102-770 |
5.60e-160 |
|
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: 506.62 E-value: 5.60e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLP-VYDAVVVAGYRGKKRIEAPPHIFSISDNAY-QFM---LTDRENQSVL 176
Cdd:cd14890 3 LLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtQLIqsgVLDPSNQSII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 177 ITGESGAGKTVNTKRVIQYFATIA---ALGSKKDQAQQSSGKIQ--GSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKF 251
Cdd:cd14890 83 ISGESGAGKTEATKIIMQYLARITsgfAQGASGEGEAASEAIEQtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGKF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 252 IRIHFGTSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTnPYDFPMISQGEITVKSIDDVE 331
Cdd:cd14890 163 IEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 332 EFIATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGT-EVADKIAYLLGLNSADMLKALCYPRVKV 410
Cdd:cd14890 242 AFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQLFV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 411 GNEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 490
Cdd:cd14890 322 GGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKLQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 491 QFFNHTMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIE-----KPlGIFSILeEECMFPKASDT----------TFKNK 555
Cdd:cd14890 402 RHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgkvngKP-GIFITL-DDCWRFKGEEAnkkfvsqlhaSFGRK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 556 LIDQHLGKNRA----FEKPKPGKGKaeaHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLlcflyaahasa 631
Cdd:cd14890 479 SGSGGTRRGSSqhphFVHPKFDADK---QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI----------- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 632 eadtgskkggkkkggSFQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRK 711
Cdd:cd14890 545 ---------------REVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQ 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 712 GFPSRILYGDFKQRYKVLNASVipegqfiDNKKASEKLLGSI-DVDHTQYKFGHTKVFFK 770
Cdd:cd14890 610 GFALREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKMlGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
103-770 |
1.82e-157 |
|
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: 500.75 E-value: 1.82e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 103 LYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGESG 182
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 183 AGKTVNTKRVIQYfatIAALgSKKDQAqqsSGkiqgsLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGKL 262
Cdd:cd01385 84 SGKTESTNFLLHH---LTAL-SQKGYG---SG-----VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 263 ASADIETYLLEKSRVTFQLSAERSYHIFYQLMtAHKPELIDALLITTNPYDFPMISQGE-ITVKSIDDVEEFIATDTAID 341
Cdd:cd01385 152 RGAVVEKYLLEKSRIVSQEKNERNYHVFYYLL-AGASEEERKELHLKQPEDYHYLNQSDcYTLEGEDEKYEFERLKQAME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 342 ILGFTADEKFNIYKLTGAVMHHGNMKFKQK--QREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQ 419
Cdd:cd01385 231 MVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 420 TVPQVNNAVSALCKSVYEKMFLWMVIRINEML----DTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 495
Cdd:cd01385 311 KLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 496 TMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKASDTTFKNKLiDQHLGKNRAFEKPKpgk 574
Cdd:cd01385 391 HIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAKF-KQQHKDNKYYEKPQ--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 575 gKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNK------------------LLCFLYAAHASAEA--- 633
Cdd:cd01385 466 -VMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAfvreligidpvavfrwavLRAFFRAMAAFREAgrr 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 634 --------------DTGSKKGGKKKGGSFQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRC 699
Cdd:cd01385 545 raqrtaghsltlhdRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRY 624
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316056572 700 NGVLEGIRICRKGFPSRILYGDFKQRYKVLnasvIPEGQfIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd01385 625 TGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
100-770 |
3.42e-157 |
|
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: 498.92 E-value: 3.42e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLP-VYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLIT 178
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 179 GESGAGKTVNTKRVIQYFATIAalgskkdqaqqssGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGT 258
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA-------------GGLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 259 SGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLiTTNPYDFPmisqGEITVKSID---DVEEFIA 335
Cdd:cd14903 148 NGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLD-SANECAYT----GANKTIKIEgmsDRKHFAR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 336 TDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAE--PDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNE 413
Cdd:cd14903 223 TKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 414 MVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 493
Cdd:cd14903 303 VYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 494 NHTMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFEKPKPG 573
Cdd:cd14903 383 TQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 574 KgkaeAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEADTGSKKGGKKKGGS-----F 648
Cdd:cd14903 462 R----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRggaltT 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 649 QTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKV 728
Cdd:cd14903 538 TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1316056572 729 LnasvIPEGQFIDNKKAS--EKLLGSIDVDH-TQYKFGHTKVFFK 770
Cdd:cd14903 618 F----LPEGRNTDVPVAErcEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
106-770 |
3.75e-154 |
|
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: 490.43 E-value: 3.75e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 106 LKDRFASWMIYTYSGLFCVVVNPYKWLP-VYDavvVAGYRGKKRIEA-----PPHIFSISDNAYQFMLTDR----ENQSV 175
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYD---VPGFDSQRKEEAtasspPPHVFSIAERAYRAMKGVGkgqgTPQSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 176 LITGESGAGKTVNTKRVIQYFATIAALGSKKDQAQQSSGkIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIH 255
Cdd:cd14892 84 VVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAAN-AHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 256 FGTSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMtAHKPELIDALLITTNPYDFPMISQGE-ITVKSIDDVEEFI 334
Cdd:cd14892 163 YNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLL-AGLDANENAALELTPAESFLFLNQGNcVEVDGVDDATEFK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 335 ATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVAD--KIAYLLGLNSADMLKALCYpRVKVGn 412
Cdd:cd14892 242 QLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvaKAAGLLGVDAAELMFKLVT-QTTST- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 413 emvTKGQ------TVPQVNNAVSALCKSVYEKMFLWMVIRINEM----------LDTKQARAFFIGVLDIAGFEIFDFNS 476
Cdd:cd14892 320 ---ARGSvleiklTAREAKNALDALCKYLYGELFDWLISRINAChkqqtsgvtgGAASPTFSPFIGILDIFGFEIMPTNS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 477 LEQLCINFTNEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIEK-PLGIFSILEEECMFP-KASDTTFKN 554
Cdd:cd14892 397 FEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 555 KLIDQHLGKNRAFEKPKPGKgkaeAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYqKSGNKllcflyaahasaead 634
Cdd:cd14892 476 IYHQTHLDKHPHYAKPRFEC----DEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLL-RSSSK--------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 635 tgskkggkkkggsfqtvsavFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFP 714
Cdd:cd14892 536 --------------------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFP 595
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316056572 715 SRILYGDFKQRYKVL-------NASVIPEGQFIDNKKASEKLLGSIDVDHTQykFGHTKVFFK 770
Cdd:cd14892 596 IRRQFEEFYEKFWPLarnkagvAASPDACDATTARKKCEEIVARALERENFQ--LGRTKVFLR 656
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
100-768 |
6.08e-153 |
|
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: 486.99 E-value: 6.08e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGY------RGKKRIEAPPHIFSISDNAYQFMLTDRE-- 171
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 172 --NQSVLITGESGAGKTVNTKRVIQYFATIAALGSKKDQAQQSSgkiqgSLEDQIVAANPLLEAYGNAKTVRNDNSSRFG 249
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERE-----NVRDRVLESNPILEAFGNARTNRNNNSSRFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 250 KFIRIHFGTSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNP-YDFPMISQGEITVKSID 328
Cdd:cd14901 156 KFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEeYKYLNSSQCYDRRDGVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 329 DVEEFIATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEV-ADKIAYLLGLNSADMLKALCYPR 407
Cdd:cd14901 236 DSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLAnVRAACDLLGLDMDVLEKTLCTRE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 408 VKVGNEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEML----DTKQARafFIGVLDIAGFEIFDFNSLEQLCIN 483
Cdd:cd14901 316 IRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIayseSTGASR--FIGIVDIFGFEIFATNSLEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 484 FTNEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFGMDlAACIELIE-KPLGIFSILEEECMFPKASDTTFKNKLIDQhLG 562
Cdd:cd14901 394 FANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 563 KNRAFEKPKPGKGKAEahFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCflyaahasaeadtgskkggk 642
Cdd:cd14901 472 KHASFSVSKLQQGKRQ--FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS-------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 643 kkggsfQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDF 722
Cdd:cd14901 530 ------STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAF 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1316056572 723 KQRYKVLNASVIPEGQFIDNKKASEKLLGSIDV----DHTQYKFGHTKVF 768
Cdd:cd14901 604 VHTYSCLAPDGASDTWKVNELAERLMSQLQHSElnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
102-770 |
7.24e-152 |
|
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: 484.26 E-value: 7.24e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGES 181
Cdd:cd01387 3 VLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 182 GAGKTVNTKRVIQYFATIAalgskkdqaqQSSGKIQgslEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFgTSGK 261
Cdd:cd01387 83 GSGKTEATKLIMQYLAAVN----------QRRNNLV---TEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 262 LASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDAL-LITTNPYdFPMISQGEITVKSIDDVEEFIATDTAI 340
Cdd:cd01387 149 IVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYgLQEAEKY-FYLNQGGNCEIAGKSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 341 DILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEpdGTEVADK-----IAYLLGLNSADMLKALCYPRVKVGNEMV 415
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQE--GVSVGSDaeiqwVAHLLQISPEGLQKALTFKVTETRRERI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 416 TKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 495
Cdd:cd01387 306 FTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 496 TMFVLEQEEYKKEGIDWEFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKASDTTFKNKLIDQHlGKNRAFEKPKPGk 574
Cdd:cd01387 386 HVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPRMP- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 575 gkaEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHAsAEADTGSKKGGKKKGGSFQ----T 650
Cdd:cd01387 463 ---LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHR-AQTDKAPPRLGKGRFVTMKprtpT 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 651 VSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLN 730
Cdd:cd01387 539 VAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLV 618
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1316056572 731 ASVIPEGQFIDNKKA-SEKLLGSIDVDhtQYKFGHTKVFFK 770
Cdd:cd01387 619 ALKLPRPAPGDMCVSlLSRLCTVTPKD--MYRLGATKVFLR 657
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
102-770 |
4.84e-149 |
|
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: 475.23 E-value: 4.84e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGES 181
Cdd:cd01379 3 IVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 182 GAGKTVNTKRVIQYfatIAALGSKKDQaqqssgkiqgSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd01379 83 GAGKTESANLLVQQ---LTVLGKANNR----------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 262 LASADIETYLLEKSRVTFQLSAERSYHIFYQLMT--AHKPELIDALLITTNP----YDFPMISQgEITVKSIdDVEEFIA 335
Cdd:cd01379 150 VTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAglAEDKKLAKYKLPENKPprylQNDGLTVQ-DIVNNSG-NREKFEE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 336 TDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQ----AEPDGTEVADKIAYLLGLNSADMLKALcyprvkVG 411
Cdd:cd01379 228 IEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEAL------TS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 412 NEMVTKGQT------VPQVNNAVSALCKSVYEKMFLWMVIRINEML--DTKQA-RAFFIGVLDIAGFEIFDFNSLEQLCI 482
Cdd:cd01379 302 HSVVTRGETiirnntVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASdEPLSIGILDIFGFENFQKNSFEQLCI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 483 NFTNEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFG-----MDLaacieLIEKPLGIFSILEEECMFPKASDTTFKNKLi 557
Cdd:cd01379 382 NIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKF- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 558 dQHLGKNRAFEKPKpgkgKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLcflyaahasaeadtgs 637
Cdd:cd01379 456 -HNNIKSKYYWRPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV---------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 638 kkggkkkggsFQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRI 717
Cdd:cd01379 515 ----------RQTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRI 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1316056572 718 LYGDFKQRYKVL--NASVIPEGqfidNKKASEKLLGSIDVDHtqYKFGHTKVFFK 770
Cdd:cd01379 585 LFADFLKRYYFLafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
102-770 |
1.43e-144 |
|
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: 463.88 E-value: 1.43e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLP-VYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGE 180
Cdd:cd14873 3 IMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 181 SGAGKTVNTKRVIQYFATIAalgskKDQAQQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14873 83 SGAGKTESTKLILKFLSVIS-----QQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 261 KLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTnPYDFPMISQ-GEITVKSIDDVEEFIATDTA 339
Cdd:cd14873 158 NIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST-PENYHYLNQsGCVEDKTISDQESFREVITA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 340 IDILGFTADEKFNIYKLTGAVMHHGNMKFkqkqreeqAEPDGTEVADKIAY-----LLGLNSADMLKALCYPRVKVGNEM 414
Cdd:cd14873 237 MEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKTALgrsaeLLGLDPTQLTDALTQRSMFLRGEE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 415 VTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAfFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 494
Cdd:cd14873 309 ILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 495 HTMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQHlGKNRAFEKPKpgk 574
Cdd:cd14873 388 KHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPR--- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 575 gKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGnklLCFLYAAHASAEADTGSKKGGKKKGGSFQTVSAV 654
Cdd:cd14873 463 -VAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESR---FDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 655 FRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL-NASV 733
Cdd:cd14873 539 FKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLmRNLA 618
|
650 660 670
....*....|....*....|....*....|....*..
gi 1316056572 734 IPEgqfiDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14873 619 LPE----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
102-770 |
1.99e-142 |
|
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: 457.23 E-value: 1.99e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKK-RIEAPPHIFSISDNAYQFMLTDRENQSVLITGE 180
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 181 SGAGKTVNTKRVIQYFATIaalgskkdqaqqsSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKL-------------SPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 261 KLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLItTNPYDFPMISQGEITVKSIDDVEEF----IAT 336
Cdd:cd14897 150 QLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELeyyrQMF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 337 DTAIDIL---GFTADEKFNIYKLTGAVMHHGNMKFkqkqrEEQAEPDGTEVADK-----IAYLLGLNSADMLKALCYPRV 408
Cdd:cd14897 229 HDLTNIMkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVN 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 409 KVGNEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQ-----ARAFFIGVLDIAGFEIFDFNSLEQLCIN 483
Cdd:cd14897 304 TIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKdfqimTRGPSIGILDMSGFENFKINSFDQLCIN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 484 FTNEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKASDTTFKNKLIDqHLG 562
Cdd:cd14897 384 LSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNK-YCG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 563 KNRAFEKPKPGKgkaeAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHasaeadtgskkggk 642
Cdd:cd14897 462 ESPRYVASPGNR----VAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY-------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 643 kkggsfqtvsavFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDF 722
Cdd:cd14897 524 ------------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDF 591
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1316056572 723 KQRYKVL-----NASVIPEGQFIDNKKasekllgsiDVDHTQYKFGHTKVFFK 770
Cdd:cd14897 592 VKRYKEIcdfsnKVRSDDLGKCQKILK---------TAGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
102-729 |
1.45e-138 |
|
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: 446.29 E-value: 1.45e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLP-VYDAVVVAGY-----------RGKKRIEAPPHIFSISDNAYQFM--- 166
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 167 -LTDRENQSVLITGESGAGKTVNTKRVIQYFATIaalGSKKDQAQQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNS 245
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQA---GDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 246 SRFGKFIRIHFGTSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMtahkpelidallittnpydfpmISQGEITVK 325
Cdd:cd14900 160 SRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMA----------------------IGASEAARK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 326 SiddvEEFIATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVA-------DKIAYLLGLNSAD 398
Cdd:cd14900 218 R----DMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 399 MLKALCYPRVKVGNEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEML-----DTKQARAFFIGVLDIAGFEIFD 473
Cdd:cd14900 294 LEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 474 FNSLEQLCINFTNEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKASDTTF 552
Cdd:cd14900 374 KNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 553 KNKLIdQHLGKNRAFEKPKPGKGKaeAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNkllcflyaahasae 632
Cdd:cd14900 453 ASKLY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYGLQ-------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 633 adtgskkggkkkggsfqtvsavFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKG 712
Cdd:cd14900 516 ----------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAG 573
|
650
....*....|....*..
gi 1316056572 713 FPSRILYGDFKQRYKVL 729
Cdd:cd14900 574 FPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
102-770 |
2.51e-134 |
|
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: 436.00 E-value: 2.51e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLP-VYDAVVVAGY------RGKKRI--EAPPHIFSISDNAYQFMLTDREN 172
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYkeqiiqNGEYFDikKEPPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 173 QSVLITGESGAGKTVNTKRVIQYFATIAALGSKKDQAQQ------SSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSS 246
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTltssirATSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 247 RFGKFIRIHFG-TSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFP--MISQGE-I 322
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSGDRydYLKKSNcY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 323 TVKSIDDVEEFIATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQ--REEQAEPDGTEVADKIAYLLGLNSADML 400
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 401 KALCYPRVKVGNEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEML--------DTKQARAFFIGVLDIAGFEIF 472
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 473 DFNSLEQLCINFTNEKLQQFFNHTMFVLEQEEYKKEGIDWEF--IDFgMDLAACIELIEK-PLGIFSILEEECMFPKASD 549
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 550 TTFKNKLIDQHlGKNRAFEKPKPGKGKAeahFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHA 629
Cdd:cd14907 482 EKLLNKIKKQH-KNNSKLIFPNKINKDT---FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGED 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 630 SAEADTGSKKGGKKKGGSFqtVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRIC 709
Cdd:cd14907 558 GSQQQNQSKQKKSQKKDKF--LGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVR 635
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316056572 710 RKGFPSRILYGDFKQRYKVLNASVIpegqfidnkkasekllgsidvdhtqykFGHTKVFFK 770
Cdd:cd14907 636 KQGYPYRKSYEDFYKQYSLLKKNVL---------------------------FGKTKIFMK 669
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
100-770 |
2.19e-133 |
|
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: 432.83 E-value: 2.19e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLP-VYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLIT 178
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 179 GESGAGKTVNTKRVIQYFATIAalGSKKDqaqqssgkiqgSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGT 258
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA--GGRKD-----------KTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 259 SGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMT-AHKPELIDALLITTNPYDFPMISQGEITVKSIDDVEEFIATD 337
Cdd:cd14904 148 RGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAgLSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 338 TAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVAdKIAYLLGLNSADMLKALCYPRVKVGNEMVTK 417
Cdd:cd14904 228 KSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLS-QVAKMLGLPTTRIEEALCNRSVVTRNESVTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 418 GQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAF-FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHT 496
Cdd:cd14904 307 PLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 497 MFVLEQEEYKKEGIDWEFIDFgMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQH--LGKNRAFEKPKPGK 574
Cdd:cd14904 387 VFKTVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 575 gkaeAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYaahASAEADTGSKKGGK-KKGGSFQTVSA 653
Cdd:cd14904 466 ----TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF---GSSEAPSETKEGKSgKGTKAPKSLGS 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 654 VFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLnasV 733
Cdd:cd14904 539 QFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM---F 615
|
650 660 670
....*....|....*....|....*....|....*...
gi 1316056572 734 IPEGQFIDNKKASEKLLGSIDVDHT-QYKFGHTKVFFK 770
Cdd:cd14904 616 PPSMHSKDVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
46-830 |
3.98e-132 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 434.84 E-value: 3.98e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 46 LYVKCK-LIKKDGSKVT---VETDGGKTLTVKEDDIHPRNPP-KFDKIEDMAMMTHLNEPCVLYNLKDRFASWMIYTYSG 120
Cdd:PTZ00014 51 MFAKCLvLPGSTGEKLTlkqIDPPTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTAD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 121 LFCVVVNPYKWLPVYDAVVVAGYR-GKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGESGAGKTVNTKRVIQYFATi 199
Cdd:PTZ00014 131 PLLVAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 200 aalGSKKDQaqqsSGKIQgsleDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGKLASADIETYLLEKSRVTF 279
Cdd:PTZ00014 210 ---SKSGNM----DLKIQ----NAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 280 QLSAERSYHIFYQLMTAHKPELIDAL-LITTNPYDFpmISQGEITVKSIDDVEEFIATDTAIDILGFTADEKFNIYKLTG 358
Cdd:PTZ00014 279 QEDDERSYHIFYQLLKGANDEMKEKYkLKSLEEYKY--INPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 359 AVMHHGNMKFKQKQREEQAE-----PDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQTVPQVNNAVSALCK 433
Cdd:PTZ00014 357 GVLLLGNVEIEGKEEGGLTDaaaisDESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSK 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 434 SVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFVLEQEEYKKEGIDWE 513
Cdd:PTZ00014 437 AVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTE 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 514 FIDFGMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLIDQhLGKNRAFekpKPGKGKAEAHFSLVHYAGTVDYN 593
Cdd:PTZ00014 517 ELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTN-LKNNPKY---KPAKVDSNKNFVIKHTIGDIQYC 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 594 ITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAhasaeadtgsKKGGKKKGGSFQTVSAVFRENLGKLMTNLRSTHPHF 673
Cdd:PTZ00014 593 ASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEG----------VEVEKGKLAKGQLIGSQFLNQLDSLMSLINSTEPHF 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 674 VRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASVIpEGQFIDNKKASEKLLGSI 753
Cdd:PTZ00014 663 IRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVS-NDSSLDPKEKAEKLLERS 741
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 754 DVDHTQYKFGHTKVFFKAGLLGTLEEMRDEKLAS---LVTMTQALCRGYVMRKefvKMMERRDAIYTVQYNVRSFMNVKN 830
Cdd:PTZ00014 742 GLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAwepLVSVLEALILKIKKKR---KVRKNIKSLVRIQAHLRRHLVIAE 818
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
102-770 |
9.03e-132 |
|
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: 427.92 E-value: 9.03e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFAS--WMIYTYSGLFCVVVNPYKWLPVYDavvVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRE---NQSVL 176
Cdd:cd14891 3 ILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLPEPD---KSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQSIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 177 ITGESGAGKTVNTKRVIQYFATIAALGSK--KDQAQQSSGKIQG---SLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKF 251
Cdd:cd14891 80 ISGESGAGKTETSKIILRFLTTRAVGGKKasGQDIEQSSKKRKLsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFGKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 252 IRIHFGTSG-KLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLItTNPYDFPMISQ-GEITVKSIDD 329
Cdd:cd14891 160 MKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLL-LSPEDFIYLNQsGCVSDDNIDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 330 VEEFIATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREE----QAEPDGTEVADKIAYLLGLNSADMLKALCY 405
Cdd:cd14891 239 AANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVITQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 406 PRVKVGNEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFD-FNSLEQLCINF 484
Cdd:cd14891 319 REIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLINY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 485 TNEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFGmDLAACIELI-EKPLGIFSILEEECMFPKASDTTFKNKLIDQHlGK 563
Cdd:cd14891 399 ANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH-KR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 564 NRAFEKPKPgKGKAEAhFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKsgnkllcflyaahasaeadtgskkggkk 643
Cdd:cd14891 477 HPCFPRPHP-KDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLAS---------------------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 644 kggsfqtvSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFK 723
Cdd:cd14891 527 --------SAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELV 598
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1316056572 724 QRYK-VLNASVIPegQFIDNKKA-SEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14891 599 DVYKpVLPPSVTR--LFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-770 |
2.15e-131 |
|
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: 427.40 E-value: 2.15e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 101 CVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFML----TDRENQSVL 176
Cdd:cd14889 2 VLLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 177 ITGESGAGKTVNTKRVIQYFATIAALGSKkdqaqqssgkiqgsLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHF 256
Cdd:cd14889 82 ISGESGAGKTESTKLLLRQIMELCRGNSQ--------------LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 257 gTSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQL---MTAHKPELIDALLITTNPYDFPMISQGEITVKSIDDVEEF 333
Cdd:cd14889 148 -RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 334 IatdTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREE-QAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGN 412
Cdd:cd14889 227 C---NAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 413 EMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQ---ARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 489
Cdd:cd14889 304 EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDdssVELREIGILDIFGFENFAVNRFEQACINLANEQL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 490 QQFFNHTMFVLEQEEYKKEGIDWEFIDFgMDLAACIEL-IEKPLGIFSILEEECMFPKASDTTFKNKLiDQHLGKNRAFE 568
Cdd:cd14889 384 QYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 569 KPKPGKGKaeahFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEADTGSKKGGKKK---- 644
Cdd:cd14889 462 KSRSKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAgsdn 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 645 --GGSFQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDF 722
Cdd:cd14889 538 fnSTRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEF 617
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1316056572 723 KQRYKVLnasvIPEGQFIDNKKASEKLLGSIDVdhTQYKFGHTKVFFK 770
Cdd:cd14889 618 AERYKIL----LCEPALPGTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
100-727 |
3.20e-130 |
|
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: 426.23 E-value: 3.20e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLP---------VYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFML-TD 169
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdlysesqlnAYKASMTSTSPVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 170 RENQSVLITGESGAGKTVNTKRVIQYFATIAALGSKKDQAQQSSGKIQgsleDQIVAANPLLEAYGNAKTVRNDNSSRFG 249
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVEIG----KRILQTNPILESFGNAQTIRNDNSSRFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 250 KFIRIHFGTSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFPMISQG----EITVK 325
Cdd:cd14902 157 KFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGpsfaRKRAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 326 SIDDVEEFIATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKqkqrEEQAEPDGTEVA-------DKIAYLLGLNSAD 398
Cdd:cd14902 237 ADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFT----AENGQEDATAVTaasrfhlAKCAELMGVDVDK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 399 MLKALCYPRVKVGNEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFF---------IGVLDIAGF 469
Cdd:cd14902 313 LETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 470 EIFDFNSLEQLCINFTNEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFGmDLAACIELIE-KPLGIFSILEEECMFPKAS 548
Cdd:cd14902 393 ESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 549 DTTFKNKLIDQHLGknrafekpkpgkgkaEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAA- 627
Cdd:cd14902 472 NQALSTKFYRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADe 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 628 -HASAEADTGSKKGGKKKGGSFQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGI 706
Cdd:cd14902 537 nRDSPGADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAV 616
|
650 660
....*....|....*....|.
gi 1316056572 707 RICRKGFPSRILYGDFKQRYK 727
Cdd:cd14902 617 RIARHGYSVRLAHASFIELFS 637
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
100-736 |
4.63e-128 |
|
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: 418.93 E-value: 4.63e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRG-----KKRIEAP----PHIFSISDNAYQFMLTD- 169
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQegllrSQGIESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 170 RENQSVLITGESGAGKTVNTKRVIQYFATIAALGSKKDQAQQSSGKiqGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFG 249
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGK--LSIMDRVLQSNPILEAFGNARTLRNDNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 250 KFIRIHFGTSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTA------HKPELIDALLITTN-PYDFPMISQGEI 322
Cdd:cd14908 159 KFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGgdeeehEKYEFHDGITGGLQlPNEFHYTGQGGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 323 -TVKSIDDVEEFIATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKIAY---LLGLNSAD 398
Cdd:cd14908 239 pDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVDK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 399 MLKALCYPRVKVGNEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEML---DTKQARAfFIGVLDIAGFEIFDFN 475
Cdd:cd14908 319 LLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInweNDKDIRS-SVGVLDIFGFECFAHN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 476 SLEQLCINFTNEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFGmDLAACIELIE-KPLGIFSILEEECMFP-KASDTTFK 553
Cdd:cd14908 398 SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 554 NKLIDQHL-------GKNRAFEKPKPGKGKaeAHFSLVHYAGTVDYNI-TGWLDKNKDPLNESVVQLYQKSGNkllcfly 625
Cdd:cd14908 477 SRLYETYLpeknqthSENTRFEATSIQKTK--LIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESGQQ------- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 626 aahasaeadtgskkggkkkggsfqtvsavFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEG 705
Cdd:cd14908 548 -----------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEA 598
|
650 660 670
....*....|....*....|....*....|.
gi 1316056572 706 IRICRKGFPSRILYGDFKQRYKVLnASVIPE 736
Cdd:cd14908 599 VRVARSGYPVRLPHKDFFKRYRML-LPLIPE 628
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
100-770 |
2.91e-120 |
|
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: 395.51 E-value: 2.91e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEA-PPHIFSISDNAYQFMLTDRENQSVLIT 178
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLTKlPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 179 GESGAGKTVNTKRVIQYFATiaalgskkdqaqQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGT 258
Cdd:cd14876 81 GESGAGKTEATKQIMRYFAS------------AKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVAS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 259 SGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDAL-LITTNPYDFpmISQGEITVKSIDDVEEFIATD 337
Cdd:cd14876 149 EGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYhLLGLKEYKF--LNPKCLDVPGIDDVADFEEVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 338 TAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQ-----AEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGN 412
Cdd:cd14876 227 ESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 413 EMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQF 492
Cdd:cd14876 307 QEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 493 FNHTMFVLEQEEYKKEGIDWEFIDFgMDLAACIE-LIEKPLGIFSILEEECMFPKASDTTFKNKLIDQhLGKNRafeKPK 571
Cdd:cd14876 387 FIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSNG---KFK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 572 PGKGKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAhasaeadtgsKKGGKKKGGSFQTV 651
Cdd:cd14876 462 PAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG----------VVVEKGKIAKGSLI 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 652 SAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNA 731
Cdd:cd14876 532 GSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDL 611
|
650 660 670
....*....|....*....|....*....|....*....
gi 1316056572 732 SvIPEGQFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14876 612 G-IANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-770 |
7.51e-120 |
|
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: 396.25 E-value: 7.51e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLP-VYDavvVAGYRGK--KRIEAPPHIFSISDNAYQFMLT-------D 169
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 170 RENQSVLITGESGAGKTVNTKRVIQYFATIaalgSKKDQAQQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFG 249
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAES----SKHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 250 KFIRIHFG-----TSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPE-LIDALLITTNPYDFPMISQGEIT 323
Cdd:cd14895 154 KFVRMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmKLELQLELLSAQEFQYISGGQCY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 324 VKS--IDDVEEFIATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVA---------------- 385
Cdd:cd14895 234 QRNdgVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqq 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 386 --DKIAYLLGLNSADMLKALCYPRVKVGNEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQAR------ 457
Cdd:cd14895 314 hlDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFAlnpnka 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 458 -----AFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFGmDLAACIELIE-KP 531
Cdd:cd14895 394 ankdtTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 532 LGIFSILEEECMFPKASDTTFKNKLIdQHLGKNRAFEKPKpgKGKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQ 611
Cdd:cd14895 473 SGIFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFS 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 612 LYQKSGN---KLLCFLYAAHASAEADTGSKKGGKKKGGSFQT-VSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGL 687
Cdd:cd14895 550 VLGKTSDahlRELFEFFKASESAELSLGQPKLRRRSSVLSSVgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQ 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 688 MENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASvipegQFIDNKKASEkLLGSIDVDHTQykFGHTKV 767
Cdd:cd14895 630 FDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAA-----KNASDATASA-LIETLKVDHAE--LGKTRV 701
|
...
gi 1316056572 768 FFK 770
Cdd:cd14895 702 FLR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
100-770 |
2.75e-117 |
|
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: 386.83 E-value: 2.75e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITG 179
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 180 ESGAGKTVNTKRVIQYfatIAALGSKKDQAQqssgkiqgslEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFgTS 259
Cdd:cd14896 81 HSGSGKTEAAKKIVQF---LSSLYQDQTEDR----------LRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 260 GKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLItTNPYDFPMISQGEI-TVKSIDDVEEFIATDT 338
Cdd:cd14896 147 GVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 339 AIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQ---AEPDGTEVadKIAYLLGLNSADMLKALCYPRVKVGN-EM 414
Cdd:cd14896 226 ALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevaAVSSWAEI--HTAARLLQVPPERLEGAVTHRVTETPyGR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 415 VTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFF--IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQF 492
Cdd:cd14896 304 VSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 493 FNHTMFVLEQEEYKKEGIDWEFIDfGMDLAACIELI-EKPLGIFSILEEECMFPKASDTTFKNKlIDQHLGKNRAFEKPK 571
Cdd:cd14896 384 SSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQK-CHYHHGDHPSYAKPQ 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 572 ---PgkgkaeaHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEADTGSKKggkkkggsf 648
Cdd:cd14896 462 lplP-------VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP--------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 649 qTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKV 728
Cdd:cd14896 526 -TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGA 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1316056572 729 LNAsvipEGQ--FIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14896 605 LGS----ERQeaLSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
106-770 |
5.27e-110 |
|
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: 366.13 E-value: 5.27e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 106 LKDRFASWMIYTYSGLFCVVVNPYKWLP-VYDAVVVAGYRGKKRI-----EAPPHIFSISDNAYQFMLTDRENQSVLITG 179
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 180 ESGAGKTVNTKRVIQYFATIAALGSKKDQaqqssgkiqgsleDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTS 259
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTDVQ-------------SLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 260 GKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDAL-LITTNPYDFpmISQGEI-TVKSIDDVEEFIATD 337
Cdd:cd14886 154 GGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLgFKSLESYNF--LNASKCyDAPGIDDQKEFAPVR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 338 TAIDILgFTADEKFNIYKLTGAVMHHGNMKFKQKQR---EEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEM 414
Cdd:cd14886 232 SQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNET 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 415 VTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 494
Cdd:cd14886 311 IISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 495 HTMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIEKP-LGIFSILEEECMFPKASDTTFKNKlIDQHLgKNRAFekpKPG 573
Cdd:cd14886 391 NQVFKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSS-CKSKI-KNNSF---IPG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 574 KGkAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCflyaahasaEADTGSKKGGKKKGGSFqtVSA 653
Cdd:cd14886 465 KG-SQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVN---------KAFSDIPNEDGNMKGKF--LGS 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 654 VFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL---N 730
Cdd:cd14886 533 TFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishN 612
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1316056572 731 ASVIPEGQfiDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14886 613 SSSQNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
102-729 |
2.13e-108 |
|
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: 361.86 E-value: 2.13e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLP-VYDAVVVAGYRGKKRIEA-PPHIFSISDNAYQFMLTDRE--NQSVLI 177
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 178 TGESGAGKTVNTKRVIQYFATIAAlgskkDQAQQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFG 257
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAA-----SPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 258 TSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMT-AHKPELIDALLitTNPYDFPMISQGEITVksidDVEEFIAT 336
Cdd:cd14880 158 RAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKgASADERLQWHL--PEGAAFSWLPNPERNL----EEDCFEVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 337 DTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEP--DGTEVADKI-AYLLGLNSADMLKALCYPRVKVGNE 413
Cdd:cd14880 232 REAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQpmDDTKESVRTsALLLKLPEDHLLETLQIRTIRAGKQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 414 MVTKGQTVPQV--NNAVSALCKSVYEKMFLWMVIRINEMLDTKQAR-AFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 490
Cdd:cd14880 312 QQVFKKPCSRAecDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 491 QFFNHTMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFEK 569
Cdd:cd14880 392 QHFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 570 PKPGKgkaEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAhasAEADTGSKKGGKKKGGSFQ 649
Cdd:cd14880 471 NKLSR---EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPA---NPEEKTQEEPSGQSRAPVL 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 650 TVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL 729
Cdd:cd14880 545 TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLL 624
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
102-732 |
1.13e-107 |
|
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: 361.60 E-value: 1.13e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLP-VYDAVVVAGYRGKKRI-EAPPHIFSISDNAYQFMLTDRENQSVLITG 179
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQNkSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 180 ESGAGKTVNTKRVIQYFatIAALGSKKDQAQQSSGKiQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHF-GT 258
Cdd:cd14906 83 ESGSGKTEASKTILQYL--INTSSSNQQQNNNNNNN-NNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 259 SGKLASADIETYLLEKSRVTFQLSAER-SYHIFYQLMTAHKPELIDALLITTNPYDFPMISQGEITVKSI---------- 327
Cdd:cd14906 160 DGKIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsn 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 328 -----DDVEEFIATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQ---REEQAEPDGTEVADKIAYLLGLNSADM 399
Cdd:cd14906 240 hnnktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 400 LKALCYPRVKVGNE--MVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRIN-EMLDTKQAR----------AFFIGVLDI 466
Cdd:cd14906 320 KQALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINrKFNQNTQSNdlaggsnkknNLFIGVLDI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 467 AGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIE-KPLGIFSILEEECMFP 545
Cdd:cd14906 400 FGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMP 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 546 KASDTTFKNKLIDQHLGKNRAFEKpKPGKGKaeahFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLY 625
Cdd:cd14906 479 KGSEQSLLEKYNKQYHNTNQYYQR-TLAKGT----LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 626 AAHASAEADTGSKKGGKKkggsfqTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEG 705
Cdd:cd14906 554 QQQITSTTNTTKKQTQSN------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNT 627
|
650 660
....*....|....*....|....*..
gi 1316056572 706 IRICRKGFPSRILYGDFKQRYKVLNAS 732
Cdd:cd14906 628 IKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
102-727 |
1.98e-107 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 360.95 E-value: 1.98e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLP-VYDAVVVAGYR-------GKKRIEA---PPHIFSISDNAYQFMLTDR 170
Cdd:cd14899 3 ILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQNG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 171 ENQSVLITGESGAGKTVNTKRVIQYFATIAALGSKKDQAQQSSGKIQG----SLEDQIVAANPLLEAYGNAKTVRNDNSS 246
Cdd:cd14899 83 RSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPPASpsrtTIEEQVLQSNPILEAFGNARTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 247 RFGKFIRIHF-GTSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAH----KPELIDALLITTNPYDFPMISQGE 321
Cdd:cd14899 163 RFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 322 ITVK--SIDDVEEFIATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQ--KQREEQAEPDGTEVA----------DK 387
Cdd:cd14899 243 CSKRrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfTK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 388 IAYLLGLNSADMLKALCYPRVKVGNEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEML---------------D 452
Cdd:cd14899 323 AAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesdvD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 453 TKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFGMDlAACIELIE-KP 531
Cdd:cd14899 403 DEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhRP 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 532 LGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFEKPKPGKGKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQ 611
Cdd:cd14899 482 IGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAAQ 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 612 LYQKSGNKLLCFLYAAHASAEADTGSKKGGKKKGGSFQTVSAV--------FRENLGKLMTNLRSTHPHFVRCLIPNESK 683
Cdd:cd14899 562 LLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIaavsvgtqFKIQLNELLSTVRATTPRYVRCIKPNDSH 641
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1316056572 684 TPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 727
Cdd:cd14899 642 VGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
102-770 |
6.96e-105 |
|
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: 351.80 E-value: 6.96e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMI-YTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEA-PPHIFSISDNAY-QFMLTDRENQSVLIT 178
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVVIS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 179 GESGAGKTVNTKRVIQYFATIAALGSKKDQAQQSSGKIQGSLEdqivAANPLLEAYGNAKTVRNDNSSRFGKFIRIHF-G 257
Cdd:cd14875 83 GESGSGKTENAKMLIAYLGQLSYMHSSNTSQRSIADKIDENLK----WSNPVMESFGNARTVRNDNSSRFGKYIKLYFdP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 258 TSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFPMISQGEITV------KSIDDVE 331
Cdd:cd14875 159 TSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKTLDDAH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 332 EFIATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKiAYLLGLNSADMLKalCYpRVKVG 411
Cdd:cd14875 239 EFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFLTA-CRLLQLDPAKLRE--CF-LVKSK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 412 NEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQ--ARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 489
Cdd:cd14875 315 TSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQLCINYANESL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 490 QQFFNHTMFVLEQEEYKKEGIDWEFIDFGmDLAACIELIE-KPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNRAFE 568
Cdd:cd14875 395 QNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 569 KPkpgKGKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASaEADTGskkggkkkggsf 648
Cdd:cd14875 474 LP---KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKG-LARRK------------ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 649 QTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDF-KQRYK 727
Cdd:cd14875 538 QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFcRYFYL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1316056572 728 VLNASVIPEGQFIDNKKASEKLLGS----IDVDHTQYKFGHTKVFFK 770
Cdd:cd14875 618 IMPRSTASLFKQEKYSEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
102-770 |
5.55e-100 |
|
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: 338.52 E-value: 5.55e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGES 181
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 182 GAGKTVNTKRVIQYFATIAALGSKKdqaqQSSGKIQgsledqivAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAAGSVGGV----LSVEKLN--------AALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 262 LASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALL---ITTNPYDF--PMISQGEITvksiDDVEEFIAT 336
Cdd:cd01386 151 LASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHlnqLAESNSFGivPLQKPEDKQ----KAAAAFSKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 337 DTAIDILGFTADEKFNIYKLTGAVMHHGN---MKFKQKQREEQAEPdgtEVADKIAYLLGLNSADMLKALCYPRVKVGNE 413
Cdd:cd01386 227 QAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 414 MVTKGQTVPQVNN------------AVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFN------ 475
Cdd:cd01386 304 QSTTSSGQESPARsssggpkltgveALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrga 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 476 SLEQLCINFTNEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPL---------------GIFSILEE 540
Cdd:cd01386 384 TFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPqqalvrsdlrdedrrGLLWLLDE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 541 ECMFPKASDTTFKNKLIdQHLGKNRAFEKPKP-GKGKAEAHFSLVHYAGT--VDYNITGWLDKNK-DPLNESVVQLYQKS 616
Cdd:cd01386 464 EALYPGSSDDTFLERLF-SHYGDKEGGKGHSLlRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQES 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 617 GNKLlcflyAAHASaeadtgskkggkkkggsfQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPN-----------ESKTP 685
Cdd:cd01386 543 QKET-----AAVKR------------------KSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagkderstsSPAAG 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 686 GLMENF-LVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL----NASVIPEGQFIDNKKASEKLLGSIDVDHTQY 760
Cdd:cd01386 600 DELLDVpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLapplTKKLGLNSEVADERKAVEELLEELDLEKSSY 679
|
730
....*....|
gi 1316056572 761 KFGHTKVFFK 770
Cdd:cd01386 680 RIGLSQVFFR 689
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
102-770 |
1.50e-93 |
|
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: 318.68 E-value: 1.50e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYR---GKKRIEAPPHIFSISDNAYQFMLTDRENQSVLIT 178
Cdd:cd14878 3 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFILS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 179 GESGAGKTVNTKRVIQYFATiaalgskkdqaqqSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGT 258
Cdd:cd14878 83 GERGSGKTEASKQIMKHLTC-------------RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 259 SGK-LASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITtNPYDFPMISQGE----ITVKSIDDVEEF 333
Cdd:cd14878 150 RKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQTMredvSTAERSLNREKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 334 IATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNE 413
Cdd:cd14878 229 AVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 414 MVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEML----DTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 489
Cdd:cd14878 309 MIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 490 QQFFNHTMFVLEQEEYKKEGIDWEFI-DFGMDLAACIELIEKPLGIFSILEEECMFPKASDTTFKNKLidQHL----GKN 564
Cdd:cd14878 389 HHYINEVLFLQEQTECVQEGVTMETAySPGNQTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKL--QSLlessNTN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 565 RAFEKPKPGKGKAE-----AHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAhasaeadtgskk 639
Cdd:cd14878 467 AVYSPMKDGNGNVAlkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQS------------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 640 ggkkkggSFQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILY 719
Cdd:cd14878 535 -------KLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSF 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1316056572 720 GDFKQRYKVLnASVIPEGQfidnKKASEKLLGSIDVDHTQ---YKFGHTKVFFK 770
Cdd:cd14878 608 SDFLSRYKPL-ADTLLGEK----KKQSAEERCRLVLQQCKlqgWQMGVRKVFLK 656
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
100-770 |
2.03e-87 |
|
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: 302.72 E-value: 2.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFAS--------WMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRE 171
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 172 NQSVLITGESGAGKTVNTKRVIQYFATIaalgSKKDQAQQSSGkiqgsLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKF 251
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAV----SDRRHGADSQG-----LEARLLQSGPVLEAFGNAHTVLNANSSRFGKM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 252 IRIHFGTSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAhkpELIDALLITTNPYDFPMISqgeitvksidDVE 331
Cdd:cd14887 152 LLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNA---AVAAATQKSSAGEGDPEST----------DLR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 332 EFIATDTAIDILGftaDEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGT--------EVADKIAYLLGLNS------- 396
Cdd:cd14887 219 RITAAMKTVGIGG---GEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvgceETAADRSHSSEVKClssglkv 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 397 --------ADMLKALCYPRVKVGNEMVTKGQTVPQVNNAVS------------ALCKSVYEKMFLWMVIRINEML----- 451
Cdd:cd14887 296 teasrkhlKTVARLLGLPPGVEGEEMLRLALVSRSVRETRSffdldgaaaardAACKNLYSRAFDAVVARINAGLqrsak 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 452 --------DTKQARAF-FIGVLDIAGFEIF---DFNSLEQLCINFTNEKLQQFFNHTMFVLEQEEYKKEGIDWEFI---- 515
Cdd:cd14887 376 psesdsdeDTPSTTGTqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsaf 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 516 DFGMDLAAC--------IELIEKP--------------LGIFSILEEE-CMFPKASDTTFKNKLIDQHLGKNRA----FE 568
Cdd:cd14887 456 PFSFPLASTltsspsstSPFSPTPsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKNIInsakYK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 569 KPKPGKGKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLyqksgnkllcFLYAAHASAEADTGSKKGGKKKGGSF 648
Cdd:cd14887 536 NITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERL----------FLACSTYTRLVGSKKNSGVRAISSRR 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 649 QTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKv 728
Cdd:cd14887 606 STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYE- 684
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1316056572 729 lnaSVIPEG--QFIDNKKASEKLLGSIDVDHTQYKFGHTKVFFK 770
Cdd:cd14887 685 ---TKLPMAlrEALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
102-770 |
1.51e-86 |
|
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: 297.70 E-value: 1.51e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKwlpVYDaVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGES 181
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQ---VID-VDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 182 GAGKTVNTKRVIQYFATiaalGSKKDQaqqssgKIQGSLEDqivaANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd14937 79 GSGKTEASKLVIKYYLS----GVKEDN------EISNTLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 262 LASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPyDFPMISQGEITVKSIDDVEEFIATDTAID 341
Cdd:cd14937 145 IVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 342 ILGFTaDEKFNIYKLTGAVMHHGNMKFKQ-----KQREEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGNEMVT 416
Cdd:cd14937 224 KMNMH-DMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 417 KGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHT 496
Cdd:cd14937 303 IPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 497 MFVLEQEEYKKEGIDWEFIDFGMDlAACIELIEKPLGIFSILEEECMFPKASDTTfknkLIDQHLGKNRAFEKPKPGKGK 576
Cdd:cd14937 383 VYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKYASTKKD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 577 AEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEADTGSkkggkkkggsfQTVSAVFR 656
Cdd:cd14937 458 INKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRK-----------NLITFKYL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 657 ENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRIcRKGFPSRILYGDFKQRYKVLNASVIPE 736
Cdd:cd14937 527 KNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKD 605
|
650 660 670
....*....|....*....|....*....|....
gi 1316056572 737 GQFIDNKKASEKLLGSIDVDhtQYKFGHTKVFFK 770
Cdd:cd14937 606 SSLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
102-733 |
3.35e-80 |
|
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: 277.16 E-value: 3.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKwlpvydavVVAGYRGKKRIE-----APPHIFSISDNAYQFMLTdRENQSVL 176
Cdd:cd14898 3 TLEILEKRYASGKIYTKSGLVFLALNPYE--------TIYGAGAMKAYLknyshVEPHVYDVAEASVQDLLV-HGNQTIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 177 ITGESGAGKTVNTKRVIQYFAtiaalgskkdqaqqSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHF 256
Cdd:cd14898 74 ISGESGSGKTENAKLVIKYLV--------------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 257 gtSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAH----KPELIDALLITTNPYDFPMISqgeitvksiddvEE 332
Cdd:cd14898 140 --DGKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKrlniKNDFIDTSSTAGNKESIVQLS------------EK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 333 FIATDTAIDILGFTADEKfnIYKLTGAVMHHGNMKFKQkqrEEQAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGN 412
Cdd:cd14898 206 YKMTCSAMKSLGIANFKS--IEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 413 EMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAffIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQF 492
Cdd:cd14898 281 ETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQND 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 493 FNHTMFVLEQEEYKKEGIDWEFIDFgMDLAACIELIEKPLGIFSILEEECMFPKAsdtTFKNKLIDQHlGKNRAFEKPkp 572
Cdd:cd14898 359 FIKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWG---NVKNLLVKIK-KYLNGFINT-- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 573 gkgKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVqlyqksGNKLLcflyaahasaeadtgskkggkKKGGSFQTVS 652
Cdd:cd14898 432 ---KARDKIKVSHYAGDVEYDLRDFLDKNREKGQLLIF------KNLLI---------------------NDEGSKEDLV 481
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 653 AVFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 732
Cdd:cd14898 482 KYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGIT 561
|
.
