|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-774 |
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: 1480.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAIVAALGDTPGKKTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYDYHFCSQGVTTVDNLDDGEELMATDH 338
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 339 AMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKG 418
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 419 QNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 499 VLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDMSFKAKLYDNHIGKSPNFQKPRPDKKRKY 578
Cdd:cd14927 401 ILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 579 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDPPKSGIKEKRKKAASFQTVSQL 658
Cdd:cd14927 481 EAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEDPKSGVKEKRKKAASFQTVSQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 659 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPAAI 738
Cdd:cd14927 561 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAI 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 1394781870 739 PDDKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14927 641 PDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-774 |
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: 1343.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAIVAALGdtpgkKTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASS-----KKKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYDYHFCSQGVTTVDNLDDGEELMATDH 338
Cdd:cd01377 156 TGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 339 AMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKG 418
Cdd:cd01377 236 AFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 419 QNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd01377 316 QNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 499 VLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKP-LGILSILEEECMFPKASDMSFKAKLYDNHIGKSPNFQKPrpdKKRK 577
Cdd:cd01377 396 VLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKP---KPKK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 578 YEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDppksgiKEKRKKAASFQTVSQ 657
Cdd:cd01377 473 SEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGG------GKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 658 LHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPAA 737
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*..
gi 1394781870 738 IPDDkFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd01377 627 IPKG-FDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-774 |
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: 1175.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAIVAALGDtPGKKTqapatktgGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIE-SKKKL--------GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKpELQDMLLLSLNPYDYHFCSQGVTTVDNLDDGEELMATDH 338
Cdd:cd14929 152 RGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 339 AMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKG 418
Cdd:cd14929 231 AMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 419 QNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14929 311 QNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 499 VLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDMSFKAKLYDNHIGKSPNFQKPRPDKKrKY 578
Cdd:cd14929 391 VLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKK-KF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 579 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDPPKsgiKEKRKKAASFQTVSQL 658
Cdd:cd14929 470 EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQFG---EKKRKKGASFQTVASL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 659 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPAAI 738
Cdd:cd14929 547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTF 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 1394781870 739 PDDKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14929 627 PKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-774 |
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: 1146.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 100 SVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 180 SGAGKTVNTKRVIQYFAIVAALGDTPGKKTqapaTKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 259
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKKKD----SKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYDYHFCSQGVTTVDNLDDGEELMATDHA 339
Cdd:cd14913 158 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 340 MDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKGQ 419
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 420 NVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFV 499
Cdd:cd14913 318 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 500 LEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDMSFKAKLYDNHIGKSPNFQKPRPDKKRKyE 579
Cdd:cd14913 398 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRA-E 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDPPKSGikeKRKKAASFQTVSQLH 659
Cdd:cd14913 477 AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKV---AKKKGSSFQTVSALF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 660 KENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPAAIP 739
Cdd:cd14913 554 RENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIP 633
|
650 660 670
....*....|....*....|....*....|....*
gi 1394781870 740 DDKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14913 634 EGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-774 |
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: 1099.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 100 SVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 180 SGAGKTVNTKRVIQYFAIVAALGDTpGKKTQAPATktgGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 259
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDR-SKKDQTPGK---GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYDYHFCSQGVTTVDNLDDGEELMATDHA 339
Cdd:cd14917 158 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 340 MDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKGQ 419
Cdd:cd14917 238 FDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 420 NVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFV 499
Cdd:cd14917 318 NVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 500 LEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDMSFKAKLYDNHIGKSPNFQKPRpDKKRKYE 579
Cdd:cd14917 398 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPR-NIKGKPE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSAtseDPPKSGIKEKRKKAASFQTVSQLH 659
Cdd:cd14917 477 AHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGA---DAPIEKGKGKAKKGSSFQTVSALH 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 660 KENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPAAIP 739
Cdd:cd14917 554 RENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 633
|
650 660 670
....*....|....*....|....*....|....*
gi 1394781870 740 DDKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14917 634 EGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-774 |
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: 1070.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 100 SVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 180 SGAGKTVNTKRVIQYFAIVAALGDTpGKKTQAPATKtgGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 259
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDR-SKKENPNANK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYDYHFCSQGVTTVDNLDDGEELMATDHA 339
Cdd:cd14916 159 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 340 MDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKGQ 419
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 420 NVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFV 499
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 500 LEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDMSFKAKLYDNHIGKSPNFQKPRpDKKRKYE 579
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPR-NVKGKQE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDPPKSgiKEKRKKAASFQTVSQLH 659
Cdd:cd14916 478 AHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKG--KGGKKKGSSFQTVSALH 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 660 KENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPAAIP 739
Cdd:cd14916 556 RENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 635
|
650 660 670
....*....|....*....|....*....|....*
gi 1394781870 740 DDKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14916 636 EGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-774 |
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: 1042.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 100 SVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 180 SGAGKTVNTKRVIQYFAIVAALGDtpgKKTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 259
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGD---KKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYDYHFCSQGVTTVDNLDDGEELMATDHA 339
Cdd:cd14923 159 GKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 340 MDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKGQ 419
Cdd:cd14923 239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 420 NVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFV 499
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 500 LEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDMSFKAKLYDNHIGKSPNFQKPRPdKKRKYE 579
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKP-AKGKAE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDPPKSGiKEKRKKAASFQTVSQLH 659
Cdd:cd14923 478 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSGGSK-KGGKKKGSSFQTVSAVF 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 660 KENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPAAIP 739
Cdd:cd14923 557 RENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIP 636
|
650 660 670
....*....|....*....|....*....|....*
gi 1394781870 740 DDKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14923 637 EGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-774 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1038.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 87 IEDMAMLTHLNEASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 167 RNRENQSMLITGESGAGKTVNTKRVIQYFAIVAALGdtpgkktqapATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSS 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSG----------SAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 247 RFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFCSQ-GVTTVD 325
Cdd:pfam00063 151 RFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLSQsGCYTID 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 326 NLDDGEELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLH 405
Cdd:pfam00063 230 GIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 406 PRVKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLD-TKLARQFFIGVLDIAGFEIFEYNSFEQLCINF 484
Cdd:pfam00063 310 RRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDvKTIEKASFIGVLDIYGFEIFEKNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 485 TNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIE-KPLGILSILEEECMFPKASDMSFKAKLYDNHiGK 563
Cdd:pfam00063 390 VNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 564 SPNFQKPRPdkkrKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDPPKSG-I 642
Cdd:pfam00063 468 HPHFQKPRL----QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGkS 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 643 KEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRIL 722
Cdd:pfam00063 544 TPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRIT 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1394781870 723 YADFKQRYRILNPAAIPDDkFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:pfam00063 624 FQEFVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-774 |
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: 1027.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 100 SVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 180 SGAGKTVNTKRVIQYFAIVAALGDTpgKKTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 259
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYDYHFCSQGVTTVDNLDDGEELMATDHA 339
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 340 MDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKGQ 419
Cdd:cd14910 240 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 420 NVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFV 499
Cdd:cd14910 320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 500 LEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDMSFKAKLYDNHIGKSPNFQKPRPdKKRKYE 579
Cdd:cd14910 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKVE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEdpPKSGIKEKRKKAASFQTVSQLH 659
Cdd:cd14910 479 AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAE--EGGGKKGGKKKGSSFQTVSALF 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 660 KENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPAAIP 739
Cdd:cd14910 557 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 636
|
650 660 670
....*....|....*....|....*....|....*
gi 1394781870 740 DDKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14910 637 EGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-774 |
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: 1025.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 101 VLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 181 GAGKTVNTKRVIQYFAIVAALGDtpgkKTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPSG 260
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGE----KKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 261 KLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYDYHFCSQGVTTVDNLDDGEELMATDHAM 340
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 341 DILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKGQN 420
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 421 VEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVL 500
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 501 EQEEYKKEGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDMSFKAKLYDNHIGKSPNFQKPRPdKKRKYEA 580
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKV-VKGKAEA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 581 HFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDPPKSGIKekrKKAASFQTVSQLHK 660
Cdd:cd14918 478 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAK---KKGSSFQTVSALFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 661 ENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPAAIPD 740
Cdd:cd14918 555 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE 634
|
650 660 670
....*....|....*....|....*....|....
gi 1394781870 741 DKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14918 635 GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-774 |
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: 1025.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 100 SVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 180 SGAGKTVNTKRVIQYFAIVAALGDTpgKKTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 259
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYDYHFCSQGVTTVDNLDDGEELMATDHA 339
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 340 MDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKGQ 419
Cdd:cd14915 240 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 420 NVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFV 499
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 500 LEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDMSFKAKLYDNHIGKSPNFQKPRPdKKRKYE 579
Cdd:cd14915 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDppKSGIKEKRKKAASFQTVSQLH 659
Cdd:cd14915 479 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEG--GGGKKGGKKKGSSFQTVSALF 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 660 KENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPAAIP 739
Cdd:cd14915 557 RENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 636
|
650 660 670
....*....|....*....|....*....|....*
gi 1394781870 740 DDKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14915 637 EGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-774 |
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: 1025.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAIVAAlgdtPGKKTQAPATKtgGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGA----SKKTDEAAKSK--GSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYDYHFCSQGVTTVDNLDDGEELMATDH 338
Cdd:cd14909 155 TGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 339 AMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKG 418
Cdd:cd14909 235 AFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 419 QNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14909 315 RNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 499 VLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDMSFKAKLYDNHIGKSPNFQKPRPDKKRKY 578
Cdd:cd14909 395 VLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 579 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDPPKSGikEKRKKAASFQTVSQL 658
Cdd:cd14909 475 AAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKG--GRGKKGGGFATVSSA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 659 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPAAI 738
Cdd:cd14909 553 YKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGI 632
|
650 660 670
....*....|....*....|....*....|....*.
gi 1394781870 739 PDDKfvDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14909 633 QGEE--DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-774 |
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: 1019.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 100 SVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 180 SGAGKTVNTKRVIQYFAIVAALGDTpgKKTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 259
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYDYHFCSQGVTTVDNLDDGEELMATDHA 339
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 340 MDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKGQ 419
Cdd:cd14912 240 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 420 NVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFV 499
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 500 LEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDMSFKAKLYDNHIGKSPNFQKPRPdKKRKYE 579
Cdd:cd14912 400 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKV-VKGKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDPPKSGIKEKRKKAASFQTVSQLH 659
Cdd:cd14912 479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAKKGGKKKGSSFQTVSALF 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 660 KENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPAAIP 739
Cdd:cd14912 559 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 638
|
650 660 670
....*....|....*....|....*....|....*
gi 1394781870 740 DDKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14912 639 EGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-774 |
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: 1019.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAIVAALGdtpgkKTQAPATktgGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTG-----KQSSDGK---GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYDYHFCSQGVTTVDNLDDGEELMATDH 338
Cdd:cd14934 153 TGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 339 AMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKG 418
Cdd:cd14934 233 AFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 419 QNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14934 313 QNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 499 VLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDMSFKAKLYDNHIGKSPNFQKPRPDKKRKY 578
Cdd:cd14934 393 VLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKGP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 579 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYEnyvsatsEDPPKSGIKeKRKKAASFQTVSQL 658
Cdd:cd14934 473 EAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFK-------EEEAPAGSK-KQKRGSSFMTVSNF 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 659 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPAAI 738
Cdd:cd14934 545 YREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVI 624
|
650 660 670
....*....|....*....|....*....|....*.
gi 1394781870 739 PDDkFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14934 625 PQG-FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-786 |
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: 997.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 80 NPPKFDMIEDMAMLTHLNEASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIAD 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 160 NAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAIVAAlgdtpgkktqapATKTGGTLEDQVIEANPAMEAFGNAKT 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG------------SNTEVGSVEDQILESNPILEAFGNAKT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 240 LRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFCSQ 319
Cdd:smart00242 149 LRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLK-SPEDYRYLNQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 320 GVT-TVDNLDDGEELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEA-DGTESADKAAYLMGISSA 397
Cdd:smart00242 228 GGClTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTvKDKEELSNAAELLGVDPE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 398 DLIKGLLHPRVKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSF 477
Cdd:smart00242 308 ELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 478 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIE-KPLGILSILEEECMFPKASDMSFKAKL 556
Cdd:smart00242 388 EQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 557 YDNHiGKSPNFQKPRpdkkRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSAtsed 636
Cdd:smart00242 467 NQHH-KKHPHFSKPK----KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSN---- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 637 ppksgiKEKRKKaasFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKG 716
Cdd:smart00242 538 ------AGSKKR---FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAG 608
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 717 FPNRILYADFKQRYRILNPAAIPDDKFvDSRKATEKLLSSLDLDHTQFKFGHTKVFFKAGLLGHLEEMRD 786
Cdd:smart00242 609 FPYRLPFDEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1123 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 880.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 36 RAWIPDEKEAYLEIEI-KESSGGKVIVETKDKQTRV---VKEDDMQQ--MNPPKFDMIEDMAMLTHLNEASVLYNLKRRY 109
Cdd:COG5022 11 GCWIPDEEKGWIWAEIiKEAFNKGKVTEEGKKEDGEsvsVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPAVLHNLEKRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 110 SHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGESGAGKTVNTK 189
Cdd:COG5022 91 NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 190 RVIQYFAIVAAlGDTPGKktqapatktgGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDI 269
Cdd:COG5022 171 RIMQYLASVTS-SSTVEI----------SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 270 YLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFCSQG-VTTVDNLDDGEELMATDHAMDILGFSND 348
Cdd:COG5022 240 YLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQ-NPKDYIYLSQGgCDKIDGIDDAKEFKITLDALKTIGIDEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 349 EKYGCYKIVGAIMHFGNMKFKqKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKGQNVEQVVYAV 428
Cdd:COG5022 319 EQDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 429 GALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKE 508
Cdd:COG5022 398 DSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 509 GIEWVFIDFgLDLQACIDLIEK--PLGILSILEEECMFPKASDMSFKAKLYDN-HIGKSPNFQKPR-PDKKrkyeahFEL 584
Cdd:COG5022 478 GIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRfRDNK------FVV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 585 VHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYvsatsedppksgikEKRKKAASFQTVSQLHKENLN 664
Cdd:COG5022 551 KHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE--------------ENIESKGRFPTLGSRFKESLN 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 665 KLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPAAIPDDKFV 744
Cdd:COG5022 617 SLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYT 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 745 ---DSRKATEKLLSSLDLDHTQFKFGHTKVFFKAGLLGHLEEMRDERLAKILTMLQARIRGRLMRIEYQKIISRRDALYT 821
Cdd:COG5022 697 wkeDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQV 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 822 IQWNIRAFNVVKNWSWMKLFFKIKPLLRSAQTEKEMATMKEEFQKLKEALEKsEAKRKELEEKQVTMIQEKNDLALQLQA 901
Cdd:COG5022 777 IQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKR-EKKLRETEEVEFSLKAEVLIQKFGRSL 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 902 EQDNLADAEERCDLLIKAKIQLEAKVKELTERVEDEEEINSdLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHAten 981
Cdd:COG5022 856 KAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISS-LKLVNLELESEIIELKKSLSSDLIENLEFKTELIA--- 931
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 982 KVKNLIEEMAALDEVIAKLTKEKKALQeahqqalddLQAEEDKVNTLTkakVKLEQQVDDLESSLEQEKKIRMDLERAKR 1061
Cdd:COG5022 932 RLKKLLNNIDLEEGPSIEYVKLPELNK---------LHEVESKLKETS---EEYEDLLKKSTILVREGNKANSELKNFKK 999
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394781870 1062 KLEGdlklTQESVMDLENDKQQLEEK---------LKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARI 1123
Cdd:COG5022 1000 ELAE----LSKQYGALQESTKQLKELpvevaelqsASKIISSESTELSILKPLQKLKGLLLLENNQLQARY 1066
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-774 |
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: 833.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRR-SEVPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 178 GESGAGKTVNTKRVIQYFAIVAALGDTPGKKTQApatktggTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSAS-------SIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 258 PSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYDYHF----CSQGVTTVDNLDDGEEL 333
Cdd:cd00124 154 PTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDDAEEF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 334 MATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREE--QAEADGTESADKAAYLMGISSADLIKGLLHPRVKVG 411
Cdd:cd00124 234 QELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 412 NEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQF--FIGVLDIAGFEIFEYNSFEQLCINFTNEKL 489
Cdd:cd00124 314 GETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEStsFIGILDIFGFENFEVNSFEQLCINYANEKL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 490 QQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIE-KPLGILSILEEECMFPKASDMSFKAKLYDNHIGKSPNFQ 568
Cdd:cd00124 394 QQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 569 KPRPDKKrkyeaHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSqnkllsavyenyvsatsedppksgikekrkk 648
Cdd:cd00124 473 KKRKAKL-----EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG------------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 649 aASFqtvsqlhKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQ 728
Cdd:cd00124 517 -SQF-------RSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLK 588
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1394781870 729 RYRILNPAAiPDDKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd00124 589 RYRILAPGA-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-774 |
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: 797.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAIVAAL---GDTPGKKTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 255
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 256 FGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFCSQGVTTVDNLDDGEELMA 335
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 336 TDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYV 415
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 416 TKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLD-TKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFN 494