gi 1316056572 733 V 733
Cdd:cd14898 562 L 562
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
106-769 |
3.74e-80 |
|
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: 279.05 E-value: 3.74e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 106 LKDRFASWMIYTY---SGLfcVVVNPYKWLPVYDAVVVAGYR-------GKKRIEAPPHIFSISDNAYQFMLTDRENQSV 175
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 176 LITGESGAGKTVNTKRVIQYFATIAALGSKkdqaqqsSGKIQGsledQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIH 255
Cdd:cd14879 88 VFLGETGSGKSESRRLLLRQLLRLSSHSKK-------GTKLSS----QISAAEFVLDSFGNAKTLTNPNASRFGRYTELQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 256 FGTSGKLASADIETYLLEKSRVTfQLSA-ERSYHIFYQLMTAHKPELID----------ALLITTNPYDFPMISQgeitv 324
Cdd:cd14879 157 FNERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQhlglddpsdyALLASYGCHPLPLGPG----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 325 ksIDDVEEFIATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQ--REEQAEPDGTEVADKIAYLLGLNSADMLKA 402
Cdd:cd14879 231 --SDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVSPEDLETS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 403 LCYPRVKVGNEMVT-----KGQTvpqvNNAVSaLCKSVYEKMFLWMVIRINEML-DTKQARAFFIGVLDIAGFEIFD--- 473
Cdd:cd14879 309 LTYKTKLVRKELCTvfldpEGAA----AQRDE-LARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSstg 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 474 FNSLEQLCINFTNEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFgMDLAACIELI-EKPLGIFSILEEEC-MFPKASDTT 551
Cdd:cd14879 384 GNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTDEQ 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 552 FKNKLIDQHLGKNRAFEKPKPGKGKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNkllcflyaahasa 631
Cdd:cd14879 463 MLEALRKRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRGATQ------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 632 eadtgskkggkkkggsfqtvsavFRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRK 711
Cdd:cd14879 530 -----------------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRV 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1316056572 712 GFPSRILYGDFKQRYKvlnasviPEGQFIDNKKASEKLLGSIDVDHTQYKFGHTKVFF 769
Cdd:cd14879 587 EYVVSLEHAEFCERYK-------STLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
100-718 |
2.14e-71 |
|
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: 254.45 E-value: 2.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLP-VYDAVVVAGYRGKKRIEA-------PPHIFSISDNAYQFMLTDRE 171
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 172 NQSVLITGESGAGKTVNTKRVIQYFATIaalgskKDQAQQSSgkiqgsLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKF 251
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI------QTDSQMTE------RIDKLIYINNILESMSNATTIKNNNSSRCGRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 252 IRIHFGT---------SGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITTNPYDFPMISQGE- 321
Cdd:cd14884 149 NLLIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEs 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 322 -----------ITVKSIDDVEEFIATDTA-----IDILGFTADEKFNI---YKLTGAVMHHGNMKFKQKqreeqaepdgt 382
Cdd:cd14884 229 hqkrsvkgtlrLGSDSLDPSEEEKAKDEKnfvalLHGLHYIKYDERQInefFDIIAGILHLGNRAYKAA----------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 383 evadkiAYLLGLNSADMLKALCYPRVKVGNEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRIN---------EMLDT 453
Cdd:cd14884 298 ------AECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekDESDN 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 454 KQARAF---FIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFVLEQEEYKKEGIDW--EFIDFGMDLAACIELI 528
Cdd:cd14884 372 EDIYSIneaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICcsDVAPSYSDTLIFIAKI 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 529 EKPLGIFSILEEECMfpKASDTTFKNKLID-----QHLGKNRA-FEKPKPGKGKAEAH------FSLVHYAGTVDYNITG 596
Cdd:cd14884 452 FRRLDDITKLKNQGQ--KKTDDHFFRYLLNnerqqQLEGKVSYgFVLNHDADGTAKKQnikkniFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 597 WLDKNKDPLNESVVQLYQKSGNKLLcflyaahasaeadtgSKKGGKKKGGSFQTVSAVFRENLGKLMTNLRSTHPHFVRC 676
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFL---------------REANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRC 594
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1316056572 677 LIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRIL 718
Cdd:cd14884 595 FLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
102-750 |
2.35e-68 |
|
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: 244.25 E-value: 2.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPvyDAVVVAGYRGKKRieAPPHIFSISDNAYQFMLTDREnQSVLITGES 181
Cdd:cd14881 3 VMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPL--APQLLKVVQEAVRQQSETGYP-QAIILSGTS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 182 GAGKTVNTKRVIQYFATIAALGSKKDQAQQssgkiqgsledqIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFgTSGK 261
Cdd:cd14881 78 GSGKTYASMLLLRQLFDVAGGGPETDAFKH------------LAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDGA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 262 LASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDAL-LITTNPYDFPMISQGEITVKSIDDVEEFIATDTAI 340
Cdd:cd14881 145 LYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLhLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKACL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 341 DILGFtadeKF-NIYKLTGAVMHHGNMKFKQKQREEQAEPDGTEVaDKIAYLLGLNSADMLKALcYPRVKVgnemvTKGQ 419
Cdd:cd14881 225 GILGI----PFlDVVRVLAAVLLLGNVQFIDGGGLEVDVKGETEL-KSVAALLGVSGAALFRGL-TTRTHN-----ARGQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 420 TVPQVNNAVS------ALCKSVYEKMFLWMVIRINEMLD-----TKQARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEK 488
Cdd:cd14881 294 LVKSVCDANMsnmtrdALAKALYCRTVATIVRRANSLKRlgstlGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAET 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 489 LQQFFNHTMFVLEQEEYKKEGIDWEF-IDFgMDLAACIELIEK-PLGIFSILEEECMfPKASDTTFKNKLIDQHLGKNRA 566
Cdd:cd14881 374 MQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 567 FEkPKPgkgKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGnkllC-FLYAAHASaeadtgskkggkkkg 645
Cdd:cd14881 452 FE-AKP---QDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN----CnFGFATHTQ--------------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 646 gSFQTvsavfreNLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQR 725
Cdd:cd14881 509 -DFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNAR 580
|
650 660
....*....|....*....|....*
gi 1316056572 726 YKVLnASVIPEGQFIDNKKASEKLL 750
Cdd:cd14881 581 YRLL-APFRLLRRVEEKALEDCALI 604
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
103-727 |
4.07e-65 |
|
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: 237.18 E-value: 4.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 103 LYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRI----------EAPPHIFSISDNAYQFMLTDREN 172
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 173 QSVLITGESGAGKTVNTKRVIQYFATIAALGSKKDQAQQSSGKIQgSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFI 252
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLH-PIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 253 RIHFGTSGKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTA--HKPELIDALLITTNPYDFPMISQG--EITVKSID 328
Cdd:cd14893 163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGvqHDPTLRDSLEMNKCVNEFVMLKQAdpLATNFALD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 329 --DVEEFIATDTAIDIlgfTADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDG--TEVADKIAYLLGLNSADMLKALC 404
Cdd:cd14893 243 arDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGAnsTTVSDAQSCALKDPAQILLAAKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 405 ----------YPRV-----KVGNEMVT--KGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEML----DTKQARAFFIG- 462
Cdd:cd14893 320 levepvvldnYFRTrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVINs 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 463 ----VLDIAGFEIFD--FNSLEQLCINFTNEKLQQFF-------NHTMFVLEQEEYKKEGIDWEFIDFGMDLAACIELIE 529
Cdd:cd14893 400 qgvhVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvqntlaiNFSFLEDESQQVENRLTVNSNVDITSEQEKCLQLFE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 530 -KPLGIFSILEEECMFPKASDTTFKNKLIDQHlGKNRAFEKPKPGKGKAEAH----------FSLVHYAGTVDYNITGWL 598
Cdd:cd14893 480 dKPFGIFDLLTENCKVRLPNDEDFVNKLFSGN-EAVGGLSRPNMGADTTNEYlapskdwrllFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 599 DKNKDPLNESVVQLYQKSGNKLLCFLYAAH---ASAEADTGSKKGGKKKGGSFQTVSAVFRE--NLGK------------ 661
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVLHAVGAAQmaaASSEKAAKQTEERGSTSSKFRKSASSAREskNITDsaatdvynqada 638
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316056572 662 LMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 727
Cdd:cd14893 639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
102-729 |
1.95e-63 |
|
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: 229.37 E-value: 1.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYrgkkrieappHIFSISDNAYQFMLTDREN-QSVLITGE 180
Cdd:cd14874 3 IAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGGE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 181 SGAGKTVNTKRVIQYfatIAALGSKKDQAQQSSgkiqgsledqivAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSG 260
Cdd:cd14874 73 SGSGKSYNAFQVFKY---LTSQPKSKVTTKHSS------------AIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 261 KLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDALLITtNPYDFPMISQGEITVKSIDDVEEFIATDTAI 340
Cdd:cd14874 138 LTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GLQKFFYINQGNSTENIQSDVNHFKHLEDAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 341 DILGFTADEKFNIYKLTGAVMHHGNMKFKQKqREEQAEPDGTEVADK-----IAYLLGLNsADMLKALCYPRVKVGNEMv 415
Cdd:cd14874 217 HVLGFSDDHCISIYKIISTILHIGNIYFRTK-RNPNVEQDVVEIGNMsevkwVAFLLEVD-FDQLVNFLLPKSEDGTTI- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 416 tkgqTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQARAFfIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 495
Cdd:cd14874 294 ----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV-ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 496 TMFVLEQEEYKKEGIDwefIDFGM----DLAACIELI-EKPLGIFSILEEECMFPKASDTTFKNKLIDQHLGKNrAFEKp 570
Cdd:cd14874 369 HSFHDQLVDYAKDGIS---VDYKVpnsiENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRS-SYGK- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 571 kpGKGKAEAHFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLYAAHASAEADtgskkggkkkggsfQT 650
Cdd:cd14874 444 --ARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSD--------------MI 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 651 VSAVFRENLG--KLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKV 728
Cdd:cd14874 508 VSQAQFILRGaqEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRC 587
|
.
gi 1316056572 729 L 729
Cdd:cd14874 588 L 588
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
102-729 |
1.89e-60 |
|
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: 220.77 E-value: 1.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 102 VLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGES 181
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 182 GAGKTVNTKRVIQYfatIAALGSKKDQAQQssgkiqgsledQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGK 261
Cdd:cd14882 83 YSGKTTNARLLIKH---LCYLGDGNRGATG-----------RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 262 LASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPE--LIDALLITTNPYDFPMISQGEITVKSI---DD----VEE 332
Cdd:cd14882 149 MSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQnrLKEYNLKAGRNYRYLRIPPEVPPSKLKyrrDDpegnVER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 333 FIATDTAIDILGFTADEKFNIYKLTGAVMHHGNMKFKQKQREeqAEPDGTEVADKIAYLLGLNSADMLKALCYPRVKVGN 412
Cdd:cd14882 229 YKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLIKGG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 413 EMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTkqARAFF-----IGVLDIAGFEIFDFNSLEQLCINFTNE 487
Cdd:cd14882 307 SAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRAVFgdkysISIHDMFGFECFHRNRLEQLMVNTLNE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 488 KLQQFFNHTMFVLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPLGIFSILEEecmfpkASDTtfknkLIDQHLGKNRAF 567
Cdd:cd14882 385 QMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD------ASRS-----CQDQNYIMDRIK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 568 EKPKPGKGKAEAH-FSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNkllcflyaahasaeaDTGSKKGGKKKGG 646
Cdd:cd14882 454 EKHSQFVKKHSAHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLD---------------ESVKLMFTNSQVR 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 647 SFQTVSAVFR----ENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVLEGIRICRKGFPSRILYGDF 722
Cdd:cd14882 519 NMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEF 598
|
....*..
gi 1316056572 723 KQRYKVL 729
Cdd:cd14882 599 LRRYQFL 605
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
106-621 |
1.93e-59 |
|
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: 218.81 E-value: 1.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 106 LKDRFASWMIYTYSGLFCVVVNPYKWLP-VYDAVVVAGYRGKKRIeaPPHIFSISDNAYQFMLTDRENQSVLITGESGAG 184
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRRGL--PPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 185 KTVNTKRVIQYFATIAALGSKkdqaqqssgkiqgSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRIHFGTSGKLAS 264
Cdd:cd14905 85 KSENTKIIIQYLLTTDLSRSK-------------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 265 ADIETYLLEKSRVTFQLSAERSYHIFYQLMTAHKPELIDAL-LITTNPYDFpMISQGEITVKSIDDVEEFIATDTAIDIL 343
Cdd:cd14905 152 AKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYqLGDINSYHY-LNQGGSISVESIDDNRVFDRLKMSFVFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 344 GFTADEKFNIYKLTGAVMHHGNMKFKQKQREeqaepdgTEVADKIAYllglnsADMLKALCYPRVKVGNEMVTKgQTVPq 423
Cdd:cd14905 231 DFPSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDRTLI------ESLSHNITFDSTKLENILISD-RSMP- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 424 VNNAVS---ALCKSVYEKMFLWMVIRINEMLDTKQaRAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFVL 500
Cdd:cd14905 296 VNEAVEnrdSLARSLYSALFHWIIDFLNSKLKPTQ-YSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 501 EQEEYKKEGIDWEFIDFGMDLAACIELIEKplgIFSILEEECMFPKASDTTFKNKLiDQHLGKNRAFEKpKPGKgkaeah 580
Cdd:cd14905 375 EQREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL-QNFLSRHHLFGK-KPNK------ 443
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1316056572 581 FSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLL 621
Cdd:cd14905 444 FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYL 484
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
122-254 |
1.57e-57 |
|
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: 196.80 E-value: 1.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 122 FCVVVNPYKWLPVY-DAVVVAGYRGKKRIEAPPHIFSISDNAYQFMLTDRENQSVLITGESGAGKTVNTKRVIQYFATIA 200
Cdd:cd01363 1 VLVRVNPFKELPIYrDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1316056572 201 ALGSKKDQAQQSSG--KIQGSLEDQIVAANPLLEAYGNAKTVRNDNSSRFGKFIRI 254
Cdd:cd01363 81 FNGINKGETEGWVYltEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-768 |
8.47e-46 |
|
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: 178.11 E-value: 8.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 100 PCVLYNLKDRFASWMIYTYSGLFCVVVNPYKWLPVYDAVVVAGYrgkKRIEAPPHI----FSISDNAYQFMLTDRENQSV 175
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKY---KCIDCIEDLslneYHVVHNALKNLNELKRNQSI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 176 LITGESGAGKTVNTKRVIQYFA----------TIAALGSKKDQAQQSSGKIQGSLEDQIVAANPLLEAYGNAKTVRNDNS 245
Cdd:cd14938 78 IISGESGSGKSEIAKNIINFIAyqvkgsrrlpTNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 246 SRFGKFIRIHFGTSgKLASADIETYLLEKSRVTFQLSAERSYHIFYQLMTAhKPELIDALLITTNPYDFPMISQGEITVK 325
Cdd:cd14938 158 SRFSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIING-SSDKFKKMYFLKNIENYSMLNNEKGFEK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 326 SIDDVEEFIATDTAIDILGFTADEKFNIYKLTGAVMHHGN-------------MKFKQKQRE----------EQAEPDGT 382
Cdd:cd14938 236 FSDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 383 EVADKIAYL----LGLNSADMLKALCYPRVkVGNEMVTKGQTVPQVNNAVSALCKSVYEKMFLWMVIRINEMLDTKQ--- 455
Cdd:cd14938 316 DENVKNLLLacklLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQnin 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 456 ARAFFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHTMFVLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPL--G 533
Cdd:cd14938 395 INTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 534 IFSILEEECMfPKASDTTFKNKLIDQHLGKNRAFEKPKPGKGKAEAhFSLVHYAGTVDYNITGWLDKNKDPLNESVVQLY 613
Cdd:cd14938 475 LFSLLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 614 QKSGNKLL---CFLYAAHASAE---------ADTGSKKGGKKKGGSFQTVSAVFRENLGKLMTNLRSTHPHFVRCLIPNE 681
Cdd:cd14938 553 KQSENEYMrqfCMFYNYDNSGNiveekrrysIQSALKLFKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNE 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 682 SK--TPGLMENfLVIHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAsvipegqfiDNKKASEKLLGSIDVDHTQ 759
Cdd:cd14938 633 SKreLCSFDAN-IVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYE 702
|
....*....
gi 1316056572 760 YKFGHTKVF 768
Cdd:cd14938 703 WMIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1148-1930 |
1.53e-32 |
|
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: 138.65 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1148 EEISERLEEAGGATaaqiemnkkreaefqKLRRDLEESTLQHEATAAALrKKQADSVAELGEQIDNLQRVKQKLEK---- 1223
Cdd:TIGR02168 155 EERRAIFEEAAGIS---------------KYKERRKETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERykel 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1224 -------EKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLE 1296
Cdd:TIGR02168 219 kaelrelELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1297 EKEALV-------SQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKAN 1369
Cdd:TIGR02168 299 RLEQQKqilrerlANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1370 SEVAQWRSKYEtdaiqrteELEEAKKKLAQRLQEAEESIEavnskcaSLEKTKQRLQGEVEDLMTDVERAN--SLAANLD 1447
Cdd:TIGR02168 379 EQLETLRSKVA--------QLELQIASLNNEIERLEARLE-------RLEDRRERLQQEIEELLKKLEEAElkELQAELE 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1448 KKqrnfDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEA---LDQLETMKRENKNLQQEI-------SDLT 1517
Cdd:TIGR02168 444 EL----EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVkallknqSGLS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1518 EQIGETGKSIHELEKAKKTVETEKSE-IQAAL----EEAEGTLEH-EESKILRVQ-LELNQVKseiDRKLAEKDEEMEQI 1590
Cdd:TIGR02168 520 GILGVLSELISVDEGYEAAIEAALGGrLQAVVvenlNAAKKAIAFlKQNELGRVTfLPLDSIK---GTEIQGNDREILKN 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1591 KRNSQRVIDSMQSTldaevrsrndALRVKKKMEGDLNEMEI--QLSHANRQAAEAQKQLRNVQgqlKDAQLHLDDAVRGQ 1668
Cdd:TIGR02168 597 IEGFLGVAKDLVKF----------DPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGYRIVT---LDGDLVRPGGVITG 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1669 EDMKEQVAMVERRNglmvaEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDA 1748
Cdd:TIGR02168 664 GSAKTNSSILERRR-----EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1749 VQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENlamkggkkQLQKLEQRVRELET 1828
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE--------ELKALREALDELRA 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1829 EVEGEQKRGADAVKGVRKYERRVKELTYQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEME 1908
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
810 820
....*....|....*....|..
gi 1316056572 1909 EAQERADIAESQVNKLRAKSRD 1930
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSE 912
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
839-1735 |
2.43e-31 |
|
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: 134.80 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 839 KIKPLLKSAETEKELQNMKENYEKMQSDLttALAKKKELEEKMVSLLQEKNDLQLQVASevenlsdaeerceglikskiq 918
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEE--------------------- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 919 LEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTK 998
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 999 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLaqesimdLENDKQ 1078
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER-------LEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1079 QSDEKIKKKDFEISQLLSKIE--DEQSLGAQLQKKIKELqarieeleeeieaeraarAKVEKQRADLSRELEEISERLEE 1156
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEeaELKELQAELEELEEEL------------------EELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1157 AggataaqiemnkkrEAEFQKLRRDLEEStlqheataaalrKKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDLS 1236
Cdd:TIGR02168 473 A--------------EQALDAAERELAQL------------QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLS 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1237 SNMEAVAKAKGNLEKmcrTLEDQLSEIKSKNDENVRQlnDINAQKarlQTENGeFARQLEEKEALVSQLTRGKQAFTQQI 1316
Cdd:TIGR02168 527 ELISVDEGYEAAIEA---ALGGRLQAVVVENLNAAKK--AIAFLK---QNELG-RVTFLPLDSIKGTEIQGNDREILKNI 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1317 EELKRHIEEEVKAKNALAHAVQSARHDCdLLREQFEEEQEAKAELQRGMS---------KANSEVAQWRSKYETDAIQRT 1387
Cdd:TIGR02168 598 EGFLGVAKDLVKFDPKLRKALSYLLGGV-LVVDDLDNALELAKKLRPGYRivtldgdlvRPGGVITGGSAKTNSSILERR 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1388 EELEEAKKKLAqrlqEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEES 1467
Cdd:TIGR02168 677 REIEELEEKIE----ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1468 QAELEGAQKEARSLSTELFKMKNSYEEALD-------QLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETE 1540
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAeieeleaQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1541 KSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEIDrKLAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALRVKK 1620
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1621 KMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQL-KDAQLHLDDAVRGQEDMKEQVAMVERRnglmvaeIEELRAALEQT 1699
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRR-------LKRLENKIKEL 984
|
890 900 910
....*....|....*....|....*....|....*.
gi 1316056572 1700 ERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLE 1735
Cdd:TIGR02168 985 GPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
916-1798 |
1.54e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 132.10 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 916 KIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECS------ELKKDIDDLELTLAKVEKEKHAtenkvknltEEMATQ 989
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEkaerykELKAELRELELALLVLRLEELR---------EELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 990 DEAIAKLTKEKKALQEAhqqtlddLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEqekklrmDLERAKRKLEGDLKLAQES 1069
Cdd:TIGR02168 245 QEELKEAEEELEELTAE-------LQELEEKLEELRLEVSELEEEIEELQKELY-------ALANEISRLEQQKQILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1070 IMDLENDKQQSDEkikkkdfEISQLLSKIEDEQSLGAQLQKKIKELQArieeleeeieaeraarakvekqradlsrELEE 1149
Cdd:TIGR02168 311 LANLERQLEELEA-------QLEELESKLDELAEELAELEEKLEELKE----------------------------ELES 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1150 ISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAalrkkqadsvaelgeQIDNLQRVKQKLEKEKSEFK 1229
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN---------------EIERLEARLERLEDRRERLQ 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1230 MEIDDLSSNMEAVAKAKgnLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGK 1309
Cdd:TIGR02168 421 QEIEELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1310 QAFtqqiEELKRHIEEEVKAKNALAHAVQSARhdcDLLReqFEEEQEAKAELQRG-------MSKANSEVAQWRSKYETD 1382
Cdd:TIGR02168 499 ENL----EGFSEGVKALLKNQSGLSGILGVLS---ELIS--VDEGYEAAIEAALGgrlqavvVENLNAAKKAIAFLKQNE 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1383 AIQRT--EELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLM------TDVERANSLAANLDKKQRNF- 1453
Cdd:TIGR02168 570 LGRVTflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLggvlvvDDLDNALELAKKLRPGYRIVt 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1454 ---------------------------------DKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLE 1500
Cdd:TIGR02168 650 ldgdlvrpggvitggsaktnssilerrreieelEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS 729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1501 TMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEIDRKL 1580
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1581 AEKDEEMEQIKRNSQRViDSMQSTLDAEVRSRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLH 1660
Cdd:TIGR02168 810 AELTLLNEEAANLRERL-ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1661 LDDAVRGQEDMKEQVAMVERRNGLMVAEIEELRAALEQTERSRKVAEQELvdaservgllhSQNSSLLNTKKKLETDLV- 1739
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI-----------DNLQERLSEEYSLTLEEAe 957
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316056572 1740 QVQGEVDDAVQEARNAEDKAKKAITD------AAMmaEELKKEQDTSAHLERMKKNLEVTVKDLQ 1798
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENKIKElgpvnlAAI--EEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1138-1875 |
2.51e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 128.25 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1138 KQRADLSRELEEISERLEEA-GGATAAQIEmnkKREAEFQKLRRDLEESTLQHEATAAALRKKQADsVAELGEQIDNLQR 1216
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELeLALLVLRLE---ELREELEELQEELKEAEEELEELTAELQELEEK-LEELRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1217 VKQKLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLE 1296
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1297 EKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSAR---HDCDLLREQFEEEQEA---------KAELQRG 1364
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEarlERLEDRRERLQQEIEEllkkleeaeLKELQAE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1365 MSKANSEVAQWRSKYEtDAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVED------------- 1431
Cdd:TIGR02168 442 LEELEEELEELQEELE-RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkallknqsglsg 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1432 ------------------------------LMTDVERANSLAANLdkKQRNFDKVL-------------------AEWKQ 1462
Cdd:TIGR02168 521 ilgvlselisvdegyeaaieaalggrlqavVVENLNAAKKAIAFL--KQNELGRVTflpldsikgteiqgndreiLKNIE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1463 KYEESQAELEGAQKEARSLSTELF---KMKNSYEEALDQLETMKRENK---------------------------NLQQE 1512
Cdd:TIGR02168 599 GFLGVAKDLVKFDPKLRKALSYLLggvLVVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsaktnssilERRRE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1513 ISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLaekdEEMEQIKR 1592
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE----ERIAQLSK 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1593 NSQRVIDSMQSTLDAEVRSRNDALRVKKKM---EGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQE 1669
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIeelEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1670 DMKEQVAMVERRNGLMVAEIEELRAALEQTERSRKVAEQELVDASERVgllhSQNSSLLNTKKKLETDLVQVQGEVDDAV 1749
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER----ASLEEALALLRSELEELSEELRELESKR 910
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1750 QEARNAEDKAKKAITDAAMMAEELKKEQDTSahLERMKKNLEVTvkdlqhrLDEAENLaMKGGKKQLQKLEQRVRELETE 1829
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRIDNL--QERLSEEYSLT-------LEEAEAL-ENKIEDDEEEARRRLKRLENK 980
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1316056572 1830 VEGEQKRGADAVKGVRKYERRVKELTYQTEEDKKNITRLQDLVDKL 1875
Cdd:TIGR02168 981 IKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
847-1598 |
1.11e-25 |
|
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: 116.32 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 847 AETEKELQNMKENYEkmqsdLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEglikskiQLEAKLKET 926
Cdd:TIGR02169 210 AERYQALLKEKREYE-----GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE-------EIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 927 TERLED--EEEINA------ELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTK 998
Cdd:TIGR02169 278 NKKIKDlgEEEQLRvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 999 EKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQ 1078
Cdd:TIGR02169 358 EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1079 QSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQR------------------ 1140
Cdd:TIGR02169 438 ELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseervrggraveevlk 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1141 ----------ADLSRELEEISERLEEAGG-----------ATAAQ-IEMNKKREA------EFQKLRRDLEESTLQHEAT 1192
Cdd:TIGR02169 518 asiqgvhgtvAQLGSVGERYATAIEVAAGnrlnnvvveddAVAKEaIELLKRRKAgratflPLNKMRDERRDLSILSEDG 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1193 AAALrkkqADSVAELGEQIDNLQR-------VKQKLEKEKS---EFKM-----EIDDLSSNMEAVAKAKGNLEKMCRTLE 1257
Cdd:TIGR02169 598 VIGF----AVDLVEFDPKYEPAFKyvfgdtlVVEDIEAARRlmgKYRMvtlegELFEKSGAMTGGSRAPRGGILFSRSEP 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1258 DQLSEIKSKNDENVRQLNDINAQKARLQTENGEF-------ARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAK 1330
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELsqelsdaSRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1331 NALAHAVQSARHDCDLLREQFEEEQEAKAEL------------QRGMSKANSEVAQWRSkyetdaiqRTEELEEAKKKLA 1398
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLearlshsripeiQAELSKLEEEVSRIEA--------RLREIEQKLNRLT 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1399 QRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEA 1478
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1479 RSLSTELFKMKNSYEEALDQLETMKRENKnlqqEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQA----------AL 1548
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnmlaiqEY 981
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1316056572 1549 EEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKD----EEMEQIKRNSQRVI 1598
Cdd:TIGR02169 982 EEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRevfmEAFEAINENFNEIF 1035
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
921-1807 |
1.15e-25 |
|
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: 116.32 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 921 AKLKETTERLEDEEEINAELTAKKRKLEDECSELKKdIDDLELTLAKVE-----KEKHATENKVKNLTEEMATQDEAIAK 995
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 996 LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKaktkleqqvddlEGSLEQEKKLRmDLERAKRKLEGDLKLAQESIMDLEN 1075
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGE------------EEQLRVKEKIG-ELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1076 DKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLE 1155
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1156 EAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQadsvAELGEQIDNLQRVKQKLEKEKSEFKmeiddl 1235
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA----LEIKKQEWKLEQLAADLSKYEQELY------ 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1236 ssnmeavakakgNLEKMCRTLEDQLSEIKskndenvRQLNDINAQKARLQTENGEFARQLEEKEA-------LVSQLTRG 1308
Cdd:TIGR02169 473 ------------DLKEEYDRVEKELSKLQ-------RELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGSV 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1309 KQAFTQQIEELKRH------IEEEVKAKNA--LAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYE 1380
Cdd:TIGR02169 534 GERYATAIEVAAGNrlnnvvVEDDAVAKEAieLLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1381 TD---AIQRT---EELEEAKK--------KLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANL 1446
Cdd:TIGR02169 614 PAfkyVFGDTlvvEDIEAARRlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSL 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1447 DKKQRNFDKVLAEWKQKYEESQAELEGAQKEArslstelfkmknsyEEALDQLETMKRENKNLQQEISDLTEQIGETGKS 1526
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEI--------------EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1527 IHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQL-ELNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQstl 1605
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELsKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ--- 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1606 daEVRSRNDALRVKKKMEGD-LNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQlhlddavRGQEDMKEQVAMVERRNGL 1684
Cdd:TIGR02169 837 --ELQEQRIDLKEQIKSIEKeIENLNGKKEELEEELEELEAALRDLESRLGDLK-------KERDELEAQLRELERKIEE 907
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1685 MVAEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLntkkkletDLVQVQGEVDDAVQEARNAEDKAKKAIt 1764
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL--------SLEDVQAELQRVEEEIRALEPVNMLAI- 978
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 1316056572 1765 daammaEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENL 1807
Cdd:TIGR02169 979 ------QEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
843-1412 |
3.01e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 114.65 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 843 LLKSAETEKELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAK 922
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 923 LKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKA 1002
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1003 LQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDE 1082
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1083 KIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIE--ELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGA 1160
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1161 TAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEFkmeIDDLSSNME 1240
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL---GDTLLGRTL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1241 AVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELK 1320
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1321 RHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELqrgmskansevaqwrSKYETDAIQRTEELEEAKKKLaQR 1400
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL---------------EEEALEELPEPPDLEELEREL-ER 771
|
570
....*....|..
gi 1316056572 1401 LQEAEESIEAVN 1412
Cdd:COG1196 772 LEREIEALGPVN 783
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
224-715 |
3.20e-24 |
|
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: 110.99 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 224 IVAANPLLEAYGNAKTVRNDNSSRFGKF--IRIHFGTSG---KLASADIETYLLEKSRVTFQLSAER------SYHIFYq 292
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERGRESgdqnelNFHILY- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 293 lmtahkpelidALLITTNPYDFPMISQGEITVKSID--------------------------DVEEFIATDTAIDILGFT 346
Cdd:cd14894 328 -----------AMVAGVNAFPFMRLLAKELHLDGIDcsaltylgrsdhklagfvskedtwkkDVERWQQVIDGLDELNVS 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 347 ADEKFNIYKLTGAVMHHGNMKFKQKQREEQAEPDGT---EVADKIAYLLGLNSADMLKALCYPR---VKVGNEMVTKGQT 420
Cdd:cd14894 397 PDEQKTIFKVLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 421 VPQVNNAVSALCKSVYEKMFLWMVIRINE--------------MLDTKQAR---AFFIGVLDIAGFEIFDFNSLEQLCIN 483
Cdd:cd14894 477 KGQVNHVRDTLARLLYQLAFNYVVFVMNEatkmsalstdgnkhQMDSNASApeaVSLLKIVDVFGFEDLTHNSLDQLCIN 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 484 FTNEKLQQFFNHTMFVLEQEEYKKEGIDWEfidfgmdlAACIELIEKPLGIFSILEEECMFPKASDTTF-----KNKLID 558
Cdd:cd14894 557 YLSEKLYAREEQVIAVAYSSRPHLTARDSE--------KDVLFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 559 QHLGKNRAFEKPKPGK--GKAEAH---------FSLVHYAGTVDYNITGWLDKNKDPLNESVVQLYQKSGNKLLCFLY-- 625
Cdd:cd14894 629 RNIYDRNSSRLPEPPRvlSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLne 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 626 AAHASAEADTGSKKGGKKKGGSFQTVSAV--FRENLGKLMTNLRSTHPHFVRCLIPNESKTPGLMENFLVIHQLRCNGVL 703
Cdd:cd14894 709 SSQLGWSPNTNRSMLGSAESRLSGTKSFVgqFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLI 788
|
570
....*....|..
gi 1316056572 704 EGIRICRKGFPS 715
Cdd:cd14894 789 RQMEICRNSSSS 800
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1123-1913 |
8.40e-24 |
|
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: 110.16 E-value: 8.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1123 EEEIEAERAARAKVEKQRADLSRELEEISERLEEaggataAQIEMNKKReaEFQKLRRDLEEstlqHEATAAALRKKQAD 1202
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLER------LRREREKAE--RYQALLKEKRE----YEGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1203 svaelgEQIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEAVAkakgnlekmcRTLEDQLSEIKSKNDENVRQ----LNDIN 1278
Cdd:TIGR02169 237 ------RQKEAIERQLASLEEELEKLTEEISELEKRLEEIE----------QLLEELNKKIKDLGEEEQLRvkekIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1279 AQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAK 1358
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1359 AELQRgmskansEVAQWRSKYEtDAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVER 1438
Cdd:TIGR02169 381 AETRD-------ELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1439 AnslaanlDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTElfkmknsyeeaLDQLETMKRENKNLQQEISDLTE 1518
Cdd:TIGR02169 453 Q-------EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE-----------LAEAEAQARASEERVRGGRAVEE 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1519 QIGETGKSIHELEKAKKTVeteKSEIQAALEEAEG------TLEHE-----------ESKILRVQ-LELNQVKSE----- 1575
Cdd:TIGR02169 515 VLKASIQGVHGTVAQLGSV---GERYATAIEVAAGnrlnnvVVEDDavakeaiellkRRKAGRATfLPLNKMRDErrdls 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1576 ---------IDRKLAEKDEEMEQIKR---NSQRVIDSMQS-----------TLDAEV-----------RSRNDALRVKKK 1621
Cdd:TIGR02169 592 ilsedgvigFAVDLVEFDPKYEPAFKyvfGDTLVVEDIEAarrlmgkyrmvTLEGELfeksgamtggsRAPRGGILFSRS 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1622 MEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMKEQVAMVERRNGLMVAEIEELRAALEQTER 1701
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1702 SRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDLvqVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDTSA 1781
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1782 HLERMKKNLEVTVKDLQHRL----DEAENLAMKGGKK--QLQKLEQRVRELETEVEGEQKRGADAVKGVRKYERRVKELT 1855
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIksieKEIENLNGKKEELeeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 1316056572 1856 YQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQANSHMSrLRKVQHEMEEAQER 1913
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEE 966
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
916-1537 |
1.98e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.87 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 916 KIQLEAKLKETTERLEDEEEINAELTAKKRKLEdecsELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAK 995
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELE----ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 996 LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLEN 1075
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1076 DKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLE 1155
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1156 EAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDL 1235
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1236 SSNMEAVAKAkgnlekmcrTLEDQLSEIKSKNDENVRQLndINAQKAR---------LQTENGEFARQLEEKEALVSQLT 1306
Cdd:COG1196 533 EAAYEAALEA---------ALAAALQNIVVEDDEVAAAA--IEYLKAAkagratflpLDKIRARAALAAALARGAIGAAV 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1307 RGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHdcdlLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYETDAIQR 1386
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALR----RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1387 TEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEE 1466
Cdd:COG1196 678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316056572 1467 SQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTV 1537
Cdd:COG1196 758 EPPDLEELERELERLEREIEALGPVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1314-1927 |
2.25e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.49 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1314 QQIEELKR-----------HIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVaqwrskyetd 1382
Cdd:COG1196 200 RQLEPLERqaekaeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL---------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1383 aiqrtEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQ 1462
Cdd:COG1196 270 -----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1463 KYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKS 1542
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1543 EIQAALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRnsqrvidsmqstLDAEVRSRNDALRVKKKM 1622
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL------------LEAALAELLEELAEAAAR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1623 EGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDmkeQVAMVERRNGLMVAEIEELRAALEQTERS 1702
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL---EAALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1703 RKVAEQELVDASERVGLLHSQNSSLLntKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAH 1782
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARG--AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1783 LERmkknlevtvkdlqhrldeaenLAMKGGKKQLQKLEQRVRELETEVEGEQKRGADAVKGVRKYERRVKELTYQTEEDK 1862
Cdd:COG1196 648 EVT---------------------LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316056572 1863 KNITRLQDLVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEEAQ----ERADIAESQVNKLRAK 1927
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEElpepPDLEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1254-1831 |
9.38e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.56 E-value: 9.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1254 RTLEDQLSEIKSKndENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNAL 1333
Cdd:COG1196 216 RELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1334 AHAVQSARHDCDLLREQFEEEQEAKAELQRgmskansEVAQWrskyETDAIQRTEELEEAKKKLAQRLQEAEESIEAVns 1413
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEE-------ELAEL----EEELEELEEELEELEEELEEAEEELEEAEAEL-- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1414 kcASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYE 1493
Cdd:COG1196 361 --AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1494 EALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQA---ALEEAEGTLEHEESKILRVQLELN 1570
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAArllLLLEAEADYEGFLEGVKAALLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1571 QVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNV 1650
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1651 QGQLKDAQLHLDDAVRGQEDMKEQVamVERRNGLMVAEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLNT 1730
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLL--GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1731 KKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLAMK 1810
Cdd:COG1196 677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL 756
|
570 580
....*....|....*....|.
gi 1316056572 1811 GGKKQLQKLEQRVRELETEVE 1831
Cdd:COG1196 757 PEPPDLEELERELERLEREIE 777
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1290-1854 |
5.31e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.86 E-value: 5.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1290 EFARQLEEKEALVSQLTRgkQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKAN 1369
Cdd:COG1196 217 ELKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1370 SEVAQwrskyetdAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKK 1449
Cdd:COG1196 295 AELAR--------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1450 QRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHE 1529
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1530 LEKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEM---EQIKRNSQRVIDSMQSTLD 1606
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflEGVKAALLLAGLRGLAGAV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1607 AEVRSrnDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQL--RNVQGQLKDAQLHLDDAVRGQEDMKEQVAMVERRNGL 1684
Cdd:COG1196 527 AVLIG--VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYlkAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1685 MVAEIEElrAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAIT 1764
Cdd:COG1196 605 ASDLREA--DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1765 DAAmmAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLEQRVRELETEVEGEQKRGADAVKG- 1843
Cdd:COG1196 683 ELA--ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPp 760
|
570
....*....|....*....
gi 1316056572 1844 --------VRKYERRVKEL 1854
Cdd:COG1196 761 dleelereLERLEREIEAL 779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
872-1605 |
8.87e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 103.68 E-value: 8.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 872 AKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLED-E 950
Cdd:PTZ00121 1205 ARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElK 1284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 951 CSELKKDIDDLEltlaKVEKEKHATENKVKnlTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAEEdkvntltKAKTK 1030
Cdd:PTZ00121 1285 KAEEKKKADEAK----KAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE-------AAKAE 1351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1031 LEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQK 1110
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK 1431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1111 KIKELQARIEELEEEIEAeraarakveKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEfqKLRRDLEESTLQ-H 1189
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEA---------KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD--EAKKKAEEAKKKaD 1500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1190 EATAAALRKKQADSVAELGEQidnlqrvKQKLEKEKSEFKMEIDDLSSnmeavAKAKGNLEKMCRTLEDQLSEIKSKNDE 1269
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKKAEEA-------KKADEAKKAEEAKKADEAKK-----AEEKKKADELKKAEELKKAEEKKKAEE 1568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1270 NVRQLNDINAQKARlqtenGEFARQLEEKEaLVSQLTRGKQAFTQQIEELKRhiEEEVKAKNALAHAVQSARHDCDLLRE 1349
Cdd:PTZ00121 1569 AKKAEEDKNMALRK-----AEEAKKAEEAR-IEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1350 QFEEEQEAKAELQRGMSKANSEVAQWRSKYETDAiQRTEEL----EEAKKKLAQRLQEAEES--IEAVNSKCASLEKTKQ 1423
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkkaeEDEKKAAEALKKEAEEAkkAEELKKKEAEEKKKAE 1719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1424 RLQGEVEDLMTDVERAnslaanldKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSY-EEALDQLETM 1502
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAViEEELDEEDEK 1791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1503 KR-ENKNLQQEISDLTEQIGETGKSIHELEKAKKtvETEKSEIQAALEEAEGTLEhEESKILRVQLELNQVKSEIDRKLA 1581
Cdd:PTZ00121 1792 RRmEVDKKIKDIFDNFANIIEGGKEGNLVINDSK--EMEDSAIKEVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKEA 1868
|
730 740 750
....*....|....*....|....*....|....
gi 1316056572 1582 ----EKD------EEMEQIKRNSQRVIDSMQSTL 1605
Cdd:PTZ00121 1869 dfnkEKDlkeddeEEIEEADEIEKIDKDDIEREI 1902
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
928-1865 |
1.45e-21 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 102.84 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 928 ERLEDEEEIN--AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEkhatenkVKNLTEEmatqdeaiaKLTKEK-KALQ 1004
Cdd:TIGR02169 154 ERRKIIDEIAgvAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQ-------LERLRRE---------REKAERyQALL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1005 EAHQQTLDDLQAEEdkVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQ-QSDEK 1083
Cdd:TIGR02169 218 KEKREYEGYELLKE--KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1084 IKKKDFEISQLLSKIEDEQSLGAQLQKKIKELqarieeleeeieaeraarakvEKQRADLSRELEEISERLEEAGGATAA 1163
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKL---------------------EAEIDKLLAEIEELEREIEEERKRRDK 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1164 QIEMNKKREAEFQKLRRDLEEStlqhEATAAALRKKQADSVAELGE----------QIDNLQRVKQKLEKEKSEFKMEID 1233
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEV----DKEFAETRDELKDYREKLEKlkreinelkrELDRLQEELQRLSEELADLNAAIA 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1234 DLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFT 1313
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1314 QQIEELKRHIE-------EEVKAKNALAHAVQSARHDcdllREQF---EEEQEAKAELQ----RGMSKAN----SEVAQW 1375
Cdd:TIGR02169 511 AVEEVLKASIQgvhgtvaQLGSVGERYATAIEVAAGN----RLNNvvvEDDAVAKEAIEllkrRKAGRATflplNKMRDE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1376 RSK----YETDAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQ----RLQGEVED---LMTDVERANSLAA 1444
Cdd:TIGR02169 587 RRDlsilSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKyrmvTLEGELFEksgAMTGGSRAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1445 NLDKKQRnfdKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETG 1524
Cdd:TIGR02169 667 LFSRSEP---AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1525 KSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQLELNQvkSEIDRKLAEKDEEMEQIKRNSQRVIDsmqst 1604
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLRE----- 816
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1605 ldaevrsrndalrvkkkMEGDLNEmeiqlSHANRQAAEAQKQlrnvqgqlkdaqlhldDAVRGQEDMKEQVAMVErrngl 1684
Cdd:TIGR02169 817 -----------------IEQKLNR-----LTLEKEYLEKEIQ----------------ELQEQRIDLKEQIKSIE----- 853
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1685 mvAEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQnssllntKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAIT 1764
Cdd:TIGR02169 854 --KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE-------RDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1765 DAAMMAEELKkeqdtsaHLERMKKNLEVtvkdlqhrlDEAENLAMKGGKKQLQKLEQRVRELET-------EVEGEQKRG 1837
Cdd:TIGR02169 925 KLEALEEELS-------EIEDPKGEDEE---------IPEEELSLEDVQAELQRVEEEIRALEPvnmlaiqEYEEVLKRL 988
|
970 980 990
....*....|....*....|....*....|.
gi 1316056572 1838 ADAV--KGVRKYERR-VKELTYQTEEDKKNI 1865
Cdd:TIGR02169 989 DELKekRAKLEEERKaILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1143-1736 |
1.61e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.32 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1143 LSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADsVAELGEQIDNLQRVKQKLE 1222
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-EYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1223 KEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALV 1302
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1303 SQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSarhdcdlLREQFEEEQEAKAELQRgmskANSEVAQWRSKYETD 1382
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEE-------LEEALAELEEEEEEEEE----ALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1383 AIQRTEELEEAKKKLAQRLQEAEESIEAVNSKcASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRnfDKVLAEWKQ 1462
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEA-AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA--VAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1463 KYEESQAELEGAQKEARSLST--------ELFKMKNSYEEALDQLETMKREN--KNLQQEISDLTEQIGETGKSIHELEK 1532
Cdd:COG1196 535 AYEAALEAALAAALQNIVVEDdevaaaaiEYLKAAKAGRATFLPLDKIRARAalAAALARGAIGAAVDLVASDLREADAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1533 AKKTVET--EKSEIQAALEEAEGTLEHEESKILRVQLE---LNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTLDA 1607
Cdd:COG1196 615 YYVLGDTllGRTLVAARLEAALRRAVTLAGRLREVTLEgegGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1608 EVRSRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMKEQVAMVERRnglmVA 1687
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE----LE 770
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1316056572 1688 EIEELRAALEqtersrKV---AEQELVDASERVGLLHSQNSSLLNTKKKLET 1736
Cdd:COG1196 771 RLEREIEALG------PVnllAIEEYEELEERYDFLSEQREDLEEARETLEE 816
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1250-1933 |
3.14e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 102.14 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1250 EKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTE---NGEFARQLEE--KEALVSQLTRGKQAFTQQIEELKRHIE 1324
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEakkKAEDARKAEEarKAEDARKAEEARKAEDAKRVEIARKAE 1161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1325 EEVKAKNAL----AHAVQSARHDCDLLR----EQFEEEQEAKAELQRGMSKANSEVAQWRSKYETDAIQRTEEL----EE 1392
Cdd:PTZ00121 1162 DARKAEEARkaedAKKAEAARKAEEVRKaeelRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAkkdaEE 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1393 AKKKLAQRLQEA----EESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQ 1468
Cdd:PTZ00121 1242 AKKAEEERNNEEirkfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAK 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1469 AELEGAQKEARSLstelfkmKNSYEEALDQLETMKRENKNLQQEISdlteqigetgKSIHELEKAKKTVETEKSEIQAAL 1548
Cdd:PTZ00121 1322 KKAEEAKKKADAA-------KKKAEEAKKAAEAAKAEAEAAADEAE----------AAEEKAEAAEKKKEEAKKKADAAK 1384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1549 EEAEGTLEHEESKilrVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALR-----VKKKME 1623
Cdd:PTZ00121 1385 KKAEEKKKADEAK---KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKkkaeeAKKAEE 1461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1624 GDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMK---EQVAMVERRNGLMVAEIEELRAALEQTE 1700
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkadEAKKAEEAKKADEAKKAEEAKKADEAKK 1541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1701 RSRKVAEQELVDASErvgLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQ-EARNAEDKAKKAITDAAMMAEELKKEQDT 1779
Cdd:PTZ00121 1542 AEEKKKADELKKAEE---LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1780 SAHLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLEQRVRELETEVEGEQKRGADAVKGVRKYERRVKELTYQTE 1859
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 1860 EDKKNitrlqdlVDKLQLKVKAYKRQAEE---AEEQANSHMSRLRKVQHEMEEAQERADIAESQVNKLRAKSRDVGK 1933
Cdd:PTZ00121 1699 EEAKK-------AEELKKKEAEEKKKAEElkkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1204-1831 |
1.98e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.86 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1204 VAELGEQIDNLQRVKQKLEKEKsEFKMEIDDLSSnmEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKAR 1283
Cdd:COG1196 195 LGELERQLEPLERQAEKAERYR-ELKEELKELEA--ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1284 LQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQR 1363
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1364 GMSKANSEVAQWRSKYETDAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKcASLEKTKQRLQGEVEDLMTDVERANSLA 1443
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL-EELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1444 ANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETmKRENKNLQQEISDLTEQIGET 1523
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-AAARLLLLLEAEADYEGFLEG 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1524 GKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEE------MEQIKRNSQRV 1597
Cdd:COG1196 510 VKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGratflpLDKIRARAALA 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1598 IDSMQSTLDAEVRSRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMKEQVAM 1677
Cdd:COG1196 590 AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1678 VERRNGLMVAEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAED 1757
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1758 KAKKAITDAAMMAEELKKEQDTsahLERMKKNLEvTV--------KDLQHRLDEaenlaMKGGKKQLQK----LEQRVRE 1825
Cdd:COG1196 750 EEALEELPEPPDLEELERELER---LEREIEALG-PVnllaieeyEELEERYDF-----LSEQREDLEEaretLEEAIEE 820
|
....*.
gi 1316056572 1826 LETEVE 1831
Cdd:COG1196 821 IDRETR 826
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1390-1925 |
3.38e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.09 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1390 LEEA--------KKKLA-QRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLmtdvERANSLAANLDKKQ--------RN 1452
Cdd:COG1196 161 IEEAagiskykeRKEEAeRKLEATEENLERLEDILGELERQLEPLERQAEKA----ERYRELKEELKELEaellllklRE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1453 FDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDL-------TEQIGETGK 1525
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiarlEERRRELEE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1526 SIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTL 1605
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1606 DAEVRsRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMKEQVAMVERRNGLM 1685
Cdd:COG1196 397 ELAAQ-LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1686 VAEIEELRAALEQTERSRKVAEQELVDASERV-GLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNA--EDKAKKA 1762
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLeGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAalQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1763 ITDAAMMAEELKKEQD---TSAHLERMKKNLEVTVKDLQHRLDEAENLAM--------------------KGGKKQLQKL 1819
Cdd:COG1196 556 DEVAAAAIEYLKAAKAgraTFLPLDKIRARAALAAALARGAIGAAVDLVAsdlreadaryyvlgdtllgrTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1820 EQRVRELETEVEGEQKRGADAVKGVRKYERRVKELTYQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQANSHMSR 1899
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
570 580
....*....|....*....|....*.
gi 1316056572 1900 LRKVQHEMEEAQERADIAESQVNKLR 1925
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEEL 741
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
968-1776 |
5.26e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.90 E-value: 5.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 968 VEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAEEdkvnTLTKAKTKLEQQVDDLEGSLEQEKK 1047
Cdd:PTZ00121 1041 VLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADE----ATEEAFGKAEEAKKTETGKAEEARK 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1048 LrmdlERAKRKLEgDLKLAQESimDLENDKQQSDEKIKKKDFEISQLLSKIED----EQSLGAQLQKKIKELQARIEELE 1123
Cdd:PTZ00121 1117 A----EEAKKKAE-DARKAEEA--RKAEDARKAEEARKAEDAKRVEIARKAEDarkaEEARKAEDAKKAEAARKAEEVRK 1189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1124 EEIEAERAARAKVEK-QRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLR--RDLEESTLQHEATAAALRKKQ 1200
Cdd:PTZ00121 1190 AEELRKAEDARKAEAaRKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEeeRNNEEIRKFEEARMAHFARRQ 1269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1201 ADSVAELGEQIDNLQR---VKQKLEKEKSEFKMEIDDLSSNMEAVAKAKgNLEKMCRTLEDQLSEIKSKNDENVRQlndI 1277
Cdd:PTZ00121 1270 AAIKAEEARKADELKKaeeKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKKKAEEAKKA---A 1345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1278 NAQKARLQTENGEFARQLEEKEALVSQLTRGKQaftqQIEELKRHIEEEVKAKNALAHAvQSARHDCDLLREQFEEEQEA 1357
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK----KADAAKKKAEEKKKADEAKKKA-EEDKKKADELKKAAAAKKKA 1420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1358 KAELQRGMSKANSEVAQWRSKYETDAIQRTEELEEAKKKlAQRLQEAEESIEAVNSKCASLEKTKqrlqgeVEDLMTDVE 1437
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKA-EEAKKKAEEAKKADEAKKKAEEAKK------ADEAKKKAE 1493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1438 RANSLAANLDKKQRnfDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMknsyEEALDQLETMKRENKNLQQEISDLT 1517
Cdd:PTZ00121 1494 EAKKKADEAKKAAE--AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA----EEKKKADELKKAEELKKAEEKKKAE 1567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1518 EQIGETGKSIHELEKAK--KTVETEKSEIQAALEEAEGTLEHEESKilrvQLELNQVKSEIDRKLAEKDEEMEQIKRNSQ 1595
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEeaKKAEEARIEEVMKLYEEEKKMKAEEAK----KAEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1596 RVIDSMQSTLDAEVRSRNDALRVKKKMEGDLNEMEiQLSHANRQAAEAQKQLRNVQGQLKDAQlhldDAVRGQEDMKEQV 1675
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE-EAKKAEEDEKKAAEALKKEAEEAKKAE----ELKKKEAEEKKKA 1718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1676 AMVERRNGLMVAEIEELRaalEQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNA 1755
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAK---KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
810 820
....*....|....*....|.
gi 1316056572 1756 EDKAKKAITDAAMMAEELKKE 1776
Cdd:PTZ00121 1796 VDKKIKDIFDNFANIIEGGKE 1816
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1197-1925 |
5.79e-19 |
|
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: 94.36 E-value: 5.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1197 RKKQADSVAELGEQIDNLQRVKQKLE--KEKSE-FKMEIDDLSSNMEAVAKAKGNLEKMcRTLEDQLSEIKSKndENVRQ 1273
Cdd:TIGR02169 155 RRKIIDEIAGVAEFDRKKEKALEELEevEENIErLDLIIDEKRQQLERLRREREKAERY-QALLKEKREYEGY--ELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1274 LNDINAQKARLQtengefaRQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAhavqsarhdcdllreqfEE 1353
Cdd:TIGR02169 232 KEALERQKEAIE-------RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG-----------------EE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1354 EQeakAELQRGMSKANSEVAQWRSKyetdaiqrTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLM 1433
Cdd:TIGR02169 288 EQ---LRVKEKIGELEAEIASLERS--------IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1434 TDVeranslaanldkkqrnfdkvlAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEI 1513
Cdd:TIGR02169 357 EEY---------------------AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEEL 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1514 SDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEH-------EESKILRVQLELNQVKSEIDRKLAEKDEE 1586
Cdd:TIGR02169 416 QRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQlaadlskYEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1587 MEQIKRNSQRVIDS--MQSTLDAEVR-------------------------SRNDALRVK------------KKMEGD-- 1625
Cdd:TIGR02169 496 EAQARASEERVRGGraVEEVLKASIQgvhgtvaqlgsvgeryataievaagNRLNNVVVEddavakeaiellKRRKAGra 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1626 ----LNEMEIQLSHANRQA-----------AEAQKQLRNVQGQLKDAQLHLDDAVRGQEDM------------------- 1671
Cdd:TIGR02169 576 tflpLNKMRDERRDLSILSedgvigfavdlVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMgkyrmvtlegelfeksgam 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1672 -----------------KEQVAMVERRNGLMVAEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKL 1734
Cdd:TIGR02169 656 tggsraprggilfsrsePAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1735 ETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMkknlevtvkDLQHRLDEAENLAMKgGKK 1814
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR---------LSHSRIPEIQAELSK-LEE 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1815 QLQKLEQRVRELETEVEGEQKRGADAVKGVRKYERRVKELTYQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQAN 1894
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
810 820 830
....*....|....*....|....*....|.
gi 1316056572 1895 SHMSRLRKVQHEMEEAQERADIAESQVNKLR 1925
Cdd:TIGR02169 886 DLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
976-1599 |
9.47e-19 |
|
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: 93.16 E-value: 9.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 976 ENKVKNLTEEMATQDEAIAKLTKEKKALQeahqqtlDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERA 1055
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLD-------KNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1056 KRKLEGDLKLAQESIMDLENDKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAK 1135
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1136 VEKQRADLSRELEEISERLeeaggataAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQ 1215
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLL--------SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1216 RVKQKLEKEKSEFKMEIDDLSSNmeavakakgnlEKMCRTLEDQLSEIKSKndenvrqLNDINAQKArlQTENGEFARQL 1295
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQKELEQN-----------NKKIKELEKQLNQLKSE-------ISDLNNQKE--QDWNKELKSEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1296 EEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSarhdcdlLREQFEEEQEAKAELQRGMSKANSEVaqw 1375
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSE-------KQRELEEKQNEIEKLKKENQSYKQEI--- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1376 rskyetdaiqrtEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDK 1455
Cdd:TIGR04523 387 ------------KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1456 VLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKK 1535
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316056572 1536 TVETEKSEIQAALEEAEGTLEHE--ESKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQRVID 1599
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1210-1889 |
2.04e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 92.05 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1210 QIDNLQRVKQKLEKEKSEFKMEIDdlssNMEAVAKAKGNLEKMCRTLEDQLSEIKskndenvRQLNDINAQKARLQTENG 1289
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIE----RLEKFIKRTENIEELIKEKEKELEEVL-------REINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1290 EFARQLEEKEALVSQltrgkqaftqqIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQ--RGMSK 1367
Cdd:PRK03918 225 KLEKEVKELEELKEE-----------IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1368 ANSEVAQWRSKYEtdaiQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMtdveranslaanld 1447
Cdd:PRK03918 294 EYIKLSEFYEEYL----DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE-------------- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1448 kkqrnfdkVLAEWKQKYEESQAELEGAQK-EARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKS 1526
Cdd:PRK03918 356 --------ELEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1527 IHELEKAKKTVETEKSEIqaaleeaegTLEHEESKILRVQLELNQVKSEidrkLAEKDEEMEQIKRNSQRVidsmqstld 1606
Cdd:PRK03918 428 IEELKKAKGKCPVCGREL---------TEEHRKELLEEYTAELKRIEKE----LKEIEEKERKLRKELREL--------- 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1607 AEVRSRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQ----LRNVQGQLKDAQLHLDDAVRGQEDMKEQVAMVERRn 1682
Cdd:PRK03918 486 EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEeyekLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK- 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1683 glmVAEIEELRAALEQTERSRKVAEQELVDasERVGLLHSQNSSLLNTKkkletdlvqvqgevdDAVQEARNAEDKAKKA 1762
Cdd:PRK03918 565 ---LDELEEELAELLKELEELGFESVEELE--ERLKELEPFYNEYLELK---------------DAEKELEREEKELKKL 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1763 ITDAAMMAEELkkeQDTSAHLERMKKNLEvtvkDLQHRLDEAENlamKGGKKQLQKLEQRVRELETEVEGEQKRGADAVK 1842
Cdd:PRK03918 625 EEELDKAFEEL---AETEKRLEELRKELE----ELEKKYSEEEY---EELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1316056572 1843 GVRKYERRVKELTYQTEEDKKnITRLQDLVDKLQLKVKAYKRQAEEA 1889
Cdd:PRK03918 695 TLEKLKEELEEREKAKKELEK-LEKALERVEELREKVKKYKALLKER 740
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
845-1459 |
4.30e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 91.28 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 845 KSAETEKELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAKLK 924
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 925 ETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEK---- 1000
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGerya 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1001 KALQEAHQQTLDDLQAEEDKVNT----LTKAK----------TKLEQQVDDLEGSLEQ------------EKKLR----- 1049
Cdd:TIGR02169 539 TAIEVAAGNRLNNVVVEDDAVAKeaieLLKRRkagratflplNKMRDERRDLSILSEDgvigfavdlvefDPKYEpafky 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1050 --------MDLERAKR--------KLEGDL--------------KLAQESIMDLENDKQQSDEKIKKKDFEISQLLSKIE 1099
Cdd:TIGR02169 619 vfgdtlvvEDIEAARRlmgkyrmvTLEGELfeksgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELR 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1100 DEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAggataaqiemnkkrEAEFQKLR 1179
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV--------------KSELKELE 764
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1180 RDLEEstlqHEATAAALRKKQADSVAELG-EQIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLED 1258
Cdd:TIGR02169 765 ARIEE----LEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1259 QLSEIKSKNDENVRQLNDINAQKArlqtengEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQ 1338
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKE-------ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1339 SARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSkyETDAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASL 1418
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS--LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDEL 991
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1316056572 1419 EKTKQRLQGEVEDL-----MTDVERANSLAANLDKKQRNFDKVLAE 1459
Cdd:TIGR02169 992 KEKRAKLEEERKAIlerieEYEKKKREVFMEAFEAINENFNEIFAE 1037
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
939-1591 |
5.42e-18 |
|
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: 90.46 E-value: 5.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 939 ELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEmatQDEAIAKLTKEKKALQEAHQqtldDLQAEE 1018
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQ---IKDLNDKLKKNKDKINKLNS----DLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1019 DKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDEKIKKKDFEISQLLSKI 1098
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1099 EDEQSLGAQLQKKIKELQarieELEEEIEAERAARAKVEKQRADLSRELEEISERLEEaggataaqiemnkkREAEFQKL 1178
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLK----KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE--------------KTTEISNT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1179 RRDLEESTLQHEATAAALRKKQadsvaelgEQIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEA-----VAKAKGNLEKMC 1253
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQ--------KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1254 RTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKrhieeevKAKNAL 1333
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE-------SQINDL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1334 AHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYEtDAIQRTEELEEAKKKLAQRLQEAEESIEAVNS 1413
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK-DLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1414 KCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKnsYE 1493
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD--FE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1494 EALDQLETMKRENknlQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAE---GTLEHEESKILRVQLELN 1570
Cdd:TIGR04523 554 LKKENLEKEIDEK---NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEkkiSSLEKELEKAKKENEKLS 630
|
650 660
....*....|....*....|.
gi 1316056572 1571 QVKSEIDRKLAEKDEEMEQIK 1591
Cdd:TIGR04523 631 SIIKNIKSKKNKLKQEVKQIK 651
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1137-1904 |
1.08e-17 |
|
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: 90.18 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1137 EKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTlqHEATAAALRKKqaDSVAELGEQIDNLQR 1216
Cdd:pfam15921 102 EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV--HELEAAKCLKE--DMLEDSNTQIEQLRK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1217 VKQKLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKM-CRTLEDQLSEIkskndenVRQLN-DINAQKARLQTENGEFARQ 1294
Cdd:pfam15921 178 MMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMhFRSLGSAISKI-------LRELDtEISYLKGRIFPVEDQLEAL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1295 LEEKEALVSQLTRGKQaftQQIEELKRHIEEEVkakNALAHAVQSARHDCDLLREQFEEEQEA----KAELQRGMSKANS 1370
Cdd:pfam15921 251 KSESQNKIELLLQQHQ---DRIEQLISEHEVEI---TGLTEKASSARSQANSIQSQLEIIQEQarnqNSMYMRQLSDLES 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1371 EVAQWRSkyetdaiqrteELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQR-------LQGEVEDLMTDV-ERANSL 1442
Cdd:pfam15921 325 TVSQLRS-----------ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQfsqesgnLDDQLQKLLADLhKREKEL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1443 AANLDKKQRNFDKVLAEwKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALD-QLETMKRENKNLQQeISDLTEQIG 1521
Cdd:pfam15921 394 SLEKEQNKRLWDRDTGN-SITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMErQMAAIQGKNESLEK-VSSLTAQLE 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1522 ETG----KSIHELEKAKKTVETEK---SEIQAALEEAEGTLEHEESKIL----RVQL---ELNQVKSEIDR--------- 1578
Cdd:pfam15921 472 STKemlrKVVEELTAKKMTLESSErtvSDLTASLQEKERAIEATNAEITklrsRVDLklqELQHLKNEGDHlrnvqtece 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1579 ----KLAEKDEEMEQIKRNsqrvIDSMQSTLDAEVRSRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQL 1654
Cdd:pfam15921 552 alklQMAEKDKVIEILRQQ----IENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1655 KDAQLHLDDAVRGQEDMKEQVAMVERRNGLMVAEIEELRAALEQTERSRKVAEQELVDASERVGLlhsqnssllnTKKKL 1734
Cdd:pfam15921 628 SDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMET----------TTNKL 697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1735 ETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDL---QHRLDEAENlamkg 1811
Cdd:pfam15921 698 KMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNAnkeKHFLKEEKN----- 772
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1812 gkkqlqKLEQrvrELETeVEGEQKRGADAVKGVRKYERRVKEltyqteedkkNITRLQDLVDKLQLKVKA----YKRQAE 1887
Cdd:pfam15921 773 ------KLSQ---ELST-VATEKNKMAGELEVLRSQERRLKE----------KVANMEVALDKASLQFAEcqdiIQRQEQ 832
|
810
....*....|....*..
gi 1316056572 1888 EAEEQANSHMSRLRKVQ 1904
Cdd:pfam15921 833 ESVRLKLQHTLDVKELQ 849
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
958-1587 |
1.31e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 89.74 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 958 IDDLELTLAKVEKEKHATENKVKNLTEEMAtQDEAIAKLTKEKKalqeahqqtlDDLQAEEDKVNTLTKAKTKLEQQVDD 1037
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIK-RTENIEELIKEKE----------KELEEVLREINEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1038 LEGSLEQEKKLRMDLERAKRKLEGDLKlaqeSIMDLENDKQQSDEKIKKKDFEISQLLSKIEDeqslgaqlQKKIKELQA 1117
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEG----SKRKLEEKIRELEERIEELKKEIEELEEKVKE--------LKELKEKAE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1118 RIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGgATAAQIEMNKKREAEFQKLRRDLEESTLQHE------A 1191
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE-EKEERLEELKKKLKELEKRLEELEERHELYEeakakkE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1192 TAAALRKKQAD-SVAELGEQIDNLQRVKQKLEKE-------KSEFKMEIDDLSSNMEAVAKAKGNlekmCRTLEDQLSEI 1263
Cdd:PRK03918 373 ELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEiskitarIGELKKEIKELKKAIEELKKAKGK----CPVCGRELTEE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1264 KSKN--DENVRQLNDINAQKARLQTENGEFARQLEEKEALV---SQLTRGKQAFTQQI---EELKRHIEEEVKAKNalah 1335
Cdd:PRK03918 449 HRKEllEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLkkeSELIKLKELAEQLKeleEKLKKYNLEELEKKA---- 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1336 avqsarhdcdllrEQFEEEQEAKAELQRGMSKANSEvaqwrskyetdaIQRTEELEEAKKKLAQRLQEAEESIEAVNSKC 1415
Cdd:PRK03918 525 -------------EEYEKLKEKLIKLKGEIKSLKKE------------LEKLEELKKKLAELEKKLDELEEELAELLKEL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1416 ASLE-KTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKvLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSY-- 1492
Cdd:PRK03918 580 EELGfESVEELEERLKELEPFYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYse 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1493 ---EEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQaALEEAEGTLEHEESKILRVQLEL 1569
Cdd:PRK03918 659 eeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE-KLEKALERVEELREKVKKYKALL 737
|
650
....*....|....*....
gi 1316056572 1570 N-QVKSEIDRKLAEKDEEM 1587
Cdd:PRK03918 738 KeRALSKVGEIASEIFEEL 756
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
843-1565 |
2.80e-17 |
|
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: 88.49 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 843 LLKSAETEKELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAK 922
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 923 LKETTERLEDEEEINAEltakKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNL--------TEEMATQDEAIA 994
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEE----QLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAplaahikaVTQIEQQAQRIH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 995 KLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQ--ESIMD 1072
Cdd:TIGR00618 314 TELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQqkTTLTQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1073 LENDKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISE 1152
Cdd:TIGR00618 394 KLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1153 RLEEAGGATAAQIEMNKKREA---EFQKLRRDLEESTLQHEATAAALRKKQADS---------VAELGEQIDNLQRVKQK 1220
Cdd:TIGR00618 474 QLQTKEQIHLQETRKKAVVLArllELQEEPCPLCGSCIHPNPARQDIDNPGPLTrrmqrgeqtYAQLETSEEDVYHQLTS 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1221 LEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRqlndinaQKARLQTENGEFARQLEEKEA 1300
Cdd:TIGR00618 554 ERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE-------AEDMLACEQHALLRKLQPEQD 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1301 LVS-QLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKy 1379
Cdd:TIGR00618 627 LQDvRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTL- 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1380 etdaiqrTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDlmtdvERANSLAANLDKKQRNFDKVLAE 1459
Cdd:TIGR00618 706 -------LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH-----QARTVLKARTEAHFNNNEEVTAA 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1460 WK--QKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKR-ENKNLQQEISDLTEQIGETGKSIHELEKA-KK 1535
Cdd:TIGR00618 774 LQtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRLEEKSATLGEITHQlLK 853
|
730 740 750
....*....|....*....|....*....|
gi 1316056572 1536 TVETEKSEIQAALEEAEGTLEHEESKILRV 1565
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAKIIQLSDKLNGINQ 883
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1294-1828 |
2.88e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 88.56 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1294 QLEEKEA--LVSQLTRGKQAFTQQIEELKRHIEEEVKAKnalahavqSARHDCDLLREQFEEEQEAKAELQRGMSKANSE 1371
Cdd:PRK02224 195 QIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQAR--------ETRDEADEVLEEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1372 VAQWRSKYET------DAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAAN 1445
Cdd:PRK02224 267 IAETEREREElaeevrDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1446 LDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEE-------ALDQLETMKRENKNLQQEISDLTE 1518
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEElrerfgdAPVDLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1519 QIGETGKSIHELEKAKKTVET--------------EKSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEIDR-----K 1579
Cdd:PRK02224 427 REAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERaedlvE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1580 LAEKDEEMEQIKRNSQRVIDSMQSTLDAEvRSRNDALRvKKKMEGDlNEMEIQLSHANRQAAEAQKQLRNVqGQLKDAQL 1659
Cdd:PRK02224 507 AEDRIERLEERREDLEELIAERRETIEEK-RERAEELR-ERAAELE-AEAEEKREAAAEAEEEAEEAREEV-AELNSKLA 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1660 HLDDAVRGQEDMKEQVAMVErRNGLMVAEIEELRAALEQTERSRKvaeQELVDASERvgllhsqnssllntKKKLEtdlv 1739
Cdd:PRK02224 583 ELKERIESLERIRTLLAAIA-DAEDEIERLREKREALAELNDERR---ERLAEKRER--------------KRELE---- 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1740 qvqGEVDDA-VQEARNAEDKAKKAITDAAMMAEELKKEQDtsahlermkkNLEVTVKDLQHRLDEAENLamkggKKQLQK 1818
Cdd:PRK02224 641 ---AEFDEArIEEAREDKERAEEYLEQVEEKLDELREERD----------DLQAEIGAVENELEELEEL-----RERREA 702
|
570
....*....|
gi 1316056572 1819 LEQRVRELET 1828
Cdd:PRK02224 703 LENRVEALEA 712
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1418-1911 |
4.85e-17 |
|
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: 87.87 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1418 LEKTKQRLQGEVEDLMTDVERANSLAanlDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALD 1497
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELH---EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1498 QLETMKRENKNLQQEISDLTEQIGETGKSiHElekakkTVETEKSEIQAALEEAEGTLEHEESKIlrVQLELNQVKSEID 1577
Cdd:pfam15921 153 ELEAAKCLKEDMLEDSNTQIEQLRKMMLS-HE------GVLQEIRSILVDFEEASGKKIYEHDSM--STMHFRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1578 RKLAEKDEEMEQIKRNSQRVIDSMQsTLDAEVRSRNDAL--RVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLK 1655
Cdd:pfam15921 224 KILRELDTEISYLKGRIFPVEDQLE-ALKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1656 DAQlhlddavrgqEDMKEQVAMVERRNGLMVAEIEELRAALEQTERsrkVAEQELVDASERVGLLHSQnssllntkkkle 1735
Cdd:pfam15921 303 IIQ----------EQARNQNSMYMRQLSDLESTVSQLRSELREAKR---MYEDKIEELEKQLVLANSE------------ 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1736 tdLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEaENLamkggkkQ 1815
Cdd:pfam15921 358 --LTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD-RNM-------E 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1816 LQKLEQRVRELETEVEGEQKRGADAVKGVRKYERRVKELTYQTEEDKKNITRLQDLVDKLQLKVKAYKR----------Q 1885
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERtvsdltaslqE 507
|
490 500
....*....|....*....|....*..
gi 1316056572 1886 AEEAEEQANSHMSRLR-KVQHEMEEAQ 1911
Cdd:pfam15921 508 KERAIEATNAEITKLRsRVDLKLQELQ 534
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1137-1890 |
7.08e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.89 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1137 EKQRADlsRELEEISERLEEAGGATAAQIEMNKKREAEFQKLR--RDLEESTLQHEA-TAAALRKKQADSVAELGEQIDN 1213
Cdd:PTZ00121 1085 EDNRAD--EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEdaRKAEEARKAEDArKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1214 LQRVKQKLEKEKSEfkmeiddlssNMEAVAKAkgnlEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARlQTENGEFAR 1293
Cdd:PTZ00121 1163 ARKAEEARKAEDAK----------KAEAARKA----EEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAE 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1294 QLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVA 1373
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA 1307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1374 QWRSKYETDAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDlmtdvERANSLAANLDKKQRNF 1453
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-----AEAAEKKKEEAKKKADA 1382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1454 DKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKA 1533
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEA 1462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1534 KKTVEtEKSEIQAALEEAEGTLEHEESKilrVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQRviDSMQSTLDAEVRSRN 1613
Cdd:PTZ00121 1463 KKKAE-EAKKADEAKKKAEEAKKADEAK---KKAEEAKKKADEAKKAAEAKKKADEAKKAEEA--KKADEAKKAEEAKKA 1536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1614 DALRV---KKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLhlddAVRGQEDMKEQVAMVERRNGLMVAEie 1690
Cdd:PTZ00121 1537 DEAKKaeeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE----AKKAEEARIEEVMKLYEEEKKMKAE-- 1610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1691 ELRAALEQTERSRKV--AEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAEDkAKKAITDAAM 1768
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE-AKKAEEDEKK 1689
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1769 MAEELKKEQDTSAHLERMKKNLEVTVKdlqhrldEAENLamkggKKQLQKLEQRVRELETEVEGEQKRGADAVKgvrkye 1848
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEKK-------KAEEL-----KKAEEENKIKAEEAKKEAEEDKKKAEEAKK------ 1751
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1316056572 1849 rrvkeltyqTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAE 1890
Cdd:PTZ00121 1752 ---------DEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
844-1519 |
7.61e-17 |
|
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: 87.15 E-value: 7.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 844 LKSAETEKELQNMKENYEKMQSDLTTALAkkkeleekmvsllqekndlqlqvaseveNLSDAEERCEGLIKSKIQLEAKL 923
Cdd:pfam01576 419 ARLSESERQRAELAEKLSKLQSELESVSS----------------------------LLNEAEGKNIKLSKDVSSLESQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 924 KETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKAL 1003
Cdd:pfam01576 471 QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1004 QEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLegDLKLAQESIMDLEN--DKQQSD 1081
Cdd:pfam01576 551 QRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKF--DQMLAEEKAISARYaeERDRAE 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1082 EKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGAT 1161
Cdd:pfam01576 629 AEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDEL 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1162 AAQIEMNKKREAEFQKLR----RDLEESTLQHEATAAALRKKQADSVAELGE---QIDNLQRVKQKLEkeksefkMEIDD 1234
Cdd:pfam01576 709 QATEDAKLRLEVNMQALKaqfeRDLQARDEQGEEKRRQLVKQVRELEAELEDerkQRAQAVAAKKKLE-------LDLKE 781
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1235 LSSNMEAVAKAKGNLEKMCRTLEDQLSEIKskndenvRQLNDINAQKARLQTENGEFARQLEEKEALVSQLT-------R 1307
Cdd:pfam01576 782 LEAQIDAANKGREEAVKQLKKLQAQMKDLQ-------RELEEARASRDEILAQSKESEKKLKNLEAELLQLQedlaaseR 854
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1308 GKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKY--ETDAIQ 1385
Cdd:pfam01576 855 ARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELaaERSTSQ 934
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1386 RTE----ELEEAKKKLAQRLQEAEESIEA-VNSKCASLEKTKQRLQGEVEdlmtdVERANSLAANldKKQRNFDKVLAEW 1460
Cdd:pfam01576 935 KSEsarqQLERQNKELKAKLQEMEGTVKSkFKSSIAALEAKIAQLEEQLE-----QESRERQAAN--KLVRRTEKKLKEV 1007
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1316056572 1461 KQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQ 1519
Cdd:pfam01576 1008 LLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATES 1066
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
920-1276 |
1.17e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 86.65 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 920 EAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKE 999
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1000 KKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDK-- 1077
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaa 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1078 -----QQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISE 1152
Cdd:TIGR02168 836 terrlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1153 RLEEAGGATAA----QIEMNKKREAEFQKLR---RDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEK 1225
Cdd:TIGR02168 916 ELEELREKLAQlelrLEGLEVRIDNLQERLSeeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEY 995
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1316056572 1226 SEFKMEIDDLSSNMEAVAKAKGNLEKmcrTLEDQLSEIKSKNDENVRQLND 1276
Cdd:TIGR02168 996 EELKERYDFLTAQKEDLTEAKETLEE---AIEEIDREARERFKDTFDQVNE 1043
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1055-1827 |
2.13e-16 |
|
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: 85.94 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1055 AKRKLEGDLKLAQESIMDLENDKQQSDEKIKKKDFEISQllSKIEdeqslgaqLQKKIKELQARIEELEEEIEAERAARA 1134
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQ--SVID--------LQTKLQEMQMERDAMADIRRRESQSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1135 KVEKQRADLSRELEEISERLEEAGGATAAQIEMNKK----REAEFQKLRR---DLEE------------STLQHEATAAA 1195
Cdd:pfam15921 142 DLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKmmlsHEGVLQEIRSilvDFEEasgkkiyehdsmSTMHFRSLGSA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1196 LRKKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDLssnmeaVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLN 1275
Cdd:pfam15921 222 ISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELL------LQQHQDRIEQLISEHEVEITGLTEKASSARSQAN 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1276 DINAQKARLQ----TENGEFARQLEEKEALVSQLT----RGKQAFTQQIEELKRHIeeeVKAKNALAHAVQSarhdcdll 1347
Cdd:pfam15921 296 SIQSQLEIIQeqarNQNSMYMRQLSDLESTVSQLRselrEAKRMYEDKIEELEKQL---VLANSELTEARTE-------- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1348 REQFEEE--------QEAKAELQRGMSKANSEVAQWRSKYETDA-------------------IQRTEELEEAKKKLAQ- 1399
Cdd:pfam15921 365 RDQFSQEsgnlddqlQKLLADLHKREKELSLEKEQNKRLWDRDTgnsitidhlrrelddrnmeVQRLEALLKAMKSECQg 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1400 -------RLQEAEESIEAVNSKCASLEKTKQRLQGEVEDL------MTDVERANS-LAANLDKKQRNFDKVLAEWKQKYE 1465
Cdd:pfam15921 445 qmerqmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakkmtLESSERTVSdLTASLQEKERAIEATNAEITKLRS 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1466 ESQAELEgaqkEARSLSTELFKMKNSYEEALDQLETMKRENKN---LQQEISDLTEQIGETGKSIHELEKAKKTVETEKS 1542
Cdd:pfam15921 525 RVDLKLQ----ELQHLKNEGDHLRNVQTECEALKLQMAEKDKVieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIN 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1543 EIQAALEEAEGTLEHEESKILRVQ-----LELNQVK-----SEIDRKLAEKDEEMEQI---KRNSQRVIDSMqsTLDAEV 1609
Cdd:pfam15921 601 DRRLELQEFKILKDKKDAKIRELEarvsdLELEKVKlvnagSERLRAVKDIKQERDQLlneVKTSRNELNSL--SEDYEV 678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1610 RSRNdaLRVK-KKMEGDLNEMEIQLshanrqaaeaqkqlrnvqgqlKDAQlhlddavrgqedmkeqvamverrnglmvAE 1688
Cdd:pfam15921 679 LKRN--FRNKsEEMETTTNKLKMQL---------------------KSAQ----------------------------SE 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1689 IEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAM 1768
Cdd:pfam15921 708 LEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNK 787
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316056572 1769 MAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQ-KLEQR--VRELE 1827
Cdd:pfam15921 788 MAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRlKLQHTldVKELQ 849
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
874-1428 |
4.11e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 84.71 E-value: 4.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 874 KKELEEKmvsllqEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTakkrkledecsE 953
Cdd:PRK02224 193 KAQIEEK------EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE-----------T 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 954 LKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKE---KKALQEAHQQTLDDLQAEEDKV-NTLTKAKT 1029
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglDDADAEAVEARREELEDRDEELrDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1030 KLEQQVDDLEGSLEQEKKLRmdlERAKRKlegdlklaQESIMDLENDKQQSDEKIKKKDFEISQLLSKIEDeqslgaqLQ 1109
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLE---ERAEEL--------REEAAELESELEEAREAVEDRREEIEELEEEIEE-------LR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1110 KKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAA--------------QIEMNKKREAEF 1175
Cdd:PRK02224 398 ERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1176 QKLRRDLEESTLQHEATAAALrkKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRT 1255
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERL--ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1256 LEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFAR------QLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKA 1329
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaAIADAEDEIERLREKREALAELNDERRERLAEKRER 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1330 KNALAHAVQSARhdcdllreqFEEEQEAKAELQRGMSKANSEVAQWRSkyETDAIQRT--------EELEEAKKKLAQrL 1401
Cdd:PRK02224 636 KRELEAEFDEAR---------IEEAREDKERAEEYLEQVEEKLDELRE--ERDDLQAEigavenelEELEELRERREA-L 703
|
570 580
....*....|....*....|....*..
gi 1316056572 1402 QEAEESIEAVNSKCASLEKTKQRLQGE 1428
Cdd:PRK02224 704 ENRVEALEALYDEAEELESMYGDLRAE 730
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
845-1862 |
6.05e-16 |
|
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: 84.33 E-value: 6.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 845 KSAETEKELQNMKENYEKMQSDLTTALAKKKELE-EKMVSLLQEkndlqlqvaSEVENLSDAEERCEGLIKSKIQLEAKL 923
Cdd:TIGR00606 201 KVQEHQMELKYLKQYKEKACEIRDQITSKEAQLEsSREIVKSYE---------NELDPLKNRLKEIEHNLSKIMKLDNEI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 924 KETTERLEDEEEINAELTAKKRKLEDECSELKKDIDdleltlakvekekHATENKVKNLTEEMATQDEAIAKLTKEKKAL 1003
Cdd:TIGR00606 272 KALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNHQRTVREKERELVDCQRELEKLNKERRLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1004 QEAH-----QQTLDDLQAEEDKVNTLTKAKTKLEQQ----VDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLE 1074
Cdd:TIGR00606 339 NQEKtellvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1075 NDKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEiserl 1154
Cdd:TIGR00606 419 SKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKN----- 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1155 eeaggataAQIEMNKKREAEFQKLRRDLEEStlqheataaalRKKQADSVAELGEQIDNLQRVkQKLEKEKSEFKMEIDD 1234
Cdd:TIGR00606 494 --------SLTETLKKEVKSLQNEKADLDRK-----------LRKLDQEMEQLNHHTTTRTQM-EMLTKDKMDKDEQIRK 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1235 LSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTR------G 1308
Cdd:TIGR00606 554 IKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcG 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1309 KQAFTQQIEELKRHIEEEVKAKNALAHAvqSARHDcDLLREQFEEEQEAKAELQRgmskansevaqwrskyetdAIQRTE 1388
Cdd:TIGR00606 634 SQDEESDLERLKEEIEKSSKQRAMLAGA--TAVYS-QFITQLTDENQSCCPVCQR-------------------VFQTEA 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1389 ELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQ 1468
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1469 AELE---GAQKEARSLSTELFKMKNSYEEaldqletMKRENKNLQQEISDLteQIGETGKSIHELEKAKKTVETEKSEIQ 1545
Cdd:TIGR00606 772 TLLGtimPEEESAKVCLTDVTIMERFQME-------LKDVERKIAQQAAKL--QGSDLDRTVQQVNQEKQEKQHELDTVV 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1546 AALEEAEGTLEHEESKILRVQLELNQVKSEiDRKLAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALRVKKKMEGD 1625
Cdd:TIGR00606 843 SKIELNRKLIQDQQEQIQHLKSKTNELKSE-KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKD 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1626 LNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMKEQVAMVERRNglmvaeIEELRAALEQTERSRKv 1705
Cdd:TIGR00606 922 QQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETE------LNTVNAQLEECEKHQE- 994
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1706 aeqelvdaservgllhsqnssllntkkKLETDLVQVQGEVDDAVQEarnaedkakkaitdaammaEELKKEQDTSAHLER 1785
Cdd:TIGR00606 995 ---------------------------KINEDMRLMRQDIDTQKIQ-------------------ERWLQDNLTLRKREN 1028
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 1786 MKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLEQRVRELETEVEGEQKRGADAVKgvrKYERRVKELTYQTEEDK 1862
Cdd:TIGR00606 1029 ELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIK---HFKKELREPQFRDAEEK 1102
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
839-1606 |
8.99e-16 |
|
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: 83.63 E-value: 8.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 839 KIKPLLKSAETEKELQNMKENYEKMQS-DLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVEN---------------L 902
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRQSViDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNtvheleaakclkedmL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 903 SDAEERCEGLIKSKIQLEAKLKETTERLEDEEEinaeltAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNL 982
Cdd:pfam15921 166 EDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEE------ASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 983 TEEMATQDEAIAKLTKEK-KALQEAHQQTLDDLQAE-EDKVNTLTKAKTKLEQQVDDLEGSLEqekklrMDLERAKRklE 1060
Cdd:pfam15921 240 IFPVEDQLEALKSESQNKiELLLQQHQDRIEQLISEhEVEITGLTEKASSARSQANSIQSQLE------IIQEQARN--Q 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1061 GDLKLAQESimDLENdkqqsdekikkkdfEISQLLSKIEDEQSLgaqLQKKIKELQARIEELEEEIEAERAARAKVEKQR 1140
Cdd:pfam15921 312 NSMYMRQLS--DLES--------------TVSQLRSELREAKRM---YEDKIEELEKQLVLANSELTEARTERDQFSQES 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1141 ADLSRELEEISERLEEAGGATAAQIEMNKK-------REAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDN 1213
Cdd:pfam15921 373 GNLDDQLQKLLADLHKREKELSLEKEQNKRlwdrdtgNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1214 LQRVKQKLEKeksefkmeIDDLSSNMEAVakakgnlEKMCRTLEDQLSEIKSKNDENVRQLNDINAQkarLQtengEFAR 1293
Cdd:pfam15921 453 IQGKNESLEK--------VSSLTAQLEST-------KEMLRKVVEELTAKKMTLESSERTVSDLTAS---LQ----EKER 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1294 QLEEKEALVSQLTRGKQAFTQQIEELK------RHIEEEVKAKNalahaVQSARHD--CDLLREQFEEEQEAKAELQRGM 1365
Cdd:pfam15921 511 AIEATNAEITKLRSRVDLKLQELQHLKnegdhlRNVQTECEALK-----LQMAEKDkvIEILRQQIENMTQLVGQHGRTA 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1366 SKANSEVAQwrskYETDAIQRTEELEEAK----------KKLAQRLQEAE-ESIEAVNSKCASLEKTKQrLQGEVEDLMT 1434
Cdd:pfam15921 586 GAMQVEKAQ----LEKEINDRRLELQEFKilkdkkdakiRELEARVSDLElEKVKLVNAGSERLRAVKD-IKQERDQLLN 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1435 DVERA----NSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEAL-------DQLETMK 1503
Cdd:pfam15921 661 EVKTSrnelNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMkvamgmqKQITAKR 740
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1504 RENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEK 1583
Cdd:pfam15921 741 GQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQF 820
|
810 820
....*....|....*....|....
gi 1316056572 1584 DEEMEQIKRNSQRVID-SMQSTLD 1606
Cdd:pfam15921 821 AECQDIIQRQEQESVRlKLQHTLD 844
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1304-1911 |
9.95e-16 |
|
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: 83.63 E-value: 9.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1304 QLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVaqwrskyeTDA 1383
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL--------RNQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1384 IQRT-EELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQrlqgEVEDLMTDVERANSlaanldkkqrnfdkvlaewKQ 1462
Cdd:pfam15921 147 LQNTvHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ----EIRSILVDFEEASG-------------------KK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1463 KYEESQAEL-------EGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKN-----LQQEISDLTEQIGETGKSIHEL 1530
Cdd:pfam15921 204 IYEHDSMSTmhfrslgSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHEVEITGL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1531 EKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQLEL----NQVKSEI---------------------DRKLAEKDE 1585
Cdd:pfam15921 284 TEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLestvSQLRSELreakrmyedkieelekqlvlaNSELTEART 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1586 EMEQIKRNSQRVIDSMQSTLdAEVRSRNDALRVKKKMEGDLNEME----IQLSHANRQAAEAQKQLRNVQGQLKDaqlhL 1661
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLL-ADLHKREKELSLEKEQNKRLWDRDtgnsITIDHLRRELDDRNMEVQRLEALLKA----M 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1662 DDAVRGQedMKEQVAMVERRNGLMvAEIEELRAALEQT-ERSRKVAEQ-----ELVDASERVglLHSQNSSLLNTKKKLE 1735
Cdd:pfam15921 439 KSECQGQ--MERQMAAIQGKNESL-EKVSSLTAQLESTkEMLRKVVEEltakkMTLESSERT--VSDLTASLQEKERAIE 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1736 ---TDLVQVQGEVDDAVQEA---RNAEDKAKKAITDAA----MMAEELKKEQDTSAHLERM-----------------KK 1788
Cdd:pfam15921 514 atnAEITKLRSRVDLKLQELqhlKNEGDHLRNVQTECEalklQMAEKDKVIEILRQQIENMtqlvgqhgrtagamqveKA 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1789 NLEVTVKDLQHRLDEAENLAMKGGKKqLQKLEQRVRELETEVEGEQKRGADAVKGVRKYERRVKELTyqtEEDKKNITRL 1868
Cdd:pfam15921 594 QLEKEINDRRLELQEFKILKDKKDAK-IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLL---NEVKTSRNEL 669
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1316056572 1869 QDLVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEEAQ 1911
Cdd:pfam15921 670 NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTR 712
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
850-1542 |
1.26e-15 |
|
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: 82.76 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 850 EKELQNMKENYEKMQSDLttalaKKKELEEKmvsllqeknDLQLQVASEVENLSDAEERCEGLIKSKIQLEAKLKETTER 929
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNEL-----KNKEKELK---------NLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 930 LE----DEEEINAELTAKKR---KLEDECSELKKDIDdleltlaKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKA 1002
Cdd:TIGR04523 98 INklnsDLSKINSEIKNDKEqknKLEVELNKLEKQKK-------ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1003 LQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLErakrKLEGDLKLAQESIMDLENDKQQSDE 1082
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQIS----ELKKQNNQLKDNIEKKQQEINEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1083 KIKKKDFEISQLLSKIEDEQSlgaQLQKKIKELQarieeleeeieaeraaraKVEKQRADLSRELEEISERLEeaggata 1162
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKK---QLSEKQKELE------------------QNNKKIKELEKQLNQLKSEIS------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1163 aqiEMNKKREAEFQK-LRRDLEESTLQHEATAAALRKKQaDSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEA 1241
Cdd:TIGR04523 299 ---DLNNQKEQDWNKeLKSELKNQEKKLEEIQNQISQNN-KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1242 VAKAKG-------NLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQ 1314
Cdd:TIGR04523 375 LKKENQsykqeikNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1315 QIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYETdAIQRTEELEEAK 1394
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS-LKEKIEKLESEK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1395 KKLAQRLQEAEESIEAVNS--KCASLEKTKQRLQGEVEDL---MTDVERANS----LAANLDKKQRNFDKVLAEWKQKYE 1465
Cdd:TIGR04523 534 KEKESKISDLEDELNKDDFelKKENLEKEIDEKNKEIEELkqtQKSLKKKQEekqeLIDQKEKEKKDLIKEIEEKEKKIS 613
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 1466 ESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKS 1542
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELS 690
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
841-1682 |
3.02e-15 |
|
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: 81.94 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 841 KPLLKSAETEKELQNMKENYEKmqSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLE 920
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKL--QELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 921 AKLKETTER----LEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKL 996
Cdd:pfam02463 254 ESSKQEIEKeeekLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 997 TKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEgDLKLAQESIMDLEND 1076
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL-ELKSEEEKEAQLLLE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1077 KQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEE 1156
Cdd:pfam02463 413 LARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1157 AGGATAAQIEMNKKREAEFQKLRRDLEEStLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDLS 1236
Cdd:pfam02463 493 QKLEERSQKESKARSGLKVLLALIKDGVG-GRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1237 SNMEAVAKAKGNLEKmcrtleDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQI 1316
Cdd:pfam02463 572 ELPLGARKLRLLIPK------LKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1317 EELKR-----HIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEvaQWRSKYETDAIQRTEELE 1391
Cdd:pfam02463 646 SGLRKgvsleEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKE--QREKEELKKLKLEAEELL 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1392 EAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEvEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAEL 1471
Cdd:pfam02463 724 ADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKE-EKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1472 EGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEA 1551
Cdd:pfam02463 803 LRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1552 EGTLE----HEESKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALRVKKKMEGDLN 1627
Cdd:pfam02463 883 KLKDEleskEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERN 962
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1316056572 1628 E-MEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMKEQVAMVERRN 1682
Cdd:pfam02463 963 KrLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQR 1018
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
910-1630 |
4.31e-15 |
|
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: 81.31 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 910 EGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQ 989
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 990 DEAIAKLTKEKkalqEAHQQTLDDLQaeedkvNTLTKAKTKLEQqvddlegsleqekkLRMDLERAKRKLEGDLKLAQES 1069
Cdd:pfam05483 168 AEKTKKYEYER----EETRQVYMDLN------NNIEKMILAFEE--------------LRVQAENARLEMHFKLKEDHEK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1070 IMDLENDKQQsdeKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEE 1149
Cdd:pfam05483 224 IQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1150 ISERLEEAggataaqIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADS---VAELGEQIDNLQRV----KQKLE 1222
Cdd:pfam05483 301 IKMSLQRS-------MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHsfvVTEFEATTCSLEELlrteQQRLE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1223 KEKSEFK---MEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENvRQLNDInAQKARLQTENGEFARQLEEK- 1298
Cdd:pfam05483 374 KNEDQLKiitMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEK-KQFEKI-AEELKGKEQELIFLLQAREKe 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1299 ----EALVSQLTRGKQAFTQQIEELKRHIEEEvKAKNALAHAvqsarhDCDLLREQFEEEQEAKAELQRGMSKANSEVAQ 1374
Cdd:pfam05483 452 ihdlEIQLTAIKTSEEHYLKEVEDLKTELEKE-KLKNIELTA------HCDKLLLENKELTQEASDMTLELKKHQEDIIN 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1375 WRsKYETDAIQRTEELEEAKKKLAQRLQEAEESI----EAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQ 1450
Cdd:pfam05483 525 CK-KQEERMLKQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1451 RNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMkreNKNLQQEISDltEQIGETgKSIHEL 1530
Cdd:pfam05483 604 ENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEI---IDNYQKEIED--KKISEE-KLLEEV 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1531 EKAKKTVEtEKSEIQaalEEAEGTLEHeesKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQRViDSMQSTLDAEVR 1610
Cdd:pfam05483 678 EKAKAIAD-EAVKLQ---KEIDKRCQH---KIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQ-SSAKAALEIELS 749
|
730 740
....*....|....*....|.
gi 1316056572 1611 S-RNDALRVKKKMEGDLNEME 1630
Cdd:pfam05483 750 NiKAELLSLKKQLEIEKEEKE 770
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
845-1456 |
4.91e-15 |
|
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: 81.26 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 845 KSAETEKELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQL----- 919
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqqeie 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 920 -------EAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKV---KNLTEEMATQ 989
Cdd:TIGR02168 425 ellkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslERLQENLEGF 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 990 DEAIAKLTKEKK-------------------------ALQEAHQQTL-DDLQAEEDKVNTLTKAKT-------------- 1029
Cdd:TIGR02168 505 SEGVKALLKNQSglsgilgvlselisvdegyeaaieaALGGRLQAVVvENLNAAKKAIAFLKQNELgrvtflpldsikgt 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1030 --------KLEQQ------------------------------VDDLEGSLEQEKKLRMDL------------------E 1053
Cdd:TIGR02168 585 eiqgndreILKNIegflgvakdlvkfdpklrkalsyllggvlvVDDLDNALELAKKLRPGYrivtldgdlvrpggvitgG 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1054 RAKRKLeGDLKLAQEsIMDLENDKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAAR 1133
Cdd:TIGR02168 665 SAKTNS-SILERRRE-IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1134 AKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQAdsvaELGEQIDN 1213
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA----ELTLLNEE 818
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1214 LQRVKQK---LEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGE 1290
Cdd:TIGR02168 819 AANLRERlesLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1291 FARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEeevKAKNALAHAVQSarhdcdlLREQFEEEQEAKAELqrgMSKANS 1370
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLE---GLEVRIDNLQER-------LSEEYSLTLEEAEAL---ENKIED 965
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1371 EVAQWRskyetdaiQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANL---- 1446
Cdd:TIGR02168 966 DEEEAR--------RRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERfkdt 1037
|
730
....*....|.
gi 1316056572 1447 -DKKQRNFDKV 1456
Cdd:TIGR02168 1038 fDQVNENFQRV 1048
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1314-1899 |
7.45e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 80.73 E-value: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1314 QQIEELKRHIEEEVKAKNALAHAVQSARH--DCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYETDAIqrtEELE 1391
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL---EELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1392 EAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGE-VEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAE 1470
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1471 LEGAQKEARSLSTELFKMKNSYEEALDQLETMKREnknLQQEISDLTEQIgetgksiHELEKAKKTVETEKSEIQAALEE 1550
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEI-------ASLERRKSNIPARLLALRDALAE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1551 AEGTLEHEeskiLRVQLELNQVKSE-------IDRKL---------AEKDEE--MEQIKRNSQR---VIDSMQSTLDAEV 1609
Cdd:COG4913 452 ALGLDEAE----LPFVGELIEVRPEeerwrgaIERVLggfaltllvPPEHYAaaLRWVNRLHLRgrlVYERVRTGLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1610 RSRNDALRVKKKMEGDLN------EMEIQlSHANRQAAEAQKQLRN------VQGQLKDaqlhldDAVRGQEDMKEQVam 1677
Cdd:COG4913 528 RPRLDPDSLAGKLDFKPHpfrawlEAELG-RRFDYVCVDSPEELRRhpraitRAGQVKG------NGTRHEKDDRRRI-- 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1678 veRRNGLM----VAEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDLvqvqgEVDDAVQEAR 1753
Cdd:COG4913 599 --RSRYVLgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1754 NAEDKAkkaitdaammaEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAenlamkggKKQLQKLEQRVRELETEVEGE 1833
Cdd:COG4913 672 ELEAEL-----------ERLDASSDDLAALEEQLEELEAELEELEEELDEL--------KGEIGRLEKELEQAEEELDEL 732
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316056572 1834 QKRGADAVKGVRKYERRVKELTYQTEEDKKnitRLQDLVDKLQLKVKAYKRQAEEAEEQANSHMSR 1899
Cdd:COG4913 733 QDRLEAAEDLARLELRALLEERFAAALGDA---VERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1037-1650 |
8.39e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 80.73 E-value: 8.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1037 DLEGSLEQEKKLRMDLERAKRKLEgdlkLAQESIMDLEndkqqsdeKIKKKDFEISQLLSKIEDEQSLGAQL-----QKK 1111
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALE----DAREQIELLE--------PIRELAERYAAARERLAELEYLRAALrlwfaQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1112 IKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIE-----MNKKRE------AEFQKLRR 1180
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEreierLERELEererrrARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1181 DLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQL 1260
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1261 SEIKSKNDENVR---QLNDINAQKARLQT--EN--GEFARQL---EEKEALVSQL---TRGKQAF-TQQIEELKRHIEEE 1326
Cdd:COG4913 450 AEALGLDEAELPfvgELIEVRPEEERWRGaiERvlGGFALTLlvpPEHYAAALRWvnrLHLRGRLvYERVRTGLPDPERP 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1327 VKAKNALAHAVQSARHDC-----DLLREQF-------EEE--QEAKAELQRGMSKANSEVAQ------WRSKYET--DAI 1384
Cdd:COG4913 530 RLDPDSLAGKLDFKPHPFrawleAELGRRFdyvcvdsPEElrRHPRAITRAGQVKGNGTRHEkddrrrIRSRYVLgfDNR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1385 QRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEdlmtdveranslaanldkkqrnfdkvlaewkqkY 1464
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE---------------------------------Y 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1465 EESQAELEGAQKEARSLSTELFKMknsyEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEI 1544
Cdd:COG4913 657 SWDEIDVASAEREIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1545 QAALEEAEGTLEHEESKIL---RVQLELNQVKSEIDRKLAEK-DEEMEQIKRNSQRVIDSMQ----------STLDAEVR 1610
Cdd:COG4913 733 QDRLEAAEDLARLELRALLeerFAAALGDAVERELRENLEERiDALRARLNRAEEELERAMRafnrewpaetADLDADLE 812
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 1611 SRNDALRVKKKMEGD------------LNEMEIQ-----LSHANRQAAEAQKQLRNV 1650
Cdd:COG4913 813 SLPEYLALLDRLEEDglpeyeerfkelLNENSIEfvadlLSKLRRAIREIKERIDPL 869
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
897-1538 |
1.33e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.72 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 897 SEVENLSDAEERCEGLIKSKIQ-LEAKLKETTERLEDEEEINAELtAKKRKLEDECSELKKDIDDLELTLAKVEKEKHAT 975
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKeLEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 976 ENKVKNLTEEMATQDEAIAKLTKEKKALQEahqqtlddLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEqekklrmdlera 1055
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELKE--------LKEKAEEYIKLSEFYEEYLDELREIEKRLS------------ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1056 krKLEGDLKLAQESIMDLENDKQQSdEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAK 1135
Cdd:PRK03918 318 --RLEEEINGIEERIKELEEKEERL-EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1136 -VEKQRADLSRELEEISER---LEEAGGATAAQIEMNKKREAEFQKLRRDLEEstlQHEataaalrkkqADSVAELGEQI 1211
Cdd:PRK03918 395 eLEKAKEEIEEEISKITARigeLKKEIKELKKAIEELKKAKGKCPVCGRELTE---EHR----------KELLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1212 DNLQRVKQKLEKEKSEFKMEIDDLssnmEAVAKAKGNLEKMcRTLEDQLSEIKSKndenvrqLNDINAQKARlqtENGEF 1291
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELREL----EKVLKKESELIKL-KELAEQLKELEEK-------LKKYNLEELE---KKAEE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1292 ARQLEEKEALVSqltrgkqaftQQIEELKRHIEEEVKAKNALAhavqsarhdcdLLREQFEEEQEAKAELQRgmskansE 1371
Cdd:PRK03918 527 YEKLKEKLIKLK----------GEIKSLKKELEKLEELKKKLA-----------ELEKKLDELEEELAELLK-------E 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1372 VAQWRSKYETDAIQRTEELEEAKKKLaqrlqeaeesIEAVNSkcaslEKTKQRLQGEVEDLMTDVERANSLAANLDKKQR 1451
Cdd:PRK03918 579 LEELGFESVEELEERLKELEPFYNEY----------LELKDA-----EKELEREEKELKKLEEELDKAFEELAETEKRLE 643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1452 NFDKVLAEWKQKYeeSQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEIsdltEQIGETGKSIHELE 1531
Cdd:PRK03918 644 ELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL----EEREKAKKELEKLE 717
|
....*..
gi 1316056572 1532 KAKKTVE 1538
Cdd:PRK03918 718 KALERVE 724
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1313-1929 |
1.47e-14 |
|
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: 79.83 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1313 TQQIEELKRHIEEEVKAKNALAHAvQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYETdaiqRTEELEE 1392
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKA-ESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAA----RKQELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1393 AKKKLAQRLQEAEEsieavnsKCASLEKTKQRLQGEVEDLMTDVERANSLAANLdkkqrNFDKVLAEWK-QKYEESQAEL 1471
Cdd:pfam01576 76 ILHELESRLEEEEE-------RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKL-----QLEKVTTEAKiKKLEEDILLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1472 EGA----QKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAA 1547
Cdd:pfam01576 144 EDQnsklSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1548 LEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEMEQIkRNSQRVIDSMQSTLDAEVRSRNDALRVKKKMEGDLN 1627
Cdd:pfam01576 224 IAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI-RELEAQISELQEDLESERAARNKAEKQRRDLGEELE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1628 EMEIQLSHANRQAAeAQKQLRNVQGQ-LKDAQLHLDDAVRGQEdmkEQVAMVERRNGlmvAEIEELRAALEQT------- 1699
Cdd:pfam01576 303 ALKTELEDTLDTTA-AQQELRSKREQeVTELKKALEEETRSHE---AQLQEMRQKHT---QALEELTEQLEQAkrnkanl 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1700 ERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDT 1779
Cdd:pfam01576 376 EKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1780 SAHLERMKKNLEVTVKDLQHRLDEAenlamkggKKQLQKLEQRVRELETEVEGEQKRGADAVKGVRKYERRVK------- 1852
Cdd:pfam01576 456 NIKLSKDVSSLESQLQDTQELLQEE--------TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLStlqaqls 527
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 1853 ELTYQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEEAQERADIAESQVNKLRAKSR 1929
Cdd:pfam01576 528 DMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQK 604
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
966-1442 |
3.73e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.16 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 966 AKVEKEKHAT----ENKVKNLTEEMATQDE--AIAKLTKEKKALQ-EAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDL 1038
Cdd:PRK02224 198 EKEEKDLHERlnglESELAELDEEIERYEEqrEQARETRDEADEVlEEHEERREELETLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1039 EGSLEQEKKLRMDLERAKRKLEGDLKL-------AQESIMDLENDKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKK 1111
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1112 IKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEA 1191
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1192 TAAALRKKQ--------------------ADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEK 1251
Cdd:PRK02224 438 ARERVEEAEalleagkcpecgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1252 McRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKN 1331
Cdd:PRK02224 518 R-EDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRT 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1332 ALAhAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYETDAIqrteelEEAKkklaQRLQEAEESIEAV 1411
Cdd:PRK02224 597 LLA-AIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARI------EEAR----EDKERAEEYLEQV 665
|
490 500 510
....*....|....*....|....*....|.