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 495 HHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDMSFKAKLYDNHiGKSPNFQKprpdK 574
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMK----T 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 575 KRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENY-VSATSEDPPKSGIKEKRKKAASFQ 653
Cdd:cd14911 475 DFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAeIVGMAQQALTDTQFGARTRKGMFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 654 TVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRIL 733
Cdd:cd14911 555 TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 634
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1394781870 734 NPAAIPdDKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14911 635 TPNVIP-KGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-774 |
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: 775.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAIVAAlgDTPGKKTQApatkTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVAS--SHKGRKDHN----IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLLSLNpyDYHFCSQGVTTVDNLDDGEELMATD 337
Cdd:cd14920 155 TGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKsDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 338 HAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTK 417
Cdd:cd14920 233 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 418 GQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLD-TKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHH 496
Cdd:cd14920 313 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 497 MFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDMSFKAKLYDNHiGKSPNFQKPRpd 573
Cdd:cd14920 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPR-- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 574 kKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENY-----VSATSEDPPKSGIKEKRKK 648
Cdd:cd14920 470 -QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgLDQVTGMTETAFGSAYKTK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 649 AASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQ 728
Cdd:cd14920 549 KGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1394781870 729 RYRILNPAAIPdDKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14920 629 RYEILTPNAIP-KGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-774 |
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: 727.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAIVAALGDTpgKKTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKT--KKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFCSQGVTTVDNLDDGEELMATDH 338
Cdd:cd14932 159 NGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLE-DYSKYRFLSNGNVTIPGQQDKELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 339 AMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKG 418
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 419 QNVEQVVYAVGALAKATYDRMFKWLVTRINRTLD-TKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHM 497
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 498 FVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDMSFKAKLYDNHiGKSPNFQKPrpdK 574
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQ-GNNPKFQKP---K 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 575 KRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDpPKSGIKEK-----RKKA 649
Cdd:cd14932 474 KLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLD-KVAGMGESlhgafKTRK 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 650 ASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQR 729
Cdd:cd14932 553 GMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1394781870 730 YRILNPAAIPDDkFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14932 633 YEILTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-774 |
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: 696.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 100 SVLYNLKRRYS-HWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAIVaalGDTPGKKTQapatktggtLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATV---GGSSSGETQ---------VEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGK-KPELQDmLLLSLNPYDYHFCSQGVTTVDNLDDGEELMATD 337
Cdd:cd01380 150 NYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKE-LHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 338 HAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTK 417
Cdd:cd01380 229 KALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 418 GQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQF--FIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNH 495
Cdd:cd01380 309 PLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhsFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 496 HMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDMSFKAKLYDNHIGK-SPNFQKPRPDK 574
Cdd:cd01380 389 HVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 575 KRkyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNkllsavyenyvsatsedppksgikekRKKaasfqT 654
Cdd:cd01380 468 TA-----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN--------------------------RKK-----T 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 655 VSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILN 734
Cdd:cd01380 512 VGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLL 591
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1394781870 735 PAAIPDDKfvDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd01380 592 PSKEWLRD--DKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-774 |
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: 696.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAIVAAlgDTPGKKTqapaTKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVAS--SHKGKKD----TSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLLSLNpyDYHFCSQGVTTVDNLDDGEELMATD 337
Cdd:cd14921 155 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 338 HAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTK 417
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 418 GQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLD-TKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHH 496
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 497 MFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDMSFKAKLYDNHiGKSPNFQKPrpd 573
Cdd:cd14921 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKP--- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 574 KKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENY--------VSATSEDPPKSGIKEK 645
Cdd:cd14921 469 KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqMAKMTESSLPSASKTK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 646 RkkaASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAD 725
Cdd:cd14921 549 K---GMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1394781870 726 FKQRYRILNPAAIPDDkFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14921 626 FRQRYEILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-774 |
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: 693.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAIVAALGDTpgKKTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKT--KKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFCSQGVTTVDNLDDGEELMATDH 338
Cdd:cd15896 159 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLE-NYNNYRFLSNGNVTIPGQQDKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 339 AMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKG 418
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 419 QNVEQVVYAVGALAKATYDRMFKWLVTRINRTLD-TKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHM 497
Cdd:cd15896 318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 498 FVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDMSFKAKLYDNHiGKSPNFQKPrpdK 574
Cdd:cd15896 398 FILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKP---K 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 575 KRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDpPKSGIKEK----RKKAA 650
Cdd:cd15896 474 KLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLD-KVSGMSEMpgafKTRKG 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 651 SFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRY 730
Cdd:cd15896 553 MFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1394781870 731 RILNPAAIPDDkFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd15896 633 EILTPNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-774 |
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: 686.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAIVAalgdtpgkkTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVA---------SSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlnPYD-YHFCSQGVTTVDNLDDGEELMATD 337
Cdd:cd14919 152 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE--PYNkYRFLSNGHVTIPGQQDKDMFQETM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 338 HAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTK 417
Cdd:cd14919 230 EAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 418 GQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLD-TKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHH 496
Cdd:cd14919 310 AQTKEQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 497 MFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDMSFKAKLYDNHiGKSPNFQKPrpd 573
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKP--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 574 KKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENY--------VSATSEDPPKSGIKEK 645
Cdd:cd14919 466 KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldqVAGMSETALPGAFKTR 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 646 RkkaASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAD 725
Cdd:cd14919 546 K---GMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQE 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1394781870 726 FKQRYRILNPAAIPDDkFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14919 623 FRQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-774 |
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: 675.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAIVAAlgdTPgKKTQAPATKtgGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVAS---SP-KGRKEPGVP--GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYdYHFCSQGVTTVDNlDDGEELMATDH 338
Cdd:cd14930 155 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 339 AMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKG 418
Cdd:cd14930 233 SLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 419 QNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDtKLARQ--FFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHH 496
Cdd:cd14930 313 QTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 497 MFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDMSFKAKLYDNHiGKSPNFQKPRpd 573
Cdd:cd14930 392 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPR-- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 574 kKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENY--------VSATSEDPPKSgikek 645
Cdd:cd14930 469 -HLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVegivgleqVSSLGDGPPGG----- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 646 RKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAD 725
Cdd:cd14930 543 RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1394781870 726 FKQRYRILNPAAIPDDkFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14930 623 FRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-774 |
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: 652.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAIVAalgdtpGKKTqapatktggTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAIS------GQHS---------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFCSQG-VTTVDNLDDGEELMATD 337
Cdd:cd01381 146 NGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELG-DASDYYYLTQGnCLTCEGRDDAAEFADIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 338 HAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQRE--EQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYV 415
Cdd:cd01381 225 SAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 416 TKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFF---IGVLDIAGFEIFEYNSFEQLCINFTNEKLQQF 492
Cdd:cd01381 305 VSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 493 FNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLI-EKPLGILSILEEECMFPKASDMSFKAKLYDNHiGKSPNFQKPr 571
Cdd:cd01381 385 FVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 572 pdkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSedppksgikEKRKKAas 651
Cdd:cd01381 462 ---KSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGS---------ETRKKS-- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 652 fQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYR 731
Cdd:cd01381 528 -PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYR 606
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1394781870 732 ILNPAAIPDDKfVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd01381 607 VLVPGIPPAHK-TDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-774 |
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: 642.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 100 SVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 180 SGAGKTVNTKRVIQYFAIVaalgdTPGKKTQAPATKtggtleDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV-----SGGSESEVERVK------DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYDYHFCSQGVTTVDNLDDGEELMATDHA 339
Cdd:cd01378 151 GEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 340 MDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADgTESADKAAYLMGISSADLIKGLLHPRVKVGNEY---VT 416
Cdd:cd01378 231 MKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 417 KGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQ-FFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNH 495
Cdd:cd01378 310 VPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 496 hmFVL--EQEEYKKEGIEWVFIDFgLDLQACIDLIE-KPLGILSILEEECMFP-KASDMSFKAKLydNHIGKSPNFQKPR 571
Cdd:cd01378 390 --LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL--NQLFSNHPHFECP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 572 PDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSedppksgikEKRKKAAS 651
Cdd:cd01378 465 SGHFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDS---------KKRPPTAG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 652 FQTvsqlhKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYR 731
Cdd:cd01378 536 TKF-----KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYK 610
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1394781870 732 ILNPAAIPDDKFvDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd01378 611 LLSPKTWPAWDG-TWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-774 |
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: 634.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 100 SVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 180 SGAGKTVNTKRVIQYFAIVaalgdtpgkktqapaTKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAV---------------TNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDAS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKK--PELQDMLLLsLNPYDYHFCSQ-GVTTVDNLDDGEELMAT 336
Cdd:cd14883 147 GHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKEKLKL-GEPEDYHYLNQsGCIRIDNINDKKDFDHL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 337 DHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAE-ADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYV 415
Cdd:cd14883 226 RLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 416 TKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNH 495
Cdd:cd14883 306 EIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 496 HMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIEK-PLGILSILEEECMFPKASDMSFKAKLYDNHiGKSPNFQKPrpdK 574
Cdd:cd14883 386 YVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKP---D 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 575 KRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAV--YENYVSATSEDPPKSGIKEKRKKAASF 652
Cdd:cd14883 461 RRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELftYPDLLALTGLSISLGGDTTSRGTSKGK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 653 QTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRI 732
Cdd:cd14883 541 PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLC 620
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1394781870 733 LNPAAI-PDDKfvDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14883 621 LDPRARsADHK--ETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-774 |
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: 617.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 100 SVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYkGKRRSEvPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY-RQKLLD-SPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 180 SGAGKTVNTKRVIQYfaiVAALGDTpgkktqapatktGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 259
Cdd:cd01383 80 SGAGKTETAKIAMQY---LAALGGG------------SSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLnPYDYHFCSQ-GVTTVDNLDDGEELMATDH 338
Cdd:cd01383 145 GKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQsNCLTIDGVDDAKKFHELKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 339 AMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKG 418
Cdd:cd01383 224 ALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 419 QNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDT-KLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHM 497
Cdd:cd01383 304 LTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 498 FVLEQEEYKKEGIEWVFIDFgLDLQACIDLIE-KPLGILSILEEECMFPKASDMSFKAKLyDNHIGKSPNFQKPRpdkkr 576
Cdd:cd01383 384 FKLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER----- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 577 kyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDPPKSgikeKRKKAASF-QTV 655
Cdd:cd01383 457 --GGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASRKALPLT----KASGSDSQkQSV 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 656 SQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNP 735
Cdd:cd01383 531 ATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLP 610
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1394781870 736 --AAIPDDKFVDSRkateKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd01383 611 edVSASQDPLSTSV----AILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-774 |
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: 591.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLP-VYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 178 GESGAGKTVNTKRVIQYFAIVAALGDTPGKktqapatktggTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGR-----------SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 258 PSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFCSQGVT-TVDNLDDGEELMAT 336
Cdd:cd01384 150 DAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLK-DPKQFHYLNQSKCfELDGVDDAEEYRAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 337 DHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKqkqreEQAEADGTESADK--------AAYLMGISSADLIKGLLHPRV 408
Cdd:cd01384 229 RRAMDVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEksefhlkaAAELLMCDEKALEDALCKRVI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 409 KVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEK 488
Cdd:cd01384 304 VTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 489 LQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIE-KPLGILSILEEECMFPKASDMSFKAKLYDNhIGKSPNF 567
Cdd:cd01384 384 LQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 568 QKPrpdkKRKYEAhFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYEnyvsatsEDPPksgikEKRK 647
Cdd:cd01384 462 SKP----KLSRTD-FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFP-------PLPR-----EGTS 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 648 KAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFK 727
Cdd:cd01384 525 SSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1394781870 728 QRYRILNPAAipDDKFVDSRKATEKLLSSLDLDhtQFKFGHTKVFFK 774
Cdd:cd01384 605 DRFGLLAPEV--LKGSDDEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-774 |
1.82e-174 |
|
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: 546.68 E-value: 1.82e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLP-VYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLR----NRENQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 174 MLITGESGAGKTVNTKRVIQYFAIVAAlGDTPGKKTQAPAT-----KTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITS-GFAQGASGEGEAAseaieQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 249 GKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFCSQGVTTVDNLD 328
Cdd:cd14890 160 GKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQ-TPVEYFYLRGECSSIPSCD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 329 DGEELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGT-ESADKAAYLMGISSADLIKGLLHPR 407
Cdd:cd14890 239 DAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 408 VKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNE 487
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 488 KLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIE-KPLGILSILE--EECMFPKAS--DMSFKAKLYDNHIG 562
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFItlDDCWRFKGEeaNKKFVSQLHASFGR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 563 KS------------PNFQKPRPDKKRkyeaHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLlsavyenyv 630
Cdd:cd14890 478 KSgsggtrrgssqhPHFVHPKFDADK----QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI--------- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 631 satsedppksgikekRKKAASFQTVSQLHkenlnKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGI 710
Cdd:cd14890 545 ---------------REVSVGAQFRTQLQ-----ELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAI 604
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394781870 711 RICRKGFPNRILYADFKQRYRILNPAAipddkfvDSRKATEKLLSS-LDLDHTQFKFGHTKVFFK 774
Cdd:cd14890 605 QIRQQGFALREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKmLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-774 |
2.01e-174 |
|
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: 546.08 E-value: 2.01e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLP-VYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 178 GESGAGKTVNTKRVIQYfaivaaLGDTPGKktqapatkTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd01382 81 GESGAGKTESTKYILRY------LTESWGS--------GAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 258 PSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLlslnpydyhfcsqgvtTVDNLDDGEELMATD 337
Cdd:cd01382 147 EKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 338 HAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREE----QAEADGTESADKAAYLMGISSADLIKGLLHpRVKVGNE 413
Cdd:cd01382 211 KAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSgggcNVKPKSEQSLEYAAELLGLDQDELRVSLTT-RVMQTTR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 414 YVTKGQ------NVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKlARQFFIGVLDIAGFEIFEYNSFEQLCINFTNE 487
Cdd:cd01382 290 GGAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFE-TSSYFIGVLDIAGFEYFEVNSFEQFCINYCNE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 488 KLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIE-KPLGILSILEEECMFPKASDMSFKAKLYDNHiGKSPN 566
Cdd:cd01382 369 KLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKH-KNHFR 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 567 FQKPRPDKKRKY------EAhFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYEnyvsATSEDPPKS 640
Cdd:cd01382 447 LSIPRKSKLKIHrnlrddEG-FLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFE----SSTNNNKDS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 641 giKEKRKKaASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNR 720
Cdd:cd01382 522 --KQKAGK-LSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSR 598
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1394781870 721 ILYADFKQRYRILNPAAIPDdkfVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd01382 599 TSFHDLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-774 |
2.98e-170 |
|
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: 534.35 E-value: 2.98e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAIVAalGDTPGkktqapatktggtLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVA--GSTNG-------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlnpYDYHFCSQ-GVTTVDNLDDGEELMATD 337
Cdd:cd14872 146 RGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSS---AAYGYLSLsGCIEVEGVDDVADFEEVV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 338 HAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESAD---KAAYLMGISSADLIKGLLHPRVKVgney 414
Cdd:cd14872 223 LAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDvlkEVATLLGVDAATLEEALTSRLMEI---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 415 vtKGQNV-------EQVVYAVGALAKATYDRMFKWLVTRINRTLD-TKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTN 486
Cdd:cd14872 299 --KGCDPtripltpAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 487 EKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIEK-PLGILSILEEECMFPKASDMSFKAKLYDNHIGKSp 565
Cdd:cd14872 377 EKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 566 NFQkprPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYenyvsatsedPPKSGiKEK 645
Cdd:cd14872 455 TFV---YAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF----------PPSEG-DQK 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 646 RKKAasfqTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAD 725
Cdd:cd14872 521 TSKV----TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHER 596
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1394781870 726 FKQRYRILnPAAIPDDKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14872 597 FLKRYRFL-VKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
854-1931 |
1.42e-169 |
|
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: 547.85 E-value: 1.42e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 854 EKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKVKELTER 933
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 934 VEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQ 1013
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1014 ALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKDF 1093
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1094 EMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGATAIQLEMNK 1173
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1174 KREAEFLKLRRDLEEATLQHESTAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANA 1253
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1254 EKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKS 1333
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1334 KNALAHALQASRHDCDLLREQYEEEVEAKSELQRSLSKANAEVAQWRTKYETDAiQRTEELEEAKKKLAIRLQEAEEAVE 1413
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1414 AAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQ---KY--EETQAELEASQKESRSLSte 1488
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAisaRYaeERDRAEAEAREKETRALS-- 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1489 lfkLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHEESKTLR 1568
Cdd:pfam01576 641 ---LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLR 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1569 IQLELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQ 1648
Cdd:pfam01576 718 LEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAV 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1649 KMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQN 1728
Cdd:pfam01576 798 KQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGK 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1729 TGLINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEA 1808
Cdd:pfam01576 878 SALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1809 EQIALKGGKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKR 1888
Cdd:pfam01576 958 EGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKR 1037
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|...
gi 1394781870 1889 QYEEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRAR 1931
Cdd:pfam01576 1038 QLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-772 |
1.91e-169 |
|
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: 532.83 E-value: 1.91e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVY------KGKRRSEVPPHIYSIADNAYNDMLRNRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 171 --NQSMLITGESGAGKTVNTKRVIQYFAIVAAlgdtpgKKTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS------ATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 249 GKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKP-ELQDMLLLSLNPYDYHFCSQGVTTVDNL 327
Cdd:cd14901 155 GKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSdELHALGLTHVEEYKYLNSSQCYDRRDGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 328 DDGEELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAY-LMGISSADLIKGLLHP 406
Cdd:cd14901 235 DDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACdLLGLDMDVLEKTLCTR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 407 RVKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTL---DTKLARQfFIGVLDIAGFEIFEYNSFEQLCIN 483
Cdd:cd14901 315 EIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaysESTGASR-FIGIVDIFGFEIFATNSLEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 484 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIE-KPLGILSILEEECMFPKASDMSFKAKLYDNhIG 562
Cdd:cd14901 394 FANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 563 KSPNFQKprpDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAvyenyvsatsedppksgi 642
Cdd:cd14901 472 KHASFSV---SKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------------------ 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 643 kekrkkaasfqTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRIL 722
Cdd:cd14901 531 -----------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFP 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1394781870 723 YADFKQRYRILNPAAIPDDKFVDSRKATEKLLSSLDL----DHTQFKFGHTKVF 772
Cdd:cd14901 600 HDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSElnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-774 |
2.50e-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: 524.64 E-value: 2.50e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLP-VYTAPVVAVYKGKRRSEvPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSISK-SPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 178 GESGAGKTVNTKRVIQYFAIVAAlgdtpgkktqaPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF- 256
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGS-----------EDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFs 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 257 --------GPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSG-----------------------KKPELQDML 305
Cdd:cd14888 149 klkskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAareakntglsyeendeklakgadAKPISIDMS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 306 L-LSLNPYDYHFCSqGVTTVDNLDDGEELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQA---EADG 381
Cdd:cd14888 229 SfEPHLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASC 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 382 TESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLD-TKLARQFF 460
Cdd:cd14888 308 TDDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 461 IGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLI-EKPLGILSILE 539
Cdd:cd14888 388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 540 EECMFPKASDMSFKAKLYDNHIGKSpnfqkpRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQN 619
Cdd:cd14888 467 EECFVPGGKDQGLCNKLCQKHKGHK------RFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKN 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 620 KLLSAVYENYVSATSEDPPksgikEKRKkaasFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLH 699
Cdd:cd14888 541 PFISNLFSAYLRRGTDGNT-----KKKK----FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNE 611
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394781870 700 QLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPaaipddkfvdsrkatekllSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14888 612 QLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN-------------------GEGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-774 |
3.09e-165 |
|
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: 521.24 E-value: 3.09e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAIVAALGDTPgkktqapatktggtLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNL--------------VTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-E 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLsLNPYDYHFCSQGVTT-VDNLDDGEELMATD 337
Cdd:cd01387 146 GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGL-QEAEKYFYLNQGGNCeIAGKSDADDFRRLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 338 HAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQRE---EQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEY 414
Cdd:cd01387 225 AAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRER 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 415 VTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFN 494
Cdd:cd01387 305 IFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 495 HHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLI-EKPLGILSILEEECMFPKASDMSFKAKLYDNHiGKSPNFQKPRPD 573
Cdd:cd01387 385 KHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPRMP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 574 kkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDPPKSGIKEKRKKAASFQ 653
Cdd:cd01387 463 -----LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGKGRFVTMKPRTP 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 654 TVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRIL 733
Cdd:cd01387 538 TVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1394781870 734 NPAAIPDDKFVDSRkatEKLLSSLD--LDHTQFKFGHTKVFFK 774
Cdd:cd01387 618 VALKLPRPAPGDMC---VSLLSRLCtvTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-774 |
2.34e-164 |
|
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: 517.98 E-value: 2.34e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 100 SVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 180 SGAGKTVNTKRVIQYfaiVAALGDTPGKktqapatktggTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 259
Cdd:cd01379 82 SGAGKTESANLLVQQ---LTVLGKANNR-----------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPE--LQDMLL-LSLNPYDYHFCSQGVTTVDNLD-DGEELMA 335
Cdd:cd01379 148 GAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDkkLAKYKLpENKPPRYLQNDGLTVQDIVNNSgNREKFEE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 336 TDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQ----AEADGTESADKAAYLMGISSADLIKGLLHPRVKVG 411
Cdd:cd01379 228 IEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 412 NEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTL--DTKLA-RQFFIGVLDIAGFEIFEYNSFEQLCINFTNEK 488
Cdd:cd01379 308 GETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASdEPLSIGILDIFGFENFQKNSFEQLCINIANEQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 489 LQQFFNHHMFVLEQEEYKKEGIEWVFIDFG-----LDLqacidLIEKPLGILSILEEECMFPKASDMSFKAKLYDNHigK 563
Cdd:cd01379 388 IQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--K 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 564 SPNFQKPRPDkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSavyenyvsatsedppksgik 643
Cdd:cd01379 461 SKYYWRPKSN-----ALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR-------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 644 ekrkkaasfQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILY 723
Cdd:cd01379 516 ---------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILF 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1394781870 724 ADFKQRYRILNPAAipDDKFVDSRKATEKLLSSLDLDHtqFKFGHTKVFFK 774
Cdd:cd01379 587 ADFLKRYYFLAFKW--NEEVVANRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-774 |
3.74e-164 |
|
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: 518.56 E-value: 3.74e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLP-VYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 178 GESGAGKTVNTKRVIQYFAIVAalgdtpgkktqapatktgGTLED----QVIEANPAMEAFGNAKTLRNDNSSRFGKFIR 253
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA------------------GGLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 254 IHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFcSQGVTTVDNLDDGEEL 333
Cdd:cd14903 143 LQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSA-NECAYTG-ANKTIKIEGMSDRKHF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 334 MATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAE--ADGTESADKAAYLMGISSADLIKGLLHPRVKVG 411
Cdd:cd14903 221 ARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 412 NEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQ 491
Cdd:cd14903 301 GDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 492 FFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDMSFKAKLYDNHIGKSPNFQKPR 571
Cdd:cd14903 381 KFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPR 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 572 PDKkrkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDPPKSGIKEKRK--KA 649
Cdd:cd14903 460 TSR-----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRrgGA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 650 ASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQR 729
Cdd:cd14903 535 LTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDK 614
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1394781870 730 YRILNPAAipDDKFVDSRKATEKLLSSLDLDH-TQFKFGHTKVFFK 774
Cdd:cd14903 615 FWLFLPEG--RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-774 |
2.15e-160 |
|
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: 507.80 E-value: 2.15e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLP-VYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 178 GESGAGKTVNTKRVIQYFAIVA--ALGDTPGKKTQapatktggTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 255
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISqqSLELSLKEKTS--------CVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 256 FGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFCSQ-GVTTVDNLDDGEELM 334
Cdd:cd14873 153 ICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLNQsGCVEDKTISDQESFR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 335 ATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFkqkqreeqAEADGTESADK-----AAYLMGISSADLIKGLLHPRVK 409
Cdd:cd14873 232 EVITAMEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMF 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 410 VGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKlaRQF-FIGVLDIAGFEIFEYNSFEQLCINFTNEK 488
Cdd:cd14873 304 LRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGK--EDFkSIGILDIFGFENFEVNHFEQFNINYANEK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 489 LQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDMSFKAKLYDNHiGKSPNFQ 568
Cdd:cd14873 382 LQEYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 569 KPRPDkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDPPKSGIKEKRKk 648
Cdd:cd14873 460 KPRVA-----VNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRP- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 649 aasfqTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQ 728
Cdd:cd14873 534 -----TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYK 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1394781870 729 RYRILNPAAIPDDkfvDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14873 609 RYKVLMRNLALPE---DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-774 |
2.71e-159 |
|
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: 506.14 E-value: 2.71e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYfaiVAALgdtpgkktqapATKTGGT-LEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd01385 81 ESGSGKTESTNFLLHH---LTAL-----------SQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 258 PSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGkKPELQDMLLLSLNPYDYHFCSQGVT-TVDNLDDGEELMAT 336
Cdd:cd01385 147 ENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAG-ASEEERKELHLKQPEDYHYLNQSDCyTLEGEDEKYEFERL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 337 DHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQK--QREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEY 414
Cdd:cd01385 226 KQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGET 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 415 VTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTL----DTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQ 490
Cdd:cd01385 306 LILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 491 QFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIE-KPLGILSILEEECMFPKASDMSFKAKlYDNHIGKSPNFQK 569
Cdd:cd01385 386 YYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 570 PrpdkkRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQN-----------------KLLSAVYENY--- 629
Cdd:cd01385 464 P-----QVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSafvreligidpvavfrwAVLRAFFRAMaaf 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 630 -------------VSATSEDPPKSGIKEKRKKAASfQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFL 696
Cdd:cd01385 539 reagrrraqrtagHSLTLHDRTTKSLLHLHKKKKP-PSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDEL 617
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394781870 697 VLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPAAIpdDKFVDSRKateKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd01385 618 VLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGL--ISSKEDIK---DFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-774 |
2.87e-158 |
|
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: 502.37 E-value: 2.87e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLP-VYTAPVVAVYKG--KRRSEVPPHIYSIADNAYNDMLRNR----EN 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 172 QSMLITGESGAGKTVNTKRVIQYFAIVAALGDtpGKKTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKF 251
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAK--GASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 252 IRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKpELQDMLLLSLNPYDYHFCSQG-VTTVDNLDDG 330
Cdd:cd14892 159 IQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGnCVEVDGVDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 331 EELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQ--KQREEQAEADGTESADKAAYLMGISSADLIKGLLhPRV 408
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLV-TQT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 409 KVGneyvTKGQNVE------QVVYAVGALAKATYDRMFKWLVTRINR----------TLDTKLARQFFIGVLDIAGFEIF 472
Cdd:cd14892 317 TST----ARGSVLEikltarEAKNALDALCKYLYGELFDWLISRINAchkqqtsgvtGGAASPTFSPFIGILDIFGFEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 473 EYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIEK-PLGILSILEEECMFP-KASDM 550
Cdd:cd14892 393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 551 SFKAKLYDNHIGKSPNFQKPRPDKKrkyeaHFELVHYAGVVPYNIIGWLDKNKDPLnetvvaifqksQNKLLSAVyenyv 630
Cdd:cd14892 472 QLLTIYHQTHLDKHPHYAKPRFECD-----EFVLRHYAGDVTYDVHGFLAKNNDNL-----------HDDLRDLL----- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 631 satsedppksgikEKRKKaasFQTvsqlhkeNLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGI 710
Cdd:cd14892 531 -------------RSSSK---FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVV 587
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394781870 711 RICRKGFPNRILYADFKQRYRIL-----NPAAIPDDK--FVDSRKATEKLLSSLDLDhtQFKFGHTKVFFK 774
Cdd:cd14892 588 RIRREGFPIRRQFEEFYEKFWPLarnkaGVAASPDACdaTTARKKCEEIVARALERE--NFQLGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-774 |
3.32e-146 |
|
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: 468.02 E-value: 3.32e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKR-RSEVPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 178 GESGAGKTVNTKRVIQYFAIVAALGDTpgkktqapatktggTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDS--------------DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 258 PSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFCSQGVTTVDNLDDGEEL---- 333
Cdd:cd14897 147 ENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLE-DPDCHRILRDDNRNRPVFNDSEELeyyr 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 334 -MATDHA--MDILGFSNDEKYGCYKIVGAIMHFGNMKFkqkqrEEQAEADGTESADK-----AAYLMGISSADLIKGLLH 405
Cdd:cd14897 226 qMFHDLTniMKLIGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALIS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 406 PRVKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTK-----LARQFFIGVLDIAGFEIFEYNSFEQL 480
Cdd:cd14897 301 NVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDkdfqiMTRGPSIGILDMSGFENFKINSFDQL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 481 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLI-EKPLGILSILEEECMFPKASDMSFKAKLyDN 559
Cdd:cd14897 381 CINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 560 HIGKSPNFQKPRPDKkrkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVsatsedppk 639
Cdd:cd14897 459 YCGESPRYVASPGNR-----VAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSYF--------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 640 sgikekrkkaasfqtvsqlhKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPN 719
Cdd:cd14897 525 --------------------KRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPI 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1394781870 720 RILYADFKQRYRILNPAaiPDDKFVDSRKATEKLLSSLDLDhtQFKFGHTKVFFK 774
Cdd:cd14897 585 RIKYEDFVKRYKEICDF--SNKVRSDDLGKCQKILKTAGIK--GYQFGKTKVFLK 635
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-774 |
6.55e-143 |
|
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: 459.76 E-value: 6.55e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 101 VLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDML----RNRENQSMLI 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 177 TGESGAGKTVNTKRVIQYFAIVAalgdtpgkktqapatKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC---------------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 257 gPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLsLNPYDYHFCSQGVTTVDNLDD-GEELMA 335
Cdd:cd14889 148 -RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGL-LDPGKYRYLNNGAGCKREVQYwKKKYDE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 336 TDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREE-QAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEY 414
Cdd:cd14889 226 VCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 415 VTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKL-----ARQffIGVLDIAGFEIFEYNSFEQLCINFTNEKL 489
Cdd:cd14889 306 IQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDdssveLRE--IGILDIFGFENFAVNRFEQACINLANEQL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 490 QQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDL-IEKPLGILSILEEECMFPKASDMSFKAKLyDNHIGKSPNFQ 568
Cdd:cd14889 384 QYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 569 KPRpDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDPPKSGIKEKRKK 648
Cdd:cd14889 462 KSR-SKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSD 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 649 AASF---QTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAD 725
Cdd:cd14889 537 NFNStrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAE 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1394781870 726 FKQRYRIL-NPAAIPDDKfvdsrKATEKLLSSLDLdhTQFKFGHTKVFFK 774
Cdd:cd14889 617 FAERYKILlCEPALPGTK-----QSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-774 |
1.90e-142 |
|
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: 457.97 E-value: 1.90e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRY--SHWMIYTYSGLFCVTINPYKWLPvytAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRE---NQS 173
Cdd:cd14891 1 AGILHNLEERSklDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 174 MLITGESGAGKTVNTKRVIQYFAIVAALGDTPGKKTQAPATKT----GGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFG 249
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKrklsVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 250 KFIRIHFGPSG-KLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLsLNPYDYHFCSQ-GVTTVDNL 327
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLL-LSPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 328 DDGEELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKA----AYLMGISSADLIKGL 403
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEAlataAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 404 LHPRVKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFE-YNSFEQLCI 482
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 483 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLI-EKPLGILSILEEECMFPKASDMSFKAKLYDNHi 561
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 562 GKSPNFqkPRPDKKRKYEAhFELVHYAGVVPYNIIGWLDKNKDplnetvvaifqksqnkLLSAVYENYVSAtsedppksg 641
Cdd:cd14891 475 KRHPCF--PRPHPKDMREM-FIVKHYAGTVSYTIGSFIDKNND----------------IIPEDFEDLLAS--------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 642 ikekrkkAASFQTVSQlhkenlnKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRI 721
Cdd:cd14891 527 -------SAKFSDQMQ-------ELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRV 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1394781870 722 LYADFKqryRILNPAAIPDDK--FVDSRKA-TEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14891 593 TYAELV---DVYKPVLPPSVTrlFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-739 |
2.81e-139 |
|
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: 448.60 E-value: 2.81e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 100 SVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLP-VYTAPVVAVY-----------KGKRRSEVPPHIYSIADNAYNDMLR 167
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 168 NR----ENQSMLITGESGAGKTVNTKRVIQYFAIVaalGDTPGKkTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRND 243
Cdd:cd14900 82 GLngvmSDQSILVSGESGSGKTESTKFLMEYLAQA---GDNNLA-ASVSMGKSTSGIAAKVLQTNILLESFGNARTLRND 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 244 NSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPElqdmlllSLNPYDYhfcsqgvtt 323
Cdd:cd14900 158 NSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEA-------ARKRDMY--------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 324 vdnlddgEELMAtdhAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTE-------SADKAAYLMGISS 396
Cdd:cd14900 222 -------RRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDlapssiwSRDAAATLLSVDA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 397 ADLIKGLLHPRVKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTL-----DTKLARQFFIGVLDIAGFEI 471
Cdd:cd14900 292 TKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 472 FEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLI-EKPLGILSILEEECMFPKASDM 550
Cdd:cd14900 372 FPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECVMPKGSDT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 551 SFKAKLYdNHIGKSPNFQKPRPDKKRkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIfqksqnkllsavyenyv 630
Cdd:cd14900 451 TLASKLY-RACGSHPRFSASRIQRAR---GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDL----------------- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 631 satsedppksgikekrkkaasFQTVSQLhKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGI 710
Cdd:cd14900 510 ---------------------FVYGLQF-KEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAV 567
|
650 660
....*....|....*....|....*....