gi 1316056572 1412 NSKCASLEKTKQRLQGEVEDLMTDVERANSL 1442
Cdd:PRK02224 666 EEKLDELREERDDLQAEIGAVENELEELEEL 696
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
839-1515 |
7.98e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.49 E-value: 7.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 839 KIKPLLKSAETEKELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDlqlqvasevenlsdaeerceglikskiq 918
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD---------------------------- 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 919 lEAKLKETTERLEDEEEINAELTAKKrkledeCSELKKdiddleltlaKVEKEKHATENKVKnlTEEMATQDEAIAKLTK 998
Cdd:PTZ00121 1382 -AAKKKAEEKKKADEAKKKAEEDKKK------ADELKK----------AAAAKKKADEAKKK--AEEKKKADEAKKKAEE 1442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 999 EKKAlQEAHQqtlddlQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKlrmdLERAKRKLEGDLKLAQESimdlendkq 1078
Cdd:PTZ00121 1443 AKKA-DEAKK------KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK----ADEAKKKAEEAKKKADEA--------- 1502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1079 QSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIeeleeeieaeraarakvEKQRADLSRELEEISERLEEag 1158
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE-----------------EKKKADELKKAEELKKAEEK-- 1563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1159 gataAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEfkmeiddlssn 1238
Cdd:PTZ00121 1564 ----KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA----------- 1628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1239 mEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDInAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEE 1318
Cdd:PTZ00121 1629 -EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE-AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1319 LKRHIEEEVKAKNALAHAVQSARHDCDLLREQfEEEQEAKAELQRGMSKANSEVAQWRSKYETDAIQRTEEL-----EEA 1393
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeavieEEL 1785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1394 KKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAewKQKYEESQAELEG 1473
Cdd:PTZ00121 1786 DEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFE--KHKFNKNNENGED 1863
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1316056572 1474 AQKEARSlSTELFKMKNSYEEALDQLETMKRENKNLQQEISD 1515
Cdd:PTZ00121 1864 GNKEADF-NKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
894-1492 |
1.13e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.88 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 894 QVASEVENLSDAEERCEglikskiqleaKLKETTERLEDEEEINAELTAKKRKLEdecselKKDIDDLELTLAKVEKEKH 973
Cdd:COG4913 229 ALVEHFDDLERAHEALE-----------DAREQIELLEPIRELAERYAAARERLA------ELEYLRAALRLWFAQRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 974 ATENKVKNLTEEMATQDEAIAKLTKEKKALQEahqqTLDDLQAEEDKVNTltKAKTKLEQQVDDLEGSLEQEKKLRMDLE 1053
Cdd:COG4913 292 LLEAELEELRAELARLEAELERLEARLDALRE----ELDELEAQIRGNGG--DRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1054 RAKRKL-------EGDLKLAQESIMDLENDKQQSDEKIKKKDFEISQLLSKIEDEQslgAQLQKKIKELqarieeleeei 1126
Cdd:COG4913 366 ALLAALglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL---RELEAEIASL----------- 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1127 eaeraarakvEKQRADLSRELEEISERLEEAGGATAAQ-------IEMnKKREAEFQK--------LRRDL--EEstlQH 1189
Cdd:COG4913 432 ----------ERRKSNIPARLLALRDALAEALGLDEAElpfvgelIEV-RPEEERWRGaiervlggFALTLlvPP---EH 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1190 EATAAA------LRKK-QADSVAELGEQIDNLQRVKQ----KLEKEKSEFKMEIDDLSSNMEAVAKakgnlekmCRTLED 1258
Cdd:COG4913 498 YAAALRwvnrlhLRGRlVYERVRTGLPDPERPRLDPDslagKLDFKPHPFRAWLEAELGRRFDYVC--------VDSPEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1259 QLSEIKS-------KNDENVRQLNDINAQKARLQT--ENgefARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKA 1329
Cdd:COG4913 570 LRRHPRAitragqvKGNGTRHEKDDRRRIRSRYVLgfDN---RAKLAALEAELAELEEELAEAEERLEALEAELDALQER 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1330 KNALAHAVQSARHDCDLLREQfEEEQEAKAELQRgMSKANSEVaqwrskyetdaiqrtEELEEAKKKLAQRLQEAEESIE 1409
Cdd:COG4913 647 REALQRLAEYSWDEIDVASAE-REIAELEAELER-LDASSDDL---------------AALEEQLEELEAELEELEEELD 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1410 AVNSKCASLEKTKQRLQGEVEDLMTDVERANSLA-----ANLDKK--QRNFDKVLAEWKQKYEEsqaELEGAQKEARSLS 1482
Cdd:COG4913 710 ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelrALLEERfaAALGDAVERELRENLEE---RIDALRARLNRAE 786
|
650
....*....|
gi 1316056572 1483 TELFKMKNSY 1492
Cdd:COG4913 787 EELERAMRAF 796
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1376-1926 |
1.47e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.26 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1376 RSKYETDAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSL---AANLDKKQRN 1452
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELekeLESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1453 FDKVLAEWKQKYEESQAELEGAQKEARSLsTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEK 1532
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1533 AKKTVE---TEKSEIQAALEEAEGTLEHEEsKILRVQLELNQVKSEID----RKLAEKDEEMEQIKRNSQRVID---SMQ 1602
Cdd:PRK03918 336 KEERLEelkKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTgltpEKLEKELEELEKAKEEIEEEISkitARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1603 STLDAEVRSRNDALRVKKKMEGD--LNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAqlhlddavrgqEDMKEQVAMVER 1680
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEI-----------EEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1681 rnglmvaEIEELRAALEQTERSRKVAEQelvdaservgllhsqnssLLNTKKKLETDLVQvqgEVDDAVQEARNAEDKAK 1760
Cdd:PRK03918 484 -------ELEKVLKKESELIKLKELAEQ------------------LKELEEKLKKYNLE---ELEKKAEEYEKLKEKLI 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1761 KAITDAAMMAEELKKEQDtsahLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLEQRVRELEtEVEGEQKRGADA 1840
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDA 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1841 VKGVRKYERRVKELTYQTEEDKKNITRLQDLVDKLQLKVKAYKRQ--AEEAEEQANSHM---SRLRKVQHEMEEAQERAD 1915
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEELREEYLelsRELAGLRAELEELEKRRE 690
|
570
....*....|.
gi 1316056572 1916 IAESQVNKLRA 1926
Cdd:PRK03918 691 EIKKTLEKLKE 701
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
845-1363 |
1.53e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.23 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 845 KSAETEKELQNMKENYEKMQSDLTTALAKKKELEEKmvslLQEKNDLQlqvaSEVENLSDAEERCEgliKSKIQLEAKLK 924
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEVLEEHEER----REELETLE----AEIEDLRETIAETE---REREELAEEVR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 925 ETTERLEDEEEINAELTAK-------KRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLT 997
Cdd:PRK02224 283 DLRERLEELEEERDDLLAEaglddadAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELR 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 998 KEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKlaqesimDLENDK 1077
Cdd:PRK02224 363 EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA-------ELEATL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1078 QQSDEKIKK--------------KDFEISQLLSKIEDEqslgaqlQKKIKELqarieeleeeieaeraarakvEKQRADL 1143
Cdd:PRK02224 436 RTARERVEEaealleagkcpecgQPVEGSPHVETIEED-------RERVEEL---------------------EAELEDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1144 SRELEEISERLEEAGGATAAQIEMNKKREAefqklRRDLEESTLQHEATAAALRKKQA---DSVAELGEQIDNLQRVKQK 1220
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIERLEER-----REDLEELIAERRETIEEKRERAEelrERAAELEAEAEEKREAAAE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1221 LEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKmcrtLEDQLSEIKSKNDENVR------QLNDINAQKARLQTENGEFARQ 1294
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLER----IRTLLAAIADAEDEIERlrekreALAELNDERRERLAEKRERKRE 638
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316056572 1295 LEEK--EALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQR 1363
Cdd:PRK02224 639 LEAEfdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEA 709
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
928-1831 |
2.33e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 75.78 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 928 ERLEDEEEI-----NAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKA 1002
Cdd:pfam02463 154 RRLEIEEEAagsrlKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1003 LQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDE 1082
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1083 KIKKKDFEISQLLSK-IEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGAT 1161
Cdd:pfam02463 314 EKLKESEKEKKKAEKeLKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1162 AAQIEM--NKKREAEFQKLRRDLEESTLQheataaALRKKQADSVAELGEQIDNLQRvKQKLEKEKSEfkmeiddlssnM 1239
Cdd:pfam02463 394 EEELELksEEEKEAQLLLELARQLEDLLK------EEKKEELEILEEEEESIELKQG-KLTEEKEELE-----------K 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1240 EAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEfarqlEEKEALVSQLTRGKQAFTQQIEEL 1319
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKAR-----SGLKVLLALIKDGVGGRIISAHGR 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1320 KRHIEEEVKAKNALAHAVqsarhdCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYETDAIQRTEELEEAKKKLAQ 1399
Cdd:pfam02463 531 LGDLGVAVENYKVAISTA------VIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1400 RLQEAEESIEAVNSKCASLEKTKQRlqgEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEAR 1479
Cdd:pfam02463 605 LAQLDKATLEADEDDKRAKVVEGIL---KDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQEL 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1480 SLSTELFKMKNsyeEALDQLETMKRENKNLQQEISDLTEQIGETgksiheLEKAKKTVETEKSEIQAALEEAEGTLEHEE 1559
Cdd:pfam02463 682 QEKAESELAKE---EILRRQLEIKKKEQREKEELKKLKLEAEEL------LADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1560 SKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRsRNDALRVKKKMEGDLNEMEIQLSHANRQ 1639
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL-RALEEELKEEAELLEEEQLLIEQEEKIK 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1640 AAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMKEQVAMVERRNGLMVAEIEELRAALEQTERSRKVAEQELVDASERVGL 1719
Cdd:pfam02463 832 EEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL 911
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1720 LHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAItdaamMAEELKKEQDTSAHLERMKKNL----EVTVK 1795
Cdd:pfam02463 912 LEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNK-----EEEEERNKRLLLAKEELGKVNLmaieEFEEK 986
|
890 900 910
....*....|....*....|....*....|....*.
gi 1316056572 1796 DLQHRLDEAENLAMKGGKKQLQKLEQRVRELETEVE 1831
Cdd:pfam02463 987 EERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1347-1924 |
3.09e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.46 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1347 LREQFEEEQEAkaELQRGMSKANSEVAqwrskyETDAIqrTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEktkqRLQ 1426
Cdd:PRK02224 192 LKAQIEEKEEK--DLHERLNGLESELA------ELDEE--IERYEEQREQARETRDEADEVLEEHEERREELE----TLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1427 GEVEDLMTDVERAnslaanlDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELfkmknsyEEALDQLETMKREN 1506
Cdd:PRK02224 258 AEIEDLRETIAET-------EREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADA-------EAVEARREELEDRD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1507 KNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKIlrvqlelnqvkSEIDRKLAEKDEE 1586
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV-----------EDRREEIEELEEE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1587 MEQikrNSQRVIDSMQSTLDAEVRsRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRnvQGQLKDAQLHLDDA-- 1664
Cdd:PRK02224 393 IEE---LRERFGDAPVDLGNAEDF-LEELREERDELREREAELEATLRTARERVEEAEALLE--AGKCPECGQPVEGSph 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1665 VRGQEDMKEQVAMVERRNGLMVAEIEELRAALEQTERSRKVAEQ--ELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQ 1742
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRieRLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1743 GEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDT-SAHLERMKKnLEVTVKDLQHRLDEAENLAMKGG--------- 1812
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAElKERIESLER-IRTLLAAIADAEDEIERLREKREalaelnder 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1813 KKQLQKLEQRVRELETEVEGeqkrgaDAVKGVRkyERRVKELTYQTEEDKKnITRLQDLVDKLQLKVKAYKRQAEEAEE- 1891
Cdd:PRK02224 626 RERLAEKRERKRELEAEFDE------ARIEEAR--EDKERAEEYLEQVEEK-LDELREERDDLQAEIGAVENELEELEEl 696
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1316056572 1892 -----QANSHMSRLRKVQHEMEEAQE-----RADIAESQVNKL 1924
Cdd:PRK02224 697 rerreALENRVEALEALYDEAEELESmygdlRAELRQRNVETL 739
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1626-1927 |
3.80e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1626 LNEMEIQLSHANRQAAEAQK------QLRNVQGQLkdAQLHLDDAVRGQEDMKEQVAMVERRNGLMVAEIEELRAALEQT 1699
Cdd:COG1196 195 LGELERQLEPLERQAEKAERyrelkeELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1700 ERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDT 1779
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1780 SAHLERMKKNLEVTVKDLQHRLDEAENLAmKGGKKQLQKLEQRVRELETEVEGEQKRGADAvkgvrkyERRVKELTYQTE 1859
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEEL-EELAEELLEALRAAAELAAQLEELEEAEEAL-------LERLERLEEELE 424
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316056572 1860 EDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEEAQERADIAESQVNKLRAK 1927
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1202-1806 |
9.65e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.80 E-value: 9.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1202 DSVAELGEQIDNLQRVKQKLEKEKSEFKM--EIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSknDENVRQLNDINA 1279
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQRRL--ELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1280 QKARLQTENGEFARQLEEKEALVSQLTRGKQAF-TQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAK 1358
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1359 AELQRGMSKANSEVAQWRSKYETDAIQRTEELEEAKKKLAQRLQE-----------AEESIEAVNSKCASLEKTKQRLQ- 1426
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiaslerrksniPARLLALRDALAEALGLDEAELPf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1427 -GEVEDLMTD-------VERA-NSLAANLDKKQRNFDKVLaEW-----------KQKYEESQAELEGAQKEARSLSTELF 1486
Cdd:COG4913 463 vGELIEVRPEeerwrgaIERVlGGFALTLLVPPEHYAAAL-RWvnrlhlrgrlvYERVRTGLPDPERPRLDPDSLAGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1487 KMKNSYEEALDQL-------------ETMKRENKNLQQE--ISDLTE--------------QIGETGKS-IHELEKAKKT 1536
Cdd:COG4913 542 FKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRAITRAgqVKGNGTrhekddrrrirsryVLGFDNRAkLAALEAELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1537 VETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEID-----RKLAEKDEEMEQIKRNSqrvidsmqstldaevrs 1611
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaeREIAELEAELERLDASS----------------- 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1612 rndalrvkkkmeGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMKEQV-AMVERRNGLMVAEIE 1690
Cdd:COG4913 685 ------------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLeAAEDLARLELRALLE 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1691 ELRAALEQTERSRKVAEQelvdaservglLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMA 1770
Cdd:COG4913 753 ERFAAALGDAVERELREN-----------LEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALL 821
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1316056572 1771 EELkKEQDTSAHLERMKKNLEVT----VKDLQHRLDEAEN 1806
Cdd:COG4913 822 DRL-EEDGLPEYEERFKELLNENsiefVADLLSKLRRAIR 860
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
845-1704 |
1.18e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 73.84 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 845 KSAETEKELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEkndlqLQVASEVENLSDAEERCEGLIKskiQLEAKLK 924
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQD-----YQAASDHLNLVQTALRQQEKIE---RYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 925 ETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKhatenkvkNLTEEMATQ-DEAIAKLTKEKKAL 1003
Cdd:PRK04863 359 ELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQAL--------DVQQTRAIQyQQAVQALERAKQLC 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1004 QEAH------QQTLDDLQAEEDkvnTLTKAKTKLEQQVDDLEGSLEQ-EKKLR--------MDLERAKRKlegdlklAQE 1068
Cdd:PRK04863 431 GLPDltadnaEDWLEEFQAKEQ---EATEELLSLEQKLSVAQAAHSQfEQAYQlvrkiageVSRSEAWDV-------ARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1069 SIMDLENDKQQSD--EKIKKKDFEISQLLSKIEDEQSLGAQLQKK-IKELQARIEeleeeieaeraarakVEKQRADLSR 1145
Cdd:PRK04863 501 LLRRLREQRHLAEqlQQLRMRLSELEQRLRQQQRAERLLAEFCKRlGKNLDDEDE---------------LEQLQEELEA 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1146 ELEEISERLEEAGgatAAQIEMNKKREaefqklrrDLEESTLQHEATAAALRKKQaDSVAELGEQ----IDNLQRV---- 1217
Cdd:PRK04863 566 RLESLSESVSEAR---ERRMALRQQLE--------QLQARIQRLAARAPAWLAAQ-DALARLREQsgeeFEDSQDVteym 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1218 KQKLEKEKsEFKMEIDDLSSNMEAV--------AKAKGNLEKMcRTLEDQ-----LSEI-----------------KSKN 1267
Cdd:PRK04863 634 QQLLERER-ELTVERDELAARKQALdeeierlsQPGGSEDPRL-NALAERfggvlLSEIyddvsledapyfsalygPARH 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1268 DENVRQLNDINAQKARL---------------QTENGEFARQLEEKEALVSQLTR-------------GKQAFTQQIEEL 1319
Cdd:PRK04863 712 AIVVPDLSDAAEQLAGLedcpedlyliegdpdSFDDSVFSVEELEKAVVVKIADRqwrysrfpevplfGRAAREKRIEQL 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1320 KRHIEEEVKAKNALAHAVQsarhDCDLLREQFE-------------EEQEAKAELQRGMSKANSEVAQwrskyetdaiqr 1386
Cdd:PRK04863 792 RAEREELAERYATLSFDVQ----KLQRLHQAFSrfigshlavafeaDPEAELRQLNRRRVELERALAD------------ 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1387 teeLEEAKKKLAQRLQEAEESIEAVNsKCASLEKTKQR--LQGEVEDLMTDVERANSLAANLDKKQRNFDKV-------- 1456
Cdd:PRK04863 856 ---HESQEQQQRSQLEQAKEGLSALN-RLLPRLNLLADetLADRVEEIREQLDEAEEAKRFVQQHGNALAQLepivsvlq 931
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1457 -----LAEWKQKYEESQAELEGAQKEARSLsTELFKMKN--SYEEALDQLEtmkrenknlqqEISDLTEQIGEtgksihE 1529
Cdd:PRK04863 932 sdpeqFEQLKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAhfSYEDAAEMLA-----------KNSDLNEKLRQ------R 993
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1530 LEKAkktvETEKSEIQAALEEAEGTLeheeSKILRVQLELnqvKSEIDRK---LAEKDEEMEQI---------KRNSQRv 1597
Cdd:PRK04863 994 LEQA----EQERTRAREQLRQAQAQL----AQYNQVLASL---KSSYDAKrqmLQELKQELQDLgvpadsgaeERARAR- 1061
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1598 idsmQSTLDAEV---RSRNDALrvkkkmEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVR--GQEDMK 1672
Cdd:PRK04863 1062 ----RDELHARLsanRSRRNQL------EKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRlvKDNGVE 1131
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*....
gi 1316056572 1673 EQV--------------AMVERRNGLM---VAEIEELRAALEQTERSRK 1704
Cdd:PRK04863 1132 RRLhrrelaylsadelrSMSDKALGALrlaVADNEHLRDVLRLSEDPKR 1180
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
845-1418 |
1.24e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 73.67 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 845 KSAETEKELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAKLK 924
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 925 ETTERLEDEEEIN--------------AELTAKKRKLEDECSELKKDIDDLELTLA------------------------ 966
Cdd:pfam01576 535 EDAGTLEALEEGKkrlqrelealtqqlEEKAAAYDKLEKTKNRLQQELDDLLVDLDhqrqlvsnlekkqkkfdqmlaeek 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 967 -----------KVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQV 1035
Cdd:pfam01576 615 aisaryaeerdRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQV 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1036 DDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESI-MDLENDKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQ------- 1107
Cdd:pfam01576 695 EEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFeRDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQavaakkk 774
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1108 LQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTl 1187
Cdd:pfam01576 775 LELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASE- 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1188 QHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKS-- 1265
Cdd:pfam01576 854 RARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSts 933
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1266 KNDENVRQlndinaqkaRLQTENGEFARQLEEKEALV-SQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDC 1344
Cdd:pfam01576 934 QKSESARQ---------QLERQNKELKAKLQEMEGTVkSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKL 1004
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316056572 1345 DLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYEtDAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASL 1418
Cdd:pfam01576 1005 KEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE-EAEEEASRANAARRKLQRELDDATESNESMNREVSTL 1077
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1384-1934 |
2.95e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1384 IQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEwKQK 1463
Cdd:PRK03918 154 ILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKE-VKE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1464 YEESQAELEGAQKEARSLSTELFKMknsyEEALDQLETMKREnknLQQEISDLTEQIGETgKSIHELEKAKKTVETEKSE 1543
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKL----EEKIRELEERIEE---LKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1544 IQAALEEAEGTLEHEESKILRVQLELNQVkSEIDRKLAEKDEEMEQIKRNSQRvidsmqstLDAEVRSRNDALRVKKKME 1623
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKEL-EEKEERLEELKKKLKELEKRLEE--------LEERHELYEEAKAKKEELE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1624 gdlnemEIQLSHANRQAAEAQKQLRNVQgqlkdaqlhlddavRGQEDMKEQVAMVERRNGLMVAEIEELRAALEQTERSR 1703
Cdd:PRK03918 376 ------RLKKRLTGLTPEKLEKELEELE--------------KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1704 K---VAEQELvDASERVGLLHSQNSSLLNTKKKLEtdlvqvqgEVDDAVQEARNAEDKAKKAITDAammaEELKKEQDTS 1780
Cdd:PRK03918 436 GkcpVCGREL-TEEHRKELLEEYTAELKRIEKELK--------EIEEKERKLRKELRELEKVLKKE----SELIKLKELA 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1781 AHLERMKKNLE-VTVKDLQHRLDEAENLamkggKKQLQKLEQRVRELETEVEGEQ---KRGADAVKGVRKYERRVKELTY 1856
Cdd:PRK03918 503 EQLKELEEKLKkYNLEELEKKAEEYEKL-----KEKLIKLKGEIKSLKKELEKLEelkKKLAELEKKLDELEEELAELLK 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1857 QTEEdkKNITRLQDLVDKLQLKVKAYKR--QAEEAEEQANSHMSRLRKVQHEMEEAQERADIAESQVNKLRAKSRDVGKS 1934
Cdd:PRK03918 578 ELEE--LGFESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
866-1277 |
3.05e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.99 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 866 DLTTALAKKKELEEKMVSLLQEKNDLQL-------QVASEVENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINA 938
Cdd:PRK02224 308 DAEAVEARREELEDRDEELRDRLEECRVaaqahneEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 939 ELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAkltkEKKALQEA------------ 1006
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE----EAEALLEAgkcpecgqpveg 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1007 --HQQTLDDlqaEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRmDLERAKRKLEGDLKLAQESIMDLENDKQQSDEKI 1084
Cdd:PRK02224 464 spHVETIEE---DRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERA 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1085 KKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSrELEEISERLEEAGGATAAQ 1164
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIERLREKREAL 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1165 IEMNKKREAEFQKLR---RDLEEsTLQHEATAAALRKKQ---------ADSVAELGEQIDNLQR----VKQKLEkEKSEF 1228
Cdd:PRK02224 619 AELNDERRERLAEKRerkRELEA-EFDEARIEEAREDKEraeeyleqvEEKLDELREERDDLQAeigaVENELE-ELEEL 696
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1229 KMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENV-RQLNDI 1277
Cdd:PRK02224 697 RERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLeRMLNET 746
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1492-1938 |
3.73e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.87 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1492 YEEALDQLETMKRENKNLQQeISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEgtLEHEESKILRVQLELNQ 1571
Cdd:COG4913 237 LERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1572 VKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALRVKKKMEGDLNEMEIQLSHA----NRQAAEAQKQL 1647
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeefAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1648 RNVQGQLKDAQLHLDDAVRGQEDMKEQ-------VAMVERRNGLMVAEIEELRAALEqteRSRKVAEQEL--------VD 1712
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRElreleaeIASLERRKSNIPARLLALRDALA---EALGLDEAELpfvgelieVR 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1713 ASERV------GLLHSQNSSLL--------------NTKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEE 1772
Cdd:COG4913 471 PEEERwrgaieRVLGGFALTLLvppehyaaalrwvnRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAW 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1773 LKKEQ---------DTSAHLER----------MKKNLEVTVKDLQHRLDE--------AENLAMKggKKQLQKLEQRVRE 1825
Cdd:COG4913 551 LEAELgrrfdyvcvDSPEELRRhpraitragqVKGNGTRHEKDDRRRIRSryvlgfdnRAKLAAL--EAELAELEEELAE 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1826 LETEVEG---------EQKRGADAVKGVRKYERRVKELTY---QTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQA 1893
Cdd:COG4913 629 AEERLEAleaeldalqERREALQRLAEYSWDEIDVASAEReiaELEAELERLDASSDDLAALEEQLEELEAELEELEEEL 708
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1316056572 1894 NSHMSRLRKVQHEMEEAQERADIAESQVNKLRAKSRDVGKSDAAE 1938
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1147-1596 |
6.70e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 6.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1147 LEEISERLEEAGGATAAQIEMNKKreaEFQKLRRDLEESTLQHEATAAALRKKQadsvaELGEQIDNLQRVKQKLEKEKS 1226
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLK---ELKELEEELKEAEEKEEEYAELQEELE-----ELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1227 EFKMEIdDLSSNMEAVAKAKGNLEkmcrTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLE----EKEALV 1302
Cdd:COG4717 120 KLEKLL-QLLPLYQELEALEAELA----ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlslATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1303 SQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHdcDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYETD 1382
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN--ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1383 ------AIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKV 1456
Cdd:COG4717 273 ltiagvLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1457 LAEWKQkyEESQAELEGAQKEARSLsteLFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKA--K 1534
Cdd:COG4717 353 LREAEE--LEEELQLEELEQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAldE 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316056572 1535 KTVETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKS--EIDRKLAEKDEEMEQIKRNSQR 1596
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEE 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1249-1713 |
6.76e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 6.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1249 LEKMCRTLEDQLSEIKSKNDE-NVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQaftqQIEELKRHIEEEV 1327
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPElNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA----ELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1328 KAKNALAHAVQSARHDCDLLR-----EQFEEEQEAKAELQRGMSKANSEVAQWRSkyetdaiQRTEELEEAKKKLAQRLQ 1402
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAElperlEELEERLEELRELEEELEELEAELAELQE-------ELEELLEQLSLATEEELQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1403 EAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDK-----------VLAEWKQKYEESQAEL 1471
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1472 EGAQKEARSL----STELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIG-ETGKSIHELEKAKKTVEtEKSEIQA 1546
Cdd:COG4717 276 AGVLFLVLGLlallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIE-ELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1547 ALEEAEGTLEHEESKILRVQLeLNQVKSEIDRKLAEKDEEMEQIKRNSQRvIDSMQSTLDAEVRSRNDALRvkkkmEGDL 1626
Cdd:COG4717 355 EAEELEEELQLEELEQEIAAL-LAEAGVEDEEELRAALEQAEEYQELKEE-LEELEEQLEELLGELEELLE-----ALDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1627 NEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQE--DMKEQVAMVERRNGLMVAEIEELRAALEQTERSRK 1704
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEARE 507
|
....*....
gi 1316056572 1705 VAEQELVDA 1713
Cdd:COG4717 508 EYREERLPP 516
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1425-1931 |
7.30e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 70.97 E-value: 7.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1425 LQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEgAQKEARSLSTELFKMKNSYEEALDQLET--- 1501
Cdd:pfam01576 7 MQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETE-LCAEAEEMRARLAARKQELEEILHELESrle 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1502 --------MKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEiqaaLEEAEGTLEHEESKILRVQLELNQVK 1573
Cdd:pfam01576 86 eeeersqqLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKK----LEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1574 SEIDRKLAEKDEE---MEQIKRNSQRVIDSMQSTLDAEVRSRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNV 1650
Cdd:pfam01576 162 SEFTSNLAEEEEKaksLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1651 QGQLKDAQLHLDDAvrgqedmKEQVAMVERRNGLMVAEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLNT 1730
Cdd:pfam01576 242 EEELQAALARLEEE-------TAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1731 KKkletdlvqvqgevddAVQEARNaedKAKKAITDAAMMAEELKKEQDtsAHLERMKKNLEVTVKDLQHRLDEAENLAMk 1810
Cdd:pfam01576 315 TA---------------AQQELRS---KREQEVTELKKALEEETRSHE--AQLQEMRQKHTQALEELTEQLEQAKRNKA- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1811 GGKKQLQKLEQRVRELETEVEGEQKRGADAVKGVRKYERRVKELtyqteedkknitrlqdlvdklQLKVKAYKRQAEEAE 1890
Cdd:pfam01576 374 NLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQEL---------------------QARLSESERQRAELA 432
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1316056572 1891 EQANSHMSRLRKVQHEMEEAQERADIAESQVNKLRAKSRDV 1931
Cdd:pfam01576 433 EKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT 473
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1493-1915 |
8.31e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 8.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1493 EEALDQLETM--KRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEheeskilrvqlELN 1570
Cdd:PRK02224 186 RGSLDQLKAQieEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-----------ELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1571 QVKSEIDrKLAEKDEEMEQIKRNSQRVIDSMQSTLDaEVRSRNDALRVKKKME-GDLNEMEIQLSHANRQAAEAQKQLRN 1649
Cdd:PRK02224 255 TLEAEIE-DLRETIAETEREREELAEEVRDLRERLE-ELEEERDDLLAEAGLDdADAEAVEARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1650 VQGQLKDAQLHLDDAVRGQEDMKEQVAMVERRNGLMVAEIEELRAALEQTERSRKVAEQELVDASERVG----------- 1718
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvdlgnaed 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1719 ---LLHSQNSSLLNTKKKLETDLvqvqGEVDDAVQEARNAEDKAK-----KAITDAAMmAEELKKEQDTSAHLERMKKNL 1790
Cdd:PRK02224 413 fleELREERDELREREAELEATL----RTARERVEEAEALLEAGKcpecgQPVEGSPH-VETIEEDRERVEELEAELEDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1791 EVTVKDLQHRLDEAEnlamkggkkQLQKLEQRVRELETEVEGEQKRGADAVKGVrkyerrvkeltyqtEEDKKNITRLQD 1870
Cdd:PRK02224 488 EEEVEEVEERLERAE---------DLVEAEDRIERLEERREDLEELIAERRETI--------------EEKRERAEELRE 544
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1316056572 1871 LVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEEAQERAD 1915
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
33-77 |
1.09e-11 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 60.91 E-value: 1.09e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1316056572 33 DAKSAYFVVDEADLYVKCKLIKKDGSKVTVETDGGKTLTVKEDDI 77
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1272-1908 |
1.17e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 70.14 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1272 RQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLRE-- 1349
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKEtc 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1350 ------------QFEEEQEAKAELQRGMSKANSEVAQWRSKYETDAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCAS 1417
Cdd:pfam05483 165 arsaektkkyeyEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1418 LEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEEsqaelegaqkearsLSTELFKMKNSYEEALD 1497
Cdd:pfam05483 245 LLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDH--------------LTKELEDIKMSLQRSMS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1498 QLETMKRENKNLQQEISDLTEqigETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEID 1577
Cdd:pfam05483 311 TQKALEEDLQIATKTICQLTE---EKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQ 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1578 RKLAEKdEEMEQIKRNSQRVIDSMQSTLDaevrSRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDA 1657
Cdd:pfam05483 388 KKSSEL-EEMTKFKNNKEVELEELKKILA----EDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAI 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1658 QLHLDDAVRGQEDMKEQVAMVERRNGLMVAEIEELraALEQTERSRkvaeqelvDASERVGLLHSQNSSLLNTKKKLETD 1737
Cdd:pfam05483 463 KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL--LLENKELTQ--------EASDMTLELKKHQEDIINCKKQEERM 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1738 LVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAenlamkggKKQLQ 1817
Cdd:pfam05483 533 LKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL--------KKQIE 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1818 KLEQRVRELETEVEGEQKRGADAVKGVRKYERRVKELTYQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQANSHM 1897
Cdd:pfam05483 605 NKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIA 684
|
650
....*....|.
gi 1316056572 1898 SRLRKVQHEME 1908
Cdd:pfam05483 685 DEAVKLQKEID 695
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1205-1710 |
1.35e-11 |
|
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: 69.77 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1205 AELGEQIDNLQRVKQKLEKEKSEFKMEIDDLssnmeavakakgnlEKMCRTLEDQLSEIKSKNDE---NVRQLNDINAQK 1281
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIEL--------------EKKASALKRQLDRESDRNQElqkRIRLLEKREAEA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1282 ARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVkakNALAHAVQSARHDCDLLREQFEEEQEAKAEL 1361
Cdd:pfam05557 68 EEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNEL---SELRRQIQRAELELQSTNSELEELQERLDLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1362 QRGMSKANSEVAQWRSKYET--DAIQRTEELEeakKKLAQRLQEAEEsIEAVNSKCAS---LEKTKQRLQGEVEDLMTDV 1436
Cdd:pfam05557 145 KAKASEAEQLRQNLEKQQSSlaEAEQRIKELE---FEIQSQEQDSEI-VKNSKSELARipeLEKELERLREHNKHLNENI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1437 ERANSLAANLDKKQRNFDKvlaewkqkYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQL---ETMKRENKNLQQEI 1513
Cdd:pfam05557 221 ENKLLLKEEVEDLKRKLER--------EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLrspEDLSRRIEQLQQRE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1514 SDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEID--RKLAEK-DEEMEQi 1590
Cdd:pfam05557 293 IVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDgyRAILESyDKELTM- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1591 KRNSQRVIDSMQSTLDaevrsrndalrVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKdaqlhlddAVRGQED 1670
Cdd:pfam05557 372 SNYSPQLLERIEEAED-----------MTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQ--------ALRQQES 432
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1316056572 1671 MKEQVAMVERRNGLMvAEIEELRAALEQTERSRKVAEQEL 1710
Cdd:pfam05557 433 LADPSYSKEEVDSLR-RKLETLELERQRLREQKNELEMEL 471
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1215-1894 |
1.43e-11 |
|
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: 69.66 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1215 QRVKQKLEKEKSEFK---MEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLqteNGEF 1291
Cdd:TIGR04523 36 KQLEKKLKTIKNELKnkeKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKI---NSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1292 ARQLEEKEALVSQLTRGKQaftqQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSE 1371
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKLEK----QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1372 VAQWRSKYetdaiQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQR 1451
Cdd:TIGR04523 189 IDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1452 NFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALD-----QLETMKRENKNLQQEISDLTEQIGETGKS 1526
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNkelksELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1527 IHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEIdRKLAEKDEEMEQIKRNSQRVIDSMQStld 1606
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI-NDLESKIQNQEKLNQQKDEQIKKLQQ--- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1607 aevrsrndalrvkkkmEGDLNEMEIQLSHANRqaAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMKEQVAMVERrnglmv 1686
Cdd:TIGR04523 420 ----------------EKELLEKEIERLKETI--IKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR------ 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1687 aEIEELRAALEQTERSRKVAEQEL-------VDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAvqearnaEDKA 1759
Cdd:TIGR04523 476 -SINKIKQNLEQKQKELKSKEKELkklneekKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL-------EDEL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1760 KKaitdaamMAEELKKEqdtsahlermkkNLEVTVKDLQHRLDEAENlAMKGGKKQLQKLEQRVRELETEVEgeqkrgaD 1839
Cdd:TIGR04523 548 NK-------DDFELKKE------------NLEKEIDEKNKEIEELKQ-TQKSLKKKQEEKQELIDQKEKEKK-------D 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1316056572 1840 AVKGVRKYERRVKELTYQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQAN 1894
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1189-1926 |
1.45e-11 |
|
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: 69.87 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1189 HEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIksknd 1268
Cdd:pfam12128 228 RDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEK----- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1269 envrqlndINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAftqQIEELKRHIEEEVKAKNALAHavQSARHDCdllr 1348
Cdd:pfam12128 303 --------RDELNGELSAADAAVAKDRSELEALEDQHGAFLDA---DIETAAADQEQLPSWQSELEN--LEERLKA---- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1349 eQFEEEQEAKAELQRGMSKANSEVAqwrskyetDAIQRTEELEEAKKKLAQRLQEAEES-IEAVNSKCAS-LEKTKQRLQ 1426
Cdd:pfam12128 366 -LTGKHQDVTAKYNRRRSKIKEQNN--------RDIAGIKDKLAKIREARDRQLAVAEDdLQALESELREqLEAGKLEFN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1427 GEVEDLMTDVE----RANSLAANLDKK--QRNFDKVLaewkqkyEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLE 1500
Cdd:pfam12128 437 EEEYRLKSRLGelklRLNQATATPELLlqLENFDERI-------ERAREEQEAANAEVERLQSELRQARKRRDQASEALR 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1501 TMKRENKNLQQEISDLTEQ-IGETGKSIHELEKakktvetekseiqaaleEAEGTLEHEESKILRVQLELNQVKSEIDRK 1579
Cdd:pfam12128 510 QASRRLEERQSALDELELQlFPQAGTLLHFLRK-----------------EAPDWEQSIGKVISPELLHRTDLDPEVWDG 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1580 LAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALrvkkkmegdlnEMEIQLSHANRQAAEaqKQLRNVQGQLKDAQL 1659
Cdd:pfam12128 573 SVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKA-----------EEALQSAREKQAAAE--EQLVQANGELEKASR 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1660 HLDDAVRGQEDMKE---QVAMVERRNGLMVAEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLET 1736
Cdd:pfam12128 640 EETFARTALKNARLdlrRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAY 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1737 DLVqVQGEVD---DAVQEARNAEDKAKKAITDA--AMMAEELKK---EQDTSAHLERMKKNLEVTVKD------------ 1796
Cdd:pfam12128 720 WQV-VEGALDaqlALLKAAIAARRSGAKAELKAleTWYKRDLASlgvDPDVIAKLKREIRTLERKIERiavrrqevlryf 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1797 --LQHR-LDEAENLAMkggkkQLQKLEQRVRELETEVegeQKRGADAVKGVRKYERRVKELTYQTEEDKKNITRLQDLVD 1873
Cdd:pfam12128 799 dwYQETwLQRRPRLAT-----QLSNIERAISELQQQL---ARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMS 870
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1316056572 1874 KL-QLKVKAYKRQAEEAEEQANSHMSRLR-KVQHEMEEAQERADIAESQVNKLRA 1926
Cdd:pfam12128 871 KLaTLKEDANSEQAQGSIGERLAQLEDLKlKRDYLSESVKKYVEHFKNVIADHSG 925
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
851-1149 |
2.40e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 68.98 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 851 KELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKskiQLEaKLKETTERL 930
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK---QIE-NLEEKEMNL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 931 EDE-EEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQ 1009
Cdd:pfam05483 547 RDElESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1010 TLDDLQAEEDKVNT----LTKAKTKLEQQVDDLEGSLE----QEKKLRMDLERAKRKLEGDLKLAQ-----------ESI 1070
Cdd:pfam05483 627 ENKQLNAYEIKVNKleleLASAKQKFEEIIDNYQKEIEdkkiSEEKLLEEVEKAKAIADEAVKLQKeidkrcqhkiaEMV 706
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316056572 1071 MDLENDKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEE 1149
Cdd:pfam05483 707 ALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1224-1806 |
3.14e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1224 EKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEdQLSEIKSKNDE---NVRQLNDINAQKARLQTENGEfaRQLEEKEA 1300
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIE-LLEPIRELAERyaaARERLAELEYLRAALRLWFAQ--RRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1301 LVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHD-CDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKY 1379
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1380 ETDAiqrtEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAE 1459
Cdd:COG4913 376 PASA----EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1460 wkqkyeesqaELEGAQKEARSLStELFKMKNSYEEALDQLETMKRENK-NL---QQEISDLTEQIGETgksiheleKAKK 1535
Cdd:COG4913 452 ----------ALGLDEAELPFVG-ELIEVRPEEERWRGAIERVLGGFAlTLlvpPEHYAAALRWVNRL--------HLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1536 TVETEKseIQAALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLA--------EKDEEME----------QIKRNSQR- 1596
Cdd:COG4913 513 RLVYER--VRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAELGrrfdyvcvDSPEELRrhpraitragQVKGNGTRh 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1597 VIDsmqstLDAEVRSRN----DALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQgQLKDAQLHLDDAVRGQEDMK 1672
Cdd:COG4913 591 EKD-----DRRRIRSRYvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDEIDVA 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1673 EQVAMVERRNglmvAEIEELRAA---LEQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAV 1749
Cdd:COG4913 665 SAEREIAELE----AELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 1750 QEARNAEDKAkkaitdaammAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAEN 1806
Cdd:COG4913 741 DLARLELRAL----------LEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1200-1417 |
3.49e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.10 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1200 QADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINA 1279
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1280 QKARLQTENGEFARQL------EEKEALVS-----QLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLR 1348
Cdd:COG4942 98 ELEAQKEELAELLRALyrlgrqPPLALLLSpedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316056572 1349 EQFEEEQEAKAELQRGMSKANSEVAQWRSKYETDAiQRTEELEEAKKKLAQRLQEAEESIEAVNSKCAS 1417
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1074-1931 |
5.69e-11 |
|
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: 68.07 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1074 ENDKQQSDEKIKKKDFEISQLLSKIEDEQSLgaqlqKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISER 1153
Cdd:pfam02463 145 EIIAMMKPERRLEIEEEAAGSRLKRKKKEAL-----KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1154 LEEAGGATAAQIEmnkKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEID 1233
Cdd:pfam02463 220 ELEEEYLLYLDYL---KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1234 DLSSNMEavakakgNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTEngefarqLEEKEALVSQLTRGKQAFT 1313
Cdd:pfam02463 297 ELKSELL-------KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKE-------LKELEIKREAEEEEEEELE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1314 QQIEELKRHIEEEVKAK---------------NALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSK 1378
Cdd:pfam02463 363 KLQEKLEQLEEELLAKKkleserlssaaklkeEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELK 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1379 YETDAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQ-RLQGEVEDLMTDVER-ANSLAANLDKKQRNFDKV 1456
Cdd:pfam02463 443 QGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLElLLSRQKLEERSQKESkARSGLKVLLALIKDGVGG 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1457 LAEWKQKYEESQAELEGAQKEARSLSTELFKMK-NSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIhelekAKK 1535
Cdd:pfam02463 523 RIISAHGRLGDLGVAVENYKVAISTAVIVEVSAtADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSI-----AVL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1536 TVETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRNDA 1615
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1616 LRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQgQLKDAQLHLDDAVRGQEDMKEQVAMVERRNGLMVAEIEELRAA 1695
Cdd:pfam02463 678 IQELQEKAESELAKEEILRRQLEIKKKEQREKEELK-KLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSR 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1696 LEQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDL----------VQVQGEVDDAVQEARNAEDKAKKAIT- 1764
Cdd:pfam02463 757 LKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQeeelraleeeLKEEAELLEEEQLLIEQEEKIKEEELe 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1765 -DAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLAMKgGKKQLQKLEQRVRELETEVEGEQKRGADAVKG 1843
Cdd:pfam02463 837 eLALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK-LKDELESKEEKEKEEKKELEEESQKLNLLEEK 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1844 VRKYERRVKELTYQTEEDKKNITRLQ----DLVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEEAQERADIAES 1919
Cdd:pfam02463 916 ENEIEERIKEEAEILLKYEEEPEELLleeaDEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDEL 995
|
890
....*....|..
gi 1316056572 1920 QVNKLRAKSRDV 1931
Cdd:pfam02463 996 EKERLEEEKKKL 1007
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1082-1737 |
6.11e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 67.82 E-value: 6.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1082 EKIKKKDFEISQLLSKIEDEQSLGAQlqkKIKELQARIEELEEEIEAERAARAKV-EKQRA---DLSRELEEISERLEEA 1157
Cdd:pfam05483 63 EGLKDSDFENSEGLSRLYSKLYKEAE---KIKKWKVSIEAELKQKENKLQENRKIiEAQRKaiqELQFENEKVSLKLEEE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1158 GGATAAQIEMNKKREAEFQKLRRDLE---ESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEidd 1234
Cdd:pfam05483 140 IQENKDLIKENNATRHLCNLLKETCArsaEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFK--- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1235 LSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAqkarLQTENGEFARQLEEKEALVS----QLTRGKQ 1310
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTF----LLEESRDKANQLEEKTKLQDenlkELIEKKD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1311 AFTQQIEELKRHIEEEVKAKNALAHAVQSA-RHDCDLLRE---QFEEEQEAKAELQRGMSKANSEVAQWRSKYETDAiQR 1386
Cdd:pfam05483 293 HLTKELEDIKMSLQRSMSTQKALEEDLQIAtKTICQLTEEkeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-QR 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1387 TEELEEAKKKLAQRLQ----EAEESIEAVNSKCASLEKTKQRLqGEVEDLMTDveranslaanldkkQRNFDKVLAEWKQ 1462
Cdd:pfam05483 372 LEKNEDQLKIITMELQkkssELEEMTKFKNNKEVELEELKKIL-AEDEKLLDE--------------KKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1463 KYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLT-----------EQIGETGKSIHELE 1531
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTahcdklllenkELTQEASDMTLELK 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1532 KAKKTVETEKSEIQAALEEAEGTLEHE---ESKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTLDA- 1607
Cdd:pfam05483 517 KHQEDIINCKKQEERMLKQIENLEEKEmnlRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKc 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1608 ---------------EVRSRNDALRVKKKMEG--------DLNEMEIQLSHANRQAAEA----QKQL-------RNVQGQ 1653
Cdd:pfam05483 597 nnlkkqienknknieELHQENKALKKKGSAENkqlnayeiKVNKLELELASAKQKFEEIidnyQKEIedkkiseEKLLEE 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1654 LKDAQLHLDDAV--------RGQEDMKEQVAMVERRNGLMVAEIEELRAALEQTersrKVAEQElvDASERVGL---LHS 1722
Cdd:pfam05483 677 VEKAKAIADEAVklqkeidkRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLY----KNKEQE--QSSAKAALeieLSN 750
|
730
....*....|....*
gi 1316056572 1723 QNSSLLNTKKKLETD 1737
Cdd:pfam05483 751 IKAELLSLKKQLEIE 765
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1392-1619 |
7.35e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.33 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1392 EAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAEL 1471
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1472 EGAQKEARSLSTELFKMKN-----------SYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKtvetE 1540
Cdd:COG4942 100 EAQKEELAELLRALYRLGRqpplalllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA----E 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316056572 1541 KSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALRVK 1619
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
915-1522 |
8.01e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 67.44 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 915 SKIQLEAKLKETTERLEDEEEinaeltakkrkledecsELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIA 994
Cdd:pfam05483 209 ARLEMHFKLKEDHEKIQHLEE-----------------EYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKAN 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 995 KLtKEKKALQEahqqtlddlqaeeDKVNTLTKAKTKLEQQVDDLEGSLEQEKKlrmdlerAKRKLEGDLKLAQESIMDLE 1074
Cdd:pfam05483 272 QL-EEKTKLQD-------------ENLKELIEKKDHLTKELEDIKMSLQRSMS-------TQKALEEDLQIATKTICQLT 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1075 NDKQQSDEKIKKKDFEISQLLSKIEDEQ-SLGAQLQKKIKELQarieeleeeieaeraaraKVEKQRADLSRELEEISER 1153
Cdd:pfam05483 331 EEKEAQMEELNKAKAAHSFVVTEFEATTcSLEELLRTEQQRLE------------------KNEDQLKIITMELQKKSSE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1154 LEEaggataaQIEMNKKREAEFQKLRRDL-EESTLQHEataaalrKKQADSVAElgeqidNLQRVKQKLEKEKSEFKMEI 1232
Cdd:pfam05483 393 LEE-------MTKFKNNKEVELEELKKILaEDEKLLDE-------KKQFEKIAE------ELKGKEQELIFLLQAREKEI 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1233 DDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAF 1312
Cdd:pfam05483 453 HDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1313 TQQIEELKrhiEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYET------DAIQR 1386
Cdd:pfam05483 533 LKQIENLE---EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNlkkqieNKNKN 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1387 TEELEEAKKKLAQRLQEAEESIEA----VNSKCASLEKTKQRL-------QGEVED-------LMTDVERANSLAANLDK 1448
Cdd:pfam05483 610 IEELHQENKALKKKGSAENKQLNAyeikVNKLELELASAKQKFeeiidnyQKEIEDkkiseekLLEEVEKAKAIADEAVK 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1449 KQRNFDK-----------VLAEWKQKY----EESQAEL------EGAQKEAR-SLSTELFKMKNSYEEALDQLETMKREN 1506
Cdd:pfam05483 690 LQKEIDKrcqhkiaemvaLMEKHKHQYdkiiEERDSELglyknkEQEQSSAKaALEIELSNIKAELLSLKKQLEIEKEEK 769
|
650
....*....|....*.