gi 1394781870 711 RICRKGFPNRILYADFKQRYRILNPAAIP 739
Cdd:cd14900 568 RVARAGFPIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-734 |
7.61e-138 |
|
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: 446.01 E-value: 7.61e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLP-VYTAPVVAVYKGK--------RRSEVPPHIYSIADNAYNDMLRNR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 170 ENQSMLITGESGAGKTVNTKRVIQYFAIVAALGDTPGKKTQAP-----ATKTGGTLEDQVIEANPAMEAFGNAKTLRNDN 244
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 245 SSRFGKFIRIHFG-PSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPE-LQDM-LLLSLNPYDYHFCSQGV 321
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQlLQQLgLKNQLSGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 322 T-TVDNLDDGEELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQ--REEQAEADGTESADKAAYLMGISSAD 398
Cdd:cd14907 241 CyEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 399 LIKGLLHPRVKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTL--------DTKLARQFFIGVLDIAGFE 470
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 471 IFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVF--IDFgLDLQACIDLIEK-PLGILSILEEECMFPKA 547
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 548 SDMSFKAKLYDNHiGKSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYE 627
Cdd:cd14907 480 TDEKLLNKIKKQH-KNNSKLIFPNKINKDT----FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFS 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 628 NYVSATSEDPPKSGIKEKRKKaasfqTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVL 707
Cdd:cd14907 555 GEDGSQQQNQSKQKKSQKKDK-----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVL 629
|
650 660
....*....|....*....|....*..
gi 1394781870 708 EGIRICRKGFPNRILYADFKQRYRILN 734
Cdd:cd14907 630 ESIRVRKQGYPYRKSYEDFYKQYSLLK 656
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-735 |
1.29e-134 |
|
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: 438.94 E-value: 1.29e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLP-VYTAPVVAVYK--------GKRRSEVPPHIYSIADNAYNDMLRN- 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 169 RENQSMLITGESGAGKTVNTKRVIQYFAIVAAlgdtPGKKTQAPATKTGgTLEDQVIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGR----DQSSTEQEGSDAV-EIGKRILQTNPILESFGNAQTIRNDNSSRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 249 GKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDY-----HFCSQGVTT 323
Cdd:cd14902 156 GKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQ-KGGKYellnsYGPSFARKR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 324 VDNLDDGEELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESA---DKAAYLMGISSADLI 400
Cdd:cd14902 235 AVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 401 KGLLHPRVKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFF---------IGVLDIAGFEI 471
Cdd:cd14902 315 TLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGFES 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 472 FEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIE-KPLGILSILEEECMFPKASDM 550
Cdd:cd14902 395 LNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGSNQ 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 551 SFKAKLYDNHIGkspnfqkprpdkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAV--YEN 628
Cdd:cd14902 474 ALSTKFYRYHGG----------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIgaDEN 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 629 YVSATSEDPPKSGIKEKRKKAASfqtVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLE 708
Cdd:cd14902 538 RDSPGADNGAAGRRRYSMLRAPS---VSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLE 614
|
650 660
....*....|....*....|....*..
gi 1394781870 709 GIRICRKGFPNRILYADFKQRYRILNP 735
Cdd:cd14902 615 AVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-774 |
1.50e-134 |
|
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: 436.30 E-value: 1.50e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLP-VYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 178 GESGAGKTVNTKRVIQYFAIVAAlgdtpGKKTQAPAtktggtledQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG-----GRKDKTIA---------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 258 PSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSG-KKPELQDMLLLSLNPYDYHFCSQGVTTVDNLDDGEELMAT 336
Cdd:cd14904 147 GRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFAST 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 337 DHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGtESADKAAYLMGISSADLIKGLLHPRVKVGNEYVT 416
Cdd:cd14904 227 QKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNG-SQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 417 KGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQF-FIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNH 495
Cdd:cd14904 306 VPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 496 HMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIEKPLGILSILEEECMFPKASDMSFKAKLYDNH--IGKSPNFQKPRPD 573
Cdd:cd14904 386 DVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 574 KkrkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENyvsatSEDPPKSGIKEKRKKAASFQ 653
Cdd:cd14904 465 R-----TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGS-----SEAPSETKEGKSGKGTKAPK 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 654 TVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRIL 733
Cdd:cd14904 535 SLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM 614
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1394781870 734 NPAAIPDDkfvDSRKATEKLLSSLDLDHT-QFKFGHTKVFFK 774
Cdd:cd14904 615 FPPSMHSK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
61-827 |
6.82e-133 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 437.54 E-value: 6.82e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 61 VETKDKQTRVVKEDDM----QQMNPPKFDmieDMAMLTHLNEASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTA 136
Cdd:PTZ00014 71 IDPPTNSTFEVKPEHAfnanSQIDPMTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 137 PVVAVYKGKRRSE-VPPHIYSIADNAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAivaalgdtPGKKTQapatk 215
Cdd:PTZ00014 148 DWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA--------SSKSGN----- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 216 TGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILS 295
Cdd:PTZ00014 215 MDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 296 GKKPELQDML-LLSLNpyDYHFCSQGVTTVDNLDDGEELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQRE 374
Cdd:PTZ00014 295 GANDEMKEKYkLKSLE--EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEG 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 375 EQAEA-----DGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINR 449
Cdd:PTZ00014 373 GLTDAaaisdESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 450 TLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIE 529
Cdd:PTZ00014 453 TIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCG 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 530 KPLGILSILEEECMFPKASDMSFKAKLYdNHIGKSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNET 609
Cdd:PTZ00014 533 KGKSVLSILEDQCLAPGGTDEKFVSSCN-TNLKNNPKYKPAKVDSNKN----FVIKHTIGDIQYCASGFLFKNKDVLRPE 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 610 VVAIFQKSQNKLLSAVYEnyvsatsedppksGIKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTP 689
Cdd:PTZ00014 608 LVEVVKASPNPLVRDLFE-------------GVEVEKGKLAKGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKP 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 690 GAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNpAAIPDDKFVDSRKATEKLLSSLDLDHTQFKFGHT 769
Cdd:PTZ00014 675 LDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD-LAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKT 753
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394781870 770 KVFFKAGLLGHLEEMRDERLAK---ILTMLQARIRGRLMRieyQKIISRRDALYTIQWNIR 827
Cdd:PTZ00014 754 MVFLKKDAAKELTQIQREKLAAwepLVSVLEALILKIKKK---RKVRKNIKSLVRIQAHLR 811
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-774 |
8.40e-129 |
|
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: 421.24 E-value: 8.40e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYK--GKRRSE-------VPPHIYSIADNAYNDMLRN- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 169 RENQSMLITGESGAGKTVNTKRVIQYfaiVAALGDTPGKKTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLY---LTTLGNGEEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 249 GKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSG------KKPELQDMLLLSLN-PYDYHFCSQG- 320
Cdd:cd14908 158 GKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGgdeeehEKYEFHDGITGGLQlPNEFHYTGQGg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 321 VTTVDNLDDGEELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAY---LMGISSA 397
Cdd:cd14908 238 APDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 398 DLIKGLLHPRVKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQF--FIGVLDIAGFEIFEYN 475
Cdd:cd14908 318 KLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrsSVGVLDIFGFECFAHN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 476 SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIE-KPLGILSILEEECMFP-KASDMSFK 553
Cdd:cd14908 398 SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 554 AKLYDNHIgksPNFQKPRPDKKR-------KYEAHFELVHYAGVVPYNI-IGWLDKNKDPLNETVVAIFQKSQNkllsav 625
Cdd:cd14908 477 SRLYETYL---PEKNQTHSENTRfeatsiqKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESGQQ------ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 626 yenyvsatsedppksgikekrkkaasfqtvsqlHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNG 705
Cdd:cd14908 548 ---------------------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGG 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 706 VLEGIRICRKGFPNRILYADFKQRYRILNPaAIPDDKF------VDSRKATEKLL--------------SSLDLDHTQFK 765
Cdd:cd14908 595 VLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVVLswsmerLDPQKLCVKKMckdlvkgvlspamvSMKNIPEDTMQ 673
|
....*....
gi 1394781870 766 FGHTKVFFK 774
Cdd:cd14908 674 LGKSKVFMR 682
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
105-774 |
3.21e-123 |
|
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: 406.26 E-value: 3.21e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 105 LKRRYSHWMIYTYSGLFCVTINPYKWLPvytapvvAVYK-GKRRSEVP------PHIYSIADNAYNDMLR-------NRE 170
Cdd:cd14895 7 LAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDlHKYREEMPgwtalpPHVFSIAEGAYRSLRRrlhepgaSKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 171 NQSMLITGESGAGKTVNTKRVIQYFAIVA--ALGDTPGKKTQApatktggTLEDQVIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14895 80 NQTILVSGESGAGKTETTKFIMNYLAESSkhTTATSSSKRRRA-------ISGSELLSANPILESFGNARTLRNDNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 249 GKFIRIHFGP-----SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLL-SLNPYDYHFCSQGVT 322
Cdd:cd14895 153 GKFVRMFFEGheldtSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLeLLSAQEFQYISGGQC 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 323 TV--DNLDDGEELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESA--------------- 385
Cdd:cd14895 233 YQrnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvq 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 386 ---DKAAYLMGISSADLIKGLLHPRVKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRIN--------RTLDTK 454
Cdd:cd14895 313 qhlDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNsaspqrqfALNPNK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 455 LARQF---FIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDlQACIDLIE-K 530
Cdd:cd14895 393 AANKDttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEqR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 531 PLGILSILEEECMFPKASDMSFKAKLYDNHIGKSpNFQKPRPDKKrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETV 610
Cdd:cd14895 472 PSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHS-NFSASRTDQA---DVAFQIHHYAGAVRYQAEGFCEKNKDQPNAEL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 611 VAIFQKSQNKLLSAVYEnYVSATSEDPPKSGIKEKRKKAASFQTV---SQLhKENLNKLMTNLRATQPHFVRCIIPNETK 687
Cdd:cd14895 548 FSVLGKTSDAHLRELFE-FFKASESAELSLGQPKLRRRSSVLSSVgigSQF-KQQLASLLDVVQQTQTHYIRCIKPNDES 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 688 TPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPAAIPDDkfvdsrKATEKLLSSLDLDHTQfkFG 767
Cdd:cd14895 626 ASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASD------ATASALIETLKVDHAE--LG 697
|
....*..
gi 1394781870 768 HTKVFFK 774
Cdd:cd14895 698 KTRVFLR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-774 |
3.72e-123 |
|
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: 403.78 E-value: 3.72e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYfaiVAALGDTPGKKTQApatktggtledQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQF---LSSLYQDQTEDRLR-----------QPEDVLPILESFGHAKTILNANASRFGQVLRLHL-Q 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFCSQG-VTTVDNLDDGEELMATD 337
Cdd:cd14896 146 HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQ-GPETYYYLNQGgACRLQGKEDAQDFEGLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 338 HAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESAD--KAAYLMGIsSADLIKGLLHPRVKVGN-EY 414
Cdd:cd14896 225 KALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQV-PPERLEGAVTHRVTETPyGR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 415 VTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFF--IGVLDIAGFEIFEYNSFEQLCINFTNEKLQQF 492
Cdd:cd14896 304 VSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 493 FNHHMFVLEQEEYKKEGIEWVFIDfGLDLQACIDLI-EKPLGILSILEEECMFPKASDMSFKAKLYDNHiGKSPNFQKPR 571
Cdd:cd14896 384 SSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQ 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 572 ---PdkkrkyeaHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYEnyvsatsEDPPKSGIKEKRKK 648
Cdd:cd14896 462 lplP--------VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQ-------EAEPQYGLGQGKPT 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 649 AAS-FQtvsqlhkENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFK 727
Cdd:cd14896 527 LASrFQ-------QSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFL 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1394781870 728 QRYRILNPAAIPDdkFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14896 600 ARFGALGSERQEA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-774 |
1.08e-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: 397.05 E-value: 1.08e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKG-KRRSEVPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 178 GESGAGKTVNTKRVIQYFAivaalgdtpgkktqapATKTG---GTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 254
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA----------------SAKSGnmdLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 255 HFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDML-LLSLNPYDY--HFCSQgVTTVDNLDDGE 331
Cdd:cd14876 145 DVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYhLLGLKEYKFlnPKCLD-VPGIDDVADFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 332 ELMATDHAMdilGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADK-----AAYLMGISSADLIKGLLHP 406
Cdd:cd14876 224 EVLESLKSM---GLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVDDAAAISNESLevfkeACSLLFLDPEALKRELTVK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 407 RVKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTN 486
Cdd:cd14876 301 VTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 487 EKLQQFFNHHMFVLEQEEYKKEGI---EWVFIDFgldlQACID-LIEKPLGILSILEEECMFPKASDMSFKAKLYDNhIG 562
Cdd:cd14876 381 EMLQKNFIDIVFERESKLYKDEGIptaELEYTSN----AEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 563 KSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYEnyvsatsedppksGI 642
Cdd:cd14876 456 SNGKFKPAKVDSNIN----FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFE-------------GV 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 643 KEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRIL 722
Cdd:cd14876 519 VVEKGKIAKGSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRP 598
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1394781870 723 YADFKQRYRILNPaAIPDDKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14876 599 FEEFLYQFKFLDL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-731 |
3.76e-117 |
|
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: 389.07 E-value: 3.76e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLP-VYTAPVVAVYKGKRRSEV----------PPHIYSIADNAYNDMLR 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAYDHNSQFgdrvtstdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 168 NRENQSMLITGESGAGKTVNTKRVIQYFAIVAALGDTPGKKTQA---PATKTGGTLEDQVIEANPAMEAFGNAKTLRNDN 244
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESispPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 245 SSRFGKFIRIHF-GPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGK----KPELQDMLLLSLNPYDYHFCSQ 319
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 320 GVTTV--DNLDDGEELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQ--KQREEQAEADGTESA---------- 385
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 386 DKAAYLMGISSADLIKGLLHPRVKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQF------ 459
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 460 ---------FIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIE- 529
Cdd:cd14899 401 vddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEh 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 530 KPLGILSILEEECMFPKASDMSFKAKLYDNHIGKS--PNFqkpRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLN 607
Cdd:cd14899 480 RPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNshPHF---RSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFC 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 608 ETVVAIFQKSQNKLLSAV-----YENYVSATSEDPPKSGIKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCII 682
Cdd:cd14899 557 ESAAQLLAGSSNPLIQALaagsnDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIK 636
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1394781870 683 PNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYR 731
Cdd:cd14899 637 PNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-735 |
2.62e-110 |
|
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: 367.25 E-value: 2.62e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLP-VYTAPVVAVYKGKRRSE-VPPHIYSIADNAYNDMLRNRE--NQSM 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQkLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 175 LITGESGAGKTVNTKRVIQYFAIVAAlgdtpgKKTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAA------SPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 255 HFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLslnPYDYHFcSQGVTTVDNLDDgEELM 334
Cdd:cd14880 155 QLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHL---PEGAAF-SWLPNPERNLEE-DCFE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 335 ATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQA---EADGTESADKAAYLMGISSADLIKGLLHPRVKVG 411
Cdd:cd14880 230 VTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 412 neyvtKGQNVEQVVYAVG-------ALAKATYDRMFKWLVTRINRTLDTKLAR-QFFIGVLDIAGFEIFEYNSFEQLCIN 483
Cdd:cd14880 310 -----KQQQVFKKPCSRAecdtrrdCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCIN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 484 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIE-KPLGILSILEEECMFPKASDmsfkAKLYDNHIG 562
Cdd:cd14880 385 YANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSS----AAQLQTRIE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 563 KSPNFQKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDPPKSgi 642
Cdd:cd14880 460 SALAGNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSG-- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 643 kekRKKAASFQTVSQLhKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRIL 722
Cdd:cd14880 538 ---QSRAPVLTVVSKF-KASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVS 613
|
650
....*....|...