gi 1316056572 1507 KNLQQEISDLTEQIGE 1522
Cdd:pfam05483 770 EKLKMEAKENTAILKD 785
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
870-1694 |
8.05e-11 |
|
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: 67.67 E-value: 8.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 870 ALAKKKELEEKmVSLLQEKNDLQLQVASEVENLSDAEERCE----------GLIKSKIQLEAK-------LKETTERLED 932
Cdd:COG3096 287 ALELRRELFGA-RRQLAEEQYRLVEMARELEELSARESDLEqdyqaasdhlNLVQTALRQQEKieryqedLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 933 EEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKekhATEnkvknlteemATQDEAIAkLTKEKKALQEAHQQT-L 1011
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQ---ALD----------VQQTRAIQ-YQQAVQALEKARALCgL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1012 DDLqAEEDKVNTLTKAKTKLEQQVDDLegsLEQEKKLRMDlERAKRKLEGDLKL----------------AQESIMDLEN 1075
Cdd:COG3096 432 PDL-TPENAEDYLAAFRAKEQQATEEV---LELEQKLSVA-DAARRQFEKAYELvckiageversqawqtARELLRRYRS 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1076 DKQQSD--EKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKelqarieELEEEIEAERAARAKVEKQRADLSRELEEISER 1153
Cdd:COG3096 507 QQALAQrlQQLRAQLAELEQRLRQQQNAERLLEEFCQRIG-------QQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1154 ---LEEAGGATAAQIEMNKKREAEFQKLRRDLEesTLQhEATAAALrkkqaDSVAELGEQIDNLQRVKQKLEKEKSEFKM 1230
Cdd:COG3096 580 rseLRQQLEQLRARIKELAARAPAWLAAQDALE--RLR-EQSGEAL-----ADSQEVTAAMQQLLEREREATVERDELAA 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1231 EIDDLSSNMEAVAKAKGNLEKMCRTLEDQ-----LSEI-----------------KSKNDENVRQLNDINAQKARLQT-- 1286
Cdd:COG3096 652 RKQALESQIERLSQPGGAEDPRLLALAERlggvlLSEIyddvtledapyfsalygPARHAIVVPDLSAVKEQLAGLEDcp 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1287 ------------------ENGEFAR----QLEEKEALVSQLTR----GKQAFTQQIEELKRHIEEEVKAKNALAHAVQS- 1339
Cdd:COG3096 732 edlyliegdpdsfddsvfDAEELEDavvvKLSDRQWRYSRFPEvplfGRAAREKRLEELRAERDELAEQYAKASFDVQKl 811
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1340 -----------ARHDCDLLREQFEEE----QEAKAELQRGMSKANSEVAQWRSKYEtdaiQRTEELEEAKK--------- 1395
Cdd:COG3096 812 qrlhqafsqfvGGHLAVAFAPDPEAElaalRQRRSELERELAQHRAQEQQLRQQLD----QLKEQLQLLNKllpqanlla 887
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1396 --KLAQRLQEAEESIEAVNSKCASLEKTKQRLqGEVEDlmtdveransLAANLDKKQRNFDKVlaewKQKYEESQAELEG 1473
Cdd:COG3096 888 deTLADRLEELREELDAAQEAQAFIQQHGKAL-AQLEP----------LVAVLQSDPEQFEQL----QADYLQAKEQQRR 952
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1474 AQKEARSLsTELFKMKN--SYEEALDQLEtmkrenknlqqEISDLTEQIGEtgksihELEKAkktvETEKSEIQAALEEA 1551
Cdd:COG3096 953 LKQQIFAL-SEVVQRRPhfSYEDAVGLLG-----------ENSDLNEKLRA------RLEQA----EEARREAREQLRQA 1010
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1552 EGtlEHEESkiLRVQLELN---QVKSEIdrkLAEKDEEMEQIkrnSQRVIDSMQSTLDAEVRSRNDALRVKKkmeGDLNE 1628
Cdd:COG3096 1011 QA--QYSQY--NQVLASLKssrDAKQQT---LQELEQELEEL---GVQADAEAEERARIRRDELHEELSQNR---SRRSQ 1077
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316056572 1629 MEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMKEQVAM--VERR---NGLMVAEIEELRA 1694
Cdd:COG3096 1078 LEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRLARDndVERRlhrRELAYLSADELRS 1148
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1549-1938 |
1.02e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1549 EEAEGTLEHEESKILRVQLELNQVKSEIDR--KLAEKDEEMEQIKRnsqrvidsmqstlDAEVRSRNDALRVKKKMEGDL 1626
Cdd:COG1196 175 EEAERKLEATEENLERLEDILGELERQLEPleRQAEKAERYRELKE-------------ELKELEAELLLLKLRELEAEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1627 NEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVrgqedmkeqvamverrnglmvAEIEELRAAL-------EQT 1699
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELE---------------------LELEEAQAEEyellaelARL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1700 ERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDT 1779
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1780 SAHLERMKKNLEVTVKDLQHRLDEAEnlamkggkKQLQKLEQRVRELETEVEGEQKRGADAvkgvrkyERRVKELTYQTE 1859
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELE--------EAEEALLERLERLEEELEELEEALAEL-------EEEEEEEEEALE 445
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316056572 1860 EDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQanshmsrLRKVQHEMEEAQERADIAESQVNKLRAKSRDVGKSDAAE 1938
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAA-------LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
836-1508 |
5.80e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 64.68 E-value: 5.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 836 LYFKIKPLLKSAETEKELQNMKENYEKMQSDLT---------TALAKKKELEEKMVSLLQEKNDLQlQVASEVENLSDAE 906
Cdd:TIGR00606 456 LKFVIKELQQLEGSSDRILELDQELRKAERELSkaeknslteTLKKEVKSLQNEKADLDRKLRKLD-QEMEQLNHHTTTR 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 907 ERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKV 979
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 980 KNLTEEMATQDEAI----------AKLTKEKKALQEAHQQtlddLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLR 1049
Cdd:TIGR00606 615 ESKEEQLSSYEDKLfdvcgsqdeeSDLERLKEEIEKSSKQ----RAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTE 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1050 MDLERAKRKLEGDLKLAQesimdlenDKQQSDEK-IKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEA 1128
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAP--------DKLKSTESeLKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQR 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1129 ERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMnKKREAEFQKLRRDLEESTLqhEATAAALRKKQADSVAEL- 1207
Cdd:TIGR00606 763 LKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMEL-KDVERKIAQQAAKLQGSDL--DRTVQQVNQEKQEKQHELd 839
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1208 --GEQIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNdenvRQLNDINAQKARLQ 1285
Cdd:TIGR00606 840 tvVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLI----REIKDAKEQDSPLE 915
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1286 TENGEFarqLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAK-AELQRG 1364
Cdd:TIGR00606 916 TFLEKD---QQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQlEECEKH 992
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1365 MSKANSEVAQWRSKYETDAIQ------------RTEELEEAKKKLAQRLQEAEEsieavnSKCASLEKTKQRLQGEVEDL 1432
Cdd:TIGR00606 993 QEKINEDMRLMRQDIDTQKIQerwlqdnltlrkRENELKEVEEELKQHLKEMGQ------MQVLQMKQEHQKLEENIDLI 1066
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 1433 MTDVERANSLAANLDKKQRNFDKVLAEWK-QKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKN 1508
Cdd:TIGR00606 1067 KRNHVLALGRQKGYEKEIKHFKKELREPQfRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEIN 1143
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
851-1309 |
5.84e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 851 KELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQlqvaSEVENLSDAEERCEgLIKSKIQLEAKLKETTERL 930
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR----EELEKLEKLLQLLP-LYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 931 EDEEEINAELtakkRKLEDECSELKKDIDDLELTLA-KVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQ 1009
Cdd:COG4717 149 EELEERLEEL----RELEEELEELEAELAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1010 TLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDEKIKKKDF 1089
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1090 EISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKV-------EKQRADLSRELEEISERLEEAGGATA 1162
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEllreaeeLEEELQLEELEQEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1163 AQIEMNKKREAEFQKLRRDLEESTLQ-HEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEA 1241
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316056572 1242 VAKaKGNLEKMCRTLEDQLSEIKSKNDE-NVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGK 1309
Cdd:COG4717 465 LEE-DGELAELLQELEELKAELRELAEEwAALKLALELLEEAREEYREERLPPVLERASEYFSRLTDGR 532
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1462-1681 |
6.67e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 6.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1462 QKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLetmkrenKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEK 1541
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1542 SEIQAALEEaegtLEHEESKILRVQLELNQ-------VKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRND 1614
Cdd:COG4942 93 AELRAELEA----QKEELAELLRALYRLGRqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 1615 ALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMKEQVAMVERR 1681
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
844-1273 |
8.84e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 8.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 844 LKSAETEKELQNMKENYEKMQSD-LTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAK 922
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADeLKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 923 LKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHatENKVKnlTEEMATQDEAIAKLTKEKKA 1002
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIK--AAEEAKKAEEDKKKAEEAKK 1682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1003 LQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQEsimdlendkqqsde 1082
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE-------------- 1748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1083 kikkkdfeisqllSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEI---SERLEEAGG 1159
Cdd:PTZ00121 1749 -------------AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIfdnFANIIEGGK 1815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1160 ATAAQIEMNKKRE-------AEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEI 1232
Cdd:PTZ00121 1816 EGNLVINDSKEMEdsaikevADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDK 1895
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1316056572 1233 DDLSSNMEAVAKAKGNLEKMCRTLEdqLSEIKSKNDENVRQ 1273
Cdd:PTZ00121 1896 DDIEREIPNNNMAGKNNDIIDDKLD--KDEYIKRDAEETRE 1934
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
891-1116 |
8.93e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 8.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 891 LQLQVASEVENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEK 970
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 971 EKHATENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAktkLEQQVDDLEGSLEQEKKLRM 1050
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA---RREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316056572 1051 DLERAKRKLEGDLKLAQESIMDLENDKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQ 1116
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
895-1651 |
9.79e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 64.09 E-value: 9.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 895 VASEVENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRkledecSELKKDIDDLELTLAKVEKEKHA 974
Cdd:pfam12128 239 IRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 975 TENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAE-----------EDKVNTLTKAKTKL-----EQQVDDL 1038
Cdd:pfam12128 313 ADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSElenleerlkalTGKHQDVTAKYNRRrskikEQNNRDI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1039 EGSLEQEKKLRMDLERAKRKLEGDLKlAQESIMDLENDKQQSDEKIKKKDFE--ISQLLSKI------EDEQSLGAQLQK 1110
Cdd:pfam12128 393 AGIKDKLAKIREARDRQLAVAEDDLQ-ALESELREQLEAGKLEFNEEEYRLKsrLGELKLRLnqatatPELLLQLENFDE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1111 KIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRR----DLEEST 1186
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRkeapDWEQSI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1187 LQHEATAAALRKKQADSV-AELGEQIDNLQRVK---------------QKLEKEKSEFKMEIDDLSSNM----EAVAKAK 1246
Cdd:pfam12128 552 GKVISPELLHRTDLDPEVwDGSVGGELNLYGVKldlkridvpewaaseEELRERLDKAEEALQSAREKQaaaeEQLVQAN 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1247 GNLEKMCRTLEDQLSEIKSkNDENVRQLNDINAQKARLQTENGEFARQLEEK-----EALVSQLTRGKQAFTQQIEELKR 1321
Cdd:pfam12128 632 GELEKASREETFARTALKN-ARLDLRRLFDEKQSEKDKKNKALAERKDSANErlnslEAQLKQLDKKHQAWLEEQKEQKR 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1322 hieEEVKAKNALAHAVQSARHDcdllreQFEEEQEAKAELQRGMSKANSEVAQWRsKYETDAI----QRTEELEEAKKKL 1397
Cdd:pfam12128 711 ---EARTEKQAYWQVVEGALDA------QLALLKAAIAARRSGAKAELKALETWY-KRDLASLgvdpDVIAKLKREIRTL 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1398 AQRLQEAEESIEAVNSKCASLEKT----KQRLQGEVEDLMTDVERansLAANLDKKQRNFDKVLAEWKQKYEESQAELEG 1473
Cdd:pfam12128 781 ERKIERIAVRRQEVLRYFDWYQETwlqrRPRLATQLSNIERAISE---LQQQLARLIADTKLRRAKLEMERKASEKQQVR 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1474 AQKEARSLSTELFKM------------KNSYEEALDQLETMKRENKNL----QQEISDLTEQIG--------ETGKSIHE 1529
Cdd:pfam12128 858 LSENLRGLRCEMSKLatlkedanseqaQGSIGERLAQLEDLKLKRDYLsesvKKYVEHFKNVIAdhsgsglaETWESLRE 937
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1530 LEK---AKKTVETEKSEIQAALEEAEGTLEHEESKILRVQLELN-QVKSEIDRKLAEKDEEMEQIKRNSQRVIDsmqSTL 1605
Cdd:pfam12128 938 EDHyqnDKGIRLLDYRKLVPYLEQWFDVRVPQSIMVLREQVSILgVDLTEFYDVLADFDRRIASFSRELQREVG---EEA 1014
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1316056572 1606 DAEvRSRNDALRVKKKMEgdlnemEIQLSHANRQAAEAQKQLRNVQ 1651
Cdd:pfam12128 1015 FFE-GVSESAVRIRSKVS------ELEYWPELRVFVKAFRLWKSDG 1053
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
918-1164 |
1.46e-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: 62.09 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 918 QLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEmatqdeaIAKLT 997
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE-------IAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 998 KEKKALQEAHQQTLDDLQaeedKVNTLTKAKTKLEQQ-VDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLEND 1076
Cdd:COG4942 97 AELEAQKEELAELLRALY----RLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1077 KQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQArieeleeeieaeraARAKVEKQRADLSRELEEISERLEE 1156
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA--------------ELAELQQEAEELEALIARLEAEAAA 238
|
....*...
gi 1316056572 1157 AGGATAAQ 1164
Cdd:COG4942 239 AAERTPAA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1391-1595 |
1.54e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 62.15 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1391 EEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANslaANLDKKQRNFDKVLAEWKQKYEESQAE 1470
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ---AEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1471 LEGAQKEARSLST-ELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALE 1549
Cdd:COG3883 92 ARALYRSGGSVSYlDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1316056572 1550 EAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQ 1595
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
922-1537 |
1.71e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 63.00 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 922 KLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLT---K 998
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSsleD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 999 EKKALQEAHQQTLDDLQAEEDKVNtltkaktkleqqvdDLEGSLEQEKKLRMDLERAKRklegdlklaqESIMDLENDKQ 1078
Cdd:PRK01156 250 MKNRYESEIKTAESDLSMELEKNN--------------YYKELEERHMKIINDPVYKNR----------NYINDYFKYKN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1079 QSDEKikkkdfeiSQLLSKIEDEQSLGAQLQKKIKELQarieeleeeieAERAARAKVEKQRADLSRELEEISERLEEAG 1158
Cdd:PRK01156 306 DIENK--------KQILSNIDAEINKYHAIIKKLSVLQ-----------KDYNDYIKKKSRYDDLNNQILELEGYEMDYN 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1159 GATAAQIEMNKKREAEFQKLRR---DLEESTLQHEATAAALRKKQAD---SVAELGEQIDNLQRVKQKLEKEKSEFKMEI 1232
Cdd:PRK01156 367 SYLKSIESLKKKIEEYSKNIERmsaFISEILKIQEIDPDAIKKELNEinvKLQDISSKVSSLNQRIRALRENLDELSRNM 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1233 DDLSS-NMEAVAKAKGNLEKMCRTLED---QLSEIKSKNDENVRQLNDINA----QKARLQTENGEFARQLEEKEALVSQ 1304
Cdd:PRK01156 447 EMLNGqSVCPVCGTTLGEEKSNHIINHyneKKSRLEEKIREIEIEVKDIDEkivdLKKRKEYLESEEINKSINEYNKIES 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1305 LTRGKQAFTQQIEELKrhiEEEVKAkNALAHAVQSArhDCDLLREQFEEEQEAKAElqrgmskansevaqwRSKYETDAI 1384
Cdd:PRK01156 527 ARADLEDIKIKINELK---DKHDKY-EEIKNRYKSL--KLEDLDSKRTSWLNALAV---------------ISLIDIETN 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1385 Q-RTEELEEAKKKLAQRLQEAEESIEAVNSkcaSLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDkvlaewkqK 1463
Cdd:PRK01156 586 RsRSNEIKKQLNDLESRLQEIEIGFPDDKS---YIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKID--------N 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1464 YEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKREN-------KNLQQEISDLTEQIGETGKSIHELEKAKKT 1536
Cdd:PRK01156 655 YKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRarlestiEILRTRINELSDRINDINETLESMKKIKKA 734
|
.
gi 1316056572 1537 V 1537
Cdd:PRK01156 735 I 735
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
845-1590 |
1.96e-09 |
|
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: 63.15 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 845 KSAETEKELQNMKENYEKMQSDLTTALAKKKE-----LEEKMVSLLQEKNDLQLQVASEVENLSDaeeRCEGLIKSKIQL 919
Cdd:TIGR01612 994 KNNELIKYFNDLKANLGKNKENMLYHQFDEKEkatndIEQKIEDANKNIPNIEIAIHTSIYNIID---EIEKEIGKNIEL 1070
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 920 EAK--LKETTERLEDEEEINAELT---------AKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAT 988
Cdd:TIGR01612 1071 LNKeiLEEAEINITNFNEIKEKLKhynfddfgkEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKA 1150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 989 QDEAIAKLT---------KEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQvddlEGSLEQEKKLRMD-------- 1051
Cdd:TIGR01612 1151 QINDLEDVAdkaisnddpEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKD----KTSLEEVKGINLSygknlgkl 1226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1052 ----LERAKRKLEGDLKLAQESIMDLENDKQQSDEkikkkdfeisqllskIEDEQSLGAQLQKKIKELQarieELEEEIE 1127
Cdd:TIGR01612 1227 flekIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPE---------------IENEMGIEMDIKAEMETFN----ISHDDDK 1287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1128 AERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMnKKREAEFQKLRRD----LEESTLQHEATAAALRKKQADS 1203
Cdd:TIGR01612 1288 DHHIISKKHDENISDIREKSLKIIEDFSEESDINDIKKEL-QKNLLDAQKHNSDinlyLNEIANIYNILKLNKIKKIIDE 1366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1204 VAELGEQID-NLQRVKQKLEKEKSEFKMEIDDLS-----SNMEAVAKAK---GNLEKMCRTLEDQLSEiKSKNDENVRQL 1274
Cdd:TIGR01612 1367 VKEYTKEIEeNNKNIKDELDKSEKLIKKIKDDINleeckSKIESTLDDKdidECIKKIKELKNHILSE-ESNIDTYFKNA 1445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1275 NDINaQKARLQTENGEFARQlEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKN-ALAHAVQSARHdcdllREQFEE 1353
Cdd:TIGR01612 1446 DENN-ENVLLLFKNIEMADN-KSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDeADKNAKAIEKN-----KELFEQ 1518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1354 EQEAKAELQRGMSKAnsEVAQWRSKYETDAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKcaslektkqrlQGEVEDLM 1433
Cdd:TIGR01612 1519 YKKDVTELLNKYSAL--AIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKE-----------KFRIEDDA 1585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1434 TDVERANSLAANLDKKQRNFDKVL---AEWKQKYEESQAELEGAQKEARSLS-----TELFKMKNSYEEALDQLETMKRE 1505
Cdd:TIGR01612 1586 AKNDKSNKAAIDIQLSLENFENKFlkiSDIKKKINDCLKETESIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQ 1665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1506 NKNLQQEISDLTEQIGETGKSIHELEKAKKT-----VETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKSE---ID 1577
Cdd:TIGR01612 1666 KKNIEDKKKELDELDSEIEKIEIDVDQHKKNyeigiIEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEgidPN 1745
|
810
....*....|...
gi 1316056572 1578 RKLAEKDEEMEQI 1590
Cdd:TIGR01612 1746 EKLEEYNTEIGDI 1758
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1021-1592 |
1.96e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 63.00 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1021 VNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERakrklegdlklaqeSIMDLENDKQQSDEKIKKKdfeiSQLLSKIED 1100
Cdd:PRK01156 161 INSLERNYDKLKDVIDMLRAEISNIDYLEEKLKS--------------SNLELENIKKQIADDEKSH----SITLKEIER 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1101 EQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEE---ISERLEEAGGATAAQIEMNKKREAEFQK 1177
Cdd:PRK01156 223 LSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKnnyYKELEERHMKIINDPVYKNRNYINDYFK 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1178 LRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKleKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLE 1257
Cdd:PRK01156 303 YKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKK--SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1258 DQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAV 1337
Cdd:PRK01156 381 EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGT 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1338 QSARHDCDLLREQFEEE----QEAKAELQRGMSKANSEVAQWRSKYETDAIQRTEELEEAKKKLAQR---LQEAEESIEA 1410
Cdd:PRK01156 461 TLGEEKSNHIINHYNEKksrlEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESAradLEDIKIKINE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1411 VNSKCASLEKTKQRLQG-EVEDL---MTDVERANSLAANLD-----KKQRNFDKVLAEWKQKYEESQAELEGAQKEARSL 1481
Cdd:PRK01156 541 LKDKHDKYEEIKNRYKSlKLEDLdskRTSWLNALAVISLIDietnrSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKS 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1482 STELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGEtgksIHELEKAKKTVETEKSEIQAALEEAEGTLEHEES- 1560
Cdd:PRK01156 621 IREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAE----IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKAn 696
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1316056572 1561 --------KILRVQL-ELNQVKSEIDRKLaekdEEMEQIKR 1592
Cdd:PRK01156 697 rarlestiEILRTRInELSDRINDINETL----ESMKKIKK 733
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1454-1935 |
2.73e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1454 DKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYE-EALDQLETMKRENKNLQQEISDLTE-----QIGETGKSI 1527
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKaEDARKAEEARKAEDAKRVEIARKAEdarkaEEARKAEDA 1175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1528 HELEKAKKTVETEKSEIQAALEEA----EGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEMEQIKR----NSQRVID 1599
Cdd:PTZ00121 1176 KKAEAARKAEEVRKAEELRKAEDArkaeAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKaeeeRNNEEIR 1255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1600 SMQSTLDAEVRSRNDALRVKKKMEGDlnemEIQLSHANRQAAEAQK--QLRNVQGQLKDAQlhlddAVRGQEDMKEQVAM 1677
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKAD----ELKKAEEKKKADEAKKaeEKKKADEAKKKAE-----EAKKADEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1678 VERRNGLMVAEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSllnTKKKLEtdlvqvqgEVDDAVQEARNAED 1757
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE---AKKKAD--------AAKKKAEEKKKADE 1395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1758 KAKKAITDAAMmAEELKKEQDTSAHLERMKKNLEVTVK--DLQHRLDEAenlamKGGKKQLQKLEQRVRELETEVEGEQK 1835
Cdd:PTZ00121 1396 AKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEKKKadEAKKKAEEA-----KKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1836 RGADAVKGVRKYERRVKELTYQTEEDKKnitrlqdlvdklqlKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEEAQERAD 1915
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKK--------------KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
490 500
....*....|....*....|
gi 1316056572 1916 IAESQVNKLRAKSRDVGKSD 1935
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAE 1555
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
858-1458 |
2.79e-09 |
|
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: 62.55 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 858 ENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASE-VENLSDAEERCEGLIKSKIQLEAKLKETTERLEdeEEI 936
Cdd:pfam12128 347 EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVAEDDLQALE--SEL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 937 NAELTAKKRKLEDECSELKKDIDDLELTLAKV---EKEKHATENKVKNLTEEMATQDEAIAK---LTKEKKALQEAHQQT 1010
Cdd:pfam12128 425 REQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERAREEQEAANAEverLQSELRQARKRRDQA 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1011 LDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQekKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDEKIKKKDFE 1090
Cdd:pfam12128 505 SEALRQASRRLEERQSALDELELQLFPQAGTLLH--FLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYG 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1091 ISQLLSKIEDEQSLGAQlqkkiKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGAtaaqiemnkk 1170
Cdd:pfam12128 583 VKLDLKRIDVPEWAASE-----EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA---------- 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1171 reaeFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDLSSnmEAVAKAKGNLE 1250
Cdd:pfam12128 648 ----LKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKR--EARTEKQAYWQ 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1251 KMCRTLEDQLSEIKSKNDENVRQLndiNAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHieeevkak 1330
Cdd:pfam12128 722 VVEGALDAQLALLKAAIAARRSGA---KAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVR-------- 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1331 nalAHAVQSARhdcDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYETDAIQRTEELE---EAKKKLAQRLQEAEES 1407
Cdd:pfam12128 791 ---RQEVLRYF---DWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEmerKASEKQQVRLSENLRG 864
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 1408 IEAVNSKCASL--EKTKQRLQGEVEDLMTDVE----RANSLAANLDKKQRNFDKVLA 1458
Cdd:pfam12128 865 LRCEMSKLATLkeDANSEQAQGSIGERLAQLEdlklKRDYLSESVKKYVEHFKNVIA 921
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1052-1630 |
3.00e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 62.23 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1052 LERAKRKLEGDLKLAQESIMDLENDKqqsdEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEEleeeieaera 1131
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIDYLE----EKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNN---------- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1132 arakVEKQRADLSRELEEISERLEEAG--GATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGE 1209
Cdd:PRK01156 230 ----AMDDYNNLKSALNELSSLEDMKNryESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1210 QIDNLQRVKQKLEKEKSEFkmeiDDLSSNMEAVAKAKGNLEKMCRTLED---QLSEIKSKNDENVRQLNDINAQKARLQT 1286
Cdd:PRK01156 306 DIENKKQILSNIDAEINKY----HAIIKKLSVLQKDYNDYIKKKSRYDDlnnQILELEGYEMDYNSYLKSIESLKKKIEE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1287 ENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEevkaknaLAHAVQSARHDCDLLREQfEEEQEAKAELQRGMS 1366
Cdd:PRK01156 382 YSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD-------ISSKVSSLNQRIRALREN-LDELSRNMEMLNGQS 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1367 KAnsevAQWRSKYETDAIQR-TEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQG-EVEDLMTDVERANSLAA 1444
Cdd:PRK01156 454 VC----PVCGTTLGEEKSNHiINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1445 NLdKKQRNFDKVLAEWKQKYEEsqaelegAQKEARSLSTELFKMKN-SYEEALDQ-----LETMKRENKNLQQEISDLTE 1518
Cdd:PRK01156 530 DL-EDIKIKINELKDKHDKYEE-------IKNRYKSLKLEDLDSKRtSWLNALAVislidIETNRSRSNEIKKQLNDLES 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1519 QIGE-----------TGKSIHELEKAKKTVETEKSEIQA---ALEEAEGTLEHEE-----------------SKILRVQL 1567
Cdd:PRK01156 602 RLQEieigfpddksyIDKSIREIENEANNLNNKYNEIQEnkiLIEKLRGKIDNYKkqiaeidsiipdlkeitSRINDIED 681
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316056572 1568 ELNQVKSEIDRKLAEKDEEMEQIKRNSQRVidsmqSTLDAEVRSRNDALRVKKKMEGDLNEME 1630
Cdd:PRK01156 682 NLKKSRKALDDAKANRARLESTIEILRTRI-----NELSDRINDINETLESMKKIKKAIGDLK 739
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
848-1116 |
3.15e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.96 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 848 ETEKELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAKLKETT 927
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 928 ERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQEah 1007
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE-- 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1008 qqtlddlqaeedKVNTLTKAKTKLEQQVDDLEGSLEQEK--KLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDEKIK 1085
Cdd:TIGR04523 525 ------------KIEKLESEKKEKESKISDLEDELNKDDfeLKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
250 260 270
....*....|....*....|....*....|.
gi 1316056572 1086 KKDFEISQLLSKIEDEQSLGAQLQKKIKELQ 1116
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1005-1428 |
3.60e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1005 EAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLE--GDLKLAQESIMDLENDKQQSDE 1082
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1083 KIKkkdfEISQLLSKIEDEQSLGAQLQKKIKEL-QARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGAT 1161
Cdd:COG4717 154 RLE----ELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1162 aAQIEMNKKREAEFQKLRR------------------DLEESTLQHEATAAALR--------KKQADSVAELGEQIDNLQ 1215
Cdd:COG4717 230 -EQLENELEAAALEERLKEarlllliaaallallglgGSLLSLILTIAGVLFLVlgllallfLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1216 RVKQKLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDEnvRQLNDINAQKARLQTENGefarqL 1295
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE--LQLEELEQEIAALLAEAG-----V 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1296 EEKEALVSQLTRGKQAftQQIEELKRHIEEEVKAKNALAHAvQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAqw 1375
Cdd:COG4717 382 EDEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEE-LLEALDEEELEEELEELEEELEELEEELEELREELA-- 456
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1316056572 1376 RSKYETDAIQRTEELEEAKKKLAQ---RLQEAEESIEAVNSKCASLEKTKQRLQGE 1428
Cdd:COG4717 457 ELEAELEQLEEDGELAELLQELEElkaELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1066-1283 |
3.60e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1066 AQESIMDLENDKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSR 1145
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1146 ELEEISERLEE-----------------AGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELG 1208
Cdd:COG4942 98 ELEAQKEELAEllralyrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316056572 1209 EQIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKAR 1283
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
918-1303 |
6.29e-09 |
|
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: 60.68 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 918 QLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLT 997
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 998 KEKKAL---QEAHQQTLDDLqaeEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLE 1074
Cdd:pfam07888 115 EEKDALlaqRAAHEARIREL---EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1075 NDKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELqarieeleeeieaeraarakvEKQRADLS--RELEEISE 1152
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN---------------------EALLEELRslQERLNASE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1153 RLEEAGGATAAQIEMNKKR-EAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEF-KM 1230
Cdd:pfam07888 251 RKVEGLGEELSSMAAQRDRtQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELqRL 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 1231 EIDDLSSNMEAV-AKAKGNLEKMCRTLedQLSEIKSKNDENVRQLNDINAQKARLQTENGE---FARQLEEKEALVS 1303
Cdd:pfam07888 331 EERLQEERMEREkLEVELGREKDCNRV--QLSESRRELQELKASLRVAQKEKEQLQAEKQElleYIRQLEQRLETVA 405
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1041-1931 |
7.66e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 61.22 E-value: 7.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1041 SLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDEKIKKKDFEiSQLLSKIEDEQSLGAQLQKKIKELQARIE 1120
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS-REIVKSYENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1121 ELEeeieAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREA-EFQKLRRDLEESTLQHEATAAALRKK 1199
Cdd:TIGR00606 266 KLD----NEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1200 QADSVAELGE-----QIDNLQRVKQKLEKEKSEFKMEIDDLSSNME-------AVAKAKGNLEKMCRTLEDQLSEIKSKN 1267
Cdd:TIGR00606 342 KTELLVEQGRlqlqaDRHQEHIRARDSLIQSLATRLELDGFERGPFserqiknFHTLVIERQEDEAKTAAQLCADLQSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1268 DENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLL 1347
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1348 REQFeeEQEAKAELQRGMSKANSEVAQWRSKYETdaiqRTEELEEAKKKLaqrlqEAEESIEAVNSKCAS---------- 1417
Cdd:TIGR00606 502 EVKS--LQNEKADLDRKLRKLDQEMEQLNHHTTT----RTQMEMLTKDKM-----DKDEQIRKIKSRHSDeltsllgyfp 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1418 ----LEKTKQRLQGEVEDLMTDVERANSLAANLDKKQ---RNFDKVLAEWKQKYEESQAELEGAQKEarslSTELFKMKN 1490
Cdd:TIGR00606 571 nkkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKnhiNNELESKEEQLSSYEDKLFDVCGSQDE----ESDLERLKE 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1491 SYEEALDQLETMKRENKNLQQEISDLTEQ----------IGETGKSIHELEK-----------AKKTVETEKSEIQAALE 1549
Cdd:TIGR00606 647 EIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvcqrVFQTEAELQEFISdlqsklrlapdKLKSTESELKKKEKRRD 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1550 EAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALRVKKKMEGDLNEM 1629
Cdd:TIGR00606 727 EMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVER 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1630 EIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMKEQVAMVERRNGLMVAEIEEL---RAALEQTERSRKVA 1706
Cdd:TIGR00606 807 KIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELkseKLQIGTNLQRRQQF 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1707 EQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQearNAEDKAKKAITDAAMMAEELKK--------EQD 1778
Cdd:TIGR00606 887 EEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS---SKETSNKKAQDKVNDIKEKVKNihgymkdiENK 963
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1779 TSAHLERMKKNLEVTVKDLQHRLDEAEnlamkggkKQLQKLEQRVRELETEVEGE--QKRGADAVKGVRKYERRVKEL-- 1854
Cdd:TIGR00606 964 IQDGKDDYLKQKETELNTVNAQLEECE--------KHQEKINEDMRLMRQDIDTQkiQERWLQDNLTLRKRENELKEVee 1035
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1855 ---TYQTEEDKKNITRLQDLVDKLQLKVKAYKR-------QAEEAEEQANSHMSRLRKVQHEMEEAQERADIAESQVNKL 1924
Cdd:TIGR00606 1036 elkQHLKEMGQMQVLQMKQEHQKLEENIDLIKRnhvlalgRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTEL 1115
|
....*..
gi 1316056572 1925 RAKSRDV 1931
Cdd:TIGR00606 1116 VNKDLDI 1122
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
904-1213 |
8.52e-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: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 904 DAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKL----------------EDECSELKKDIDDLELT--- 964
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidvasaEREIAELEAELERLDASsdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 965 LAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAktKLEQQVDDLEGSlEQ 1044
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAAALGD-AV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1045 EKKLRMDLERAKRKLEGDLKLAQESIMDL--------ENDKQQSDEKIKKKDfEISQLLSKIEDEQsLgAQLQKKIKELQ 1116
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEELERAmrafnrewPAETADLDADLESLP-EYLALLDRLEEDG-L-PEYEERFKELL 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1117 arieeleeeieaERAARAKVEKQRADLSRELEEISERLEEA---------GGATAAQIEMNKKREAEFQKLRRDLEESTL 1187
Cdd:COG4913 841 ------------NENSIEFVADLLSKLRRAIREIKERIDPLndslkripfGPGRYLRLEARPRPDPEVREFRQELRAVTS 908
|
330 340
....*....|....*....|....*.
gi 1316056572 1188 QHEATAAALRKKQADSVAELGEQIDN 1213
Cdd:COG4913 909 GASLFDEELSEARFAALKRLIERLRS 934
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1491-1918 |
1.68e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1491 SYEEALDQLETMK-RENKNLQQEISDLTEQIGE---TGKSIHELEKAKKTVETEKSEIQAALEEAEGtlEHEESKILRVQ 1566
Cdd:COG4717 50 RLEKEADELFKPQgRKPELNLKELKELEEELKEaeeKEEEYAELQEELEELEEELEELEAELEELRE--ELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1567 LELNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQ 1646
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1647 LRNVQGQLKDAQLHLDDAVRgqedmkeqvamverrnglmvaEIEELRAALEQTERSRKVAEQE--LVDASERVGLLHSQN 1724
Cdd:COG4717 208 LAELEEELEEAQEELEELEE---------------------ELEQLENELEAAALEERLKEARllLLIAAALLALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1725 SSLLNTKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEA 1804
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1805 ENLamkggKKQLQKLEQRVRELETEVEGEQK----------------RGADAVKGVRKYERRVKELTYQTEEDKKNITRL 1868
Cdd:COG4717 347 EEL-----QELLREAEELEEELQLEELEQEIaallaeagvedeeelrAALEQAEEYQELKEELEELEEQLEELLGELEEL 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1316056572 1869 QDLVDKLQLKVKA--YKRQAEEAEEQANSHMSRLRKVQHEMEEAQERADIAE 1918
Cdd:COG4717 422 LEALDEEELEEELeeLEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
856-1310 |
2.17e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 59.45 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 856 MKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEglikskiQLEAKLKETTERLEDEEE 935
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAA-------ILQTEVDALRLRLEEKES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 936 INAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQ------ 1009
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtalt 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1010 TLDDLQAEEDKV-NTLTKAKTKLEQQVDDlegSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDEKIKKKD 1088
Cdd:pfam10174 440 TLEEALSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKD 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1089 FEISQLLSKIEDEQSLGAQLQ---KKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEIsERLEEAGGATAAQI 1165
Cdd:pfam10174 517 SKLKSLEIAVEQKKEECSKLEnqlKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEV-ERLLGILREVENEK 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1166 EMNKKREAEFQKLR----RDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQK---------LEKEKSEFKMEI 1232
Cdd:pfam10174 596 NDKDKKIAELESLTlrqmKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQlqleelmgaLEKTRQELDATK 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1233 DDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIK-----------SKNDENVRQLNDINAQKARLQTENGEFARqleEKEAL 1301
Cdd:pfam10174 676 ARLSSTQQSLAEKDGHLTNLRAERRKQLEEILemkqeallaaiSEKDANIALLELSSSKKKKTQEEVMALKR---EKDRL 752
|
....*....
gi 1316056572 1302 VSQLTRGKQ 1310
Cdd:pfam10174 753 VHQLKQQTQ 761
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1199-1913 |
2.49e-08 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 58.99 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1199 KQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLS--EIKSKNDENVRQlnd 1276
Cdd:pfam07111 63 QQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAgaEMVRKNLEEGSQ--- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1277 inaqkarlqtengefaRQLEEKEAL-VSQLTRGKQAFTQQIEELKRHIEEEVKAKNAL-------AHAVQSARHDCDLLR 1348
Cdd:pfam07111 140 ----------------RELEEIQRLhQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLetkrageAKQLAEAQKEAELLR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1349 EQF---EEEQEAKAELQRGMSKANSEVAQWRSKYETDAIQRtEELEEAKKKLAQRLQEAEESIEAVNSKCASLektKQRL 1425
Cdd:pfam07111 204 KQLsktQEELEAQVTLVESLRKYVGEQVPPEVHSQTWELER-QELLDTMQHLQEDRADLQATVELLQVRVQSL---THML 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1426 QGEVEDLMTDVERANSLAANLDKKQRNfdkVLAEWKQKYEESQAELEGAQKEARSlstelfkmknsyeealdqletmkrE 1505
Cdd:pfam07111 280 ALQEEELTRKIQPSDSLEPEFPKKCRS---LLNRWREKVFALMVQLKAQDLEHRD------------------------S 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1506 NKNLQQEISDLTEQIGETGKsihelekakktvetEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDE 1585
Cdd:pfam07111 333 VKQLRGQVAELQEQVTSQSQ--------------EQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTAS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1586 EMEQIKrnsqRVIDSMQSTLDaevrsrndalrvkkKMEGDLNEME---IQLSHANRQAAEAQKQLRNVQG----QLKDAQ 1658
Cdd:pfam07111 399 AEEQLK----FVVNAMSSTQI--------------WLETTMTRVEqavARIPSLSNRLSYAVRKVHTIKGlmarKVALAQ 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1659 LHLDDAvrgqeDMKEQVAMVERRNGLMVAEIEELRAALE-QTERSRKVAEQELVDASERVgllHSQNSSLLNTKKKLETD 1737
Cdd:pfam07111 461 LRQESC-----PPPPPAPPVDADLSLELEQLREERNRLDaELQLSAHLIQQEVGRAREQG---EAERQQLSEVAQQLEQE 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1738 LVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQdtsahlERMKKNLEVTVKDLQHRLDEaenlamkggkkQLQ 1817
Cdd:pfam07111 533 LQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQ------EIYGQALQEKVAEVETRLRE-----------QLS 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1818 KLEQRVRELETEvegeqkrGADAVKGVRKYERRVKeltyQTEEDKKNITRLQDLVDKLQLKVKAykRQAEEAEEQANSHM 1897
Cdd:pfam07111 596 DTKRRLNEARRE-------QAKAVVSLRQIQHRAT----QEKERNQELRRLQDEARKEEGQRLA--RRVQELERDKNLML 662
|
730
....*....|....*.
gi 1316056572 1898 SRLRKVQHEMEEAQER 1913
Cdd:pfam07111 663 ATLQQEGLLSRYKQQR 678
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1495-1717 |
4.99e-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: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1495 ALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKS 1574
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1575 EIDRKLAEKDEEMEQIKRNSQR----VIDSMQSTLDAEVRSR--NDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLR 1648
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQpplaLLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316056572 1649 NVQGQLKDAQLHLDDAVRGQEDMkeqVAMVERRNGLMVAEIEELRAALEQTERSRKVAEQELVDASERV 1717
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
871-1909 |
5.50e-08 |
|
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: 58.52 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 871 LAKKKELEEKMVSLLQEKNDlqlQVASEVENLSDAEERCEGLIKSKIqlEAKLKETTERLEDEEEINAELTAKKRKLEDE 950
Cdd:TIGR01612 499 LMRMKDFKDIIDFMELYKPD---EVPSKNIIGFDIDQNIKAKLYKEI--EAGLKESYELAKNWKKLIHEIKKELEEENED 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 951 CSELKKDIDDLELTLAKVEKE-------KHATENKVKNLTEE-------------MATQDEAIAKLTKE----------- 999
Cdd:TIGR01612 574 SIHLEKEIKDLFDKYLEIDDEiiyinklKLELKEKIKNISDKneyikkaidlkkiIENNNAYIDELAKIspyqvpehlkn 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1000 --------KKALQEAHQQTLDDLQAE-------------EDKVNtLTKAKTKLEQQVDDLEGSLEQEKKLRM-DLERAKR 1057
Cdd:TIGR01612 654 kdkiystiKSELSKIYEDDIDALYNElssivkenaidntEDKAK-LDDLKSKIDKEYDKIQNMETATVELHLsNIENKKN 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1058 KLEGDLKLAQESIM-DLENDKQQSDEKIKKKDFEISqllSKIEDEQSLGAQLQK---KIKELQARIEELEEEIEAERAAR 1133
Cdd:TIGR01612 733 ELLDIIVEIKKHIHgEINKDLNKILEDFKNKEKELS---NKINDYAKEKDELNKyksKISEIKNHYNDQINIDNIKDEDA 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1134 akveKQRADLSRELEEISERLEEAGGATAAQIEMNK----KREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAElge 1209
Cdd:TIGR01612 810 ----KQNYDKSKEYIKTISIKEDEIFKIINEMKFMKddflNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISD--- 882
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1210 qiDNLQRVKQKLEKEKS---EFKMEIDDLSSNMEAVAKAKGNLeKMCRTLEDQLSEIKSKNDenvrQLNDINAQKARLQT 1286
Cdd:TIGR01612 883 --DKLNDYEKKFNDSKSlinEINKSIEEEYQNINTLKKVDEYI-KICENTKESIEKFHNKQN----ILKEILNKNIDTIK 955
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1287 ENGEFARQLEEK--EALVSQLTRGKQAFTQ-QIEELKRHIEEEVKAKNALAHAVQSARHdcDLLREQFEEEQEAKAELQR 1363
Cdd:TIGR01612 956 ESNLIEKSYKDKfdNTLIDKINELDKAFKDaSLNDYEAKNNELIKYFNDLKANLGKNKE--NMLYHQFDEKEKATNDIEQ 1033
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1364 GMSKANSEVAQWRSKYETDAIQRTEELEEAKKKLAQRLQeaEESIEAVNSKCASLEKTKQRLQ-------GEVEDL--MT 1434
Cdd:TIGR01612 1034 KIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLN--KEILEEAEINITNFNEIKEKLKhynfddfGKEENIkyAD 1111
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1435 DVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKN--SYEEALDQLETMKRENKNLQQE 1512
Cdd:TIGR01612 1112 EINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDpeEIEKKIENIVTKIDKKKNIYDE 1191
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1513 ISDLTEQIGETGKSIHELEKAKKtvetekseIQAALEEAEGTLEHEeskilrvQLELNQVKSEIDRKLAEKD-EEMEQIK 1591
Cdd:TIGR01612 1192 IKKLLNEIAEIEKDKTSLEEVKG--------INLSYGKNLGKLFLE-------KIDEEKKKSEHMIKAMEAYiEDLDEIK 1256
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1592 RNSQRVIDSMQSTLD--AEVRSRNDALRVKKKME----------GDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQL 1659
Cdd:TIGR01612 1257 EKSPEIENEMGIEMDikAEMETFNISHDDDKDHHiiskkhdeniSDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQK 1336
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1660 HLDDAVRGQEDMKEQVAMVERRNGLMVaeIEELRAALEQTERSRKVAEQELvDASERVGLLHSQNSSLLNTKKKLETDLv 1739
Cdd:TIGR01612 1337 HNSDINLYLNEIANIYNILKLNKIKKI--IDEVKEYTKEIEENNKNIKDEL-DKSEKLIKKIKDDINLEECKSKIESTL- 1412
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1740 qVQGEVDDAVQearNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKL 1819
Cdd:TIGR01612 1413 -DDKDIDECIK---KIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINEL 1488
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1820 EQRV---RELETEVEGEQKRGADAVKGVRKYERRVKEL--TYQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQAN 1894
Cdd:TIGR01612 1489 KEHIdksKGCKDEADKNAKAIEKNKELFEQYKKDVTELlnKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSE 1568
|
1130
....*....|....*
gi 1316056572 1895 SHMSRLRKVQHEMEE 1909
Cdd:TIGR01612 1569 QKIKEIKKEKFRIED 1583
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1348-1632 |
6.84e-08 |
|
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: 57.83 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1348 REQFEEEQEAKA-ELQRGMSKANSEVAQWR---------SKYETDAIQRTEELE----EAKKKLAQRLQEAEESIEAvnS 1413
Cdd:pfam17380 298 QERLRQEKEEKArEVERRRKLEEAEKARQAemdrqaaiyAEQERMAMERERELErirqEERKRELERIRQEEIAMEI--S 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1414 KCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQaelEGAQKEARSLStelfkmknsyE 1493
Cdd:pfam17380 376 RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLE----------E 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1494 EALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKK----TVETEKSEIQAALEEAEGTLEHEESKILRVQLEL 1569
Cdd:pfam17380 443 ERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRdrkrAEEQRRKILEKELEERKQAMIEEERKRKLLEKEM 522
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 1570 ----NQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTldAEVRSRNDALRVKKKMEGDLNEMEIQ 1632
Cdd:pfam17380 523 eerqKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA--TEERSRLEAMEREREMMRQIVESEKA 587
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
914-1272 |
8.04e-08 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 57.46 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 914 KSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDD-LELTLAKVE-----------KEKHATENKVKN 981
Cdd:pfam09731 86 KKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEvLKEAISKAEsatavakeakdDAIQAVKAHTDS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 982 LTEEMATQDEAIAK-----LTKEKKALQEAHQQTLDDLQAEEDKVN-TLTKAKTKLEQQVDDL---EGSLEQEKKLRMDL 1052
Cdd:pfam09731 166 LKEASDTAEISREKatdsaLQKAEALAEKLKEVINLAKQSEEEAAPpLLDAAPETPPKLPEHLdnvEEKVEKAQSLAKLV 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1053 ERAK-RKLEGDLKLAQE--SIMDLENDKQQSDEKIKKKDFEisqllSKIEDEQSLGAQLQKKIKELQARIEELEEEieae 1129
Cdd:pfam09731 246 DQYKeLVASERIVFQQElvSIFPDIIPVLKEDNLLSNDDLN-----SLIAHAHREIDQLSKKLAELKKREEKHIER---- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1130 raaraKVEKQRADLSRELEEISERLEEAGGATAAQIEmnKKREAEFQKLRRDLEES---TLQHEATAAALRKKQADSVAE 1206
Cdd:pfam09731 317 -----ALEKQKEELDKLAEELSARLEEVRAADEAQLR--LEFEREREEIRESYEEKlrtELERQAEAHEEHLKDVLVEQE 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316056572 1207 LGEQIDNLQRVKQKLEKEKSEFKmeiddlssnmEAVAKAKGNLekmcRTLEDQLSEIKSKNDENVR 1272
Cdd:pfam09731 390 IELQREFLQDIKEKVEEERAGRL----------LKLNELLANL----KGLEKATSSHSEVEDENRK 441
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1386-1908 |
1.76e-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: 56.57 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1386 RTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTdveRANSLAANLDKKQRNFDKVLAEWKQKYE 1465
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQ---QIKDLNDKLKKNKDKINKLNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1466 ESQAELEGAQKearsLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQ 1545
Cdd:TIGR04523 111 EIKNDKEQKNK----LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1546 AALEEAEGTLEHEE-----------------SKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQS----- 1603
Cdd:TIGR04523 187 KNIDKIKNKLLKLElllsnlkkkiqknksleSQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEqnkik 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1604 -TLDAEVRSRNDALRVKKKMEGDLNEMEIQLSHANRQAA-----EAQKQLRNVQGQLKDAQLHLDDAVRGQEDMKEQvam 1677
Cdd:TIGR04523 267 kQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQ--- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1678 verrnglmvaeIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAED 1757
Cdd:TIGR04523 344 -----------ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1758 KAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLaMKGGKKQLQKLEQRVRELETEVEGEQKRG 1837
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT-RESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316056572 1838 ADAVKGVRKYERRVKELTYQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEME 1908
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE 562
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1428-1621 |
1.83e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.16 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1428 EVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMK--RE 1505
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1506 NKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEeskilrvqlelnqvKSEIDRKLAEKDE 1585
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK--------------KAELDEELAELEA 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1316056572 1586 EMEQIKRNSQRVIdsmqSTLDAEVRSRNDALRVKKK 1621
Cdd:COG1579 157 ELEELEAEREELA----AKIPPELLALYERIRKRKN 188
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
852-1412 |
2.49e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.06 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 852 ELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVaSEVENLSDAEERCEGLIK---SKIQLE----AKLK 924
Cdd:PRK01156 198 ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSAL-NELSSLEDMKNRYESEIKtaeSDLSMEleknNYYK 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 925 ETTERLedeEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIakltkEKKALQ 1004
Cdd:PRK01156 277 ELEERH---MKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYI-----KKKSRY 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1005 EAHQQTLDDLQAEEDKVNTLTKaktkleqQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDEKI 1084
Cdd:PRK01156 349 DDLNNQILELEGYEMDYNSYLK-------SIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1085 KKKdfeISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQ 1164
Cdd:PRK01156 422 SSK---VSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEK 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1165 IEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDnlqrvkqKLEKEKSEFK-MEIDDLSSNMEAVA 1243
Cdd:PRK01156 499 IVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHD-------KYEEIKNRYKsLKLEDLDSKRTSWL 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1244 KAKGNLEKM-CRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRH 1322
Cdd:PRK01156 572 NALAVISLIdIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGK 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1323 IeEEVKAKNALAHAVQSARHDcdlLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYETDaIQRTEELEEAKKKLAQRLQ 1402
Cdd:PRK01156 652 I-DNYKKQIAEIDSIIPDLKE---ITSRINDIEDNLKKSRKALDDAKANRARLESTIEIL-RTRINELSDRINDINETLE 726
|
570
....*....|
gi 1316056572 1403 EAEESIEAVN 1412
Cdd:PRK01156 727 SMKKIKKAIG 736
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
949-1200 |
2.80e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 949 DECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQeahqqtlDDLQAEEDKVNTLTKAK 1028
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE-------QELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1029 TKLEQQVDDLEGSLeqeKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDEKIKkkdfeisQLLSKIEDEQSLGAQL 1108
Cdd:COG4942 93 AELRAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP-------ARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1109 QKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQ 1188
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|..