gi 1394781870 723 YADFKQRYRILNP 735
Cdd:cd14880 614 HQNFVERYKLLRR 626
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-774 |
6.83e-109 |
|
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: 364.32 E-value: 6.83e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAIVAALGDTP--GKKTQApatktggtledqvieANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 256
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVlsVEKLNA---------------ALTVLEAFGNVRTALNGNATRFSQLFSLDF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 257 GPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYDYHFcsqGVTTVDNLDDGE----E 332
Cdd:cd01386 146 DQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSF---GIVPLQKPEDKQkaaaA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 333 LMATDHAMDILGFSNDEKYGCYKIVGAIMHFGN---MKFKQKQREEQAEadgTESADKAAYLMGISSADLIKGLLHPRVK 409
Cdd:cd01386 223 FSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFAR---PEWAQRAAYLLGCTLEELSSAIFKHHLS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 410 VGNEYVTKGQNVEQV------------VYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYN-- 475
Cdd:cd01386 300 GGPQQSTTSSGQESParsssggpkltgVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgs 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 476 ----SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEwvfIDFGLD---LQACIDLIEKPL---------------G 533
Cdd:cd01386 380 qrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPelsPGALVALIDQAPqqalvrsdlrdedrrG 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 534 ILSILEEECMFPKASDMSFKAKLYdNHIGKSPNFQKPRPDKKRKYEAHFELVHYAGV--VPYNIIGWLDKNK-DPLNETV 610
Cdd:cd01386 457 LLWLLDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNA 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 611 VAIFQKSQNKlLSAVyenyvsatsedppksgikekRKKAASFQTvsqlhKENLNKLMTNLRATQPHFVRCIIPN------ 684
Cdd:cd01386 536 TQLLQESQKE-TAAV--------------------KRKSPCLQI-----KFQVDALIDTLRRTGLHFVHCLLPQhnagkd 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 685 ETKTPGAMDPFLVLH------QLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPA----AIPDDKFVDSRKATEKLL 754
Cdd:cd01386 590 ERSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPltkkLGLNSEVADERKAVEELL 669
|
730 740
....*....|....*....|
gi 1394781870 755 SSLDLDHTQFKFGHTKVFFK 774
Cdd:cd01386 670 EELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-774 |
4.75e-107 |
|
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: 357.66 E-value: 4.75e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLP-VYTAPVVAVYKGKRRS-----EVPPHIYSIADNAYNDMLRNRENQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 173 SMLITGESGAGKTVNTKRVIQYFAIVAALGDTpgkktqapatktggTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFI 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSST--------------DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 253 RIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDML-LLSLNPYDYHFCSQgVTTVDNLDDGE 331
Cdd:cd14886 147 KLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLgFKSLESYNFLNASK-CYDAPGIDDQK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 332 ELMATDHAMDILgFSNDEKYGCYKIVGAIMHFGNMKFKQKQR---EEQAEADGTESADKAAYLMGISSADLIKGLLHPRV 408
Cdd:cd14886 226 EFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 409 KVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEK 488
Cdd:cd14886 305 VINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANER 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 489 LQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIEKP-LGILSILEEECMFPKASDMSFKAKLyDNHIgKSPNF 567
Cdd:cd14886 385 LQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 568 QkprPDKKRkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSavyenyvSATSEDPPKSGIKEKRK 647
Cdd:cd14886 462 I---PGKGS--QCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVN-------KAFSDIPNEDGNMKGKF 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 648 KAASFQTvsqlhkeNLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFK 727
Cdd:cd14886 530 LGSTFQL-------SIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFF 602
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1394781870 728 QRYRILNP-AAIPDDKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14886 603 HRNKILIShNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-734 |
6.28e-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: 359.68 E-value: 6.28e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLP-VYTAPVVAVYKGKRR-SEVPPHIYSIADNAYNDMLRNRENQSMLI 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 177 TGESGAGKTVNTKRVIQYfaivaaLGDTPGKKTQAPAT--KTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 254
Cdd:cd14906 81 SGESGSGKTEASKTILQY------LINTSSSNQQQNNNnnNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 255 HF-GPSGKLASADIDIYLLEKSRvIFQQPGER--SYHIYYQILSGKKPELQDMLLLSLNPYDYHFCSQGVTTVD------ 325
Cdd:cd14906 155 EFrSSDGKIDGASIETYLLEKSR-ISHRPDNInlSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISsfksqs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 326 ---------NLDDGEELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQ---REEQAEADGTESADKAAYLMG 393
Cdd:cd14906 234 snknsnhnnKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 394 ISSADLIKGLLHPRVKVGNE--YVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQ-----------FF 460
Cdd:cd14906 314 YIESVFKQALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNdlaggsnkknnLF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 461 IGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLIE-KPLGILSILE 539
Cdd:cd14906 394 IGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 540 EECMFPKASDMSFKAKLYDNHigkspnFQKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQN 619
Cdd:cd14906 473 DECIMPKGSEQSLLEKYNKQY------HNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSN 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 620 KLLSAVYENYVSATSEDppksgikekRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLH 699
Cdd:cd14906 547 FLKKSLFQQQITSTTNT---------TKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLS 617
|
650 660 670
....*....|....*....|....*....|....*
gi 1394781870 700 QLRCNGVLEGIRICRKGFPNRILYADFKQRYRILN 734
Cdd:cd14906 618 QLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIV 652
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-774 |
3.85e-106 |
|
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: 355.66 E-value: 3.85e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMI-YTYSGLFCVTINPYKWLPVYTAPVVAVY-KGKRRSEVPPHIYSIADNAYNDM-LRNRENQSML 175
Cdd:cd14875 1 ATLLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 176 ITGESGAGKTVNTKRVIQYfaivaaLGDTPGKKTQAPATKTggtLEDQVIE----ANPAMEAFGNAKTLRNDNSSRFGKF 251
Cdd:cd14875 81 ISGESGSGKTENAKMLIAY------LGQLSYMHSSNTSQRS---IADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 252 IRIHFGP-SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYDYHFCSQGVTTV------ 324
Cdd:cd14875 152 IKLYFDPtSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 325 DNLDDGEELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESAdKAAYLMGISSADLIKGLL 404
Cdd:cd14875 232 KTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLRECFL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 405 hprVKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKL--ARQFFIGVLDIAGFEIFEYNSFEQLCI 482
Cdd:cd14875 311 ---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQLCI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 483 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGlDLQACIDLIE-KPLGILSILEEECMFPKASDMSFKAKLYDNHI 561
Cdd:cd14875 388 NYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 562 GKSPNFQKPrpdkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSavyenyvSATSEDPpksg 641
Cdd:cd14875 467 NKSPYFVLP----KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIR-------TLLSTEK---- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 642 IKEKRKkaasfQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRI 721
Cdd:cd14875 532 GLARRK-----QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRR 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1394781870 722 LYADF-KQRYRILNPAAIPDDKFVDSRKATEKLLSS----LDLDHTQFKFGHTKVFFK 774
Cdd:cd14875 607 PIEQFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-774 |
4.26e-98 |
|
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: 331.78 E-value: 4.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVY---KGKRRSEVPPHIYSIADNAYNDMLRNRENQSML 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 176 ITGESGAGKTVNTKRVIQYFAivaalgdtpgkktqAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 255
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLT--------------CRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 256 FGPSGK-LASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFCSQG----VTTVDNLDDG 330
Cdd:cd14878 147 FCERKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQTmredVSTAERSLNR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 331 EELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKV 410
Cdd:cd14878 226 EKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 411 GNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTL----DTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTN 486
Cdd:cd14878 306 KGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 487 EKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACID-LIEKPLGILSILEEECMFPKASDMSFKAKLY------DN 559
Cdd:cd14878 386 EKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQsllessNT 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 560 HIGKSPNFQKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSedppk 639
Cdd:cd14878 466 NAVYSPMKDGNGNVALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLVTIA----- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 640 sgikekrkkaasfqtvSQLHKeNLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPN 719
Cdd:cd14878 541 ----------------SQLRK-SLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPV 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1394781870 720 RILYADFKQRYRILNPAAIPDDKFVDSRKATEKLLSSLDLDHTQfkFGHTKVFFK 774
Cdd:cd14878 604 RLSFSDFLSRYKPLADTLLGEKKKQSAEERCRLVLQQCKLQGWQ--MGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-774 |
8.83e-94 |
|
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: 318.88 E-value: 8.83e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYtapvVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFAivaalgdtpgkktqaPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL---------------SGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFCSQGVTTVDNLDDGEE---LMA 335
Cdd:cd14937 142 YQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIR-SENEYKYIVNKNVVIPEIDDAKDfgnLMI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 336 TDHAMDIlgfsNDEKYGCYKIVGAIMHFGNMKFKQ-----KQREEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKV 410
Cdd:cd14937 221 SFDKMNM----HDMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 411 GNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQ 490
Cdd:cd14937 297 ANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIH 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 491 QFFNHHMFVLEQEEYKKEGIEWVFIDFGLDlQACIDLIEKPLGILSILEEECMFPKASDMSFkAKLYDNHIGKSPNFQKp 570
Cdd:cd14937 377 SIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYAS- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 571 rpdKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDppksgikekRKKAA 650
Cdd:cd14937 454 ---TKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLG---------RKNLI 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 651 SFQtvsqlHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRIcRKGFPNRILYADFKQRY 730
Cdd:cd14937 522 TFK-----YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1394781870 731 RILNPAAIPDDKFVDSRKATEKLLSSLDLDhtQFKFGHTKVFFK 774
Cdd:cd14937 596 EYLDYSTSKDSSLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-737 |
1.01e-91 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 310.68 E-value: 1.01e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 100 SVLYNLKRRYSHWMIYTYSGLFCVTINPYKwlPVYTAPVVAVYKgKRRSEVPPHIYSIADNAYNDMLRNrENQSMLITGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 180 SGAGKTVNTKRVIQYFAivaalgdtpgkktqaPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgpS 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLV---------------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLlslnpyDYHFCSQGVTTVDNLDdgEELMATDHA 339
Cdd:cd14898 141 GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI------DTSSTAGNKESIVQLS--EKYKMTCSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 340 MDILGFSNDEKygCYKIVGAIMHFGNMKFKQkqrEEQAEADGTESADKAAYLMGISSADLIKGLLHPRVKVGNEYVTKGQ 419
Cdd:cd14898 213 MKSLGIANFKS--IEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 420 NVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLARQffIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFV 499
Cdd:cd14898 288 TLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 500 LEQEEYKKEGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFP--KASDMSFKAKLYDNHigkspnFQKPRPDKKRK 577
Cdd:cd14898 366 AKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAwgNVKNLLVKIKKYLNG------FINTKARDKIK 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 578 yeahfeLVHYAGVVPYNIIGWLDKNKDPLNetvVAIFQksqnkllsavyenyvsatseDPpksGIKEKRKKaasfQTVSQ 657
Cdd:cd14898 439 ------VSHYAGDVEYDLRDFLDKNREKGQ---LLIFK--------------------NL---LINDEGSK----EDLVK 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 658 LHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPAA 737
Cdd:cd14898 483 YFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-774 |
1.40e-79 |
|
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: 279.61 E-value: 1.40e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRY--------SHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRE 170
Cdd:cd14887 1 PNLLENLYQRYnkayinkeNRNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 171 NQSMLITGESGAGKTVNTKRVIQYFAIVAALgdTPGKKTQapatktggTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGK 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDR--RHGADSQ--------GLEARLLQSGPVLEAFGNAHTVLNANSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 251 FIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKK-PELQDMLLLSLNPYDYhfcsqgvttvdnldd 329
Cdd:cd14887 151 MLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVaAATQKSSAGEGDPEST--------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 330 geELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGT--------ESADKAAYLMGISS----- 396
Cdd:cd14887 216 --DLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvgceETAADRSHSSEVKClssgl 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 397 ----------ADLIKGLLHPRVKVGNEYV------------TKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTL--- 451
Cdd:cd14887 294 kvteasrkhlKTVARLLGLPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLqrs 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 452 ----------DTKLARQF-FIGVLDIAGFEIFE---YNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEG--IEWVFI 515
Cdd:cd14887 374 akpsesdsdeDTPSTTGTqTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQDCS 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 516 DFGLDLQACIDLIEKP------------------------LGILSILEEE-CMFPKASDMSFKAKLYDNHIGK----SPN 566
Cdd:cd14887 454 AFPFSFPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 567 FQKPRPDKKRKyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFqksqnklLSAVYENYVSATSEDPPKSGIKEKR 646
Cdd:cd14887 534 YKNITPALSRE-NLEFTVSHFACDVTYDARDFCRANREATSDELERLF-------LACSTYTRLVGSKKNSGVRAISSRR 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 647 KkaasfqTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADF 726
Cdd:cd14887 606 S------TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVEL 679
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1394781870 727 KQRYRILNPAAIpdDKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14887 680 WRRYETKLPMAL--REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-773 |
9.81e-79 |
|
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: 275.20 E-value: 9.81e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 96 LNEASVLYNLKRRYSHWMIYTY---SGLfcVTINPYKWLPVYTAPVVAVYK-------GKRRSEVPPHIYSIADNAYNDM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 166 LRNRENQSMLITGESGAGKTVNTKRVIQyfaivaALGD--TPGKKtqapATKtggtLEDQVIEANPAMEAFGNAKTLRND 243
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLR------QLLRlsSHSKK----GTK----LSSQISAAEFVLDSFGNAKTLTNP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 244 NSSRFGKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDY-----HFCS 318
Cdd:cd14879 145 NASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLD-DPSDYallasYGCH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 319 QGVTTVDNlDDGE---ELMAtdhAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQ--REEQAEADGTESADKAAYLMG 393
Cdd:cd14879 224 PLPLGPGS-DDAEgfqELKT---ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 394 ISSADLiKGLLHPRVK-VGNEYVTkgqnveqvVY--AVGA------LAKATYDRMFKWLVTRINrtldTKLA---RQF-- 459
Cdd:cd14879 300 VSPEDL-ETSLTYKTKlVRKELCT--------VFldPEGAaaqrdeLARTLYSLLFAWVVETIN----QKLCapeDDFat 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 460 FIGVLDIAGFEIF---EYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFgLDLQACIDLI-EKPLGIL 535
Cdd:cd14879 367 FISLLDFPGFQNRsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 536 SILEEEC-MFPKASDMSFKAKLYDNHIGKSPnFQKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDplnetvvaif 614
Cdd:cd14879 446 GILDDQTrRMPKKTDEQMLEALRKRFGNHSS-FIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGD---------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 615 qksqnkLLSAvyeNYVSAtsedppksgikekrkkaasFQTVSQLhKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDP 694
Cdd:cd14879 515 ------VLSP---DFVNL-------------------LRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDK 565
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394781870 695 FLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYrilnpaaIPDDKFVDSRKATEKLLSSLDLDHTQFKFGHTKVFF 773
Cdd:cd14879 566 RRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERY-------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-722 |
1.63e-73 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 260.61 E-value: 1.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLP-VYTAPVVAVYKGKRRSE-------VPPHIYSIADNAYNDMLRNRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 171 NQSMLITGESGAGKTVNTKRVIQYFAIVaalgdtpgkKTQAPATKtggtLEDQVIEANPAMEAFGNAKTLRNDNSSRFGK 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI---------QTDSQMTE----RIDKLIYINNILESMSNATTIKNNNSSRCGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 251 FIRIHF---------GPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSLNPYDYHFCSQGV 321
Cdd:cd14884 148 INLLIFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 322 ------------TTVDNLDDGEELMATD--------HAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQkqreeqaeadg 381
Cdd:cd14884 228 shqkrsvkgtlrLGSDSLDPSEEEKAKDeknfvallHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA----------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 382 tesadkAAYLMGISSADLIKGLLHPRVKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTL---------- 451
Cdd:cd14884 297 ------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesd 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 452 --DTKLARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEW--VFIDFGLDLQACIDL 527
Cdd:cd14884 371 neDIYSINEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICcsDVAPSYSDTLIFIAK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 528 IEKPLGILSILEEECMfpKASDMSFKAKLYDN---------HI-GKSPNFQKPRPDKKRKYEAH-FELVHYAGVVPYNII 596
Cdd:cd14884 451 IFRRLDDITKLKNQGQ--KKTDDHFFRYLLNNerqqqlegkVSyGFVLNHDADGTAKKQNIKKNiFFIRHYAGLVTYRIN 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 597 GWLDKNKDPLNETVVAIFQKSQNKLLSAVYENyvsatsedppksgikekrKKAASFQTVSQLHKENLNKLMTNLRATQPH 676
Cdd:cd14884 529 NWIDKNSDKIETSIETLISCSSNRFLREANNG------------------GNKGNFLSVSKKYIKELDNLFTQLQSTDMY 590
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1394781870 677 FVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRIL 722
Cdd:cd14884 591 YIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-738 |
2.33e-73 |
|
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: 258.65 E-value: 2.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 99 ASVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYkgkrrsevppHIYSIADNAYNDMLRNRENQSMLI-T 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNAESIVfG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 178 GESGAGKTVNTKRVIQYFaivaalgdtpgkkTQAPATKTGgTLEDQVIEAnpAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYL-------------TSQPKSKVT-TKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLYK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 258 PSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFCSQGVTTVDNLDDGEELMATD 337
Cdd:cd14874 135 RNVLTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIK-GLQKFFYINQGNSTENIQSDVNHFKHLE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 338 HAMDILGFSNDEKYGCYKIVGAIMHFGNMKFKQKQR---EEQAEADGTESADK-AAYLMGISSADLIKGLLhPRVKVGNE 413
Cdd:cd14874 214 DALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnvEQDVVEIGNMSEVKwVAFLLEVDFDQLVNFLL-PKSEDGTT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 414 YvtkgqNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLaRQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFF 493
Cdd:cd14874 293 I-----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPL-HTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 494 NHHMFVLEQEEYKKEGIEwvfIDFglDLQACID-------LIEKPLGILSILEEECMFPKASDMSFKAKLYDNHIGKSpN 566
Cdd:cd14874 367 VKHSFHDQLVDYAKDGIS---VDY--KVPNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRS-S 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 567 FQKPRpdKKRKYEahFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDppksgikekr 646
Cdd:cd14874 441 YGKAR--NKERLE--FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDM---------- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 647 kkaasFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADF 726
Cdd:cd14874 507 -----IVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTF 581
|
650
....*....|..