gi 1316056572 1189 HEATAAALRKKQ 1200
Cdd:COG4942 243 TPAAGFAALKGK 254
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1240-1474 |
2.93e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1240 EAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEEL 1319
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1320 KRHIEEEVKAknalahAVQSARHDcdllREQFEEEQEAKAELQRgMSKANSEVAQWRSKYETDAIQRTEELEEAKKKLAQ 1399
Cdd:COG4942 103 KEELAELLRA------LYRLGRQP----PLALLLSPEDFLDAVR-RLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316056572 1400 RLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGA 1474
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1429-1927 |
3.32e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.68 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1429 VEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKM------KNSYEEALDQLETM 1502
Cdd:PRK01156 185 IDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELssledmKNRYESEIKTAESD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1503 KRENKNLQQEISDLTEQ---------------IGETGKSIHELEKAKKTVETEKSEIQ---AALEEAEgTLEHEESKILR 1564
Cdd:PRK01156 265 LSMELEKNNYYKELEERhmkiindpvyknrnyINDYFKYKNDIENKKQILSNIDAEINkyhAIIKKLS-VLQKDYNDYIK 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1565 VQLELNQVKSEIDrklaekdeEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQ 1644
Cdd:PRK01156 344 KKSRYDDLNNQIL--------ELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1645 KQLRNVQGQLKDAQLHLDDAVRGQEDMKEQVAMVERRNGLMVA------------------EIEELRAALEQTERSRKVA 1706
Cdd:PRK01156 416 VKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCgttlgeeksnhiinhyneKKSRLEEKIREIEIEVKDI 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1707 EQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDTSaHLERM 1786
Cdd:PRK01156 496 DEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTS-WLNAL 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1787 KKNLEVTVKDLQHRLDEAenlamkggKKQLQKLEQRVRELETEVEgeqkrgaDAVKGVRKYERRVKELTYQTEEDKKNIT 1866
Cdd:PRK01156 575 AVISLIDIETNRSRSNEI--------KKQLNDLESRLQEIEIGFP-------DDKSYIDKSIREIENEANNLNNKYNEIQ 639
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316056572 1867 RLQDLVDKLQLKVKAYKRQA---EEAEEQANSHMSRLRKVQHEMEEAQERADIAESQVNKLRAK 1927
Cdd:PRK01156 640 ENKILIEKLRGKIDNYKKQIaeiDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLEST 703
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1241-1479 |
3.34e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1241 AVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELK 1320
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1321 RHIEEEvkaKNALAhavqsarhdcDLLREQFEEEQEAKAELqrGMSKANSEVAQWRSKYETDAIQRTEELEEAKKKLAQR 1400
Cdd:COG4942 97 AELEAQ---KEELA----------ELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316056572 1401 LQEAEESIEAvnsKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEAR 1479
Cdd:COG4942 162 LAALRAELEA---ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1326-1912 |
3.44e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.68 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1326 EVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYE--TDAIQRTEELEEAKKKLaqrlqe 1403
Cdd:PRK01156 181 EISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDMKNRY------ 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1404 aEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSt 1483
Cdd:PRK01156 255 -ESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1484 ELFKMKNSYEEaldqletMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKil 1563
Cdd:PRK01156 333 VLQKDYNDYIK-------KKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEID-- 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1564 rvQLELNQVKSEIDRKLAEKDEEMEqikrNSQRVIDSMQSTLDaEVRSRNDALRVKKKME---GDLNEMEIQ--LSHANR 1638
Cdd:PRK01156 404 --PDAIKKELNEINVKLQDISSKVS----SLNQRIRALRENLD-ELSRNMEMLNGQSVCPvcgTTLGEEKSNhiINHYNE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1639 QAAEAQKQLRNVQGQLKDaqlhLDDAVRGQEDMKEQVAMVE-RRNGLMVAEIEELRAALEQTERSrkvaEQELVDASERV 1717
Cdd:PRK01156 477 KKSRLEEKIREIEIEVKD----IDEKIVDLKKRKEYLESEEiNKSINEYNKIESARADLEDIKIK----INELKDKHDKY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1718 GLLHSQNSSL----LNTKKKLETDLVQVQGEVDdaVQEARNAEDKAKKAITDAAMMAEELKKE-QDTSAHLERMKKNLEV 1792
Cdd:PRK01156 549 EEIKNRYKSLkledLDSKRTSWLNALAVISLID--IETNRSRSNEIKKQLNDLESRLQEIEIGfPDDKSYIDKSIREIEN 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1793 TVKDLQHRLDEAEnlAMKGGKKQLQKLEQRVRELETEVEGEQKRGADAVKGVRKYERRVKELTYQTEEDKKNITRLQDLV 1872
Cdd:PRK01156 627 EANNLNNKYNEIQ--ENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTI 704
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1316056572 1873 DKLQLKVKAYKRQAEEAEEQANShMSRLRKVQHEMEEAQE 1912
Cdd:PRK01156 705 EILRTRINELSDRINDINETLES-MKKIKKAIGDLKRLRE 743
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1455-1659 |
3.94e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1455 KVLAEWKQKYEESQAEL--EGAQKEARSLSTELFKMKNSYEEALDQLETMKRENK--NLQQEISDLTEQIGETGKSIHEL 1530
Cdd:COG3206 152 AVANALAEAYLEQNLELrrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1531 EKAKKTVETEKSEIQAALEEAEGTLE--HEESKILRVQLELNQVKSEIDRKL--------------AEKDEEMEQIKRNS 1594
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPelLQSPVIQQLRAQLAELEAELAELSarytpnhpdvialrAQIAALRAQLQQEA 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1595 QRVIDSMQSTLDAeVRSRNDALR-----VKKKMEgDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQL 1659
Cdd:COG3206 312 QRILASLEAELEA-LQAREASLQaqlaqLEARLA-ELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1018-1259 |
4.40e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1018 EDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESImdlenDKQQSDEKIKkkdfEISQLLSK 1097
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIA----ELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1098 IEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQiemnkkREAEFQK 1177
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE------LRALLEE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1178 LRRDLEEstlqhEATAAALRKKQADSVAELGEQIDNL-QRVKQKLEKEKSEFKMEIDDLSSNMEAVAKakgnLEKMCRTL 1256
Cdd:COG4913 754 RFAAALG-----DAVERELRENLEERIDALRARLNRAeEELERAMRAFNREWPAETADLDADLESLPE----YLALLDRL 824
|
...
gi 1316056572 1257 EDQ 1259
Cdd:COG4913 825 EED 827
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1488-1931 |
4.62e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.84 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1488 MKNSYEEALDQLETMKRE--NKNLQQEISDLTE--QIGETGKSIHELEKAKKTVETEK-SEIQAALEEAEGTLE-----H 1557
Cdd:PRK04778 23 LRKRNYKRIDELEERKQEleNLPVNDELEKVKKlnLTGQSEEKFEEWRQKWDEIVTNSlPDIEEQLFEAEELNDkfrfrK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1558 EESKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQRV------IDSMQSTLDAEVRSRNDALrvkKKMEGDLNEMEI 1631
Cdd:PRK04778 103 AKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVeqlkdlYRELRKSLLANRFSFGPAL---DELEKQLENLEE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1632 QLSHANR--------QAAEAQKQLRNVQGQLkdaqlhlddavrgQEDMKEQVAMVERRNGLMVAEIEELRAALEQTERSR 1703
Cdd:PRK04778 180 EFSQFVEltesgdyvEAREILDQLEEELAAL-------------EQIMEEIPELLKELQTELPDQLQELKAGYRELVEEG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1704 KVAEQELVDasERVGLLHSQNSSLLNTKKKLETD-----LVQVQGEVDDAVQ------EARNAEDKAKKAITDAAMMAEE 1772
Cdd:PRK04778 247 YHLDHLDIE--KEIQDLKEQIDENLALLEELDLDeaeekNEEIQERIDQLYDilerevKARKYVEKNSDTLPDFLEHAKE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1773 LKKEqdTSAHLERMKKNLEVT------VKDLQHRLDEAENL------AMKGGKKQLQKLEQRVRELE---TEVEGEQKRG 1837
Cdd:PRK04778 325 QNKE--LKEEIDRVKQSYTLNeselesVRQLEKQLESLEKQydeiteRIAEQEIAYSELQEELEEILkqlEEIEKEQEKL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1838 ADAVKGVRKYERRVKELTYQTEEDKKNITRlqdLVDKLQLKV--KAYKRQAEEAEEQANSHMSRLRKVQHEMEEAQERAD 1915
Cdd:PRK04778 403 SEMLQGLRKDELEAREKLERYRNKLHEIKR---YLEKSNLPGlpEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLE 479
|
490
....*....|....*.
gi 1316056572 1916 IAESQVNKLRAKSRDV 1931
Cdd:PRK04778 480 EATEDVETLEEETEEL 495
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1042-1495 |
4.72e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1042 LEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDEKIKKkdfeISQLLSKIEDEQSLgAQLQKKIKELQARIEE 1121
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK----LEKLLQLLPLYQEL-EALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1122 LEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQA 1201
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1202 DSVAELgeqidNLQRVKQKLEKEKSEFK------------MEIDDLSSNMEAVAKAKGNLekmcrtLEDQLSEIKSKNDE 1269
Cdd:COG4717 231 QLENEL-----EAAALEERLKEARLLLLiaaallallglgGSLLSLILTIAGVLFLVLGL------LALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1270 NVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLRE 1349
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1350 QFEEEQE--AKAELQRGMSKANSEVAQWRSKYETDAIQRTEELEEAKKK-LAQRLQEAEESIEAVNSKCASLEKTKQRLQ 1426
Cdd:COG4717 380 GVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeLEEELEELEEELEELEEELEELREELAELE 459
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316056572 1427 GEVEDLMTDVEranslaanldkkqrnfdkvLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEA 1495
Cdd:COG4717 460 AELEQLEEDGE-------------------LAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1137-1872 |
5.07e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.34 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1137 EKQR-ADLSRELEEISER---LEEAGGATAA--QIEMNKKREAE-FQKLRRDLEESTLQHEAtaaalrkkQADSVAELGE 1209
Cdd:COG3096 304 EQYRlVEMARELEELSAResdLEQDYQAASDhlNLVQTALRQQEkIERYQEDLEELTERLEE--------QEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1210 QIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEA----------VAKAKGNLEKMCR-------TLEDQLSEIKSKNDENVR 1272
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLADYQQALDVqqtraiqyqqAVQALEKARALCGlpdltpeNAEDYLAAFRAKEQQATE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1273 QLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGkQAFTQQIEELKRHIEEEvkaknALAHAVQSARHDCDLLREQFE 1352
Cdd:COG3096 456 EVLELEQKLSVADAARRQFEKAYELVCKIAGEVERS-QAWQTARELLRRYRSQQ-----ALAQRLQQLRAQLAELEQRLR 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1353 EEQEAKAELQRGMSKANSEVaqwrskyeTDAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQgEVEDL 1432
Cdd:COG3096 530 QQQNAERLLEEFCQRIGQQL--------DAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIK-ELAAR 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1433 ----MTDVERANSLAANLDKKQRNFDKVLA----------EWKQKYEESQAELEGAQKEARSLS-------TELFKMKNS 1491
Cdd:COG3096 601 apawLAAQDALERLREQSGEALADSQEVTAamqqllererEATVERDELAARKQALESQIERLSqpggaedPRLLALAER 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1492 -------------------YEEAL----------DQLETMKRENKNLQQEISDLTEQIGET---GKSIHELEKAKKTVET 1539
Cdd:COG3096 681 lggvllseiyddvtledapYFSALygparhaivvPDLSAVKEQLAGLEDCPEDLYLIEGDPdsfDDSVFDAEELEDAVVV 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1540 EKSEIQ--------------AALEEAEGTLEHEeskilrvqlelnqvKSEIDRKLAEKDEEMEQIKR----NSQRVIDSM 1601
Cdd:COG3096 761 KLSDRQwrysrfpevplfgrAAREKRLEELRAE--------------RDELAEQYAKASFDVQKLQRlhqaFSQFVGGHL 826
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1602 QSTLD----AEVRSRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKdaqlHLDDAVRGQ--EDMKEQV 1675
Cdd:COG3096 827 AVAFApdpeAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAN----LLADETLADrlEELREEL 902
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1676 AMVE------RRNGLMVAEIEELRAALEQT---------ERSRKVAEQELVDA-----------------SERVGLLhSQ 1723
Cdd:COG3096 903 DAAQeaqafiQQHGKALAQLEPLVAVLQSDpeqfeqlqaDYLQAKEQQRRLKQqifalsevvqrrphfsyEDAVGLL-GE 981
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1724 NSSLlntKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKdlqhrlDE 1803
Cdd:COG3096 982 NSDL---NEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQAD------AE 1052
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316056572 1804 AENLA---MKGGKKQLQKLEQRVRELETEV---EGEQKrgaDAVKGVRKYERRVKELTYQTEEDKKNITRLQDLV 1872
Cdd:COG3096 1053 AEERArirRDELHEELSQNRSRRSQLEKQLtrcEAEMD---SLQKRLRKAERDYKQEREQVVQAKAGWCAVLRLA 1124
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1296-1779 |
6.52e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1296 EEKEALVSQLTRGKQAFTQQIEELkrhiEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQW 1375
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKEL----EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1376 rskyetDAIQRTEELEEAKKKLAQRLQEAEESIEAVnskcASLEKTKQRLQGEVEDLMTDVERAnslaanldkkqrnfdk 1455
Cdd:COG4717 129 ------PLYQELEALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEEL---------------- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1456 vlaeWKQKYEESQAELEGAQKEarslstelfkmknsYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKK 1535
Cdd:COG4717 183 ----LEQLSLATEEELQDLAEE--------------LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1536 TVETEKS-EIQAALEEAEGTLEHEESKILRV-------------QLELNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSM 1601
Cdd:COG4717 245 LKEARLLlLIAAALLALLGLGGSLLSLILTIagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1602 QSTLDAEVRSRNDALRVKKKMEGDLNEMEIQLSHANRQAA-----EAQKQLRNVQGQLKDAQL-----HLDDAVRGQEDM 1671
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleQEIAALLAEAGVEDEEELraaleQAEEYQELKEEL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1672 KEQVAMVERRNGLMVAEI-----EELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLNtkkklETDLVQVQGEVD 1746
Cdd:COG4717 405 EELEEQLEELLGELEELLealdeEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELE 479
|
490 500 510
....*....|....*....|....*....|...
gi 1316056572 1747 DAVQEARNAEDKAKKAITDAAMMAEELKKEQDT 1779
Cdd:COG4717 480 ELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
845-1059 |
7.46e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 845 KSAETEKELQNMKENYEKMQSDLttalakkKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAKLK 924
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKEL-------AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 925 ETTERLEDEEEINAELTAKKRKLEDECS-------------------------ELKKDIDDLELTLAKVEKEKHATENKV 979
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPlalllspedfldavrrlqylkylapARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 980 KNLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQ--EKKLRMDLERAKR 1057
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAaaERTPAAGFAALKG 253
|
..
gi 1316056572 1058 KL 1059
Cdd:COG4942 254 KL 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
860-1501 |
8.30e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 860 YEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIkskiqlEAKLKETTERLED-EEEInA 938
Cdd:COG4913 276 YLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELE------AQIRGNGGDRLEQlEREI-E 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 939 ELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAEe 1018
Cdd:COG4913 349 RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1019 dkvntltkaKTKLEQQVDDLEGSLEQekkLRMDLERAKRKLEGDLKLAQE--SIMDLENDKQQSDEK----------IKK 1086
Cdd:COG4913 428 ---------IASLERRKSNIPARLLA---LRDALAEALGLDEAELPFVGEliEVRPEEERWRGAIERvlggfaltllVPP 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1087 KDFeiSQLLSKIEDEQsLGAQLQkkIKELQARIEELEEEIEAERAARAKVE----KQRADLSRELEEIS-----ERLEEA 1157
Cdd:COG4913 496 EHY--AAALRWVNRLH-LRGRLV--YERVRTGLPDPERPRLDPDSLAGKLDfkphPFRAWLEAELGRRFdyvcvDSPEEL 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1158 GGATAA-----QIEMNKKReaeFQKLRRDLEESTLQHEATAAALrkkqadsVAELGEQIDNLQRVKQKLEKEKSEFKMEI 1232
Cdd:COG4913 571 RRHPRAitragQVKGNGTR---HEKDDRRRIRSRYVLGFDNRAK-------LAALEAELAELEEELAEAEERLEALEAEL 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1233 DDLSSNMEAvakakgnlekmCRTLEDQLSEIKsKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVsqltrgkqaf 1312
Cdd:COG4913 641 DALQERREA-----------LQRLAEYSWDEI-DVASAEREIAELEAELERLDASSDDLAALEEQLEELE---------- 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1313 tQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRgmskanSEVAQWRSKYETDAIQRT--EEL 1390
Cdd:COG4913 699 -AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR------ALLEERFAAALGDAVERElrENL 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1391 EEAKKKLAQRLQEAEESIEAVnskcasLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNfdkVLAEWKQKYEESQAE 1470
Cdd:COG4913 772 EERIDALRARLNRAEEELERA------MRAFNREWPAETADLDADLESLPEYLALLDRLEED---GLPEYEERFKELLNE 842
|
650 660 670
....*....|....*....|....*....|.
gi 1316056572 1471 LEGaqkeaRSLSTELFKMKNSYEEALDQLET 1501
Cdd:COG4913 843 NSI-----EFVADLLSKLRRAIREIKERIDP 868
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1281-1651 |
9.11e-07 |
|
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: 53.75 E-value: 9.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1281 KARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAE 1360
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1361 LqrgmskanSEVAQWRSKYETDAIQRTEELEEAKKKLAQRLQEAEesieavnskcASLEKTKQRlqgevedlmtdVERAN 1440
Cdd:pfam07888 113 L--------SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE----------TELERMKER-----------AKKAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1441 SLaanldkkqrnfdkvLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETmkrenknLQQEISDLTEQI 1520
Cdd:pfam07888 164 AQ--------------RKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1521 GETGKSIHELEKAKKTVETEKSEIQAALEEAEG---TLEHEESKILRVQLELNQVK---SEIDRKLAEKDEEMEQIKRNS 1594
Cdd:pfam07888 223 TTAHRKEAENEALLEELRSLQERLNASERKVEGlgeELSSMAAQRDRTQAELHQARlqaAQLTLQLADASLALREGRARW 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 1595 QRVIDSMQSTLDA--------------------EVRSRNDALRVKKKMEGDLNemEIQLSHANRQAAEAQKQLRNVQ 1651
Cdd:pfam07888 303 AQERETLQQSAEAdkdrieklsaelqrleerlqEERMEREKLEVELGREKDCN--RVQLSESRRELQELKASLRVAQ 377
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1135-1334 |
1.02e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1135 KVEKQRADLSRELEEISERLEEAggatAAQIEmnkKREAEFQKLRRDLEESTLQHEATAAALrKKQADSVAELGEQIDNL 1214
Cdd:COG3883 34 AAQAELDALQAELEELNEEYNEL----QAELE---ALQAEIDKLQAEIAEAEAEIEERREEL-GERARALYRSGGSVSYL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1215 QRVkqkLEKEksefkmEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQ 1294
Cdd:COG3883 106 DVL---LGSE------SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1316056572 1295 LEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALA 1334
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
870-1086 |
1.17e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 870 ALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLED 949
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 950 ECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKT 1029
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 1030 KLEQQVDDLEGSLEQEKKLRmdlERAKRKLEGDLKLAQESIMDLENDKQQSDEKIKK 1086
Cdd:COG4942 178 ALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1247-1699 |
1.69e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 53.29 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1247 GNLEKMCRTLEDQLSEIKSKND-------ENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEEL 1319
Cdd:pfam10174 243 SSLERNIRDLEDEVQMLKTNGLlhtedreEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDC 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1320 KRHIE---EEVKAKNALAHAVQSarhDCDLLREQFEEEQEAKAElqrgmskansevaqwrskyETDAIQRteeLEEAKKK 1396
Cdd:pfam10174 323 KQHIEvlkESLTAKEQRAAILQT---EVDALRLRLEEKESFLNK-------------------KTKQLQD---LTEEKST 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1397 LAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQK 1476
Cdd:pfam10174 378 LAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1477 EARSLSTELfkmknsyeeaLDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLE 1556
Cdd:pfam10174 458 QREREDRER----------LEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1557 H--EESKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSmQSTLDAEVRSRNDALR----VKKKMEGDLNEME 1630
Cdd:pfam10174 528 QkkEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEE-SGKAQAEVERLLGILRevenEKNDKDKKIAELE 606
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316056572 1631 iqlSHANRQAAEAQKQLRNV----QGQLKDAQLHLDDAVRGQEDMKEQVAMVerrnglmvaEIEELRAALEQT 1699
Cdd:pfam10174 607 ---SLTLRQMKEQNKKVANIkhgqQEMKKKGAQLLEEARRREDNLADNSQQL---------QLEELMGALEKT 667
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1668-1916 |
1.93e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1668 QEDMKEQVAMVERRNGLMVAEIEELRAALEQTERSRKV--AEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEV 1745
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1746 DdAVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEV---TVKDLQHRLDEAEnlamkggkKQLQKLEQR 1822
Cdd:COG3206 243 A-ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALR--------AQLQQEAQR 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1823 VR-ELETEVEGEQKRGADAVKGVRKYERRVKELTyqteedkknitrlqdlvdKLQLKVKAYKRQAEEAEEQANSHMSRLR 1901
Cdd:COG3206 314 ILaSLEAELEALQAREASLQAQLAQLEARLAELP------------------ELEAELRRLEREVEVARELYESLLQRLE 375
|
250
....*....|....*
gi 1316056572 1902 KVQheMEEAQERADI 1916
Cdd:COG3206 376 EAR--LAEALTVGNV 388
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1687-1923 |
2.15e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1687 AEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDA 1766
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1767 AMMAE----ELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAenlamkggKKQLQKLEQRVRELETEVEgeqkrgadavk 1842
Cdd:COG4942 114 YRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL--------RADLAELAALRAELEAERA----------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1843 gvrKYERRVKELTYQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEEAQERADIAESQVN 1922
Cdd:COG4942 175 ---ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
.
gi 1316056572 1923 K 1923
Cdd:COG4942 252 K 252
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1269-1582 |
2.18e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 51.84 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1269 ENVRQLNDINA---QKAR-LQTENGEFARQLEEKEALVS-QLTRGKQAFTQQIEELKRHIEEEVKAKnalahavqsarhd 1343
Cdd:pfam00038 4 EQLQELNDRLAsyiDKVRfLEQQNKLLETKISELRQKKGaEPSRLYSLYEKEIEDLRRQLDTLTVER------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1344 cdllreqfeeeqeAKAELQRGmsKANSEVAQWRSKYETDAIQRTeELEEAKKKLAQRLQEA-------EESIEAVNSKCA 1416
Cdd:pfam00038 71 -------------ARLQLELD--NLRLAAEDFRQKYEDELNLRT-SAENDLVGLRKDLDEAtlarvdlEAKIESLKEELA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1417 SLEKTKQR----LQGEVEDLMTDVERANSLAANLdkkqrnfDKVLAEWKQKYEEsQAELEGAQKEarslstELFKMKnsY 1492
Cdd:pfam00038 135 FLKKNHEEevreLQAQVSDTQVNVEMDAARKLDL-------TSALAEIRAQYEE-IAAKNREEAE------EWYQSK--L 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1493 EEALDQLETMKRENKNLQQEISDLTEQIgeTGKSIhELEKAKKTveteKSEIQAALEEAEGTLEHE----ESKILRVQLE 1568
Cdd:pfam00038 199 EELQQAAARNGDALRSAKEEITELRRTI--QSLEI-ELQSLKKQ----KASLERQLAETEERYELQladyQELISELEAE 271
|
330
....*....|....
gi 1316056572 1569 LNQVKSEIDRKLAE 1582
Cdd:pfam00038 272 LQETRQEMARQLRE 285
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1067-1700 |
2.22e-06 |
|
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: 52.82 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1067 QESIMDLENDKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIeeleeeieaeraarakvekqradlsre 1146
Cdd:pfam05557 5 IESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRI--------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1147 lEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQhEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKS 1226
Cdd:pfam05557 58 -RLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQ-LADAREVISCLKNELSELRRQIQRAELELQSTNSELE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1227 EFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQ------LNDINAQKARLQTENGEFARQLEEKEA 1300
Cdd:pfam05557 136 ELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQeqdseiVKNSKSELARIPELEKELERLREHNKH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1301 LvSQLTRGKQAFTQQIEELKRHIeeevkaknalahavqsarhdcdllrEQFEEEQEAKAELQRGMSKANSEVAQWRSKYE 1380
Cdd:pfam05557 216 L-NENIENKLLLKEEVEDLKRKL-------------------------EREEKYREEAATLELEKEKLEQELQSWVKLAQ 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1381 TDA--IQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGE-------VEDLMTDVERANSLAANLDK--- 1448
Cdd:pfam05557 270 DTGlnLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQElaqylkkIEDLNKKLKRHKALVRRLQRrvl 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1449 ---KQRNFDKVLAEwkqKYEESQAELEGAQKEARSLstelfkmknsyEEALDQLETMKRENKNLQQEISDLTEQIGETGK 1525
Cdd:pfam05557 350 lltKERDGYRAILE---SYDKELTMSNYSPQLLERI-----------EEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQ 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1526 SIHELEkakktVETEKSEIQAALEEAEGTLEheeskilrvqlELNQVKSEIDRKLAEKDEEMEQIKrnsqrvidsmqsTL 1605
Cdd:pfam05557 416 QAQTLE-----RELQALRQQESLADPSYSKE-----------EVDSLRRKLETLELERQRLREQKN------------EL 467
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1606 DAEVRSRNdalrvkkkMEGDLNEMEIQ-LSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMKEQVAMVERRNGL 1684
Cdd:pfam05557 468 EMELERRC--------LQGDYDPKKTKvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTST 539
|
650
....*....|....*..
gi 1316056572 1685 MVA-EIEELRAALEQTE 1700
Cdd:pfam05557 540 MNFkEVLDLRKELESAE 556
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1005-1189 |
2.31e-06 |
|
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: 50.69 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1005 EAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRM-------DLERAKRKLEGDLKLAQESImdlENDK 1077
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEaakteleDLEKEIKRLELEIEEVEARI---KKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1078 QQSDEKIKKKDFEisQLLSKIEDEQSLGAQLQKKIKELQARIEELEeeieaerAARAKVEKQRADLSRELEEISERLEEA 1157
Cdd:COG1579 80 EQLGNVRNNKEYE--ALQKEIESLKRRISDLEDEILELMERIEELE-------EELAELEAELAELEAELEEKKAELDEE 150
|
170 180 190
....*....|....*....|....*....|..
gi 1316056572 1158 GGATAAQIEmnkKREAEFQKLRRDLEESTLQH 1189
Cdd:COG1579 151 LAELEAELE---ELEAEREELAAKIPPELLAL 179
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1329-1523 |
3.00e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1329 AKNALAHAVQSARHDCDLLREqfEEEQEAKAELQRGMSKANSEVAQWRSKYETDAIQRTEELEEAKKKLAQRlqeaeesI 1408
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK-------E 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1409 EAVNSKCASLEKTKQRLQGEVEdlmtdveranslaaNLDKKQRNFDKVLAEWKQKYEESQAELEGA----QKEARS---- 1480
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEK--------------ELEQKQQELEKKEEELEELIEEQLQELERIsgltAEEAKEille 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1481 -----LSTELFKM-KNSYEEAldQLETMKRENKNLQQEISDL-TEQIGET 1523
Cdd:PRK12704 162 kveeeARHEAAVLiKEIEEEA--KEEADKKAKEILAQAIQRCaADHVAET 209
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
652-679 |
3.01e-06 |
|
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: 49.27 E-value: 3.01e-06
10 20
....*....|....*....|....*...
gi 1316056572 652 SAVFRENLGKLMTNLRSTHPHFVRCLIP 679
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
848-1351 |
3.55e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.21 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 848 ETEKELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVenlSDAEERCEGLIKSKIQLEAKLK--- 924
Cdd:PRK01156 239 SALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPV---YKNRNYINDYFKYKNDIENKKQils 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 925 ----------ETTERLEDEEEINAELTAKKRKLED---ECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDE 991
Cdd:PRK01156 316 nidaeinkyhAIIKKLSVLQKDYNDYIKKKSRYDDlnnQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 992 AIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEqekklrMDLERAKRKLEGDlKLAQESIM 1071
Cdd:PRK01156 396 ILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNME------MLNGQSVCPVCGT-TLGEEKSN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1072 DL----ENDKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQK-----------KIKELQARIEELEEEIEAERAARAKV 1136
Cdd:PRK01156 469 HIinhyNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeeinksineynKIESARADLEDIKIKINELKDKHDKY 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1137 EKQRADL-SRELEEISERLEEAGGATAA----QIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQI 1211
Cdd:PRK01156 549 EEIKNRYkSLKLEDLDSKRTSWLNALAVisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEA 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1212 DNLQRVKQKLEKEK---SEFKMEIDDLSSNmeaVAKAKGnLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARlqten 1288
Cdd:PRK01156 629 NNLNNKYNEIQENKiliEKLRGKIDNYKKQ---IAEIDS-IIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR----- 699
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316056572 1289 gefarqleeKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAhavqsarhDCDLLREQF 1351
Cdd:PRK01156 700 ---------LESTIEILRTRINELSDRINDINETLESMKKIKKAIG--------DLKRLREAF 745
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
769-1114 |
5.31e-06 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 51.87 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 769 FKAGLLGTLEEMR---------DEKLASLVTMTQALcrgyVMRKEfvKMMERRDAIytVQYNVRSFMNVKNWPWMNLYF- 838
Cdd:pfam15818 5 FKTSLLEALEELRmrreaetqyEEQIGKIIVETQEL----KWQKE--TLQNQKETL--AKQHKEAMAVFKKQLQMKMCAl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 839 ---KIKPLLKSAETEKELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVaSEVenlsdaeERCEGLIKS 915
Cdd:pfam15818 77 eeeKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLHLLAKEDHHKQL-NEI-------EKYYATITG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 916 KIQLeakLKETTERLED--EEEI--NAELTAKKRKLEDECSELKKDIDDL--ELTLAKVE-KEKHATEN--------KVK 980
Cdd:pfam15818 149 QFGL---VKENHGKLEQnvQEAIqlNKRLSALNKKQESEICSLKKELKKVtsDLIKSKVTcQYKMGEENinltikeqKFQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 981 NLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEgslEQEKKLRMDLERAKRKle 1060
Cdd:pfam15818 226 ELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALK---ENNQTLERDNELQREK-- 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1316056572 1061 gdLKLAQESIMDLENDKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKE 1114
Cdd:pfam15818 301 --VKENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQE 352
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1401-1831 |
5.38e-06 |
|
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: 51.23 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1401 LQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDkkqrNFDKVLAEWKQKYEESQAELEgaqkearS 1480
Cdd:pfam05622 2 LSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLE----SGDDSGTPGGKKYLLLQKQLE-------Q 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1481 LSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHEL-------EKAKK---TVETEKSEIQ----- 1545
Cdd:pfam05622 71 LQEENFRLETARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMdilressDKVKKleaTVETYKKKLEdlgdl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1546 ----AALEE-----AEGTLEHEE----SKILRVQLEL--NQVKsEIDRKLAE--------------KDEEMEQIKRNSQR 1596
Cdd:pfam05622 151 rrqvKLLEErnaeyMQRTLQLEEelkkANALRGQLETykRQVQ-ELHGKLSEeskkadklefeykkLEEKLEALQKEKER 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1597 VI---DSMQSTLDaEVR---------SRNDALRVKKKMEGD----------LNEMEIQLSHANRQAAEAQKQlrNVQGQL 1654
Cdd:pfam05622 230 LIierDTLRETNE-ELRcaqlqqaelSQADALLSPSSDPGDnlaaeimpaeIREKLIRLQHENKMLRLGQEG--SYRERL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1655 KDAQLHLDDAVRGQEDMKEQVAMVERRNGLMVAEIEELRAALEQTERsrkvaeqelvdaservgllHSQNSSLLntKKKL 1734
Cdd:pfam05622 307 TELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGS-------------------KAEDSSLL--KQKL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1735 ETDLVQVQgEVDDAVQEARNA-EDKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNLE---VTVKDLQHRLDEAE 1805
Cdd:pfam05622 366 EEHLEKLH-EAQSELQKKKEQiEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEkakSVIKTLDPKQNPAS 444
|
490 500
....*....|....*....|....*.
gi 1316056572 1806 NLAMKGGKKQLQKLEQRVRELETEVE 1831
Cdd:pfam05622 445 PPEIQALKNQLLEKDKKIEHLERDFE 470
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
938-1235 |
5.50e-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: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 938 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHAtENKVKNLTEE---MATQDEAIAKLTKEKKALQEAHqqtlDDL 1014
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREA-LQRLAEYSWDeidVASAEREIAELEAELERLDASS----DDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1015 QAeedkvntLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDEKIKKKDFeisQL 1094
Cdd:COG4913 688 AA-------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF---AA 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1095 LSKIEDEQSLGAQLQKKIKELQarieeleeeieaeraarAKVEKQRADLSRELEEISERLEEAGGATAAQIEmnkkREAE 1174
Cdd:COG4913 758 ALGDAVERELRENLEERIDALR-----------------ARLNRAEEELERAMRAFNREWPAETADLDADLE----SLPE 816
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316056572 1175 FQKLRRDLEESTL-QHEATAAALRKKQAdsvaelGEQIDNLQrvkQKLEKEKSEFKMEIDDL 1235
Cdd:COG4913 817 YLALLDRLEEDGLpEYEERFKELLNENS------IEFVADLL---SKLRRAIREIKERIDPL 869
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1315-1555 |
6.27e-06 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 49.72 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1315 QIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVaqwrskyeTDAIQRTEELEEAK 1394
Cdd:pfam06008 20 NLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAES--------ERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1395 KKLAQRLQEAEESIEAVNSKCASL-EKTKQRLQGEVEDLMTDVEranslAANLDKKQRNFDKVLAEWKQKYEESQAELEG 1473
Cdd:pfam06008 92 KNLIDNIKEINEKVATLGENDFALpSSDLSRMLAEAQRMLGEIR-----SRDFGTQLQNAEAELKAAQDLLSRIQTWFQS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1474 AQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEqigETGKSIHELEKAKKTVETEKSEIQAALEEAEG 1553
Cdd:pfam06008 167 PQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNL---ANQANLREFQRKKEEVSEQKNQLEETLKTARD 243
|
..
gi 1316056572 1554 TL 1555
Cdd:pfam06008 244 SL 245
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1623-1932 |
7.94e-06 |
|
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: 51.33 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1623 EGDLNEMEIQLSHANRQAAEAQKQLRNVQGqlKDAQLhlddavrgqEDMKEQVAMVERRNGLMVAEIEELRAALEqterS 1702
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEK--KHQQL---------CEEKNALQEQLQAETELCAEAEEMRARLA----A 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1703 RKVAEQELV-DASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDavQEARNAEDKAKKAITDAAM--MAEELKKEQDT 1779
Cdd:pfam01576 69 RKQELEEILhELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE--EEAARQKLQLEKVTTEAKIkkLEEDILLLEDQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1780 SAHLERMKKNLEVTVKDLQHRLDEAENLAmKGGKKQLQKLEQRVRELETEVEGEQKRGADAVKGVRKYERRVKELTYQTE 1859
Cdd:pfam01576 147 NSKLSKERKLLEERISEFTSNLAEEEEKA-KSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316056572 1860 EDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEEAQERADIAESQVNKLRAKSRDVG 1932
Cdd:pfam01576 226 ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG 298
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1108-1820 |
8.98e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.98 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1108 LQKKIKELQARIEE-LEEEIEAERAARAKVEKQRADLSRELE-EISERLEEAGGATAAQIEMNKKREaEFQKLRRDLEEs 1185
Cdd:pfam10174 1 LQAQLRDLQRENELlRRELDIKESKLGSSMNSIKTFWSPELKkERALRKEEAARISVLKEQYRVTQE-ENQHLQLTIQA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1186 tLQHEATAaalrkkQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEAVAKakgNLEKMCRTLEDQLSEIKS 1265
Cdd:pfam10174 79 -LQDELRA------QRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAK---ELFLLRKTLEEMELRIET 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1266 KN------DENVRQLNDI---NAQKARLQTENGEFARQLEEKEALVSQLtrgkQAFTQQIEELKRHIEEEVKAKNALAHA 1336
Cdd:pfam10174 149 QKqtlgarDESIKKLLEMlqsKGLPKKSGEEDWERTRRIAEAEMQLGHL----EVLLDQKEKENIHLREELHRRNQLQPD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1337 VQSARhdcdLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYETDAIQRTEELEEAK-------------KKLAQRLQE 1403
Cdd:pfam10174 225 PAKTK----ALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEvykshskfmknkiDQLKQELSK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1404 AEESIEAVNSKCASLEK----TKQRLQGEVEDLMTDVERANSLAANLDKKQRNfdkvLAEWKQKYEESQAELEGAQKEAR 1479
Cdd:pfam10174 301 KESELLALQTKLETLTNqnsdCKQHIEVLKESLTAKEQRAAILQTEVDALRLR----LEEKESFLNKKTKQLQDLTEEKS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1480 SLSTELFKMKnsyeealDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEE 1559
Cdd:pfam10174 377 TLAGEIRDLK-------DMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1560 SKILRvqlelnqVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMqSTLDAEVRSRNDALRVKKKMEGDLNEMEIQLSHANRQ 1639
Cdd:pfam10174 450 RIIER-------LKEQREREDRERLEELESLKKENKDLKEKV-SALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1640 AAEAQKQLRN----VQGQLKDAQlHLDDAVRGQEDMKEQVAMVERRNGLMV-------AEIEELRAALEQTERSRKVAEQ 1708
Cdd:pfam10174 522 LEIAVEQKKEecskLENQLKKAH-NAEEAVRTNPEINDRIRLLEQEVARYKeesgkaqAEVERLLGILREVENEKNDKDK 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1709 ELVDASERVGLLH-SQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQdtsahLERMK 1787
Cdd:pfam10174 601 KIAELESLTLRQMkEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQE-----LDATK 675
|
730 740 750
....*....|....*....|....*....|...
gi 1316056572 1788 KNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLE 1820
Cdd:pfam10174 676 ARLSSTQQSLAEKDGHLTNLRAERRKQLEEILE 708
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1483-1676 |
9.58e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1483 TELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEheesKI 1562
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG----ER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1563 LRVQLELNQVKSEIDRKLAEKD--------EEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALRVKKKMEGDLNEMEIQLS 1634
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLGSESfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1316056572 1635 HANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMKEQVA 1676
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
874-1227 |
1.03e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 874 KKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSE 953
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 954 LKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQ 1033
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1034 QVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIK 1113
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1114 ELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATA 1193
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330 340 350
....*....|....*....|....*....|....
gi 1316056572 1194 AALRKKQADSVAELGEQIDNLQRVKQKLEKEKSE 1227
Cdd:COG4372 325 AKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1195-1410 |
1.19e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1195 ALRKKQADSVAE-LGEQIDNLQRVKQKLEKEKSEFKME--IDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENV 1271
Cdd:COG3206 167 ELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1272 RQLNDINAQKARLQtENGEFARQLEEKEALVSQLTRGKQAFT----------QQIEELKRHIEEEVKAknalahAVQSAR 1341
Cdd:COG3206 247 AQLGSGPDALPELL-QSPVIQQLRAQLAELEAELAELSARYTpnhpdvialrAQIAALRAQLQQEAQR------ILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316056572 1342 HDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRskyetdAIQRteELEEAKKK---LAQRLQEAEESIEA 1410
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAELR------RLER--EVEVARELyesLLQRLEEARLAEAL 383
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1185-1595 |
1.24e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.21 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1185 STLQHEATAAALRKKQADSVaeLGEQIDNLQRvkqkLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIK 1264
Cdd:pfam10174 341 AILQTEVDALRLRLEEKESF--LNKKTKQLQD----LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1265 SKNDENVRQLNDINAQKARLQTENGEFARQLEEK----EALVSQLTRGKQAFTQQIEELKRHIEEevkaknalahavqsA 1340
Cdd:pfam10174 415 KQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKeriiERLKEQREREDRERLEELESLKKENKD--------------L 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1341 RHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYETDAIQRTEELEEAKK-----KLAQRLQEAEESIEAVNSKC 1415
Cdd:pfam10174 481 KEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKlenqlKKAHNAEEAVRTNPEINDRI 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1416 ASLEKTKQRL-------QGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFkm 1488
Cdd:pfam10174 561 RLLEQEVARYkeesgkaQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLL-- 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1489 knsyEEALDQLETMKRENKNLQqeisdLTEQIGETGKSIHELEKAKKTVetekSEIQAALEEAEG---TLEHEESKILRV 1565
Cdd:pfam10174 639 ----EEARRREDNLADNSQQLQ-----LEELMGALEKTRQELDATKARL----SSTQQSLAEKDGhltNLRAERRKQLEE 705
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1316056572 1566 QLELNQ-----VKSEIDRKLA---------------------EKDEEMEQIKRNSQ 1595
Cdd:pfam10174 706 ILEMKQeallaAISEKDANIAllelssskkkktqeevmalkrEKDRLVHQLKQQTQ 761
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1137-1857 |
1.29e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1137 EKQRA-DLSRELEEISERLEEAGGA-TAAQIEMNKKREAE--FQKLRR---DLEESTLQHEAtaaalrkkQADSVAELGE 1209
Cdd:PRK04863 305 EQYRLvEMARELAELNEAESDLEQDyQAASDHLNLVQTALrqQEKIERyqaDLEELEERLEE--------QNEVVEEADE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1210 QIDNLQRVKQKLEKEKSEFKMEIDDLSSNME--------------AVAKAKG----------NLEKMCRTLEDQLSEIKS 1265
Cdd:PRK04863 377 QQEENEARAEAAEEEVDELKSQLADYQQALDvqqtraiqyqqavqALERAKQlcglpdltadNAEDWLEEFQAKEQEATE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1266 KNDENVRQLNDinAQKARLQTENG---------------------EFARQLEEKEALVSQLtrgkQAFTQQIEELKRHIE 1324
Cdd:PRK04863 457 ELLSLEQKLSV--AQAAHSQFEQAyqlvrkiagevsrseawdvarELLRRLREQRHLAEQL----QQLRMRLSELEQRLR 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1325 EEVKAKNALAHAVQSARHDCDLlREQFEEEQEAKAELQRGMSKANSEVAQWRSKYEtdaiQRTEELEEAKKKLAQRLQEA 1404
Cdd:PRK04863 531 QQQRAERLLAEFCKRLGKNLDD-EDELEQLQEELEARLESLSESVSEARERRMALR----QQLEQLQARIQRLAARAPAW 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1405 EESIEAVNskcaslektkqRLQGEVEDLMTDVERANSLAANLDKKQRNfdkvLAEWKQKYEESQAELEGaqkEARSLS-- 1482
Cdd:PRK04863 606 LAAQDALA-----------RLREQSGEEFEDSQDVTEYMQQLLERERE----LTVERDELAARKQALDE---EIERLSqp 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1483 -----TELFKMKNS-------------------YEEAL----------DQLETMKRENKNLQQEISDL------TEQIGE 1522
Cdd:PRK04863 668 ggsedPRLNALAERfggvllseiyddvsledapYFSALygparhaivvPDLSDAAEQLAGLEDCPEDLyliegdPDSFDD 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1523 TGKSIHELEKAkktVETEKSEIQ--------------AAleeaegtlehEESKILRVQLELNqvksEIDRKLAEKDEEME 1588
Cdd:PRK04863 748 SVFSVEELEKA---VVVKIADRQwrysrfpevplfgrAA----------REKRIEQLRAERE----ELAERYATLSFDVQ 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1589 QIKRN----SQRVIDSMQSTLD----AEVRSRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKD-AQL 1659
Cdd:PRK04863 811 KLQRLhqafSRFIGSHLAVAFEadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLlADE 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1660 HLDD---AVRGQEDMKEQVAMVERRNGLMVAEIEELRAAL-------EQTERSRKVAEQELVDASERVGLL--------- 1720
Cdd:PRK04863 891 TLADrveEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLqsdpeqfEQLKQDYQQAQQTQRDAKQQAFALtevvqrrah 970
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1721 --HSQNSSLLNTK----KKLETDLVQVQGEVDDAVQEARNAEDKA----------KKAITDAAMMAEELKKE-QDTSAHL 1783
Cdd:PRK04863 971 fsYEDAAEMLAKNsdlnEKLRQRLEQAEQERTRAREQLRQAQAQLaqynqvlaslKSSYDAKRQMLQELKQElQDLGVPA 1050
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1784 -ERMKKNLEVTVKDLQHRLDEA-------------ENLAMKGGKKQLQKLEQRVRELETEVEGEQKRGADAVKGVRKY-- 1847
Cdd:PRK04863 1051 dSGAEERARARRDELHARLSANrsrrnqlekqltfCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNgv 1130
|
890
....*....|..
gi 1316056572 1848 ERRV--KELTYQ 1857
Cdd:PRK04863 1131 ERRLhrRELAYL 1142
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1107-1431 |
1.68e-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: 49.74 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1107 QLQKKIKELQARIEELEEEIEaeraaraKVEKQRADLSRELEEiSERLEEAGGATAAQIEMNKKREAEFQKL--RRDLEE 1184
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQE-------RLRQEKEEKAREVER-RRKLEEAEKARQAEMDRQAAIYAEQERMamEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1185 STLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEiddlssnMEAVAKAKGNLEKMCRTLEDQLSEIk 1264
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQE-------LEAARKVKILEEERQRKIQQQKVEM- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1265 skndENVRQLNDiNAQKARLQTENGEFARQLEekealvsQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDC 1344
Cdd:pfam17380 423 ----EQIRAEQE-EARQREVRRLEEERAREME-------RVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1345 DLLREQFEEEQEAKAE-----------LQRGMSKANSEVAQWRSKYETDAIQRTEELEEAKKKLAQRLQEAEESieavNS 1413
Cdd:pfam17380 491 EQRRKILEKELEERKQamieeerkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE----RS 566
|
330
....*....|....*...
gi 1316056572 1414 KCASLEKTKQRLQGEVED 1431
Cdd:pfam17380 567 RLEAMEREREMMRQIVES 584
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1266-1930 |
1.90e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.05 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1266 KNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVkakNALAHAVQSARHDCD 1345
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENEL---DPLKNRLKEIEHNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1346 LLREqFEEEQEAKAELQRGMSKANSEVAQWRSK--YETDaiqrtEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQ 1423
Cdd:TIGR00606 263 KIMK-LDNEIKALKSRKKQMEKDNSELELKMEKvfQGTD-----EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERR 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1424 RLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEwkqkyEESQAELEGAQKEARSLstelFKMKNSYEEaldQLETMK 1503
Cdd:TIGR00606 337 LLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS-----LATRLELDGFERGPFSE----RQIKNFHTL---VIERQE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1504 RENKNLQQEISDLTEQIGETGKSIHELEkakktveTEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLaEK 1583
Cdd:TIGR00606 405 DEAKTAAQLCADLQSKERLKQEQADEIR-------DEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIL-EL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1584 DEEMEQIKRN-SQRVIDSMQSTLDAEVRS-RNDALRVKKKMEGDLNEMEiQLSHANrqaaEAQKQLRNVQGQLKDAQLHL 1661
Cdd:TIGR00606 477 DQELRKAERElSKAEKNSLTETLKKEVKSlQNEKADLDRKLRKLDQEME-QLNHHT----TTRTQMEMLTKDKMDKDEQI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1662 -DDAVRGQEDMKEQVAMVERRNGLMvAEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQ 1740
Cdd:TIGR00606 552 rKIKSRHSDELTSLLGYFPNKKQLE-DWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1741 VQGEVDDAVqEARNAEDKAKKAITDAAMMA----------EELKKEQDTSAHL----ERMKKNLEVTVKDLQHRLDEAEN 1806
Cdd:TIGR00606 631 VCGSQDEES-DLERLKEEIEKSSKQRAMLAgatavysqfiTQLTDENQSCCPVcqrvFQTEAELQEFISDLQSKLRLAPD 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1807 lAMKGGKKQLQKLEQRVRELETEVEGEQKRGADAVKGVRKYERRVKELTYQTEEDKKNITRLQDLVDKLQLKVKAYK--- 1883
Cdd:TIGR00606 710 -KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcl 788
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316056572 1884 ----------RQAEEAEEQANSHMSRL---------RKVQHEMEEAQERADIAESQVNKLRAKSRD 1930
Cdd:TIGR00606 789 tdvtimerfqMELKDVERKIAQQAAKLqgsdldrtvQQVNQEKQEKQHELDTVVSKIELNRKLIQD 854
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
866-1037 |
2.28e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 866 DLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAKLKETTERLE-DEEEINAELTAKk 944
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkYEEQLGNVRNNK- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 945 rkledECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAEEDKvntL 1024
Cdd:COG1579 90 -----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE---L 161
|
170
....*....|...
gi 1316056572 1025 TKAKTKLEQQVDD 1037
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1272-1924 |
2.65e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1272 RQLNDINAQKARLQTENGEFARQLEEkealvsqLTRGKQAFTQQIEELKRHIEeevKAKNALAHAVQSARHDCDL--LRE 1349
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAE-------LNEAESDLEQDYQAASDHLN---LVQTALRQQEKIERYQADLeeLEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1350 QFEEEQEAKAEL--QRGMSKANSEVAQwrskyetdaiqrtEELEEAKKKLA---QRL----------QEAEESIEAVNSK 1414
Cdd:PRK04863 363 RLEEQNEVVEEAdeQQEENEARAEAAE-------------EEVDELKSQLAdyqQALdvqqtraiqyQQAVQALERAKQL 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1415 CASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQA-----ELEGAQKEARSLSTELFKMK 1489
Cdd:PRK04863 430 CGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagevSRSEAWDVARELLRRLREQR 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1490 NsyeeALDQLETMKRENKNLQQEIS---DLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQ 1566
Cdd:PRK04863 510 H----LAEQLQQLRMRLSELEQRLRqqqRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALR 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1567 LELNQVKSEIDR-------------KLAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSR--NDALRVKKKmegDLNEMEI 1631
Cdd:PRK04863 586 QQLEQLQARIQRlaarapawlaaqdALARLREQSGEEFEDSQDVTEYMQQLLERERELTveRDELAARKQ---ALDEEIE 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1632 QLSHANRQAAEAQKQL-RNVQGQL-----KDAQLH--------------------LDDAVR---GQEDMKEQVAMVER-- 1680
Cdd:PRK04863 663 RLSQPGGSEDPRLNALaERFGGVLlseiyDDVSLEdapyfsalygparhaivvpdLSDAAEqlaGLEDCPEDLYLIEGdp 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1681 ---RNGlmVAEIEEL-------------------------RAA----LEQTERSRKVAEQELVDASERVGL---LHSQNS 1725
Cdd:PRK04863 743 dsfDDS--VFSVEELekavvvkiadrqwrysrfpevplfgRAArekrIEQLRAEREELAERYATLSFDVQKlqrLHQAFS 820
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1726 SLLNTK-------------KKLETDLVQVQGEV---DDAVQEARNAEDKAKKAITDAAMMAEELKKEQDTS-----AHLE 1784
Cdd:PRK04863 821 RFIGSHlavafeadpeaelRQLNRRRVELERALadhESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETladrvEEIR 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1785 RMKKNLEVTVKDLQ---HRLDEAENLA--MKGGKKQLQKLEQRVRELETEVEgEQKRGADAVKGVRKyerRVKELTYqtE 1859
Cdd:PRK04863 901 EQLDEAEEAKRFVQqhgNALAQLEPIVsvLQSDPEQFEQLKQDYQQAQQTQR-DAKQQAFALTEVVQ---RRAHFSY--E 974
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316056572 1860 EDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEEAQERADIAESQVNKL 1924
Cdd:PRK04863 975 DAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1439-1646 |
2.74e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1439 ANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTE 1518
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1519 QIGE-------------------TGKSIHEL-----------EKAKKTVETEKSEiQAALEEAEGTLEHEESKILRVQLE 1568
Cdd:COG3883 87 ELGEraralyrsggsvsyldvllGSESFSDFldrlsalskiaDADADLLEELKAD-KAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316056572 1569 LNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQStLDAEVRSRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQ 1646
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE-LEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1581-1817 |
3.08e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1581 AEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLH 1660
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1661 LDdavRGQEDMKEQVA---MVERRNGLMV-------AEIEELRAALEQTERSRKVAEQELVDASERvglLHSQNSSLLNT 1730
Cdd:COG4942 99 LE---AQKEELAELLRalyRLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAE---LAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1731 KKKLETDLVQVQgevddaVQEARNAEDKAKKAITDAAmMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLAMK 1810
Cdd:COG4942 173 RAELEALLAELE------EERAALEALKAERQKLLAR-LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
....*..
gi 1316056572 1811 GGKKQLQ 1817
Cdd:COG4942 246 AGFAALK 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1381-1593 |
3.22e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1381 TDAIQRTEELEEAKKKLAQRLQEAEESIEAVnskcaslektkqrlqgevedlmtdveRANSLAANLDKKQRNFDKVLAEW 1460
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEF--------------------------RQKNGLVDLSEEAKLLLQQLSEL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1461 KQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALD--QLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVE 1538
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALR 304
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1316056572 1539 TE-KSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEIdRKLAEKDEEMEQIKRN 1593
Cdd:COG3206 305 AQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRLERE 359
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1457-1914 |
3.30e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1457 LAEWKQKYEESQAELEGAQKEARSLSTELfkmknSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKT 1536
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1537 VETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQstlDAEVRSRNDAL 1616
Cdd:COG4717 172 LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE---AAALEERLKEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1617 RVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLddaVRGQEDMKEQVAMVERRNGLMVAEIEELRAAL 1696
Cdd:COG4717 249 RLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLL---AREKASLGKEAEELQALPALEELEEEELEELL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1697 EQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLEtdLVQVQGEVDDAVQEArNAEDKAkkAITDAAMMAEELKKE 1776
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEA-GVEDEE--ELRAALEQAEEYQEL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1777 QDTSAHLERMKKNLEVTVKDLQHRLDEAENlamkggKKQLQKLEQRVRELETEVEGEQKRGADAvkgvrkyERRVKELty 1856
Cdd:COG4717 401 KEELEELEEQLEELLGELEELLEALDEEEL------EEELEELEEELEELEEELEELREELAEL-------EAELEQL-- 465
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1316056572 1857 qtEEDkknitrlqDLVDKLQLKVKAYKRQAEEAEEQAnshmSRLRKVQHEMEEAQERA 1914
Cdd:COG4717 466 --EED--------GELAELLQELEELKAELRELAEEW----AALKLALELLEEAREEY 509
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1402-1742 |
3.72e-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: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1402 QEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSlaaNLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSL 1481
Cdd:pfam07888 16 EEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANR---QREKEKERYKRDREQWERQRRELESRVAELKEELRQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1482 STELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESK 1561
Cdd:pfam07888 93 REKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1562 ILRVQLELNQVKSEIDR----------KLAEKDEEMEQIKRN----------SQRVIDSMQSTLdAEVRSRNDALRVKKK 1621
Cdd:pfam07888 173 RKQLQAKLQQTEEELRSlskefqelrnSLAQRDTQVLQLQDTittltqklttAHRKEAENEALL-EELRSLQERLNASER 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1622 ----MEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAvRGQ-----EDMKEQVAMVERRNGLMVAEIEEL 1692
Cdd:pfam07888 252 kvegLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREG-RARwaqerETLQQSAEADKDRIEKLSAELQRL 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1316056572 1693 RAALEQTERSRKVAEQEL--------VDASERVGLLHSQNSSLLNTKKKLETDLVQVQ 1742
Cdd:pfam07888 331 EERLQEERMEREKLEVELgrekdcnrVQLSESRRELQELKASLRVAQKEKEQLQAEKQ 388
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1568-1772 |
3.76e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1568 ELNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQStLDAEVRSRNDALRvkkKMEGDLNEMEIQLSHANRQAAEAQKQL 1647
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA-LERRIAALARRIR---ALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1648 RNVQGQLKD------------------AQLHLDDAVRGQEDMKEQVAMVERRNGLMVAEIEELRAALEQTERSRKVAEQE 1709
Cdd:COG4942 100 EAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1316056572 1710 LVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEE 1772
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
878-1080 |
3.88e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 878 EEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAKLKETTERLedeEEINAELTAKKRKLEDECSELKKD 957
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 958 IDDLELT------LAKVEKEKHATE--NKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKT 1029
Cdd:COG3883 92 ARALYRSggsvsyLDVLLGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1316056572 1030 KLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQS 1080
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
845-1006 |
4.20e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 845 KSAETEKELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSD--AEERCEGLIKSKIQ--LE 920
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraRALYRSGGSVSYLDvlLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 921 AK---------------LKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEE 985
Cdd:COG3883 111 SEsfsdfldrlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
170 180
....*....|....*....|.
gi 1316056572 986 MATQDEAIAKLTKEKKALQEA 1006
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEAA 211
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
845-1089 |
4.25e-05 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 48.62 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 845 KSAETEKELQNMKEnYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEErCEGLIKSKIQLEAKLK 924
Cdd:pfam18971 598 KAVAEAKSTGNYDE-VKKAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKDE-IFALINKEANRDARAI 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 925 ETTERLEDeeeINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQ 1004
Cdd:pfam18971 676 AYTQNLKG---IKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGINPEWISKVENLNAALN 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1005 EAHQQTLDDLqaeedkvNTLTKAKTKLEQQVDDLEGSLEQEKKL-RMDLERAKRKLEGDLKLAQESIMDLEN--DKQQSD 1081
Cdd:pfam18971 753 EFKNGKNKDF-------SKVTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKNfsKEQLAQ 825
|
....*...
gi 1316056572 1082 EKIKKKDF 1089
Cdd:pfam18971 826 QAQKNEDF 833
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
990-1115 |
5.02e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 990 DEAIAKLT-----KEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEqekklrmDLERAKRKLEGDLK 1064
Cdd:COG2433 379 EEALEELIekelpEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELE-------EKDERIERLERELS 451
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1316056572 1065 LAQESimdlENDKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKEL 1115
Cdd:COG2433 452 EARSE----ERREIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1420-1761 |
5.22e-05 |
|
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: 48.36 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1420 KTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALD-Q 1498
Cdd:pfam15964 300 QTIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKELAsQ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1499 LETMKRENKNLQQEISDLTEQIGET----GKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKS 1574
Cdd:pfam15964 380 QEKRAQEKEALRKEMKKEREELGATmlalSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLN 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1575 EIDRKLAEKDEEMEQIKRNSQRVIDsmqsTLDAEVrsrndalrvkKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQL 1654
Cdd:pfam15964 460 QTKMKKDEAEKEHREYRTKTGRQLE----IKDQEI----------EKLGLELSESKQRLEQAQQDAARAREECLKLTELL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1655 KDA--QLHLDDAVRGQ------EDMKEQVAMVERRNGLMVAEIEELRAALEQTERsrkvaeqelvdasERVGLLHSQNSS 1726
Cdd:pfam15964 526 GESehQLHLTRLEKESiqqsfsNEAKAQALQAQQREQELTQKMQQMEAQHDKTVN-------------EQYSLLTSQNTF 592
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1316056572 1727 LLNTK-------KKLETDLVQVQGEVDDAVQEARNAEDKAKK 1761
Cdd:pfam15964 593 IAKLKeecctlaKKLEEITQKSRSEVEQLSQEKEYLQDRLEK 634
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1385-1553 |
5.29e-05 |
|
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: 47.45 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1385 QRTEELEEAKKKLAQRLQEA--EESIEAVNSKCASLEKTKQR----------LQGEVEDLMTDV----ERANSLAANLDK 1448
Cdd:pfam09787 14 QKAARILQSKEKLIASLKEGsgVEGLDSSTALTLELEELRQErdllreeiqkLRGQIQQLRTELqeleAQQQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1449 KQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIH 1528
Cdd:pfam09787 94 QLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSELENRLH 173
|
170 180 190
....*....|....*....|....*....|..
gi 1316056572 1529 ELEKA---KKT----VETEKSEIQAALEEAEG 1553
Cdd:pfam09787 174 QLTETliqKQTmleaLSTEKNSLVLQLERMEQ 205
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
938-1164 |
5.31e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 938 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQ-- 1015
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1016 -AEEDKVNTLTKAK--TKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDEKIKkkdfeis 1092
Cdd:COG3883 99 gGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA------- 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316056572 1093 QLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQ 1164
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1135-1585 |
5.68e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 48.10 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1135 KVEKQRADLSRE-LEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQadsvaelgeqidn 1213
Cdd:pfam05667 178 KNSKELKEFYSEyLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGLASRLTPEEYRKRK------------- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1214 LQRVKQKLEkeksefkmeiDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNdenvrqLNDINAQKARLQTENGEFAR 1293
Cdd:pfam05667 245 RTKLLKRIA----------EQLRSAALAGTEATSGASRSAQDLAELLSSFSGSS------TTDTGLTKGSRFTHTEKLQF 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1294 QLEEKEALVSQLTRgkqafTQQIEELKRHIEEEVKAknalahavqsarhdcdlLREQFEEEQEAKAELQRGMSKANSEVA 1373
Cdd:pfam05667 309 TNEAPAATSSPPTK-----VETEEELQQQREEELEE-----------------LQEQLEDLESSIQELEKEIKKLESSIK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1374 QWRSKYETDAIQrTEELEEA---KKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVED----LMTDVERANSLAAN- 1445
Cdd:pfam05667 367 QVEEELEELKEQ-NEELEKQykvKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKhrvpLIEEYRALKEAKSNk 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1446 LDKKQRNFDKvLAEWKQKYEESQAELegAQKEarslstELFKmknsyeEALDQLETMKRENKNlqqeiSDLTEQIGETGK 1525
Cdd:pfam05667 446 EDESQRKLEE-IKELREKIKEVAEEA--KQKE------ELYK------QLVAEYERLPKDVSR-----SAYTRRILEIVK 505
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1526 SIHElekakktvetEKSEIQAALEEAEGtleheeskilrVQLELNQVKSEIDRKLAEKDE 1585
Cdd:pfam05667 506 NIKK----------QKEEITKILSDTKS-----------LQKEINSLTGKLDRTFTVTDE 544
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1623-1938 |
5.96e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1623 EGDLNEMEIQLSHANRQAAEAQ-KQLRNVQGQLKDAQLHLDDAVRGQEDMKEQVAMVERRNGLMVAEIEELRAALEQTER 1701
Cdd:PTZ00121 1044 EKDIIDEDIDGNHEGKAEAKAHvGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKK 1123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1702 SRKVAEQELVDASERVgllhsqnSSLLNTKKKLETDLVQVQGEVDDA--VQEARNAED-----KAKKAITdaAMMAEELK 1774
Cdd:PTZ00121 1124 AEDARKAEEARKAEDA-------RKAEEARKAEDAKRVEIARKAEDArkAEEARKAEDakkaeAARKAEE--VRKAEELR 1194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1775 KEQDTSA-----------HLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLEQRVRELETEVEGEQKRGADAVKG 1843
Cdd:PTZ00121 1195 KAEDARKaeaarkaeeerKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1844 VRKyeRRVKELTYQTEEDKKNITRLQDLVDKL-QLKVKAY-KRQAEEAEEQANSHMSRLRKVQHEMEEAQERADIAESQV 1921
Cdd:PTZ00121 1275 EEA--RKADELKKAEEKKKADEAKKAEEKKKAdEAKKKAEeAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA 1352
|
330
....*....|....*..
gi 1316056572 1922 NKLRAKSRDVGKSDAAE 1938
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAA 1369
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1350-1554 |
6.20e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1350 QFEEEQEAKAELQRGMSKANSEVAQWRSKYEtdaiqrteELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEV 1429
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELE--------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1430 EDLMTDVERANSLAANLDK--KQRNFDKVLAEWK-------------QKYEESQAELEGAQKEARSLSTELFKMKNSYEE 1494
Cdd:COG3883 89 GERARALYRSGGSVSYLDVllGSESFSDFLDRLSalskiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1495 ALDQLETMKRENknlQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGT 1554
Cdd:COG3883 169 AKAELEAQQAEQ---EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1316-1535 |
7.17e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.93 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1316 IEElKRHIEEEVKAKN-----ALAHAVQSARHdcdlLREQFEE-EQEAKAELQRGMSKAnsEVAQWRSKYETDAIQRTEE 1389
Cdd:COG2433 317 VEE-KLHLAREYGYDNdherdALAAALKAYDA----YKNKFERvEKKVPPDVDRDEVKA--RVIRGLSIEEALEELIEKE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1390 LEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERanslaanldKKQRNfdkvlaewkqkyEESQA 1469
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEE---------KDERI------------ERLER 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1316056572 1470 ELEGAQKEARSlstelfKMKNSYEealdqLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKK 1535
Cdd:COG2433 449 ELSEARSEERR------EIRKDRE-----ISRLDREIERLERELEEERERIEELKRKLERLKELWK 503
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
839-1060 |
7.71e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 839 KIKPLLKSAETEKELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQ 918
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 919 LEAKLKETTERLEDEEEInAELTAKKRKLEDECSELKKDIDDLElTLAKVEKEKHATENKVKNLTEEmATQDEAIAKLTK 998
Cdd:PRK02224 577 LNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREALA-ELNDERRERLAEKRERKRELEA-EFDEARIEEARE 653
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316056572 999 EKKALQEAHQQTlddlqaeEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLE 1060
Cdd:PRK02224 654 DKERAEEYLEQV-------EEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVE 708
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1385-1556 |
8.24e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1385 QRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLdKKQRNFDKVlaewkqky 1464
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKEYEAL-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1465 eesQAELEGAQKEARSLSTELFkmknsyeEALDQLETMKRENKNLQQEISDLTEQIGETGKsihELEKAKKTVETEKSEI 1544
Cdd:COG1579 95 ---QKEIESLKRRISDLEDEIL-------ELMERIEELEEELAELEAELAELEAELEEKKA---ELDEELAELEAELEEL 161
|
170
....*....|..
gi 1316056572 1545 QAALEEAEGTLE 1556
Cdd:COG1579 162 EAEREELAAKIP 173
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1502-1931 |
8.50e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.51 E-value: 8.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1502 MKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALE-EAEGTLEHEESKILRVQLELNQVK-SEIDRK 1579
Cdd:pfam10174 169 SKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHrRNQLQPDPAKTKALQTVIEMKDTKiSSLERN 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1580 LAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALRVKKKMEgdlnEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQL 1659
Cdd:pfam10174 249 IRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKID----QLKQELSKKESELLALQTKLETLTNQNSDCKQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1660 HLddavrgqEDMKEQVAMVERRNGLMVAEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSL---LNTKKK--- 1733
Cdd:pfam10174 325 HI-------EVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLkdmLDVKERkin 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1734 -LETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNL-EVTVKDLQHRLDEAENLamkg 1811
Cdd:pfam10174 398 vLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESL---- 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1812 gKKQLQKLEQRVRELETEVEGEQKRGAD--------AVKGVRKyERRVKELTYQTEEDKKNITRLQDLVDKLQlkvkayk 1883
Cdd:pfam10174 474 -KKENKDLKEKVSALQPELTEKESSLIDlkehasslASSGLKK-DSKLKSLEIAVEQKKEECSKLENQLKKAH------- 544
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1316056572 1884 rQAEEAEEQANSHMSRLRKVQHEMEEAQERADIAESQVNKLRAKSRDV 1931
Cdd:pfam10174 545 -NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREV 591
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1576-1930 |
8.75e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.59 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1576 IDRKLAEKDEEMEQIKRNSQRVIDSM--QSTLDAEVRSRNDALRVKKKMEGDLNemeiQLSHANRQAAEAQKQLRNVQGQ 1653
Cdd:PLN02939 61 SNSKLQSNTDENGQLENTSLRTVMELpqKSTSSDDDHNRASMQRDEAIAAIDNE----QQTNSKDGEQLSDFQLEDLVGM 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1654 LKDAQ---LHLDDA-VRGQEDMKEQVAMVERRNGlmvaEIEELRAALEQTERSRKVAEQELVDaserVGLLHSQnssLLN 1729
Cdd:PLN02939 137 IQNAEkniLLLNQArLQALEDLEKILTEKEALQG----KINILEMRLSETDARIKLAAQEKIH----VEILEEQ---LEK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1730 TKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDTS---AHLERMKKNLEVTVKDLQHRLDEAEN 1806
Cdd:PLN02939 206 LRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1807 LAMKGGKKQLQKLEQRVRELETEVEGEQKRGADAV---KGVRKYERRVKELTYQTEEdkKNITRLQ-DLVDKLQLKVKAY 1882
Cdd:PLN02939 286 DVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAAlvlDQNQDLRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKLL 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1316056572 1883 KRQAEEAEEQANSHmsrLRKVQHEMEEAQeraDIAESQVNKLRAKSRD 1930
Cdd:PLN02939 364 EERLQASDHEIHSY---IQLYQESIKEFQ---DTLSKLKEESKKRSLE 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1677-1927 |
8.92e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1677 MVERRNglMVAEIEELRAALEQTERsrkvAEQELVDASERVGLLhsqnssllntkkkleTDLVQVQGEVDDAVQEARNAE 1756
Cdd:COG4913 217 MLEEPD--TFEAADALVEHFDDLER----AHEALEDAREQIELL---------------EPIRELAERYAAARERLAELE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1757 D-----KAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLEQRVRELETEVE 1831
Cdd:COG4913 276 YlraalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1832 gEQKRGADavkgvrKYERRVKELTYQTEEDKKNITRLQDLVDKLqlkVKAYKRQAEEAEEQANSHMSRLRkvqhemeEAQ 1911
Cdd:COG4913 356 -ERERRRA------RLEALLAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEAALR-------DLR 418
|
250
....*....|....*.
gi 1316056572 1912 ERADIAESQVNKLRAK 1927
Cdd:COG4913 419 RELRELEAEIASLERR 434
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
846-1059 |
1.11e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.12 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 846 SAETEKELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCeglikskIQLEAKLKe 925
Cdd:pfam10174 470 LESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEEC-------SKLENQLK- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 926 TTERLEDEEEINAELTAKKRKLE-------DECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTK 998
Cdd:pfam10174 542 KAHNAEEAVRTNPEINDRIRLLEqevarykEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVA 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316056572 999 EKKALQEAHQQTLDDLqAEEDKVNTLTKAKTKLEQQVDDLEGSLEqekKLRMDLERAKRKL 1059
Cdd:pfam10174 622 NIKHGQQEMKKKGAQL-LEEARRREDNLADNSQQLQLEELMGALE---KTRQELDATKARL 678
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1470-1926 |
1.19e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.04 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1470 ELEGAQKEARSLSTELFKMKNSYEEALDQLEtmkRENKNLQQEISD----LTEQIGETGKSIHELEKAKKTVETEKSEIQ 1545
Cdd:pfam05557 62 KREAEAEEALREQAELNRLKKKYLEALNKKL---NEKESQLADAREviscLKNELSELRRQIQRAELELQSTNSELEELQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1546 AALEEAEGTLEheeskilrvqlELNQVKSEIDRKLAEKDEEMEQIKRNSQRVidSMQSTLDAEVRSRNDALRVKKKMEGD 1625
Cdd:pfam05557 139 ERLDLLKAKAS-----------EAEQLRQNLEKQQSSLAEAEQRIKELEFEI--QSQEQDSEIVKNSKSELARIPELEKE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1626 LNemeiQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDavrgQEDMKEQVAMVERRNGLMVAEIEELRAALEQTERSRKV 1705
Cdd:pfam05557 206 LE----RLREHNKHLNENIENKLLLKEEVEDLKRKLER----EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1706 AEqelvDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAEDKakkaITDAAMMAEELK------KEQDT 1779
Cdd:pfam05557 278 PE----DLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKK----IEDLNKKLKRHKalvrrlQRRVL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1780 SAHLER--MKKNLEVTVKDL---------QHRLDEAENLAMKGgKKQLQKLEQRVRELETEVeGEQKRGADAVKGVRKYE 1848
Cdd:pfam05557 350 LLTKERdgYRAILESYDKELtmsnyspqlLERIEEAEDMTQKM-QAHNEEMEAQLSVAEEEL-GGYKQQAQTLERELQAL 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1849 RRvKELTYQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEE-------QANSHMSRLRKVQHEMEEAQERADIAESQV 1921
Cdd:pfam05557 428 RQ-QESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMelerrclQGDYDPKKTKVLHLSMNPAAEAYQQRKNQL 506
|
....*
gi 1316056572 1922 NKLRA 1926
Cdd:pfam05557 507 EKLQA 511
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1309-1505 |
1.21e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1309 KQAFTQQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQwrskyetdaiqRTE 1388
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE-----------RRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1389 ELeeakKKLAQRLQEAE------------ESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKV 1456
Cdd:COG3883 87 EL----GERARALYRSGgsvsyldvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1316056572 1457 LAEwkqkYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRE 1505
Cdd:COG3883 163 KAE----LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1347-1596 |
1.26e-04 |
|
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: 46.93 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1347 LREQFEEEQEAKAELqrgMSKANSEVAQWRSKYETDAIQRTEELEEAKKKLAQRLQEAEESIEA---------------- 1410
Cdd:NF033838 101 LYELNVLKEKSEAEL---TSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEdrrnyptntyktlele 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1411 -----VNSKCASLEKTKQ-----RLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEesqAELEGAQKEARS 1480
Cdd:NF033838 178 iaesdVEVKKAELELVKEeakepRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRAD---AKLKEAVEKNVA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1481 LSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQ------------IGETGKSIHELEKAK-------------- 1534
Cdd:NF033838 255 TSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSVGEEtlpspslkpekkVAEAEKKVEEAKKKAkdqkeedrrnyptn 334
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316056572 1535 --KTVETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKdEEMEQIKRNSQR 1596
Cdd:NF033838 335 tyKTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEA-TRLEKIKTDRKK 397
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
847-1103 |
1.30e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.81 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 847 AETEKELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAKLKET 926
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 927 TER-------LEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAkltkE 999
Cdd:pfam07888 156 KERakkagaqRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEA----E 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1000 KKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEK----KLRMDLERAKRKL-EGDLKLAQESiMDLE 1074
Cdd:pfam07888 232 NEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARlqaaQLTLQLADASLALrEGRARWAQER-ETLQ 310
|
250 260
....*....|....*....|....*....
gi 1316056572 1075 NDKQQSDEKIKKKDFEISQLLSKIEDEQS 1103
Cdd:pfam07888 311 QSAEADKDRIEKLSAELQRLEERLQEERM 339
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
919-1326 |
1.33e-04 |
|
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: 46.60 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 919 LEAKLKETTERLEDEEEINAELTAKKRKLEDECSEL---KKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAK 995
Cdd:pfam19220 8 LRVRLGEMADRLEDLRSLKADFSQLIEPIEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 996 LTKEKKALQEAhqqtLDDLQAEEDKVNTLTKAKTkleQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLEN 1075
Cdd:pfam19220 88 LVARLAKLEAA----LREAEAAKEELRIELRDKT---AQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1076 DKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELqarieeleeeieaeraarakvEKQRADLSRELEEISERLE 1155
Cdd:pfam19220 161 ELATARERLALLEQENRRLQALSEEQAAELAELTRRLAEL---------------------ETQLDATRARLRALEGQLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1156 EAggataaqiemnkkrEAEFQKLRRDLEE--STLQHEATAAALRKKQADSVAELGEQIdnLQRVKQKLEKEKSEFKmeid 1233
Cdd:pfam19220 220 AE--------------QAERERAEAQLEEavEAHRAERASLRMKLEALTARAAATEQL--LAEARNQLRDRDEAIR---- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1234 dlssnmEAVAKAKGnLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFT 1313
Cdd:pfam19220 280 ------AAERRLKE-ASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLS 352
|
410
....*....|...
gi 1316056572 1314 QQIEELKRHIEEE 1326
Cdd:pfam19220 353 DRIAELTKRFEVE 365
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1149-1416 |
1.48e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.86 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1149 EISERLEEAGGATAAqiemnKKR-EAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELgeqidnLQRVKQKLEKEKSE 1227
Cdd:PRK05035 437 EIRAIEQEKKKAEEA-----KARfEARQARLEREKAAREARHKKAAEARAAKDKDAVAAA------LARVKAKKAAATQP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1228 FKMEIDDLSSNMEAVAKAKGnlekmcRTLEDQlseikskndenvrqlndinAQKARLQTENGEFARqleeKEALVSQLTR 1307
Cdd:PRK05035 506 IVIKAGARPDNSAVIAAREA------RKAQAR-------------------ARQAEKQAAAAADPK----KAAVAAAIAR 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1308 GKQAFTQQIEELKRHIEEEVKAKNALAHAVqsARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYETDAIQRT 1387
Cdd:PRK05035 557 AKAKKAAQQAANAEAEEEVDPKKAAVAAAI--ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQAN 634
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1316056572 1388 EELEE---------------AKKKLAQRLQEAEESIEAVNSKCA 1416
Cdd:PRK05035 635 AEPEEpvdprkaavaaaiarAKARKAAQQQANAEPEEAEDPKKA 678
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
948-1146 |
1.56e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 948 EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQE---AHQQTLDDLQAE------- 1017
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAeiaEAEAEIEERREElgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1018 -------EDKVNTLTKAK---------TKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSD 1081
Cdd:COG3883 95 lyrsggsVSYLDVLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1316056572 1082 EKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRE 1146
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1015-1216 |
1.84e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1015 QAEEDKVNTLTKAKTKLEQQVDDLEGSLEQ-EKKLRmdlerakrklegDLKlAQESIMDLENDKQQSDEKIKKKDFEISQ 1093
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEaEAALE------------EFR-QKNGLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1094 LLSKIEDEQSLGAQLQKKIKElqariEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAG---GATAAQI-EMNK 1169
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGS-----GPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIaALRA 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1316056572 1170 KREAEFQKLRRDLEESTLQHEATAAALR------KKQADSVAELGEQIDNLQR 1216
Cdd:COG3206 306 QLQQEAQRILASLEAELEALQAREASLQaqlaqlEARLAELPELEAELRRLER 358
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1418-1712 |
1.84e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1418 LEKTKQ-RLQGEVEDLMTDVERANSLAANLDKKQRNFDK---VLAEWKQKYEESQAELEGAQKEARslstelfkmknsye 1493
Cdd:pfam17380 293 FEKMEQeRLRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEER-------------- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1494 ealdqletmKRENKNLQQEisdlteQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEgtleheESKILrvqlelnqvK 1573
Cdd:pfam17380 359 ---------KRELERIRQE------EIAMEISRMRELERLQMERQQKNERVRQELEAAR------KVKIL---------E 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1574 SEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTLDAEvRSRndalrvkkkmegdlnEME-IQLSHANRQaaEAQKQLRNVQG 1652
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEE-RAR---------------EMErVRLEEQERQ--QQVERLRQQEE 470
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1653 QLKDAQLHLDDAVRGQEDMKEQvamverRNGLMVAEIEELRAALEQTERSRKVAEQELVD 1712
Cdd:pfam17380 471 ERKRKKLELEKEKRDRKRAEEQ------RRKILEKELEERKQAMIEEERKRKLLEKEMEE 524
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
952-1298 |
1.86e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 952 SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKL 1031
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1032 EQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDEKIKKKDFEISQLlsKIEDEQSLGAQLQKK 1111
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL--EQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1112 IKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQhEA 1191
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE-EL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1192 TAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENV 1271
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
330 340
....*....|....*....|....*..
gi 1316056572 1272 RQLNDINAQKARLQTENGEFARQLEEK 1298
Cdd:COG4372 344 QLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1453-1623 |
1.91e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1453 FDKVLAEWKQKYEESQAE--LEGAQKEARSLSTElfKMKNSYEEALDQLETMKRENKNLQQEISDLTEQigetgksiheL 1530
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKriLEEAKKEAEAIKKE--ALLEAKEEIHKLRNEFEKELRERRNELQKLEKR----------L 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1531 EKAKKTVEtEKSEiqaALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRNS-----QRVIDSMQSTL 1605
Cdd:PRK12704 92 LQKEENLD-RKLE---LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTaeeakEILLEKVEEEA 167
|
170
....*....|....*...
gi 1316056572 1606 DAEVrsrndALRVKKKME 1623
Cdd:PRK12704 168 RHEA-----AVLIKEIEE 180
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
837-1287 |
2.27e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.98 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 837 YFKIKPLLKsaETEKELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEErcegliksk 916
Cdd:PRK04778 100 FRKAKHEIN--EIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSFGPALD--------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 917 iQLEAKLKETTERLEDEEEINAE---LTAKK--RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDE 991
Cdd:PRK04778 169 -ELEKQLENLEEEFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGY 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 992 AIA--KLTKEKKALQEAHQQTLDDLqaEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQES 1069
Cdd:PRK04778 248 HLDhlDIEKEIQDLKEQIDENLALL--EELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQ 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1070 IMDLENDKQQSDEKikkkdFEISqllskiEDEQSLGAQLQKKIKELQarieeleeeiEAERAARAKVEKQRA---DLSRE 1146
Cdd:PRK04778 326 NKELKEEIDRVKQS-----YTLN------ESELESVRQLEKQLESLE----------KQYDEITERIAEQEIaysELQEE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1147 LEEISERLEEAggataaqiemnkkrEAEFQKLRRDLeestlqheataAALRKkqADSVAElgeqiDNLQRVKQKLEKEKS 1226
Cdd:PRK04778 385 LEEILKQLEEI--------------EKEQEKLSEML-----------QGLRK--DELEAR-----EKLERYRNKLHEIKR 432
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316056572 1227 efKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTE 1287
Cdd:PRK04778 433 --YLEKSNLPGLPEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEE 491
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
856-1002 |
2.75e-04 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 45.52 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 856 MKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEercegLIKSKI-QLEAKLKETTERLEdee 934
Cdd:pfam10186 17 ARNRLYELRVDLARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKLR-----LLKSEVaISNERLNEIKDKLD--- 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316056572 935 EINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKA 1002
Cdd:pfam10186 89 QLRREIAEKKKKIEKLRSSLKQRRSDLESASYQLEERRASQLAKLQNSIKRIKQKWTALHSKTAESRS 156
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1422-1575 |
3.10e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.01 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1422 KQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSL----STELFKMKNsyeeald 1497
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELedcdPTELDRAKE------- 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316056572 1498 QLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGtleHEESKILRVQLELNQVKSE 1575
Cdd:smart00787 212 KLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG---FTFKEIEKLKEQLKLLQSL 286
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1729-1930 |
3.66e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1729 NTKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLA 1808
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1809 mkggKKQLQKLEQRVREL-------ETEVEGEQKRGADAVKGVRKYERRVKELTYQTEEDKKNITRLQDLVDKLQLKVKA 1881
Cdd:COG4942 100 ----EAQKEELAELLRALyrlgrqpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1316056572 1882 YKRQAEEAEEQANSHMSRLRKVQHEMEEAQERADIAESQVNKLRAKSRD 1930
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
847-979 |
3.76e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 847 AETEKELQNMKENYEKMQSDLTTALAKKKELEEKMVSL--LQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAKLK 924
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVeaRIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1316056572 925 ETTERLEDEE----EINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKV 979
Cdd:COG1579 114 ELMERIEELEeelaELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
913-1188 |
3.79e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 913 IKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDID--------------DLELTLAKVEKEKHATENK 978
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDrqaaiyaeqermamERERELERIRQEERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 979 vKNLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQA-------EEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKlRMD 1051
Cdd:pfam17380 364 -RIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAarkvkilEEERQRKIQQQKVEMEQIRAEQEEARQREVR-RLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1052 LERAkRKLEGDLKLAQESIMDLENDKQQSDEKIKKKdfeisQLLSKIEDEQSLGAQLQKKI--KELQARIEELEEEIEAE 1129
Cdd:pfam17380 442 EERA-REMERVRLEEQERQQQVERLRQQEEERKRKK-----LELEKEKRDRKRAEEQRRKIleKELEERKQAMIEEERKR 515
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1316056572 1130 RAARAKVEKQRADLSREleeisERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQ 1188
Cdd:pfam17380 516 KLLEKEMEERQKAIYEE-----ERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE 569
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1375-1894 |
3.96e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1375 WRSKYE---TDAIQRTEE-LEEAKKKLAQ-RLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKK 1449
Cdd:PRK04778 69 WRQKWDeivTNSLPDIEEqLFEAEELNDKfRFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1450 QRNFDKVLAEWKQKYEESQAELEgaqKEARSLSTELFKMKN-----SYEEALDQLETMKRENKNLQQEISDLTEQigetg 1524
Cdd:PRK04778 149 YRELRKSLLANRFSFGPALDELE---KQLENLEEEFSQFVEltesgDYVEAREILDQLEEELAALEQIMEEIPEL----- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1525 ksiheLEKAKKTVETEKSEIQAA---LEEAEGTLEHE--ESKILRVQLELNQVKSEIDR-KLAEKDEEMEQIKRNsqrvI 1598
Cdd:PRK04778 221 -----LKELQTELPDQLQELKAGyreLVEEGYHLDHLdiEKEIQDLKEQIDENLALLEElDLDEAEEKNEEIQER----I 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1599 DSMQSTLDAEVRSRNDalrVKKKMEgdlnEMEIQLSHANRQAAEAQKQLRnvqgqlkdaqlHLDDAVRGQEDMKEQVAMV 1678
Cdd:PRK04778 292 DQLYDILEREVKARKY---VEKNSD----TLPDFLEHAKEQNKELKEEID-----------RVKQSYTLNESELESVRQL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1679 ERrnglmvaEIEELRAALEQTERsrKVAEQELVdaservgllhsqNSSLLNTKKKLETDLVQV---QGEVDDAVQEARNA 1755
Cdd:PRK04778 354 EK-------QLESLEKQYDEITE--RIAEQEIA------------YSELQEELEEILKQLEEIekeQEKLSEMLQGLRKD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1756 EDKAKKAitdaammaeelkkeqdtsahLERMKKNLEVTvkdlqHRLDEAENLAmkggkkqlqKLEQRVRELETEVEGEqk 1835
Cdd:PRK04778 413 ELEAREK--------------------LERYRNKLHEI-----KRYLEKSNLP---------GLPEDYLEMFFEVSDE-- 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1316056572 1836 rgadavkgvrkyerrVKELTYQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQAN 1894
Cdd:PRK04778 457 ---------------IEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENAT 500
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
880-1181 |
4.19e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 880 KMVSLLQEKNDL--QLQVASEVENLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEinAELTAKKRKLEDECSELKKD 957
Cdd:PRK05771 10 LIVTLKSYKDEVleALHELGVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLP--KLNPLREEKKKVSVKSLEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 958 IDDLELTLAKVEKEkhatenkVKNLTEEMATQDEAIAKLTKEKKALQEAHqqTLD-DLQAEEDKVNTLTKAKTKLEQQVD 1036
Cdd:PRK05771 88 IKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERLEPWG--NFDlDLSLLLGFKYVSVFVGTVPEDKLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1037 DLEGSLEQEKklrmdLERAKRKLEGDLKLaqesIMDLENDKQQSDEKIKKKDFE---------ISQLLSKIEDEqslgaq 1107
Cdd:PRK05771 159 ELKLESDVEN-----VEYISTDKGYVYVV----VVVLKELSDEVEEELKKLGFErleleeegtPSELIREIKEE------ 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316056572 1108 lqkkIKELqarieeleeeieaeraarakvEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRD 1181
Cdd:PRK05771 224 ----LEEI---------------------EKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSKFLKT 272
|
|
| COG6 |
smart01087 |
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ... |
1376-1511 |
4.31e-04 |
|
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localisation.
Pssm-ID: 215018 Cd Length: 598 Bit Score: 45.39 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1376 RSKYETDAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQrnfdK 1455
Cdd:smart01087 9 RSDLEKRLLKINGEFLSEFKPVAEQLQRLSEDVQKLNNSCDSMKDQLNTAKNQTQDLISEASELQEELALLELKK----K 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1316056572 1456 VLAEWKQKYEESQAELEGAQKEARSLSTELFKmknsyeeALDQLETMKRENKNLQQ 1511
Cdd:smart01087 85 LLDAFLSKFTLSQDELDVLTSREGPIDDEFFQ-------VLDKVQEIHEDCSVLLQ 133
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1250-1496 |
4.46e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 45.23 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1250 EKMCRtLEDQLSEIKS------KNDENVR-QLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRH 1322
Cdd:pfam09726 395 DALVR-LEQDIKKLKAelqasrQTEQELRsQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKR 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1323 IEEEVKAKNALahavqsarhdcdllREQFEEEQEAKAELQRGMSKANSEVAQWRSKYETDAIQRTEELEEAKKKLAQRLQ 1402
Cdd:pfam09726 474 LKAEQEARASA--------------EKQLAEEKKRKKEEEATAARAVALAAASRGECTESLKQRKRELESEIKKLTHDIK 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1403 EAEESIEAVNSKCASLEKTKQRlQGEVEDLMTdveranSLAANLDKKQRNFDKVLAEWKQKYE------ESQAELEGAQK 1476
Cdd:pfam09726 540 LKEEQIRELEIKVQELRKYKES-EKDTEVLMS------ALSAMQDKNQHLENSLSAETRIKLDlfsalgDAKRQLEIAQG 612
|
250 260
....*....|....*....|
gi 1316056572 1477 EARSLSTELFKMKNSYEEAL 1496
Cdd:pfam09726 613 QIYQKDQEIKDLKQKIAEVM 632
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1446-1928 |
4.47e-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: 45.34 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1446 LDKKQRNFDKVLAEWKQKYEESQAELEgaqKEARSLSTELFKMKNSyEEALDQLETMKRENKNLQQEISDLTEQIGETGK 1525
Cdd:TIGR00618 199 LTLRSQLLTLCTPCMPDTYHERKQVLE---KELKHLREALQQTQQS-HAYLTQKREAQEEQLKKQQLLKQLRARIEELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1526 SIHELEKAKKTVETEKSEIQAALEEAEgtLEHEESKILRVQLELNQVKSEIDRKLAEKDEEMEQiKRNSQRVIDSMQSTL 1605
Cdd:TIGR00618 275 QEAVLEETQERINRARKAAPLAAHIKA--VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ-QSSIEEQRRLLQTLH 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1606 DAEVRSRNDALRVKK-KMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDA----QLHLDDAVRGQEDMKEQVAMVER 1680
Cdd:TIGR00618 352 SQEIHIRDAHEVATSiREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDIlqreQATIDTRTSAFRDLQGQLAHAKK 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1681 RNGLMVAEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKlETDLVQVQGEVDDAVQEARNAEDKAK 1760
Cdd:TIGR00618 432 QQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ-ETRKKAVVLARLLELQEEPCPLCGSC 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1761 KAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLAmkggkKQLQKLEQRVRELETEVEGEQKRGADA 1840
Cdd:TIGR00618 511 IHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQR-----ASLKEQMQEIQQSFSILTQCDNRSKED 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1841 VKGVRKYERRV-KELTYQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEEAQERADIAES 1919
Cdd:TIGR00618 586 IPNLQNITVRLqDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL 665
|
....*....
gi 1316056572 1920 QVNKLRAKS 1928
Cdd:TIGR00618 666 SIRVLPKEL 674
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1257-1483 |
4.48e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1257 EDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHA 1336
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1337 VQSARHDCDLLR--------EQFEEEQEAKAELQRGMSKANSEVAQWRSKYE---TDAIQRTEELEEAKKKLAQRLQEAE 1405
Cdd:COG3883 95 LYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEakkAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316056572 1406 ESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLST 1483
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
828-1115 |
4.55e-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: 45.34 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 828 VKNWPWMNLYFKIKPLLKSAETEKELQNMKENYEKMQSDLTtalaKKKELEEKMVSLLQEKNDLqlqvasevenlsdAEE 907
Cdd:TIGR00618 596 LQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ----CSQELALKLTALHALQLTL-------------TQE 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 908 RCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLakvEKEKHATENKVKNLTEEMA 987
Cdd:TIGR00618 659 RVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY---DREFNEIENASSSLGSDLA 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 988 TQDEAIAKLTKEK--------KALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKL 1059
Cdd:TIGR00618 736 AREDALNQSLKELmhqartvlKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD 815
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 1060 EGDLKLAQESIM-DLENDKQQSDEKiKKKDFEISQLLSKIEDEQSLGAQLQKKIKEL 1115
Cdd:TIGR00618 816 EDILNLQCETLVqEEEQFLSRLEEK-SATLGEITHQLLKYEECSKQLAQLTQEQAKI 871
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1385-1751 |
4.88e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1385 QRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKY 1464
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1465 EESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEI 1544
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1545 QAALEEAEGTLEHEESKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALRVKKKMEG 1624
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1625 DLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMKEQVAMVERRNGLMVAEIEELRAALEQTERSRK 1704
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1316056572 1705 VAEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQE 1751
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1687-1920 |
4.92e-04 |
|
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: 44.67 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1687 AEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDA 1766
Cdd:pfam19220 27 ADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1767 AMMAEELKkeqDTSAHLERMKKNLEVTVKDLQHRLDEAENLamkggKKQLQKLEQRVRELETEVEGEQKRGADAvkgvrk 1846
Cdd:pfam19220 107 EELRIELR---DKTAQAEALERQLAAETEQNRALEEENKAL-----REEAQAAEKALQRAEGELATARERLALL------ 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316056572 1847 yerrvkeltyqtEEDKKnitRLQDLVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEEAQERADIAESQ 1920
Cdd:pfam19220 173 ------------EQENR---RLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQ 231
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1259-1421 |
5.12e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1259 QLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEE------EVK-AK- 1330
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlgNVRnNKe 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1331 -NALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAqwrskyetdaiQRTEELEEAKKKLAQRLQEAEESIE 1409
Cdd:COG1579 91 yEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA-----------ELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|..
gi 1316056572 1410 AVNSKCASLEKT 1421
Cdd:COG1579 160 ELEAEREELAAK 171
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1579-1924 |
5.42e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1579 KLAEKDEEMEQIKRNsqrvidsmQSTLDAEVRSRND-------ALRVKKKME---GDLNEMEIQLSHANRQAAEAQKQLR 1648
Cdd:COG3096 307 RLVEMARELEELSAR--------ESDLEQDYQAASDhlnlvqtALRQQEKIEryqEDLEELTERLEEQEEVVEEAAEQLA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1649 NVQ--------------GQLKDAQLHLD----------DAVRGQEDMKEQVAMVERRNGLMVAEIEELRAALEQTERSRK 1704
Cdd:COG3096 379 EAEarleaaeeevdslkSQLADYQQALDvqqtraiqyqQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVL 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1705 VAEQELVDASERvgllHSQNSsllntkKKLETdLVQVQGEVddavqEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLE 1784
Cdd:COG3096 459 ELEQKLSVADAA----RRQFE------KAYEL-VCKIAGEV-----ERSQAWQTARELLRRYRSQQALAQRLQQLRAQLA 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1785 RMKKNLevtvkdlqHRLDEAENLAMKGGKKQLQK------LEQRVRELETEVEGEQKRGADAVKGVRKYERRVKELTYQT 1858
Cdd:COG3096 523 ELEQRL--------RQQQNAERLLEEFCQRIGQQldaaeeLEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARI 594
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316056572 1859 EEDKKNITR---LQDLVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEEAQERADIAESQVNKL 1924
Cdd:COG3096 595 KELAARAPAwlaAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1296-1578 |
5.50e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1296 EEKEALVSQLtRGKQAFtqQIEELKRHIEEEVKAKnalahavqsarhdcdlLREQFEEEQEAKAELQRGMSKANSEVaqw 1375
Cdd:PRK05771 16 SYKDEVLEAL-HELGVV--HIEDLKEELSNERLRK----------------LRSLLTKLSEALDKLRSYLPKLNPLR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1376 rskyETDAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLM------TDVERANSL------A 1443
Cdd:PRK05771 74 ----EEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdLDLSLLLGFkyvsvfV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1444 ANLDKKQRNFDKVLAEWKQKYEESQAELEG-----AQKEARSLSTELFKmKNSYEE-ALDQLETMKRENKNLQQEISDLT 1517
Cdd:PRK05771 150 GTVPEDKLEELKLESDVENVEYISTDKGYVyvvvvVLKELSDEVEEELK-KLGFERlELEEEGTPSELIREIKEELEEIE 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1316056572 1518 EQIGETgksIHELEKAKKTVETeksEIQAALEEAEGTLEHEE--SKILR----VQLE-------LNQVKSEIDR 1578
Cdd:PRK05771 229 KERESL---LEELKELAKKYLE---ELLALYEYLEIELERAEalSKFLKtdktFAIEgwvpedrVKKLKELIDK 296
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1748-1915 |
5.60e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1748 AVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTvKDLQHRLDEAenlamkggKKQLQKLEQRVRELE 1827
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFE-KELRERRNEL--------QKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1828 TEVEGEQKRGADAVKGVRKYERRVKELTYQTEEDKKNItrlQDLVDKLQ-----LKVKAYKRQAEEAEEQANSHMSRLrk 1902
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI---EEQLQELErisglTAEEAKEILLEKVEEEARHEAAVL-- 174
|
170
....*....|...
gi 1316056572 1903 VQHEMEEAQERAD 1915
Cdd:PRK12704 175 IKEIEEEAKEEAD 187
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1633-1927 |
6.36e-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: 44.94 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1633 LSHANR------QAAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMKEQVAMVER------------RNGL--------MV 1686
Cdd:COG3096 274 MRHANErrelseRALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQdyqaasdhlnlvQTALrqqekierYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1687 AEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQnssllntKKKLETDLVQVQGEVDD------AVQEARNAEDKAK 1760
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEE-------VDSLKSQLADYQQALDVqqtraiQYQQAVQALEKAR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1761 KAITDAAMMAEELKKEQdtsAHLERMKKNLEVTVKDLQHRLDEAEnlamkGGKKQLQKLEQRVRELETEVEGEQKRGAdA 1840
Cdd:COG3096 427 ALCGLPDLTPENAEDYL---AAFRAKEQQATEEVLELEQKLSVAD-----AARRQFEKAYELVCKIAGEVERSQAWQT-A 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1841 VKGVRKYER------RVKELTYQTEEDKKNITRLQDLVDKLQLKVKAYKRQ---AEEAEEQANSHMSRLRKVQHEMEEAQ 1911
Cdd:COG3096 498 RELLRRYRSqqalaqRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQldaAEELEELLAELEAQLEELEEQAAEAV 577
|
330
....*....|....*.
gi 1316056572 1912 ERADIAESQVNKLRAK 1927
Cdd:COG3096 578 EQRSELRQQLEQLRAR 593
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1191-1420 |
6.38e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1191 ATAAALRKKQADSVAELGEQIDNLQRvkqklekeksefkmEIDDLSSNMEAVAKAKgnlekmcRTLEDQLSEIKSKNDEN 1270
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQA--------------ELDALQAELEELNEEY-------NELQAELEALQAEIDKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1271 VRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTR-----------GKQAFTQQIEELKRHIEEEVKA-KNALAHAVQ 1338
Cdd:COG3883 71 QAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgsesfsdflDRLSALSKIADADADLLEELKAdKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1339 SARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKyETDAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASL 1418
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
..
gi 1316056572 1419 EK 1420
Cdd:COG3883 230 AA 231
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1307-1544 |
6.59e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1307 RGKQAFTQQIEELKRHIEEEVKAKNALahavqsarhdcdllreQFEEEQEAKAELQRGMSKANSEVAQWRSkYETDAIQR 1386
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNKN----------------IEEQRKKNGENIARKQNKYDELVEEAKT-IKAEIEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1387 TEELEEakkkLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVE-------------DLMTDVERANSLAANLDKKQRNF 1453
Cdd:PHA02562 240 TDELLN----LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcptctqQISEGPDRITKIKDKLKELQHSL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1454 DKVlaewkqkyEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKA 1533
Cdd:PHA02562 316 EKL--------DTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDE 387
|
250
....*....|.
gi 1316056572 1534 KKTVETEKSEI 1544
Cdd:PHA02562 388 LDKIVKTKSEL 398
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
845-1003 |
7.75e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 845 KSAETEKELQNM-------KENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVE----------------- 900
Cdd:PHA02562 210 KNGENIARKQNKydelveeAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfqkvikmyekggvcpt 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 901 ---NLSDAEERCEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLedecSELKKDIDDLELTLAKVEKEKHATEN 977
Cdd:PHA02562 290 ctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKL----LELKNKISTNKQSLITLVDKAKKVKA 365
|
170 180
....*....|....*....|....*.
gi 1316056572 978 KVKNLTEEMATQDEAIAKLTKEKKAL 1003
Cdd:PHA02562 366 AIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1382-1676 |
8.00e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1382 DAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSL-AANLDKKQRNFDKV-LAE 1459
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALkDDNDEETRETLSTLsLRQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1460 WKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETmkrenkNLQ--QEISDLTEQIGETGKSIHELEKAKKTV 1537
Cdd:PRK11281 126 LESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYA------NSQrlQQIRNLLKGGKVGGKALRPSQRVLLQA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1538 ETEKSEIQAALEEAE----------GTLEHEES--KILRVQLELNQVKSEIDRK-LAEKDEEMEQikrnsqrvidsmQST 1604
Cdd:PRK11281 200 EQALLNAQNDLQRKSlegntqlqdlLQKQRDYLtaRIQRLEHQLQLLQEAINSKrLTLSEKTVQE------------AQS 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1316056572 1605 LDAEVRSRNDALRVKkkmEGDLNemeIQLSHANRQAAEAQKQLrnVQGQLKDAQLhLDDAVRGQEDMKEQVA 1676
Cdd:PRK11281 268 QDEAARIQANPLVAQ---ELEIN---LQLSQRLLKATEKLNTL--TQQNLRVKNW-LDRLTQSERNIKEQIS 330
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
855-1100 |
8.12e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.46 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 855 NMKENYEKMQSDLTTALAKKKELEEkmvslLQEKNDLqLQVASEVENLSDAEERCEGLiksKIQLEAKLKETTERLEDEE 934
Cdd:PLN03229 508 VLMEKIEKLKDEFNKRLSRAPNYLS-----LKYKLDM-LNEFSRAKALSEKKSKAEKL---KAEINKKFKEVMDRPEIKE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 935 EINAeltakkRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIakltkEKKALQEAHQQTLDDL 1014
Cdd:PLN03229 579 KMEA------LKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSMGLEVIGV-----TKKNKDTAEQTPPPNL 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1015 QAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKklrmdLERAKRKLEGDLKLAQEsimdLENDKQQSDEKIKKKdFEISQL 1094
Cdd:PLN03229 648 QEKIESLNEEINKKIERVIRSSDLKSKIELLK-----LEVAKASKTPDVTEKEK----IEALEQQIKQKIAEA-LNSSEL 717
|
....*.
gi 1316056572 1095 LSKIED 1100
Cdd:PLN03229 718 KEKFEE 723
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1556-1924 |
8.38e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1556 EHEESKILRVQLELNQVKSEIDRKLAEKDE-------EMEQIKRNSQRVIDSMQSTLDAEVRSRNdALRVKKKME---GD 1625
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQYrlvemarELAELNEAESDLEQDYQAASDHLNLVQT-ALRQQEKIEryqAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1626 LNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAvrgqedmKEQVAMVERRnglmvAEIEELRA--------ALE 1697
Cdd:PRK04863 357 LEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDEL-------KSQLADYQQA-----LDVQQTRAiqyqqavqALE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1698 QTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDLvqvqgevdDAVQEARNAEDKAKKAIT---------DAAM 1768
Cdd:PRK04863 425 RAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKL--------SVAQAAHSQFEQAYQLVRkiagevsrsEAWD 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1769 MAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDE---AENLAMKGGKKQLQK------LEQRVRELETEVEGEQKRGAD 1839
Cdd:PRK04863 497 VARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQqqrAERLLAEFCKRLGKNlddedeLEQLQEELEARLESLSESVSE 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1840 AVKGVRKYERRVKELTYQTEEDKKNITR---LQDLVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEEAQERADI 1916
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQA 656
|
....*...