gi 1394781870 727 KQRYRILNPAAI 738
Cdd:cd14874 582 ARQYRCLLPGDI 593
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-773 |
7.03e-72 |
|
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: 254.65 E-value: 7.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 100 SVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAvykgkRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVGNPLTLTST-----RSSPLAPQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 180 SGAGKTVNTKRVI-QYFAIVAALGDTPGKKTQApATKTggtledqvieanpAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 258
Cdd:cd14881 77 SGSGKTYASMLLLrQLFDVAGGGPETDAFKHLA-AAFT-------------VLRSLGSAKTATNSESSRIGHFIEVQV-T 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 259 SGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLS-LNPYDYHFCSQGVTTVDNLDDGEELMATD 337
Cdd:cd14881 142 DGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgYSPANLRYLSHGDTRQNEAEDAARFQAWK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 338 HAMDILG--FSNdekygCYKIVGAIMHFGNMKFKQKQREEQAEADGTEsADKAAYLMGISSADLIKGLLHPRVKVGNEYV 415
Cdd:cd14881 222 ACLGILGipFLD-----VVRVLAAVLLLGNVQFIDGGGLEVDVKGETE-LKSVAALLGVSGAALFRGLTTRTHNARGQLV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 416 TKGQNVEQVVYAVGALAKATYDRMFKWLVTRINR------TLDTKlARQFFIGVLDIAGFEIFEYNSFEQLCINFTNEKL 489
Cdd:cd14881 296 KSVCDANMSNMTRDALAKALYCRTVATIVRRANSlkrlgsTLGTH-ATDGFIGILDMFGFEDPKPSQLEHLCINLCAETM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 490 QQFFNHHMFVLEQEEYKKEGIEW-VFIDFgLDLQACIDLIEK-PLGILSILEEECMfPKASDMSFKAKLYDNHIGkSPNF 567
Cdd:cd14881 375 QHFYNTHIFKSSIESCRDEGIQCeVEVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQ-NPRL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 568 QKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKsQNKllsavyeNYVSAT-SEDppksgikekr 646
Cdd:cd14881 452 FEAKPQDDRM----FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK-QNC-------NFGFAThTQD---------- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 647 kkaasFQTvsqlhkeNLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADF 726
Cdd:cd14881 510 -----FHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAF 577
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1394781870 727 KQRYRILNPAAIP---DDKFVDSRKATEKLLSSLDLDH-----TQFKFGHTKVFF 773
Cdd:cd14881 578 NARYRLLAPFRLLrrvEEKALEDCALILQFLEAQPPSKlssvsTSWALGKRHIFL 632
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-773 |
3.45e-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: 237.56 E-value: 3.45e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 102 LYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRR----------SEVPPHIYSIADNAYNDMLRNREN 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 172 QSMLITGESGAGKTVNTKRVIQYfaiVAALGDtpGKKTQAPATKTGGTLE---DQVIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQY---LCEIGD--ETEPRPDSEGASGVLHpigQQILHAFTILEAFGNAATRQNRNSSRF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 249 GKFIRIHFGPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKK--PELQDMLLLSLNPYDYHFCSQGVTTVDN 326
Cdd:cd14893 159 AKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQADPLATN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 327 LD----DGEELMATDHAMDIlgfSNDEKYGCYKIVGAIMHFGNMKF---KQKQREEQAEADGTESADKAAYLMGISSADL 399
Cdd:cd14893 239 FAldarDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFvpdPEGGKSVGGANSTTVSDAQSCALKDPAQILL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 400 IKGLL--HPRV------------KVGNEYVT--KGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLDTKLAR------ 457
Cdd:cd14893 316 AAKLLevEPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksni 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 458 ---QFFIGVLDIAGFEIFE--YNSFEQLCINFTNEKLQQFFNHHMFV-----LEQEEYKKEGIEWV--FIDFGLDLQACI 525
Cdd:cd14893 396 vinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENRLTVnsNVDITSEQEKCL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 526 DLIE-KPLGILSILEEECMFPKASDMSFKAKLY--DNHIG--KSPN----FQKPRPDKKRKYEAHFELVHYAGVVPYNII 596
Cdd:cd14893 476 QLFEdKPFGIFDLLTENCKVRLPNDEDFVNKLFsgNEAVGglSRPNmgadTTNEYLAPSKDWRLLFIVQHHCGKVTYNGK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 597 GWLDKNKDPLNETVVAIFQKSQNKLLSAVYENYVSATSEDPPKSGIKEKRKKAASFQTVSQLHKENLN------------ 664
Cdd:cd14893 556 GLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynq 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 665 --KLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRilnpaaipddK 742
Cdd:cd14893 636 adALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK----------N 705
|
730 740 750
....*....|....*....|....*....|....*
gi 1394781870 743 FVDSRKATEKLLSSLD----LDHTQFKFGHTKVFF 773
Cdd:cd14893 706 VCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-774 |
2.90e-62 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 226.16 E-value: 2.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 100 SVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 180 SGAGKTVNTKRVIQYFAIvaaLGDTPGKKTQapatktggtledQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPS 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCY---LGDGNRGATG------------RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGST 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPE--LQDMLLLSLNPYDYHFCSQGVTTV----------DNL 327
Cdd:cd14882 147 GKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQnrLKEYNLKAGRNYRYLRIPPEVPPSklkyrrddpeGNV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 328 DDGEELMATDHAMDilgFSNDEKYGCYKIVGAIMHFGNMKFKQKQREeqAEADGTESADKAAYLMGISSADLIKGLLHPR 407
Cdd:cd14882 227 ERYKEFEEILKDLD---FNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 408 VKVGNEYVTKGQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLdtKLARQFF-----IGVLDIAGFEIFEYNSFEQLCI 482
Cdd:cd14882 302 LIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKM--SFPRAVFgdkysISIHDMFGFECFHRNRLEQLMV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 483 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKPLGILSILEEecmfpkASDMSFKAKLYDNHIG 562
Cdd:cd14882 380 NTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD------ASRSCQDQNYIMDRIK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 563 kspnfQKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLLSAVYENyvsatsedppkSGI 642
Cdd:cd14882 454 -----EKHSQFVKKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-----------SQV 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 643 KEKRKKAASFQTVSQlhkENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEGIRICRKGFPNRIL 722
Cdd:cd14882 518 RNMRTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIP 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1394781870 723 YADFKQRYRILnpaAIPDDKFVDSRKATEKLLsSLDLDHTQFKFGHTKVFFK 774
Cdd:cd14882 595 FQEFLRRYQFL---AFDFDETVEMTKDNCRLL-LIRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
105-726 |
1.42e-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: 219.19 E-value: 1.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 105 LKRRYSHWMIYTYSGLFCVTINPYKWLP-VYTAPVVAVYKGKRrsEVPPHIYSIADNAYNDMLRNRENQSMLITGESGAG 183
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 184 KTVNTKRVIQYFAivaalgdtpgkKTQAPATKTggtLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPSGKLA 263
Cdd:cd14905 85 KSENTKIIIQYLL-----------TTDLSRSKY---LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 264 SADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFCSQGVT-TVDNLDDGEELMATDHAMDI 342
Cdd:cd14905 151 GAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLG-DINSYHYLNQGGSiSVESIDDNRVFDRLKMSFVF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 343 LGFSNDEKYGCYKIVGAIMHFGNMKFKQKQREeqaeadgTESADKAaylmgissadLIKGLLH----PRVKVGNEYVT-K 417
Cdd:cd14905 230 FDFPSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDRT----------LIESLSHnitfDSTKLENILISdR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 418 GQNVEQVVYAVGALAKATYDRMFKWLVTRINRTLD-TKLARQffIGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHH 496
Cdd:cd14905 293 SMPVNEAVENRDSLARSLYSALFHWIIDFLNSKLKpTQYSHT--LGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 497 MFVLEQEEYKKEGIEWVFIDFGLDLQACIDLIEKplgILSILEEECMFPKASDMSFKAKLyDNHIGKSPNFQKpRPDKkr 576
Cdd:cd14905 371 VLKQEQREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL-QNFLSRHHLFGK-KPNK-- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 577 kyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNKLL---SAVYEnyVSATSEDPPKSGIKEKRKKAASFQ 653
Cdd:cd14905 444 -----FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLfsrDGVFN--INATVAELNQMFDAKNTAKKSPLS 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 654 TVSQL------HKENLNK-----------------------LMTNLRATQP---------HFVRCIIPNETKTPGAMDPF 695
Cdd:cd14905 517 IVKVLlscgsnNPNNVNNpnnnsgggggggnsgggsgsggsTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVK 596
|
650 660 670
....*....|....*....|....*....|....*
gi 1394781870 696 LVLHQLRCNGVLEGIRICRKGFP----NRILYADF 726
Cdd:cd14905 597 SVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-254 |
1.68e-54 |
|
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: 187.94 E-value: 1.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 121 FCVTINPYKWLPVYTAPVVAV-YKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAIVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVfYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1394781870 200 ALGDTPGK-KTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 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 ... |
100-772 |
1.90e-42 |
|
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: 168.09 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 100 SVLYNLKRRYSHWMIYTYSGLFCVTINPYKWLPVYTAPVVAVYKGKRRSE-VPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 179 ESGAGKTVNTKRVIQYFA---------IVAALGDTPGKKTQAPATKTGGTLEDQVIEANPAMEAFGNAKTLRNDNSSRFG 249
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAyqvkgsrrlPTNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 250 KFIRIHFgPSGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLLSlNPYDYHFCSQGVTTVDNLDD 329
Cdd:cd14938 162 KFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLK-NIENYSMLNNEKGFEKFSDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 330 GEELMATDHAMDILGFSNDEKYGCYKIVGAIMHFGNMK-----------FKQKQREEQAEADGTESADKAAYLMGISSAD 398
Cdd:cd14938 240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEivkafrkksllMGKNQCGQNINYETILSELENSEDIGLDENV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 399 ----LIKGLLHPRVKVGNEYVT-----------KGQNVEQVVYAVGALAKATYDRMFKWLVTRINR---TLDTKLARQFF 460
Cdd:cd14938 320 knllLACKLLSFDIETFVKYFTtnyifndsiliKVHNETKIQKKLENFIKTCYEELFNWIIYKINEkctQLQNININTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 461 IGVLDIAGFEIFEYNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWVFIDFGLDLQACID-LIEKPLGILSILE 539
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNlLVGPTEGSLFSLL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 540 EECMFPKASDMSFKAKLYDNHIGKSPNFQKPRPDKKRKyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQN 619
Cdd:cd14938 480 ENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNK--KTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 620 KLLSAVYENYVSATS----EDPPKSGIKE-----KRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTP- 689
Cdd:cd14938 558 EYMRQFCMFYNYDNSgnivEEKRRYSIQSalklfKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 690 GAMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPaaipddkfvDSRKATEKLLSSLDLDHTQFKFGHT 769
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMIGNN 708
|
...
gi 1394781870 770 KVF 772
Cdd:cd14938 709 MIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1180-1934 |
6.99e-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: 133.26 E-value: 6.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1180 LKLRRDLEEATLQHESTAAALrKKHADSVAELSEQIDNLQRVKQKLEK-----------EKSEMKMEVDDLSSNIEYLTK 1248
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1249 NKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLE 1328
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1329 EETKSKNALAHALQASRHDCDLLREQYEEEVEAKSELQRSLSKANAEVAQWRTKYETdaiQRTE--ELEEAKKKLAIRLQ 1406
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET---LRSKvaQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1407 EAEEAVeaahakcSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRnfDRIIAEWKQKYEETQAELEASQKESRSLS 1486
Cdd:TIGR02168 404 RLEARL-------ERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL--EEELEELQEELERLEEALEELREELEEAE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1487 TELFKLKNAYEES---LDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHEE 1563
Cdd:TIGR02168 475 QALDAAERELAQLqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVEN 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1564 SKTLRIQLELnQVKADVDRK--LAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEI--QLSH 1639
Cdd:TIGR02168 555 LNAAKKAIAF-LKQNELGRVtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVvdDLDN 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1640 ANRQAAEAQKMVRQLqsqIKDLQIELDDTMRHNDDLKEQAAALERRNNL--LLAEVEELRAALEQAERGRKLAEQELLEA 1717
Cdd:TIGR02168 634 ALELAKKLRPGYRIV---TLDGDLVRPGGVITGGSAKTNSSILERRREIeeLEEKIEELEEKIAELEKALAELRKELEEL 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1718 TERVNLLHSQNTGLINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQT 1797
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1798 IKDLQmrldeaeqialkggkKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLID 1877
Cdd:TIGR02168 791 IEQLK---------------EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1394781870 1878 KLQTKVKSYKRQYEEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRARSRE 1934
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
848-1751 |
9.17e-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: 132.87 E-value: 9.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 848 LRSAQTEKEMAtmkEEFQKLKEALEKSE-----AKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDllikakiQ 922
Cdd:TIGR02168 202 LKSLERQAEKA---ERYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE-------E 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 923 LEAKVKELTERVEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTK 1002
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1003 EKKALQEAHQQALDDLQAEEDKVNTLTKAkvkLEQQVDDLESSLEQEKKIRMDLERAKRKLEgdlkltqesvmdlendkq 1082
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQ---LETLRSKVAQLELQIASLNNEIERLEARLE------------------ 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1083 QLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQkkIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAG 1162
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1163 GataiQLEMNKKREAEFLKLRRDLEEATLQhestaaalRKKHADSVAELSEQIdnlqRVKQKLEKEKSEmkmevdDLSSN 1242
Cdd:TIGR02168 489 A----RLDSLERLQENLEGFSEGVKALLKN--------QSGLSGILGVLSELI----SVDEGYEAAIEA------ALGGR 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1243 IEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLAD--VSTQRARLQTESGELSRLLEEKE---------SFINQLTR 1311
Cdd:TIGR02168 547 LQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTeiQGNDREILKNIEGFLGVAKDLVKfdpklrkalSYLLGGVL 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1312 GKTSFTQMIEELKRQLEEET---------KSKNALAHAlQASRHDCDLLREQYEEEVEAK-SELQRSLSKANAEVAQWRT 1381
Cdd:TIGR02168 627 VVDDLDNALELAKKLRPGYRivtldgdlvRPGGVITGG-SAKTNSSILERRREIEELEEKiEELEEKIAELEKALAELRK 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1382 KyetdaiqrTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERAnsaaaaldkkqrnfDRII 1461
Cdd:TIGR02168 706 E--------LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL--------------EAEI 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1462 AEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTL 1541
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1542 ECEKSEIQAALEEAEGALEHEESKTLRIQLELnqvkadvdrklaekdEEFENLRRNHQRAMDSMQATLDAEAKARNEAIR 1621
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESEL---------------EALLNERASLEEALALLRSELEELSEELRELES 908
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1622 LRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDL-QIELDDTMRHNDDLKEQAAALERRnnlllaeVEELRAAL 1700
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRR-------LKRLENKI 981
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 1394781870 1701 EQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVEE 1751
Cdd:TIGR02168 982 KELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
971-1901 |
9.07e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 129.79 E-value: 9.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 971 KVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQALD--DLQAEEDKVN--TLTKAKVKLEQQVDDLESSL 1046
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykELKAELRELElaLLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1047 EQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEEL 1126
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1127 EEELEAERAARAKVEKQRAEVAReleelserleeaggataiQLEMNKKREAEFLKLRRDLEEATLQHESTAAALRKKhad 1206
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKE------------------ELESLEAELEELEAELEELESRLEELEEQLETLRSK--- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1207 sVAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEklcrtyedqLNEAKSKVDELQRQLADVSTQRA 1286
Cdd:TIGR02168 388 -VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---------LKELQAELEELEEELEELQEELE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1287 RLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKSKNALAhALQASRHDCDLLREQYEEEVEAKSELQ 1366
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK-ALLKNQSGLSGILGVLSELISVDEGYE 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1367 RSLSKANAEVAQW-RTKYETDAIQRTEELEEAKK--------------KLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQT 1431
Cdd:TIGR02168 537 AAIEAALGGRLQAvVVENLNAAKKAIAFLKQNELgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRK 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1432 EIEDL------SIDLERANSAAAALDKKQRNF----DRIIAEW--KQKYEETQAELEASQKESRSLSTELFKLKNAYEES 1499
Cdd:TIGR02168 617 ALSYLlggvlvVDDLDNALELAKKLRPGYRIVtldgDLVRPGGviTGGSAKTNSSILERRREIEELEEKIEELEEKIAEL 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1500 LDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEheesktlriqlELNQVKAD 1579
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT-----------ELEAEIEE 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1580 VDRKLAEKDEEFEnlrrnhqramdsmqatldaeakarnEAIRLRKKMEGDLNEMEIQLSHANRQAAEaqkmvrqLQSQIK 1659
Cdd:TIGR02168 766 LEERLEEAEEELA-------------------------EAEAEIEELEAQIEQLKEELKALREALDE-------LRAELT 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1660 DLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAErgrklaeQELLEATERVNLLHSQNTGLINQKKKME 1739
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELEALLNERASLE 886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1740 ADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNMEQTIKDL----QMRLDEAEQIALKg 1815
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE---LRLEGLEVRIDNLQERLseeySLTLEEAEALENK- 962
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1816 GKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSykrQYEEAEQ 1895
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE---RFKDTFD 1039
|
....*.
gi 1394781870 1896 QANSNL 1901
Cdd:TIGR02168 1040 QVNENF 1045
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1169-1931 |
9.15e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 129.79 E-value: 9.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1169 LEMNKKREAEFLKLRRDLEEATLqhesTAAALRKKhadsvaELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTK 1248
Cdd:TIGR02168 205 LERQAEKAERYKELKAELRELEL----ALLVLRLE------ELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1249 NKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLE 1328
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1329 EETKSKNALAHALQASRHDCDLLREQYEEEVEAKSELQRSLSKANAevaqwrtkyetdaiqrteELEEAKKKLairlqea 1408
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN------------------EIERLEARL------- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1409 eeaveaahakcSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRnfDRIIAEWKQKYEETQAELEASQKESRSLSTE 1488
Cdd:TIGR02168 410 -----------ERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL--EEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1489 LFKLKNAYEES---LDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAAL------------E 1553
Cdd:TIGR02168 477 LDAAERELAQLqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALggrlqavvvenlN 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1554 EAEGALEH--EESKTLRIQLELNQVKAD----VDRKLAEKDEEFENLRRNHQRAMDSMQATLD------AEAKARNEAIR 1621
Cdd:TIGR02168 557 AAKKAIAFlkQNELGRVTFLPLDSIKGTeiqgNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvLVVDDLDNALE 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1622 LRKKM---------EGDL-----------NEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAA 1681
Cdd:TIGR02168 637 LAKKLrpgyrivtlDGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1682 L-------ERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVEEAVQ 1754
Cdd:TIGR02168 717 LrkeleelSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1755 ECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKgGKKQIQKLEARVRELEGEL 1834
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELESEL 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1835 DTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQYEEAEQQANSNLVKYR-KVQHELDD 1913
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEE 955
|
810
....*....|....*...
gi 1394781870 1914 AEERADIAETQVNKLRAR 1931
Cdd:TIGR02168 956 AEALENKIEDDEEEARRR 973
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
852-1597 |
8.98e-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: 113.24 E-value: 8.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 852 QTEKEMAtmkEEFQKLKEalEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKVKELT 931
Cdd:TIGR02169 204 RREREKA---ERYQALLK--EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELN 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 932 ERVED--EEEINS------DLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKE 1003
Cdd:TIGR02169 279 KKIKDlgEEEQLRvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1004 KKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQ 1083
Cdd:TIGR02169 359 YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1084 LEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQR------------------- 1144
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseervrggraveevlka 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1145 ---------AEVARELEELSERLEEAGG--------------ATAIQL--EMNKKReAEFLKLRR--------------- 1184
Cdd:TIGR02169 519 siqgvhgtvAQLGSVGERYATAIEVAAGnrlnnvvveddavaKEAIELlkRRKAGR-ATFLPLNKmrderrdlsilsedg 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1185 ------DLEE--------------ATLQHESTAAALRKKH-------ADSVAELSEQIDNLQRVKQKLEKEKSEMKMEVD 1237
Cdd:TIGR02169 598 vigfavDLVEfdpkyepafkyvfgDTLVVEDIEAARRLMGkyrmvtlEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQ 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1238 DLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFT 1317
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1318 QMIEELKRQLEEETKSKNALAHALQasrhdcDLLREQYEEEVEaksELQRSLSKANAEVAQWRtkyetdaiQRTEELEEA 1397
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALN------DLEARLSHSRIP---EIQAELSKLEEEVSRIE--------ARLREIEQK 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1398 KKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEA 1477
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1478 SQKESRSLSTELFKLKNAYEESLDNLETLKRENKnlqeEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQaALEEAEG 1557
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIR-ALEPVNM 975
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1394781870 1558 ALEHEESKTLRIQLELNQVKADVDRK---LAEKDEEFENLRRN 1597
Cdd:TIGR02169 976 LAIQEYEEVLKRLDELKEKRAKLEEErkaILERIEEYEKKKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
856-1402 |
4.04e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.72 E-value: 4.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 856 EMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKVKELTERVE 935
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 936 DEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQAL 1015
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1016 DDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKDFEM 1095
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1096 NQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGATAIQLEMNK-- 1173
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNiv 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1174 -------KREAEFLKlRRDLEEATLQHESTAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEmkmEVDDLSSNIEYL 1246
Cdd:COG1196 553 veddevaAAAIEYLK-AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY---VLGDTLLGRTLV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1247 TKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRgktsftqMIEELKRQ 1326
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL-------ELEEALLA 701
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394781870 1327 LEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKSELQRSLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLA 1402
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1181-1931 |
5.37e-23 |
|
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: 107.46 E-value: 5.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1181 KLRRDLEEATLQHESTAAALRkkhadsvaELSEQIDNLQRVKQKLEKEKsEMKMEVDDLSSNIEYLTKNKAnaeklcrty 1260
Cdd:TIGR02169 174 KALEELEEVEENIERLDLIID--------EKRQQLERLRREREKAERYQ-ALLKEKREYEGYELLKEKEAL--------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1261 EDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKT-SFTQMIEELK---RQLEEETKSKNA 1336
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEaeiASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1337 LAHALQASRHDCDLLREQYEEEVEaksELQRSLSKANAEVAQWRTKYETDA------IQRTEELEEAKKKLAIRLQEAEE 1410
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIE---ELEREIEEERKRRDKLTEEYAELKeeledlRAELEEVDKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1411 AVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRI-------IAEWKQKYEETQAELEASQKESR 1483
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEkedkaleIKKQEWKLEQLAADLSKYEQELY 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1484 SLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGA----- 1558
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNrlnnv 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1559 -LEHEESKTLRIQ------------LELNQVKA--------------DVDRKLAEKDEEFENLRRNHQR---AMDSMQAt 1608
Cdd:TIGR02169 553 vVEDDAVAKEAIEllkrrkagratfLPLNKMRDerrdlsilsedgviGFAVDLVEFDPKYEPAFKYVFGdtlVVEDIEA- 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1609 ldaeakARNEAIRLRK-KMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNN 1687
Cdd:TIGR02169 632 ------ARRLMGKYRMvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1688 LLLAEVEELRAALEQAERGRKLAEQELLEATERvnllhsqntglinqkkkmeadIAQLTTEVEEAVQECRNAEEKAKKAI 1767
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKER---------------------LEELEEDLSSLEQEIENVKSELKELE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1768 TDAAMMAEELKKEQDTSAHLERMKKnmEQTIKDLQMRLDEAEqialkggkKQIQKLEARVRELEGELDTE-------QKK 1840
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLE--------EEVSRIEARLREIEQKLNRLtlekeylEKE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1841 TAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQYEEAEQQANSNLVKYRKVQHELDDAEERADI 1920
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
810
....*....|.
gi 1394781870 1921 AETQVNKLRAR 1931
Cdd:TIGR02169 915 KRKRLSELKAK 925
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
925-1825 |
1.04e-22 |
|
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: 106.69 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 925 AKVKELTERVEDEEEINSDLTSKKR----KLEDECAELKKdIDDLEITLAKVE-----KEKHATENKVKNLIEEMAALDE 995
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRqqleRLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 996 VIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKakvkleqqvddlESSLEQEKKIRmDLERAKRKLEGDLKLTQESVM 1075
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE------------EEQLRVKEKIG-ELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1076 DLENDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELS 1155
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1156 ERLEEAGGATAIQLEMNKKREAEFLKLRRDLEEATLQHESTAAALRKKhADSVAELSEQIDNLQRVKQKLEKEKSEMKME 1235
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK-ALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1236 VDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQ----------RQLADVSTQRArLQTESGELSRLL------ 1299
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKasiqgvhgtvAQLGSVGERYA-TAIEVAAGNRLNnvvved 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1300 -EEKESFINQLTRGKTSFTQMIEELKRQLEEETKSKNALAHALQASrhdCDLLR--EQYEEEVE---AKSELQRSLSKAN 1373
Cdd:TIGR02169 557 dAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFA---VDLVEfdPKYEPAFKyvfGDTLVVEDIEAAR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1374 AEVAQWR------------------TKYETDAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIED 1435
Cdd:TIGR02169 634 RLMGKYRmvtlegelfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1436 LSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEASQKESRSLSTElfklknayeesldnLETLKRENKNLQE 1515
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR--------------IEELEEDLHKLEE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1516 EIADLTDQISMSGktIHELEKLKKTLECEKSEIQAALEEAEGALeheESKTLRIQLelnqvkadvdrkLAEKDEEFENLR 1595
Cdd:TIGR02169 780 ALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQKL---NRLTLEKEY------------LEKEIQELQEQR 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1596 RNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDL 1675
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1676 KEQAAALERRNNLLLAEVEELRAALEQAERGRKLaEQELLEATERVNLLHSQNTGLINQKKKMEADIAQLtteveeavQE 1755
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV-QAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDEL--------KE 993
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1756 CRNAEEKAKKAITDAAMMAEELKKEQDTSAhLERMKKNMEQTIKDL-----QMRLDEAE-------QIALKGGKKQIQKL 1823
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEYEKKKREVFMEA-FEAINENFNEIFAELsggtgELILENPDdpfagglELSAKPKGKPVQRL 1072
|
..
gi 1394781870 1824 EA 1825
Cdd:TIGR02169 1073 EA 1074
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1110-1917 |
1.10e-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: 103.22 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1110 AQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVareleelserleeaggaTAIQLEMNKKREaeflKLRRDLEEA 1189
Cdd:TIGR02169 152 PVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERL-----------------DLIIDEKRQQLE----RLRREREKA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1190 tlqhESTAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKS 1269
Cdd:TIGR02169 211 ----ERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1270 -KVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKSKNALAHALQASRHDC 1348
Cdd:TIGR02169 287 eEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1349 DLLREQYEEEVEAKSELQRslskanaEVAQWRTKYEtdaiQRTEELEEAKKKLairlqeaeeaveaahakcSSLEKTKHR 1428
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRD-------ELKDYREKLE----KLKREINELKREL------------------DRLQEELQR 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1429 LQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKR 1508
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1509 ENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGA------LEHEESKTLRIQ------------ 1570
Cdd:TIGR02169 498 QARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNrlnnvvVEDDAVAKEAIEllkrrkagratf 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1571 LELNQVKA--------------DVDRKLAEKDEEFENLRRNHQR---AMDSMQA-----------TLDAE---------- 1612
Cdd:TIGR02169 578 LPLNKMRDerrdlsilsedgviGFAVDLVEFDPKYEPAFKYVFGdtlVVEDIEAarrlmgkyrmvTLEGElfeksgamtg 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1613 -AKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLA 1691
Cdd:TIGR02169 658 gSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1692 EVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADIAQltTEVEEAVQECRNAEEKAKKAITDAA 1771
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLR 815
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1772 MMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDE-AEQIALKGGKK-----QIQKLEARVRELEGELDTEQKKTAEAQ 1845
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiEKEIENLNGKKeeleeELEELEAALRDLESRLGDLKKERDELE 895
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394781870 1846 KGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQYEEaEQQANSNLVKYRKVQHELDDAEER 1917
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE-DEEIPEEELSLEDVQAELQRVEEE 966
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
861-1541 |
1.23e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.63 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 861 KEE-FQKLKEA---LEKSEAKRKELEeKQVTmiqekndlALQLQAEQ----DNLADAEERCD--LLIKAKIQLEAKVKEL 930
Cdd:COG1196 174 KEEaERKLEATeenLERLEDILGELE-RQLE--------PLERQAEKaeryRELKEELKELEaeLLLLKLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 931 TERVEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEA 1010
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1011 HQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKK 1090
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1091 KDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAkvEKQRAEVARELEELSERLEEAGGATAIQLE 1170
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA--ELEEEEEALLELLAELLEEAALLEAALAEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1171 MNKKREAEfLKLRRDLEEATLQHESTAAALRKKHADSVAELSEQIDNLQRVKQKLEKEksemkmEVDDLSSNIEYLTKNK 1250
Cdd:COG1196 483 LEELAEAA-ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA------LEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1251 ANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEE 1330
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1331 TKSKNALAHALQASRHDCDLLREQYEEEVEAKSELQRSLSKANAEVAQwrtkyETDAIQRTEELEEAKKKLAIRLQEAee 1410
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE-----LAERLAEEELELEEALLAEEEEERE-- 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1411 aveaahakcssLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEASQKESRSLSTELF 1490
Cdd:COG1196 709 -----------LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1394781870 1491 KLKN-------AYEESLDNLETLKRENKNLQEEIADLTDqismsgkTIHELEKLKKTL 1541
Cdd:COG1196 778 ALGPvnllaieEYEELEERYDFLSEQREDLEEARETLEE-------AIEEIDRETRER 828
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1320-1931 |
2.34e-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: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1320 IEELKRQLEE-ETKSKNAL-AHALQASRHDCDLlreqyEEEVEAKSELQRSLSKANAEVAQWRTKYEtDAIQRTEELEEA 1397
Cdd:COG1196 195 LGELERQLEPlERQAEKAErYRELKEELKELEA-----ELLLLKLRELEAELEELEAELEELEAELE-ELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1398 KKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEA 1477
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1478 SQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLEceksEIQAALEEAEG 1557
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL----ERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1558 ALEHEESKTLRIQLELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKmEGDLNEMEIQL 1637
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-LLLLLEAEADY 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1638 SHANRQAAEAQKmVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLea 1717
Cdd:COG1196 504 EGFLEGVKAALL-LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD-- 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1718 tervnllhsqntgLINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQT 1797
Cdd:COG1196 581 -------------KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1798 IKDLQMRLDEAEQIALKGGKKQIQKLEARVRELEGELDTEQKKTAEAQkgiRKYERRIKELTYQTEEDRKNLARMQDLID 1877
Cdd:COG1196 648 EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL---EEALLAEEEEERELAEAEEERLEEELEEE 724
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1394781870 1878 KLQTKVKSYKRQYEEAEQQANSNLvkyRKVQHELDDAEERADIAETQVNKLRAR 1931
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEELL---EEEALEELPEPPDLEELERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
843-1536 |
2.42e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 98.98 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 843 KIKPLLRSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQvtmiqekNDLALQLQAEQDNLADAEERCDLLIKAKIQ 922
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL-------EELEEQLETLRSKVAQLELQIASLNNEIER 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 923 LEAKVKELTERVEDEEEINSDLtsKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTK 1002
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1003 E---KKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAkrkLEGDLkltQESVMDLEN 1079
Cdd:TIGR02168 483 ElaqLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAA---LGGRL---QAVVVENLN 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1080 DKQQLEEKLKKKDFemnQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEK-------QRAEVARELE 1152
Cdd:TIGR02168 557 AAKKAIAFLKQNEL---GRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllgGVLVVDDLDN 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1153 ELSERLEEAGGATAIQLEMN------------KKREAEFLKLRRDLEEATLQHESTAAALRKKHAdSVAELSEQIDNLQR 1220
Cdd:TIGR02168 634 ALELAKKLRPGYRIVTLDGDlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEK-ALAELRKELEELEE 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1221 VKQKLEKEKSEMKMEVDDLSsnieyltKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLE 1300
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALR-------KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1301 EKESFINQLTRGKTSFTQMIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKSELQRSLSKANAEVAQWR 1380
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1381 TKYETDAIQRT------EELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSaaaaldKKQ 1454
Cdd:TIGR02168 866 ELIEELESELEallnerASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV------RID 939
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1455 RNFDRIIAEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEE-------SLDNLETLKRENKNLQEEIADLTDQISMS 1527
Cdd:TIGR02168 940 NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
....*....