gi 1316056572 1917 AESQVNKL 1924
Cdd:PRK04863 657 LDEEIERL 664
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1135-1297 |
9.13e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1135 KVEKQRADLSRELEEISERLEEAggatAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQ-----ADSVAELGE 1209
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAAL----EARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1210 QIDNLQRVKQKLEKEKSEFKMEIDDLSsnmEAVAKAKGNLEKmcrtLEDQLSEIKSKNDEnvrQLNDINAQKARLQTENG 1289
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELE---EELAELEAELAE----LEAELEEKKAELDE---ELAELEAELEELEAERE 166
|
....*...
gi 1316056572 1290 EFARQLEE 1297
Cdd:COG1579 167 ELAAKIPP 174
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1301-1712 |
9.72e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.12 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1301 LVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALahavqsarhdcdlLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYE 1380
Cdd:PLN02939 32 AVSCRARRRGFSSQQKKKRGKNIAPKQRSSNSK-------------LQSNTDENGQLENTSLRTVMELPQKSTSSDDDHN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1381 TDAIQRTEELEEAKKKLAQRLQEAEE----SIEAVNSKCASLEKT-----KQRLQ--GEVEDLMTDVE----RANSLAAN 1445
Cdd:PLN02939 99 RASMQRDEAIAAIDNEQQTNSKDGEQlsdfQLEDLVGMIQNAEKNilllnQARLQalEDLEKILTEKEalqgKINILEMR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1446 LDKKQRNFdKVLAEWKQKYEESQAELEGAQKEARSLSTelfkMKNSYEEAL-DQLETMKRENKNLQQEISDLTEQ---IG 1521
Cdd:PLN02939 179 LSETDARI-KLAAQEKIHVEILEEQLEKLRNELLIRGA----TEGLCVHSLsKELDVLKEENMLLKDDIQFLKAElieVA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1522 ETGKSIHELEKakktvetEKSEIQAALEEAegtleheESKILRVQLELNQVKSEIDRKLAEKDEEMEQIKRNSQRVIDSM 1601
Cdd:PLN02939 254 ETEERVFKLEK-------ERSLLDASLREL-------ESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1602 QSTLDaevrsRNDALRVKkkmegdLNEMEIQLSHANRQAAEAQKqLRNVQGQLKDAQLHLDdavRGQEDMKEQVAMVERr 1681
Cdd:PLN02939 320 ALVLD-----QNQDLRDK------VDKLEASLKEANVSKFSSYK-VELLQQKLKLLEERLQ---ASDHEIHSYIQLYQE- 383
|
410 420 430
....*....|....*....|....*....|..
gi 1316056572 1682 nglmvaEIEELRAALEQ-TERSRKVAEQELVD 1712
Cdd:PLN02939 384 ------SIKEFQDTLSKlKEESKKRSLEHPAD 409
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1060-1318 |
1.03e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1060 EGDLKLAQESIMDLENDKQQSDEKIKKKDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEEleeeieaeraARAKVEKQ 1139
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE----------AEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1140 RADLSRELEEISErleeaGGATAAQIEMnkkreaefqklrrdLEESTlqheataaalrkkqadSVAELGEQIDNLQRVKQ 1219
Cdd:COG3883 85 REELGERARALYR-----SGGSVSYLDV--------------LLGSE----------------SFSDFLDRLSALSKIAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1220 KLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKE 1299
Cdd:COG3883 130 ADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
250
....*....|....*....
gi 1316056572 1300 ALVSQLTRGKQAFTQQIEE 1318
Cdd:COG3883 210 AAAAAAAAAAAAAAAAAAA 228
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1374-1701 |
1.07e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.69 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1374 QWRSKYET-------DAIQRTEELEEAKKKLaqRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMtDVERANSLAAN- 1445
Cdd:pfam06160 49 EWRKKWDDivtkslpDIEELLFEAEELNDKY--RFKKAKKALDEIEELLDDIEEDIKQILEELDELL-ESEEKNREEVEe 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1446 LDKKQRNFDKVLAEWKQKYEESQAELE-----------------------GAQKEARSLSTELF--------------KM 1488
Cdd:pfam06160 126 LKDKYRELRKTLLANRFSYGPAIDELEkqlaeieeefsqfeeltesgdylEAREVLEKLEEETDaleelmedipplyeEL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1489 KNSYEEALDQLE----TMKREN-----KNLQQEISDLTEQIGETGKSIHELE--------------------------KA 1533
Cdd:pfam06160 206 KTELPDQLEELKegyrEMEEEGyalehLNVDKEIQQLEEQLEENLALLENLEldeaeealeeieeridqlydllekevDA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1534 KKTVETEKSEIQAALEEAEGTLEHEESKILRVQL-----------------ELNQVK-----------------SEIDRK 1579
Cdd:pfam06160 286 KKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQsytlnenelervrglekQLEELEkrydeiverleekevaySELQEE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1580 LAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALRVKKKME------------GDLNEMEIQLSHANRQAAEAQKQL 1647
Cdd:pfam06160 366 LEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELReikrlveksnlpGLPESYLDYFFDVSDEIEDLADEL 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 1648 RN-------VQGQLKDAQLHLDDAVRGQEDMKEQVAMVERrngLMV------AEIEELRAALEQTER 1701
Cdd:pfam06160 446 NEvplnmdeVNRLLDEAQDDVDTLYEKTEELIDNATLAEQ---LIQyanryrSSNPEVAEALTEAEL 509
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1623-1840 |
1.25e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1623 EGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAvrgqedmkeqvamverrnglmVAEIEELRAALEQTERS 1702
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNEL---------------------QAELEALQAEIDKLQAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1703 RKVAEQELVDASERVG--LLHSQNSSLLNTkkKLE--------TDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEE 1772
Cdd:COG3883 74 IAEAEAEIEERREELGerARALYRSGGSVS--YLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316056572 1773 LKKEQDTsahLERMKKNLEVTVKDLQHRLDEAENLaMKGGKKQLQKLEQRVRELETEVEGEQKRGADA 1840
Cdd:COG3883 152 LEAKLAE---LEALKAELEAAKAELEAQQAEQEAL-LAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
925-1222 |
1.30e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 925 ETTERLEDEEEINAEL-TAKKRKL-EDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKA 1002
Cdd:PRK11281 30 ASNGDLPTEADVQAQLdALNKQKLlEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1003 LQEAHQQTLDDLQAEEdkvntltkaktkLEQQVDDLEGSLEQEKK-----------LRMDLERAKRKLEGDLKLAQEsIm 1071
Cdd:PRK11281 110 NDEETRETLSTLSLRQ------------LESRLAQTLDQLQNAQNdlaeynsqlvsLQTQPERAQAALYANSQRLQQ-I- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1072 dlenDKQQSDEKIKKKDFEISQlLSKIEDEQS-LGAQLQKKIKELQARIEELEEEieaeraarakvEKQRADLSrelEEI 1150
Cdd:PRK11281 176 ----RNLLKGGKVGGKALRPSQ-RVLLQAEQAlLNAQNDLQRKSLEGNTQLQDLL-----------QKQRDYLT---ARI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1151 SeRLEEAggATAAQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQI------------DNLqRVK 1218
Cdd:PRK11281 237 Q-RLEHQ--LQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLlkateklntltqQNL-RVK 312
|
....
gi 1316056572 1219 QKLE 1222
Cdd:PRK11281 313 NWLD 316
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
847-1196 |
1.36e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 847 AETEKELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAKLKET 926
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 927 TERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKalqea 1006
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA----- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1007 hQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDEKIKK 1086
Cdd:COG4372 182 -EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1087 KDFEISQLLSKIEDEQSLGAQLQKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIE 1166
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
330 340 350
....*....|....*....|....*....|
gi 1316056572 1167 MNKKREAEFQKLRRDLEESTLQHEATAAAL 1196
Cdd:COG4372 341 DLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1578-1931 |
1.39e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1578 RKLAEKDEEMEQIKRNSQRVIDSMQSTLdAEVRsrnDALRVKKKMEGDLnEMEIQLS--HANR--QAAEAQKQLRNVQGQ 1653
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRL-VEMA---RELEELSARESDL-EQDYQAAsdHLNLvqTALRQQEKIERYQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1654 LKDAQLHLDDAVRGQEDMKEQVAMVERRNGLMVAEIEELR---AALEQ---TERSRKVAEQELVDASERV-GLLHSQNSS 1726
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKsqlADYQQaldVQQTRAIQYQQAVQALEKArALCGLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1727 LLNTKKKLETDLVQVQgEVDDAVQEARNAEDKAKKAIT--DAAMMA-EELKKEQDTSAHLERMKKNLEvTVKDLQHRLDE 1803
Cdd:COG3096 436 PENAEDYLAAFRAKEQ-QATEEVLELEQKLSVADAARRqfEKAYELvCKIAGEVERSQAWQTARELLR-RYRSQQALAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1804 AENLAMkggkkQLQKLEQRVRELEtEVEGEQKRGADAVKGVRKYERRVKELTYQTEEdkknitRLQDLVDKLQlKVKAYK 1883
Cdd:COG3096 514 LQQLRA-----QLAELEQRLRQQQ-NAERLLEEFCQRIGQQLDAAEELEELLAELEA------QLEELEEQAA-EAVEQR 580
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1316056572 1884 RQAEEAEEQANSHMSRLRKVQHEMEEAQERADIAESQVNKLRAKSRDV 1931
Cdd:COG3096 581 SELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEV 628
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1796-1927 |
1.41e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1796 DLQHRLDEAENLA--MKGGKKQLQKLEQRVRELETEVEGEQKRGADAVKGVRKYERRVKELTYQTEEDKKNITRLQDL-- 1871
Cdd:COG1579 11 DLQELDSELDRLEhrLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNke 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1316056572 1872 VDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEEAQERADIAESQVNKLRAK 1927
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1219-1623 |
1.51e-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: 43.52 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1219 QKLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDEN---VRQLNDINAQKARLQTENgefarql 1295
Cdd:pfam05622 3 SEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGtpgGKKYLLLQKQLEQLQEEN------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1296 eekealvSQLTRGKQAFTQQIEELKRHIEEeVKAKN----ALAHAVQSARHDCDLLREQFEEeqeakaelqrgMSKANSE 1371
Cdd:pfam05622 76 -------FRLETARDDYRIKCEELEKEVLE-LQHRNeeltSLAEEAQALKDEMDILRESSDK-----------VKKLEAT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1372 VAQWRSKYE--TDAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTK---QRLQGEVEDLMTDVERA----NSL 1442
Cdd:pfam05622 137 VETYKKKLEdlGDLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKrqvQELHGKLSEESKKADKLefeyKKL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1443 AANLDKKQRNFDKVLAEwKQKYEESQAELEGAQKEARSLSTELFKMKNSYE------------EALDQLETMKRENKNL- 1509
Cdd:pfam05622 217 EEKLEALQKEKERLIIE-RDTLRETNEELRCAQLQQAELSQADALLSPSSDpgdnlaaeimpaEIREKLIRLQHENKMLr 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1510 -------QQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESK-----ILRVQLE-----LNQV 1572
Cdd:pfam05622 296 lgqegsyRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKaedssLLKQKLEehlekLHEA 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1316056572 1573 KSEIDRKLAEKDEEMEQIKRNSQRVIDSMQSTL---DAEVRSRNDalRVKKKME 1623
Cdd:pfam05622 376 QSELQKKKEQIEELEPKQDSNLAQKIDELQEALrkkDEDMKAMEE--RYKKYVE 427
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1685-1931 |
1.64e-03 |
|
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: 43.51 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1685 MVAEI-----EELRAALEQ-------TERsRKVAEQELVDASE---RVGLLHSQnssllnTKKKLETdlVQVQGEVDDAV 1749
Cdd:TIGR02168 145 KISEIieakpEERRAIFEEaagiskyKER-RKETERKLERTREnldRLEDILNE------LERQLKS--LERQAEKAERY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1750 QEARNAEDKAKKAItdAAMMAEELKKEQDTsahLERMKKNLEVTVKDLQHRLDEAEnlamkggkKQLQKLEQRVRELETE 1829
Cdd:TIGR02168 216 KELKAELRELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELE--------EKLEELRLEVSELEEE 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1830 VEGEQKRGADAVKGVRKYERRVKELTYQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEE 1909
Cdd:TIGR02168 283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE 362
|
250 260
....*....|....*....|..
gi 1316056572 1910 AQERADIAESQVNKLRAKSRDV 1931
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETL 384
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1314-1580 |
1.67e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1314 QQIEELKRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYE---TDAIQRTEEL 1390
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDelnEKLNELREEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1391 EEAKKKLAQrLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKqrnfdKVLAEWKQKYEESQAE 1470
Cdd:COG1340 95 DELRKELAE-LNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKA-----KKALEKNEKLKELRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1471 LEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEE 1550
Cdd:COG1340 169 LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKK 248
|
250 260 270
....*....|....*....|....*....|
gi 1316056572 1551 AEGTLEHEESKilRVQLELNQVKSEIDRKL 1580
Cdd:COG1340 249 LRKKQRALKRE--KEKEELEEKAEEIFEKL 276
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
848-1322 |
1.80e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 848 ETEKELQNMKEN---YEKMQSDLTTALAKKKELE------EKMVSLLQEKNDLQLQVAS--------EVENLSDAEERCE 910
Cdd:COG4913 222 DTFEAADALVEHfddLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAAlrlwfaqrRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 911 GLIKskiQLEAKLKETTERLEDEEEINAELTAKKRKLE-DECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQ 989
Cdd:COG4913 302 AELA---RLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 990 DEAIAKLTKEKKALQEAHQQTLDDLQAE----EDKVNTLTKAKTKLEQQVDDLEGS------------------------ 1041
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEAlaeaEAALRDLRRELRELEAEIASLERRksniparllalrdalaealgldea 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1042 -----------LEQEKKLRMDLERA-----------------------KRKLEGDL-----KLAQESIMDLENDKQQSDE 1082
Cdd:COG4913 459 elpfvgelievRPEEERWRGAIERVlggfaltllvppehyaaalrwvnRLHLRGRLvyervRTGLPDPERPRLDPDSLAG 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1083 KIKKKDFEISQLLS----------KIEDEQSL----------------------------------GAQLQKKIKELQAR 1118
Cdd:COG4913 539 KLDFKPHPFRAWLEaelgrrfdyvCVDSPEELrrhpraitragqvkgngtrhekddrrrirsryvlGFDNRAKLAALEAE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1119 IEeleeeieAERAARAKVEKQRADLSRELEEISERLEeaggaTAAQIEMNKKREAEFQKLRRDLEEstlqHEATAAALRK 1198
Cdd:COG4913 619 LA-------ELEEELAEAEERLEALEAELDALQERRE-----ALQRLAEYSWDEIDVASAEREIAE----LEAELERLDA 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1199 KQADsVAELGEQIDNLQRVKQKLEKeksefkmEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQlnDIN 1278
Cdd:COG4913 683 SSDD-LAALEEQLEELEAELEELEE-------ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLE 752
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1316056572 1279 AQKARLQTEN--GEFARQLEEK-EALVSQLTRGKQAFTQQIEELKRH 1322
Cdd:COG4913 753 ERFAAALGDAveRELRENLEERiDALRARLNRAEEELERAMRAFNRE 799
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
928-1079 |
1.86e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 928 ERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATEnkvKNLTEEMatqDEAIAKltKEKKALQ--- 1004
Cdd:PRK11637 75 AQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQE---RLLAAQL---DAAFRQ--GEHTGLQlil 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1005 --EAHQQTLDDL-------QAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLEN 1075
Cdd:PRK11637 147 sgEESQRGERILayfgylnQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLES 226
|
....*...
gi 1316056572 1076 ----DKQQ 1079
Cdd:PRK11637 227 slqkDQQQ 234
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1388-1919 |
1.93e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 43.09 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1388 EELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKqrlqGEVEDLMTDVERANslaanLDKKQRNFDKVLAEWKQKyees 1467
Cdd:pfam05701 42 LELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTK----RLIEELKLNLERAQ-----TEEAQAKQDSELAKLRVE---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1468 QAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGK----SIHELEKAKKTVETEKSE 1543
Cdd:pfam05701 109 EMEQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKraeeAVSASKEIEKTVEELTIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1544 IQAALEEAEGT----LEHEESKIlRVQLELNQVKSEIDRKLAEKDEEMEQIkRNSQRVIDSMQSTLDAevrsrNDALRVK 1619
Cdd:pfam05701 189 LIATKESLESAhaahLEAEEHRI-GAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKLET-----ASALLLD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1620 KK------MEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAvrgqedmKEQVAMVERRNGLMVAEIEELR 1693
Cdd:pfam05701 262 LKaelaayMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKA-------KDEVNCLRVAAASLRSELEKEK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1694 AALEQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAitdaammAEEL 1773
Cdd:pfam05701 335 AELASLRQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAA-------REEL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1774 KKEQD----TSAHLERMKKNLEVTVKDLqhrldEAENLAMKGGKKQLQKLEqrvrelETEVEGEQKRGADAVKGVrkyer 1849
Cdd:pfam05701 408 RKAKEeaeqAKAAASTVESRLEAVLKEI-----EAAKASEKLALAAIKALQ------ESESSAESTNQEDSPRGV----- 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 1850 rvkelTYQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEE-------AQERADIAES 1919
Cdd:pfam05701 472 -----TLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEErkealkiALEKAEKAKE 543
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
852-1232 |
1.96e-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: 43.19 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 852 ELQNMKENYEKMQSDLTTALAKKKELEekmvsllqEKNDLQLQVASEVENLSDAEERCEGLIKSKIQLEAKLKETTERLE 931
Cdd:pfam05557 150 EAEQLRQNLEKQQSSLAEAEQRIKELE--------FEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 932 DEEEINAELTAKKRKLEDEcSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQDEA---IAKLTKEKKALQEAHQ 1008
Cdd:pfam05557 222 NKLLLKEEVEDLKRKLERE-EKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLsrrIEQLQQREIVLKEENS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1009 QTLDDLQAEEdkvntltKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQesimdlendkqqsdekiKKKD 1088
Cdd:pfam05557 301 SLTSSARQLE-------KARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLT-----------------KERD 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1089 FeISQLLSKIEDEQSL---GAQLQKKIKELqarieeleeeieaeraarakvEKQRADLSRELEEISERLEEAGGATAAQI 1165
Cdd:pfam05557 357 G-YRAILESYDKELTMsnySPQLLERIEEA---------------------EDMTQKMQAHNEEMEAQLSVAEEELGGYK 414
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 1166 EMNKKREAEFQKLRRDleestlqheaTAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEI 1232
Cdd:pfam05557 415 QQAQTLERELQALRQQ----------ESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMEL 471
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1706-1895 |
1.98e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1706 AEQELVDASERVGLLHSQNSSLLNTKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDT-SAHLE 1784
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1785 RMKKN------LEV--TVKDLQHRLDEAENL--AMKGGKKQLQKLEQRVRELETEVEGEQKRGADAVKGVRKYERRVKEL 1854
Cdd:COG3883 94 ALYRSggsvsyLDVllGSESFSDFLDRLSALskIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1316056572 1855 TYQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQANS 1895
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
976-1236 |
2.03e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 976 ENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAEED----KVNTLTKAKTKLEQQVDDLEGSLeqeKKLRMD 1051
Cdd:PHA02562 187 DMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKtikaEIEELTDELLNLVMDIEDPSAAL---NKLNTA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1052 LERAKRKLEgdlKLAQESIMDLEND-----KQQSDE------KIKKKDFEISQLLSKIEDEQSlgaQLQKKIKELQarie 1120
Cdd:PHA02562 264 AAKIKSKIE---QFQKVIKMYEKGGvcptcTQQISEgpdritKIKDKLKELQHSLEKLDTAID---ELEEIMDEFN---- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1121 eleeeieaeraarakvekqraDLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLrrdleestlqheataaalrkkq 1200
Cdd:PHA02562 334 ---------------------EQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL---------------------- 370
|
250 260 270
....*....|....*....|....*....|....*.
gi 1316056572 1201 ADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIDDLS 1236
Cdd:PHA02562 371 QAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1440-1679 |
2.10e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.01 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1440 NSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTEL-------FKMKNSYEEALDQLETMKRENKNLQQE 1512
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKAtqtlakaQQVNAESERTLGHAKELAEAIKNLIDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1513 ISDLTEQIGETGKSIHELekakktvetEKSEIQAALEEAEGTLEHEESKILRVQLELNQvkseidrklAEKDEEMEQIKR 1592
Cdd:pfam06008 98 IKEINEKVATLGENDFAL---------PSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAE---------AELKAAQDLLSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1593 nsqrvIDSMQSTLDAEVRSRNDALRvkkkmeGDLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGQEDMK 1672
Cdd:pfam06008 160 -----IQTWFQSPQEENKALANALR------DSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVS 228
|
....*..
gi 1316056572 1673 EQVAMVE 1679
Cdd:pfam06008 229 EQKNQLE 235
|
|
| EcCorA_ZntB-like |
cd12821 |
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily ... |
1299-1411 |
2.15e-03 |
|
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. Members of this family are found in all three kingdoms of life. It is a functionally diverse family, including the Mg2+ transporters Escherichia coli and Salmonella typhimurium CorAs (which can also transport Co2+, and Ni2+ ), and the Zn2+ transporter Salmonella typhimurium ZntB which mediates the efflux of Zn2+ (and Cd2+). It also includes two Saccharomyces cerevisiae members: the inner membrane Mg2+ transporters Mfm1p/Lpe10p, and Mrs2p, and a family of Arabidopsis thaliana members (AtMGTs) some of which are localized to distinct tissues, and not all of which can transport Mg2+. Structures of the intracellular domain of Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, such as occur in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport.
Pssm-ID: 213355 [Multi-domain] Cd Length: 285 Bit Score: 42.30 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1299 EALVSQLTRGKQAFTQQIEELKRHIEEEVKAKnALAHAVqSARHDCDLLREQFEEEQEAKAELQRGMSKANSEvaqwrSK 1378
Cdd:cd12821 110 GAIIKALLTGIDQFEEKLEELEWDLLEGNNAI-KLDRIL-ELRRELLRLTNLIEPQQEVLMALQEAFAELLFS-----ED 182
|
90 100 110
....*....|....*....|....*....|....*
gi 1316056572 1379 YET--DAIQRTEELEEAKKKLAQRLQEAEESIEAV 1411
Cdd:cd12821 183 EEElrRTLDRIERLLQLIEEYEQELDTLQDIEEVV 217
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1617-1930 |
2.15e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1617 RVKKKMEGDLNEMEiqlshANRQAAEAQKQlrnvqgqlKDAQLHLDDAVRGQEdmkEQVAMvERRNGLMVAEIEELRAAL 1696
Cdd:pfam17380 300 RLRQEKEEKAREVE-----RRRKLEEAEKA--------RQAEMDRQAAIYAEQ---ERMAM-ERERELERIRQEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1697 EQTERSRKVAEQELVDASERVGLLHSQNSSllNTKKKLEtdlvqvqgevddAVQEARNAEDKAKKAITDAAMMAEELKKE 1776
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELERLQMERQQKNE--RVRQELE------------AARKVKILEEERQRKIQQQKVEMEQIRAE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1777 QDtSAHLERMKKNLEVTVKDLQH-RLDEAENLAMKGGKKQlQKLEQRVRELETEVEGEQKRGADavkgvrkyERRVKELT 1855
Cdd:pfam17380 429 QE-EARQREVRRLEEERAREMERvRLEEQERQQQVERLRQ-QEEERKRKKLELEKEKRDRKRAE--------EQRRKILE 498
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316056572 1856 YQTEEDKKNItrLQDLVDKLQLKVKAYKRQAEEAEEQANSHMSRLRKVQHEMEE---AQERADIAESQVNKLRAKSRD 1930
Cdd:pfam17380 499 KELEERKQAM--IEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEErrrIQEQMRKATEERSRLEAMERE 574
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
912-1047 |
2.27e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.31 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 912 LIKSKIQLEAK----------LKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTL-AKVEKEKHATENKVK 980
Cdd:smart00787 121 LVKTFARLEAKkmwyewrmklLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALeEELRQLKQLEDELED 200
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1316056572 981 NLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKK 1047
Cdd:smart00787 201 CDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
877-1096 |
2.31e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.21 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 877 LEEKMVSLLQEKNDLQLQVASEVENLSDAEER--------CEGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLE 948
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAEPSRLYSLYEKeiedlrrqLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 949 DECSELKKDIDdlELTLAKVEkekhaTENKVKNLTEEMA----------------------------------------- 987
Cdd:pfam00038 103 NDLVGLRKDLD--EATLARVD-----LEAKIESLKEELAflkknheeevrelqaqvsdtqvnvemdaarkldltsalaei 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 988 -TQDEAIAKltKEKKALQEAHQQTLDDLQAEEDKVN-TLTKAKTKLEQ---QVDDLEGSLEQEKKLRMDLERAKRKLE-- 1060
Cdd:pfam00038 176 rAQYEEIAA--KNREEAEEWYQSKLEELQQAAARNGdALRSAKEEITElrrTIQSLEIELQSLKKQKASLERQLAETEer 253
|
250 260 270
....*....|....*....|....*....|....*...
gi 1316056572 1061 --GDLKLAQESIMDLENDKQQSDEKIKKKDFEISQLLS 1096
Cdd:pfam00038 254 yeLQLADYQELISELEAELQETRQEMARQLREYQELLN 291
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
903-1556 |
2.51e-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: 43.12 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 903 SDAEERCEGLIKSKIQLEAKLKETTERLEDEEEInaELTAKKRKLEDECSELKKDIDDLEltlAKVEKEKHATENKVKNL 982
Cdd:TIGR01612 1500 DEADKNAKAIEKNKELFEQYKKDVTELLNKYSAL--AIKNKFAKTKKDSEIIIKEIKDAH---KKFILEAEKSEQKIKEI 1574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 983 TEEMATQDEAIAKLTKEKKALQEAhQQTLDDLqaeEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGD 1062
Cdd:TIGR01612 1575 KKEKFRIEDDAAKNDKSNKAAIDI-QLSLENF---ENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKENGD 1650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1063 -LKLAQESIMDLENDKQQsdekIKKKDFEISQLLSKIEDEQSLGAQLQK--------KIKELqarieeleeeieaeraar 1133
Cdd:TIGR01612 1651 nLNSLQEFLESLKDQKKN----IEDKKKELDELDSEIEKIEIDVDQHKKnyeigiieKIKEI------------------ 1708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1134 AKVEKQRADLSREL-EEISERLEEAGGATAAQ-IEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAElgEQI 1211
Cdd:TIGR01612 1709 AIANKEEIESIKELiEPTIENLISSFNTNDLEgIDPNEKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITY--DEI 1786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1212 DNLQRVKQ----KLEKEKSEFKMEIDDLSSNM--EAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKarlq 1285
Cdd:TIGR01612 1787 KNTRINAQneflKIIEIEKKSKSYLDDIEAKEfdRIINHFKKKLDHVNDKFTKEYSKINEGFDDISKSIENVKNST---- 1862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1286 TENGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIeeeVKAKNALAHAVQSARhDCDLLR-------EQFEEEQEAK 1358
Cdd:TIGR01612 1863 DENLLFDILNKTKDAYAGIIGKKYYSYKDEAEKIFINI---SKLANSINIQIQNNS-GIDLFDniniailSSLDSEKEDT 1938
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1359 AELQRGMSKANSEVAQWRSKYET-----DAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASLEKTK---QRLQGEVE 1430
Cdd:TIGR01612 1939 LKFIPSPEKEPEIYTKIRDSYDTlldifKKSQDLHKKEQDTLNIIFENQQLYEKIQASNELKDTLSDLKykkEKILNDVK 2018
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1431 DLMTDVERANSLAANldkkQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALDQLETMKRENKNLQ 1510
Cdd:TIGR01612 2019 LLLHKFDELNKLSCD----SQNYDTILELSKQDKIKEKIDNYEKEKEKFGIDFDVKAMEEKFDNDIKDIEKFENNYKHSE 2094
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1316056572 1511 QEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLE 1556
Cdd:TIGR01612 2095 KDNHDFSEEKDNIIQSKKKLKELTEAFNTEIKIIEDKIIEKNDLID 2140
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1003-1556 |
2.52e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1003 LQEAHQQTL-DDLQAEEDKVNTLTKAKTKLEQQVDDL--EGSLEQEKKLRMDLERAKRKLEGDlklAQESIMDLEndKQQ 1079
Cdd:PRK10246 213 LTPEQVQSLtASLQVLTDEEKQLLTAQQQQQQSLNWLtrLDELQQEASRRQQALQQALAAEEK---AQPQLAALS--LAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1080 SDEKIKKkdfeisqLLSKIEDEQSLGAQLQKKIKE----LQARIEELEEEIEAERAARAKVEKQRADLSRELEEiSERLE 1155
Cdd:PRK10246 288 PARQLRP-------HWERIQEQSAALAHTRQQIEEvntrLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAE-HDRFR 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1156 EAGGATA---AQIEMNKKREAEFQKLRRDLEESTLQHEATAAALRKKQADSVAELGEQIDNLQRVKQKLEKEKSEFKMEI 1232
Cdd:PRK10246 360 QWNNELAgwrAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQHAEQRPLRQRLVALHGQIVPQQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1233 DDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVR---------QLNDINAQKARLQ------------------ 1285
Cdd:PRK10246 440 KRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADvkticeqeaRIKDLEAQRAQLQagqpcplcgstshpavea 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1286 ------TENGEFARQLE-EKEALVSQ--LTRGK-QAFTQQI----EELKRHIEEE---VKAKNALAHAVQSARHDCD--- 1345
Cdd:PRK10246 520 yqalepGVNQSRLDALEkEVKKLGEEgaALRGQlDALTKQLqrdeSEAQSLRQEEqalTQQWQAVCASLNITLQPQDdiq 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1346 -LLREQFEEEQE-----AKAELQRGMSKANSEVAQWRSKYEtdaiQRTEELEEAKKKLAQRLQEAEESIEAVNSKcASLE 1419
Cdd:PRK10246 600 pWLDAQEEHERQlrllsQRHELQGQIAAHNQQIIQYQQQIE----QRQQQLLTALAGYALTLPQEDEEASWLATR-QQEA 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1420 KTKQRLQGEVEDLMTDVERANSLAANL----DKKQRNFDKVLAEWKQKYEESQAelegAQKEARSLSTELFKMKNSYEEA 1495
Cdd:PRK10246 675 QSWQQRQNELTALQNRIQQLTPLLETLpqsdDLPHSEETVALDNWRQVHEQCLS----LHSQLQTLQQQDVLEAQRLQKA 750
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1316056572 1496 LDQLETMKRENKNLQQEiSDLTEQIGEtgKSIHELEKAKKTVETEKSEIQAALEEAEGTLE 1556
Cdd:PRK10246 751 QAQFDTALQASVFDDQQ-AFLAALLDE--ETLTQLEQLKQNLENQRQQAQTLVTQTAQALA 808
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1173-1501 |
2.65e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1173 AEFQKLR---RDLEES-----TLQHEATAAALRKKQADSVAELGEQidNLQRVKQKLEkeksEFKMEIDDLSSNMEAVAK 1244
Cdd:PRK04778 230 DQLQELKagyRELVEEgyhldHLDIEKEIQDLKEQIDENLALLEEL--DLDEAEEKNE----EIQERIDQLYDILEREVK 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1245 AKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINaQKARLQTENGEFARQLEEKEalvsqltrgkQAFTQQIEELKRHIE 1324
Cdd:PRK04778 304 ARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVK-QSYTLNESELESVRQLEKQL----------ESLEKQYDEITERIA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1325 EEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYET---------------DAIQRTEE 1389
Cdd:PRK04778 373 EQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEikryleksnlpglpeDYLEMFFE 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1390 LEEAKKKLAQRLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVeranslaanldkkqrnfdkVLAE----WKQKYE 1465
Cdd:PRK04778 453 VSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENA-------------------TLTEqliqYANRYR 513
|
330 340 350
....*....|....*....|....*....|....*.
gi 1316056572 1466 ESQAELEGAQKEARslstELFKmKNSYEEALDQLET 1501
Cdd:PRK04778 514 SDNEEVAEALNEAE----RLFR-EYDYKAALEIIAT 544
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1348-1567 |
2.66e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1348 REQFEEE-QEAKAELQrgmsKANSEVAQWRSKY--------ETDAIQRTEELEEAKKKLAQRLQEAEESIEAVNSKCASL 1418
Cdd:COG3206 177 LEFLEEQlPELRKELE----EAEAALEEFRQKNglvdlseeAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1419 EKTKQRLQgevedlmtdverANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEARSLSTELFKMKNSYEEALD- 1497
Cdd:COG3206 253 PDALPELL------------QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEa 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1498 QLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQL 1567
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRV 390
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1052-1211 |
3.16e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 42.44 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1052 LERAKRKLEGDLKLAQESIMDLENDKQQSDEKIKkkdfEISQLLSKIEdeqSLGAQLQKKIKELQarieeleeeieaeRA 1131
Cdd:COG1193 502 IERARELLGEESIDVEKLIEELERERRELEEERE----EAERLREELE---KLREELEEKLEELE-------------EE 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1132 ARAKVEKQRADLSRELEEISERLEEaggaTAAQIEMNKKREAEFQKLRRDLEEstLQHEATAAALRKKQADSVAELGEQI 1211
Cdd:COG1193 562 KEEILEKAREEAEEILREARKEAEE----LIRELREAQAEEEELKEARKKLEE--LKQELEEKLEKPKKKAKPAKPPEEL 635
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
898-1067 |
3.43e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 41.77 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 898 EVENLSDAEERCEGLIKSKIQLEAKLKETTERLEdeeeinAELTAKKR--KLEDECSELKKDIDDLEL--TLAKVEK--- 970
Cdd:pfam03148 124 EVELIEGIQELLQRTLEQAWEQLRLLRAARHKLE------KDLSDKKEalEIDEKCLSLNNTSPNISYkpGPTRIPPnss 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 971 -----EKHATENKVKNLTEEMATqdeaiAKLtkeKKALQEAHQQTLDDLQAEEDKVNT--------LTKAKTKLEQQVDD 1037
Cdd:pfam03148 198 tpeewEKFTQDNIERAEKERAAS-----AQL---RELIDSILEQTANDLRAQADAVNFalrkrieeTEDAKNKLEWQLKK 269
|
170 180 190
....*....|....*....|....*....|
gi 1316056572 1038 LEGSLEQEKKLRMDLERAKRKLEGDLKLAQ 1067
Cdd:pfam03148 270 TLQEIAELEKNIEALEKAIRDKEAPLKLAQ 299
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1145-1338 |
3.64e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1145 RELEEISERLEEAGGATAAQIEMNKKREA--EFQKLRRDLEEstlqheataaalrkkqadsvaELGEQIDNLQRVKQKLE 1222
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAkeEIHKLRNEFEK---------------------ELRERRNELQKLEKRLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1223 KEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDInaqkARLQTEngefarqlEEKEALV 1302
Cdd:PRK12704 93 QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI----SGLTAE--------EAKEILL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1316056572 1303 SQLtrgKQAFTQQIEELKRHIEEEVK------AKNALAHAVQ 1338
Cdd:PRK12704 161 EKV---EEEARHEAAVLIKEIEEEAKeeadkkAKEILAQAIQ 199
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1135-1329 |
3.95e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1135 KVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKlrrDLEESTLQHEataaalrkkqaDSVAELGEQIDNL 1214
Cdd:PRK05771 47 KLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIK---DVEEELEKIE-----------KEIKELEEEISEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1215 QRVKQKLEKEKSE------FKMEIDDLSSN----MEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENV------------- 1271
Cdd:PRK05771 113 ENEIKELEQEIERlepwgnFDLDLSLLLGFkyvsVFVGTVPEDKLEELKLESDVENVEYISTDKGYVyvvvvvlkelsde 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1272 --RQLNDINAQKARLQTEnGEFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKA 1329
Cdd:PRK05771 193 veEELKKLGFERLELEEE-GTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLA 251
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1240-1568 |
4.00e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1240 EAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVRQLNDINAQKARLQTENGEFARQLEEKEALVSQLTRGKQAFTQQIEEL 1319
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1320 KRHIEEEVKAKNALAHAVQSARHDCDLLREQFEEEQEAKAELQRGMSKANSEVAQWRSKYeTDAIQRTEELEEAKKKLAQ 1399
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI-AEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1400 RLQEAEESIEAVNSKCASLEKTKQRLQGEVEDLMTDVERANSLAANLDKKQRNFDKVLAEWKQKYEESQAELEGAQKEAR 1479
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1480 SLSTELFKMKNSYEEALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEE 1559
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
....*....
gi 1316056572 1560 SKILRVQLE 1568
Cdd:COG4372 325 AKKLELALA 333
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1531-1805 |
4.32e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1531 EKAKKTVET-----EKSEIQAALEEAEGTLEheeskILRVQLElnqvksEIDRKLAEKDEEMEQIKRNSQrVIDSMQSTL 1605
Cdd:COG3206 148 ELAAAVANAlaeayLEQNLELRREEARKALE-----FLEEQLP------ELRKELEEAEAALEEFRQKNG-LVDLSEEAK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1606 DAEVRsrndalrvkkkmegdLNEMEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHLDDAVRGqedmkeqvamverrnglm 1685
Cdd:COG3206 216 LLLQQ---------------LSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS------------------ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1686 vAEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLlntKKKLETDLVQVQGEVDDAVQEARNAEDKAKKAITD 1765
Cdd:COG3206 263 -PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL---RAQLQQEAQRILASLEAELEALQAREASLQAQLAQ 338
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1316056572 1766 AAmmaEELKKEQDTSAHLERMKKNLEVTVK---DLQHRLDEAE 1805
Cdd:COG3206 339 LE---ARLAELPELEAELRRLEREVEVARElyeSLLQRLEEAR 378
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
851-1097 |
4.59e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 41.59 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 851 KELQNMKENYEKMQSDLTTAL----AKKKELEEKMVSLLQE---KNDLQLQVASEVENLSDAEER--------------- 908
Cdd:pfam15742 65 KQAQQKLLDSTKMCSSLTAEWkhcqQKIRELELEVLKQAQSiksQNSLQEKLAQEKSRVADAEEKilelqqklehahkvc 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 909 -CEGLIKSKIQLEAKLKETTERLE------DEEEINAE---------------LTAKKRKLEDECSELKKDIDDLELTLA 966
Cdd:pfam15742 145 lTDTCILEKKQLEERIKEASENEAklkqqyQEEQQKRKlldqnvnelqqqvrsLQDKEAQLEMTNSQQQLRIQQQEAQLK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 967 KVEKEKHATENKVKNLTEematQDEAIAKLTKEKKALQEAHQQTLDDLQAEEDKVNtltkaktkleqqvddlEGSLEQEK 1046
Cdd:pfam15742 225 QLENEKRKSDEHLKSNQE----LSEKLSSLQQEKEALQEELQQVLKQLDVHVRKYN----------------EKHHHHKA 284
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1316056572 1047 KLRmdleRAKRKLEGDLKLAQESIMDLENDKQQSDEKIKKKDFEISQLLSK 1097
Cdd:pfam15742 285 KLR----RAKDRLVHEVEQRDERIKQLENEIGILQQQSEKEKAFQKQVTAQ 331
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1769-1927 |
5.18e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 41.84 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1769 MAEELKKEQDTSAHL-ERMKKNLEvTVKDLQHRLDEAENLAMKGGKKQLQK---LEQ-------RVRELETEVEGEQKRG 1837
Cdd:PLN03188 1066 LAEELRTELDASRALaEKQKHELD-TEKRCAEELKEAMQMAMEGHARMLEQyadLEEkhiqllaRHRRIQEGIDDVKKAA 1144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1838 ADAvkGVRKYERR-----VKELTYQTEEDKKNITRLQDLVDKLQLKVkaykRQAEEAEEQANSHMSRLRKVQHEMEEAQE 1912
Cdd:PLN03188 1145 ARA--GVRGAESKfinalAAEISALKVEREKERRYLRDENKSLQAQL----RDTAEAVQAAGELLVRLKEAEEALTVAQK 1218
|
170 180
....*....|....*....|..
gi 1316056572 1913 RADIAE-------SQVNKLRAK 1927
Cdd:PLN03188 1219 RAMDAEqeaaeayKQIDKLKRK 1240
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1575-1933 |
5.19e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1575 EIDRKLAEKDEEMEQIKRNSQRVIDSMQSTLDAEVRSRNDALRVKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQL 1654
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1655 KDAQLHLDDAVRGQEDMKEQVAMVERRNGLMVAEIEELRAALEQTERSRKVAEQELVDASERVGLLHSQNSSLLNTKKKL 1734
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1735 ETDLVQVQGEVDDAVQEARNAEDKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEVTVKDLQHRLDEAENLAMKGGKK 1814
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1815 QLQKLEQRVRELETEVEGEQKRGADAVKGVRKYERRVKELTYQTEEDKKNITRLQDLVDKLQLKVKAYKRQAEEAEEQAN 1894
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340 350
....*....|....*....|....*....|....*....
gi 1316056572 1895 SHMSRLRKVQHEMEEAQERADIAESQVNKLRAKSRDVGK 1933
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSK 361
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
910-1010 |
5.31e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 910 EGLIKSKIQLEAKLKETTERLEDEEEINAELTAKKRKLEDecsELKKDIDDLELTLAK-VEKEKHATENKVKNLTEEMAT 988
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQE---EEDKLLEEAEKEAQQaIKEAKKEADEIIKELRQLQKG 599
|
90 100
....*....|....*....|....
gi 1316056572 989 QDEAIA--KLTKEKKALQEAHQQT 1010
Cdd:PRK00409 600 GYASVKahELIEARKRLNKANEKK 623
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1210-1341 |
5.45e-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: 40.68 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1210 QIDNLQRVKQKLEKEKSEFKMEIDDLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDE---------NVRQLNDINAQ 1280
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlgnvrNNKEYEALQKE 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1316056572 1281 KARLQTENG-------EFARQLEEKEALVSQLTRGKQAFTQQIEELKRHIEEEVKAKNALAHAVQSAR 1341
Cdd:COG1579 98 IESLKRRISdledeilELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
964-1211 |
5.64e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 964 TLAKVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDdlegslE 1043
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE------E 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1044 QEKKLRMDLERAKRKLEGDLKLAQ----ESIMDL-----------ENDKQQSDEKIKKKDfEISQLLSKIEDEQslgAQL 1108
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVllgsESFSDFldrlsalskiaDADADLLEELKADKA-ELEAKKAELEAKL---AEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1109 QKKIKELQARIEELEEEIEAERAARAKVEKQRADLSRELEEISERLEEAGGATAAQIEMNKKREAEFQKLRRDLEESTLQ 1188
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260
....*....|....*....|...
gi 1316056572 1189 HEATAAALRKKQADSVAELGEQI 1211
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSA 262
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
1004-1098 |
6.50e-03 |
|
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: 39.22 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1004 QEAHQQTLDDLQAE-EDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDLENDKQQSDE 1082
Cdd:pfam11559 54 RESLNETIRTLEAEiERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIKTQFAH 133
|
90
....*....|....*.
gi 1316056572 1083 KIKKKDFEISQLLSKI 1098
Cdd:pfam11559 134 EVKKRDREIEKLKERL 149
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1690-1927 |
6.71e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1690 EELRAALEqtersrKVAEQELVDASERVGLLHSQNS-SLLNTKKKLETDLVQVQGEVDDAVQEARNAE---DKAKKAITD 1765
Cdd:PRK11281 39 ADVQAQLD------ALNKQKLLEAEDKLVQQDLEQTlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQaelEALKDDNDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1766 AAmmAEELKKEqdTSAHLERMKKNLEVTVKDLQHRLDEAENL-------------AMKGGKKQLQKLEQrvreleteveg 1832
Cdd:PRK11281 113 ET--RETLSTL--SLRQLESRLAQTLDQLQNAQNDLAEYNSQlvslqtqperaqaALYANSQRLQQIRN----------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1833 eQKRGADAVKGVRKYERRVK---ELTY---QTEEDKK---NITRLQDL----VDKLQLKVKAYKRQAEEAEEQANShmSR 1899
Cdd:PRK11281 178 -LLKGGKVGGKALRPSQRVLlqaEQALlnaQNDLQRKsleGNTQLQDLlqkqRDYLTARIQRLEHQLQLLQEAINS--KR 254
|
250 260
....*....|....*....|....*...
gi 1316056572 1900 LRKVQHEMEEAQERADIAESQVNKLRAK 1927
Cdd:PRK11281 255 LTLSEKTVQEAQSQDEAARIQANPLVAQ 282
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1494-1691 |
6.83e-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: 40.29 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1494 EALDQLETMKRENKNLQQEISDLTEQIGETGKSIHELEKAKKTVETEKSEIQAALEEAEGTLEHEESKILRVQLELNQVK 1573
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1574 SEIDRKLAEKdeEMEQIKRNsqrvidsmqstldaevrsrndalrvKKKMEGDLNEMEIQLSHANRQAAEAQKQLRNVQGQ 1653
Cdd:COG1579 87 NNKEYEALQK--EIESLKRR-------------------------ISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 1316056572 1654 LKDAQLHLDDAVrgqEDMKEQVAMVERRNGLMVAEIEE 1691
Cdd:COG1579 140 LEEKKAELDEEL---AELEAELEELEAEREELAAKIPP 174
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
967-1299 |
7.00e-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: 41.26 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 967 KVEKEKHATENKVKNLTEEMATQDEAIAKLTKEKKALQEAHQQTlddlQAEEDKVNTLTKAKTKLeqqvddlegSLEQEK 1046
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKAR----QAEMDRQAAIYAEQERM---------AMERER 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1047 KL-RMDLERAKRKLE----GDLKLAQESIMDLEN---DKQQSDEKIKKkDFEISQLLSKIEDEQslgaqlQKKIKELQAR 1118
Cdd:pfam17380 349 ELeRIRQEERKRELErirqEEIAMEISRMRELERlqmERQQKNERVRQ-ELEAARKVKILEEER------QRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1119 IEELEEEIEAERAARAKV-EKQRAdlsRELEEIseRLEEAggATAAQIEMNKKREAEFQKLRRDLEESTlQHEATAAALR 1197
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRlEEERA---REMERV--RLEEQ--ERQQQVERLRQQEEERKRKKLELEKEK-RDRKRAEEQR 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1198 KKQADSvaelgeqidNLQRVKQKLEKEKSEFKMeiddLSSNMEAVAKAKGNLEKMCRTLEDQLSEIKSKNDENVR-QLND 1276
Cdd:pfam17380 494 RKILEK---------ELEERKQAMIEEERKRKL----LEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQeQMRK 560
|
330 340
....*....|....*....|....*
gi 1316056572 1277 INAQKARLQT--ENGEFARQLEEKE 1299
Cdd:pfam17380 561 ATEERSRLEAmeREREMMRQIVESE 585
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
957-1059 |
7.68e-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: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 957 DIDDLELTLAKVEKEKHATENkvknltEEMATQDEAIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVD 1036
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100
....*....|....*....|...
gi 1316056572 1037 DLEGSLEQEKKLRMDLERAKRKL 1059
Cdd:COG0542 486 KIPELEKELAELEEELAELAPLL 508
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
852-948 |
8.23e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 852 ELQNMKENYEKMQSDLTTALAKKKELEEKMVSLLQEKNDLQLQVASEVEN-LSDAEERCEGLIKSKIQLEAKLKETTERL 930
Cdd:COG3206 264 VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRiLASLEAELEALQAREASLQAQLAQLEARL 343
|
90
....*....|....*...
gi 1316056572 931 EDEEEINAELTAKKRKLE 948
Cdd:COG3206 344 AELPELEAELRRLEREVE 361
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1200-1915 |
9.09e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.96 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1200 QADSVAELGEQIDNLQRVKQKLEKEKSEFKMEIddlssNMEAVAKAkgnlekmcRTLEDQLSE----IKSKNDENVRQln 1275
Cdd:NF041483 89 RADAERELRDARAQTQRILQEHAEHQARLQAEL-----HTEAVQRR--------QQLDQELAErrqtVESHVNENVAW-- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1276 dinAQKARLQTENgEFARQLEEKEALVSQLTRGKQAFTQQI-EELKRHIEEEVKAKNALAHAV-QSARHDCD-LLREQFE 1352
Cdd:NF041483 154 ---AEQLRARTES-QARRLLDESRAEAEQALAAARAEAERLaEEARQRLGSEAESARAEAEAIlRRARKDAErLLNAAST 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1353 EEQEAKAELQRGMSKANSEVAQWRskyetdaiQRTEELEEAKKklaQRLQEAEESI---------------EAVNSKCAS 1417
Cdd:NF041483 230 QAQEATDHAEQLRSSTAAESDQAR--------RQAAELSRAAE---QRMQEAEEALrearaeaekvvaeakEAAAKQLAS 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1418 LEKTKQ-----------RLQGEV----EDLMTDVERAnslaanLDKKQRNFDKVLAEWKQKYEESQAELEGAQ--KEARS 1480
Cdd:NF041483 299 AESANEqrtrtakeeiaRLVGEAtkeaEALKAEAEQA------LADARAEAEKLVAEAAEKARTVAAEDTAAQlaKAART 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1481 LSTELFK----MKNSYEEALDQLETMKRENK----NLQQEISDLTEQIGETGKSIHELEKAkKTVETEkseiqaalEEAE 1552
Cdd:NF041483 373 AEEVLTKasedAKATTRAAAEEAERIRREAEaeadRLRGEAADQAEQLKGAAKDDTKEYRA-KTVELQ--------EEAR 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1553 GTLEHEESKILRVQLELNQVKSEIDRKLAEKDEE----MEQIKRNSQRVIDSMQSTLDAEV-RSRNDALRVKKKMEGDLN 1627
Cdd:NF041483 444 RLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEaartAEELLTKAKADADELRSTATAESeRVRTEAIERATTLRRQAE 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1628 E-MEIQLSHANRQAAEAQKQLRNVQGQLKDAQLHL-DDAVRGQEDMKEQVA------MVERRNGLMVAEiEELRAALEQT 1699
Cdd:NF041483 524 EtLERTRAEAERLRAEAEEQAEEVRAAAERAARELrEETERAIAARQAEAAeeltrlHTEAEERLTAAE-EALADARAEA 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1700 ERSRKVAEQEL----VDASERVGLLHSQnssllntkkkLETDLVQVQGE-VDDAVQEARNAEDKAKKAITDAAMMAEELK 1774
Cdd:NF041483 603 ERIRREAAEETerlrTEAAERIRTLQAQ----------AEQEAERLRTEaAADASAARAEGENVAVRLRSEAAAEAERLK 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1775 KEQDTSAhlERMKKNLEVTVKDLQHRLDEAENLAMKGGKKQLQKLEQRVRELETEVEGEQKR------------------ 1836
Cdd:NF041483 673 SEAQESA--DRVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERareqseellasarkrvee 750
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 1837 -GADAVKGVRKYERRVKELTYQTEEDKKNItrlQDLVDKLQlkvkaykrqaeeaeEQANSHMSRLRK-VQHEME----EA 1910
Cdd:NF041483 751 aQAEAQRLVEEADRRATELVSAAEQTAQQV---RDSVAGLQ--------------EQAEEEIAGLRSaAEHAAErtrtEA 813
|
....*
gi 1316056572 1911 QERAD 1915
Cdd:NF041483 814 QEEAD 818
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
918-1070 |
9.27e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1316056572 918 QLEAKLKETTERLEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMATQD-----EA 992
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyEA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1316056572 993 IAK-LTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESI 1070
Cdd:COG1579 94 LQKeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| |