gi 1394781870 1528 GKTIHELEK 1536
Cdd:TIGR02168 1020 EEAIEEIDR 1028
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1173-1755 |
9.90e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.54 E-value: 9.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1173 KKREAEFLKLRRDLEEATLQHESTAAALRKKHA------DSVAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYL 1246
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAeleelrLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1247 TKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQ 1326
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1327 LEEETKSKNALAHALQASRHDcdllREQYEEEVEAKSELQRSLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLAIRLQ 1406
Cdd:COG1196 395 AAELAAQLEELEEAEEALLER----LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1407 EAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRN----FDRIIAEWKQKYEETQAELEAS--QK 1480
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagAVAVLIGVEAAYEAALEAALAAalQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1481 ESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALE 1560
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1561 HEESKTLRIQlELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHA 1640
Cdd:COG1196 631 RLEAALRRAV-TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1641 NRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRK-------LAEQE 1713
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEalgpvnlLAIEE 789
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1394781870 1714 LLEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVEEAVQE 1755
Cdd:COG1196 790 YEELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLE 831
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1271-1892 |
1.62e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.16 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1271 VDELQRQLADVSTQRARLQtESGELSRLLEEKESFINQLTRgkTSFTQMIEELKRQLEEETKSKNALAHALQASRHDCDL 1350
Cdd:COG1196 195 LGELERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1351 LREQYEEEVEAKSELQRSLSKANAEVAQWRTK---YETDAIQRTEELEEAKKKLAirlqeaeeaveaahakcsslektkh 1427
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDiarLEERRRELEERLEELEEELA------------------------- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1428 RLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLK 1507
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1508 RENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHEESKTLRIQLELNQVKADVDRKLAEK 1587
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1588 DEefENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKmEGDLNEmEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELdd 1667
Cdd:COG1196 487 AE--AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL-AGAVAV-LIGVEAAYEAALEAALAAALQNIVVEDDEVAA-- 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1668 tmRHNDDLKEQAAAleRRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADIAQLTT 1747
Cdd:COG1196 561 --AAIEYLKAAKAG--RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1748 EVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERmkkNMEQTIKDLQMRLDEAEQIALKGGKKQIQKLEARV 1827
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE---AELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394781870 1828 RELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQYEE 1892
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1170-1919 |
1.31e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.28 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1170 EMNKKREAEFLKLRRDLEEATLQHESTAA--ALRKKHADSVAELSEQIDNLQRVKQKLEKEksEMKMEVDDLSSNIEYLT 1247
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAeeARKAEEAKKKAEDARKAEEARKAEDARKAE--EARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1248 KNKANAEKLCRTYEDQLNEAKSKVDELQRQLadvstqrarlQTESGELSRLLEEKESFINQltrgktsftQMIEELKRQl 1327
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVRKAE----------ELRKAEDARKAEAARKAEEE---------RKAEEARKA- 1220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1328 eEETKSKNALAHALQASRHDCDLLREqyeEEVEAKSELQRSLSKANAEVAQWRTKYETDAIQRTEELEEAK-KKLAIRLQ 1406
Cdd:PTZ00121 1221 -EDAKKAEAVKKAEEAKKDAEEAKKA---EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEeKKKADEAK 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1407 EAEEAVEAAHAKCSSLEKTKhrlqteIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEASQKESRSLS 1486
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKK------ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1487 TELFKLKNAYEESLDNLETLKR--ENKNLQEEIADLTDQISMSGKTIHELEKLKKTLEcEKSEIQAALEEAEGALEHEES 1564
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAKKADEA 1449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1565 KtlriQLELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLDAEaKARNEAIRLRKKMEGDLNEMEIQLSHANRQA 1644
Cdd:PTZ00121 1450 K----KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKKAEEAKKA 1524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1645 AEAQKMvrqlqsqikdlqieldDTMRHNDDLKEqaaALERRNNLLLAEVEELRAALEqaergRKLAEQELLEATERVNLL 1724
Cdd:PTZ00121 1525 DEAKKA----------------EEAKKADEAKK---AEEKKKADELKKAEELKKAEE-----KKKAEEAKKAEEDKNMAL 1580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1725 HSQNTGLINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQTIKDL-QM 1803
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--------EELKKAEEEKKKVEQLKKKEAEEKKKAeEL 1652
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1804 RLDEAEQIALKGGKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKV 1883
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA 1732
|
730 740 750
....*....|....*....|....*....|....*....
gi 1394781870 1884 KSYKRQYEEAEQQANSNLV---KYRKVQHELDDAEERAD 1919
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKdeeEKKKIAHLKKEEEKKAE 1771
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
224-714 |
2.12e-18 |
|
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: 92.11 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 224 VIEANPAMEAFGNAKTLRNDNSSRFGKF--IRIHFGPSG---KLASADIDIYLLEKSRVIFQQ------PGERSYHIYYQ 292
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 293 ILSGKKP---------ELQ----DMLLLSLNPYDYHFCSQGVTTVDNL-DDGEELMATDHAMDILGFSNDEKYGCYKIVG 358
Cdd:cd14894 329 MVAGVNAfpfmrllakELHldgiDCSALTYLGRSDHKLAGFVSKEDTWkKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 359 AIMHFGNMKFKQKQREEQAEADGT---ESADKAAYLMGISSADLIKGLLHPR-VKVGNEYVTKGQNVE--QVVYAVGALA 432
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsVSLQSTSETFEVTLEkgQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 433 KATYDRMFKWLVTRINRT--------------LDTKLARQFFIGVL---DIAGFEIFEYNSFEQLCINFTNEKL----QQ 491
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEAtkmsalstdgnkhqMDSNASAPEAVSLLkivDVFGFEDLTHNSLDQLCINYLSEKLyareEQ 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 492 FF------NHHMFVLEQEEykkegiEWVFIdfgldlqacidlIEKPLGILSILEEECMFPKASDMS----------FKAK 555
Cdd:cd14894 569 VIavayssRPHLTARDSEK------DVLFI------------YEHPLGVFASLEELTILHQSENMNaqqeekrnklFVRN 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 556 LYDNHIGKSPNFQKPRPDKKRKYEA-----HFELVHYAGVVPYNIIGWLDKNKDPLNETVVAIFQKSQNK-LLSAVYENY 629
Cdd:cd14894 631 IYDRNSSRLPEPPRVLSNAKRHTPVllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSShFCRMLNESS 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 630 VSATSEDPPKSGIKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGAMDPFLVLHQLRCNGVLEG 709
Cdd:cd14894 711 QLGWSPNTNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQ 790
|
....*
gi 1394781870 710 IRICR 714
Cdd:cd14894 791 MEICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1427-1934 |
2.76e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.92 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1427 HRLQTEIEDLsiDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETL 1506
Cdd:COG1196 216 RELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1507 KRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHEESKTLRIQLELNQVKADVDRKLAE 1586
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1587 KDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRL------RKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKD 1660
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEeallerLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1661 LQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRA---ALEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKK 1737
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAArllLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1738 MEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAmmaeELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEA------EQI 1811
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDEVAAAAIEYLK----AAKAGRATFLPLDKIRARAALAAALARGAIGAAvdlvasDLR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1812 ALKGGKKQIQKLEA--------------RVRELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLID 1877
Cdd:COG1196 610 EADARYYVLGDTLLgrtlvaarleaalrRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1394781870 1878 KLQTKVKSYKRQYEEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRARSRE 1934
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
862-1748 |
2.95e-17 |
|
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: 88.88 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 862 EEFQKLKEALEKseakrkeLEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKVKELTERVEDEEEIN 941
Cdd:pfam02463 166 RLKRKKKEALKK-------LIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 942 SDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAA-LDEVIAKLTKEKKALQEAHQQALDDLQA 1020
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKlLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1021 EEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAK---RKLEGDLKLTQESVMDLENDKQQLEEKLKKKDFEMNQ 1097
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEeelEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1098 LNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGATAIQLEMNKKREA 1177
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1178 EFLKLRRDLEEATLQHESTAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLssnieYLTKNKANAEKLC 1257
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN-----YKVAISTAVIVEV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1258 RTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKSKnal 1337
Cdd:pfam02463 554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILK--- 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1338 aHALQASRHDCDLLREQYEEEVEAKSELQRSLSKANAEVAQWRTK-YETDAIQRTEELEEAKKKLAIRLQeaeeaveaah 1416
Cdd:pfam02463 631 -DTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKElLEIQELQEKAESELAKEEILRRQL---------- 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1417 akcsSLEKTKHRLQTEIEDLSIDLERANsaAAALDKKQRNFDRIIAEWKQKYEETQAELEASQKESRSLSTELFKLKNaY 1496
Cdd:pfam02463 700 ----EIKKKEQREKEELKKLKLEAEELL--ADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL-K 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1497 EESLDNLETLKRENKNLQEEIADLTDQIsmsgKTIHELEKLKKTLECEKSEIQAALEEAEGALEHE-ESKTLRIQLELNQ 1575
Cdd:pfam02463 773 EKELAEEREKTEKLKVEEEKEEKLKAQE----EELRALEEELKEEAELLEEEQLLIEQEEKIKEEElEELALELKEEQKL 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1576 VKADVDRKLAEKDEEFENLRRNHQramDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQ 1655
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQEL---LLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1656 SQIKDLQIELDDTMRHNDDLKEQAAAlerRNNLLLAEVEELRAALEQAERGRKLAEQ--ELLEATERVNLLHSQNTGLIN 1733
Cdd:pfam02463 926 EAEILLKYEEEPEELLLEEADEKEKE---ENNKEEEEERNKRLLLAKEELGKVNLMAieEFEEKEERYNKDELEKERLEE 1002
|
890
....*....|....*
gi 1394781870 1734 QKKKMEADIAQLTTE 1748
Cdd:pfam02463 1003 EKKKLIRAIIEETCQ 1017
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
856-1625 |
1.36e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 86.73 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 856 EMATMKEEFQKLKEALEKSEAKRKELEEK--QVTMIQEKNDLALQLQAEQDNLADAEERCDLLIKAK-IQLEAKVKELTE 932
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEEVRKAEELRKaeDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEeAKKDAEEAKKAE 1246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 933 RVEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKV---KNLIEEMAALDEVIAKLTKEKKALQE 1009
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKaeeKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1010 AHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLK 1089
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK 1406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1090 KKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAeraarakveKQRAEVARELEELSERLEEAGGATAIQL 1169
Cdd:PTZ00121 1407 ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA---------KKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1170 EMNKKREAEFLKLRRDlEEATLQHESTAAALRKKHADSVAELSEQidnlqrvKQKLEKEKSEMKMEVDDLSSNIEyltkn 1249
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKKAEEA-------KKADEAKKAEEAKKADEAKKAEE----- 1544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1250 KANAEKLCRTYEDQLNEAKSKVDELQRQladvsTQRARLQTESGELSRLLEEKEsfINQLTRGKTSFTQM-IEELKRqlE 1328
Cdd:PTZ00121 1545 KKKADELKKAEELKKAEEKKKAEEAKKA-----EEDKNMALRKAEEAKKAEEAR--IEEVMKLYEEEKKMkAEEAKK--A 1615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1329 EETKSKNALAHALQASRHDCDLLREQYEEEVEAKSELQRSLSKANAEVAQWRTKYETDAIQ----RTEELEEAKKKLAIR 1404
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKaeeaKKAEEDEKKAAEALK 1695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1405 LQEAEEAVEAAHAKCSSLEKTK-HRLQTEIEDLSIDLERAnsaaaaldKKQRNFDRIIAEWKQKYEETQAELEASQKESR 1483
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKKKaEELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1484 SLSTELFKLKNAYEEsldnlETLKRENKNLQEEIADLTDQISMSGKTIHELEK-----LKKTLECEKSEIQ-------AA 1551
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIE-----EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKegnlvINDSKEMEDSAIKevadsknMQ 1842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1552 LEEAEGALEHEESKT------------------LRIQLELNQVKADVDRKLAEKDEEFENLRRNHQ-RAMDSMQATLDAE 1612
Cdd:PTZ00121 1843 LEEADAFEKHKFNKNnengedgnkeadfnkekdLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAgKNNDIIDDKLDKD 1922
|
810 820
....*....|....*....|
gi 1394781870 1613 A-------KARNEAIRLRKK 1625
Cdd:PTZ00121 1923 EyikrdaeETREEIIKISKK 1942
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1552-1917 |
1.60e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.14 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1552 LEEAEGALEHEESK--TLRiqlELNQVKADVDR---KLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKM 1626
Cdd:COG1196 161 IEEAAGISKYKERKeeAER---KLEATEENLERledILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLREL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1627 EGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDtmrhnddLKEQAAALERRNNLLLAEVEELRAALEQAERG 1706
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEE-------LELELEEAQAEEYELLAELARLEQDIARLEER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1707 RKLAEQELLEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAH 1786
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1787 LERMKKNMEQTIKDLQMRLDEAEQiALKGGKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDR 1866
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLE-RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1394781870 1867 KNLARMQDLIDKLQTKVKSYKRQYEEAEQQANSNLVKYRKVQHELDDAEER 1917
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1284-1864 |
1.61e-16 |
|
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: 86.38 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1284 QRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEE---LKRQLEEETK---SKNALAHALQASRHDCDLLREQYEE 1357
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEknaLQEQLQAETElcaEAEEMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1358 EVEAKSELQRSLSKANAEVAQWRTKYEtdaiQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLS 1437
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLE----EQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1438 IDLERANSAAAALDKKQRNFDRIiaewKQKYEETQAELEASQKESRSLSTELFKLKNAyeesldnletLKRENKNLQEEI 1517
Cdd:pfam01576 159 ERISEFTSNLAEEEEKAKSLSKL----KNKHEAMISDLEERLKKEEKGRQELEKAKRK----------LEGESTDLQEQI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1518 ADLTDQIsmsgktihelEKLKKTLECEKSEIQAALE--EAEGALEHEESKTLR-IQLELNQVKADVD-----RKLAEK-- 1587
Cdd:pfam01576 225 AELQAQI----------AELRAQLAKKEEELQAALArlEEETAQKNNALKKIReLEAQISELQEDLEseraaRNKAEKqr 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1588 ---DEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLshanrqaaeaQKMVRQLQSQIKDLQIE 1664
Cdd:pfam01576 295 rdlGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQL----------QEMRQKHTQALEELTEQ 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1665 LDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADIAQ 1744
Cdd:pfam01576 365 LEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELES 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1745 LTTEVEEavqecrnAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQ------MRLDEAEQIALKGGKK 1818
Cdd:pfam01576 445 VSSLLNE-------AEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEdernslQEQLEEEEEAKRNVER 517
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1394781870 1819 QIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEE 1864
Cdd:pfam01576 518 QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE 563
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1616-1931 |
3.86e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.99 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1616 RNEAIRLRKKMEGDLN-------EMEIQLSHANRQAAEAQKmVRQLQSQIKDLQIELddTMRHNDDLKEQAAALErrnnl 1688
Cdd:COG1196 174 KEEAERKLEATEENLErledilgELERQLEPLERQAEKAER-YRELKEELKELEAEL--LLLKLRELEAELEELE----- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1689 llAEVEELRAALEQAERGRKLAE-------QELLEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVEEAVQECRNAEE 1761
Cdd:COG1196 246 --AELEELEAELEELEAELAELEaeleelrLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1762 KAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQIQKLEARVRELEGELDtEQKKT 1841
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE-LAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1842 AEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQYEEAEQQANSNLVKYRKVQHELDDAEERADIA 1921
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
330
....*....|
gi 1394781870 1922 ETQVNKLRAR 1931
Cdd:COG1196 483 LEELAEAAAR 492
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
852-1646 |
8.25e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.42 E-value: 8.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 852 QTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQekndlalqlQAEQDNLADAEERCDLLIKAKiqlEAKVKELT 931
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR---------KAEEARKAEDAKRVEIARKAE---DARKAEEA 1169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 932 ERVEDEEEINSdltSKKRKLEDECAELKKDIDDLEITLA-KVEKEKHATENKV---KNLIEEMAALDEVIAKLTKEKKAL 1007
Cdd:PTZ00121 1170 RKAEDAKKAEA---ARKAEEVRKAEELRKAEDARKAEAArKAEEERKAEEARKaedAKKAEAVKKAEEAKKDAEEAKKAE 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1008 QEAHQQALDDLQAEEDKVNTLTKAKVKLEQ--QVDDLESSLEQEKKIRMDLERAKRKLEgDLKLTQESVMDLENDKQQLE 1085
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEarKADELKKAEEKKKADEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAE 1325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1086 EKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVE---KQRAEVARELEELSERLEEAG 1162
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaakKKAEEKKKADEAKKKAEEDKK 1405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1163 GATAIQLEMNKKREAEflKLRRDLEEATLQHESTAAALRKKHADSVAELSEQIDNLQRVKQKLE--------KEKSEMKM 1234
Cdd:PTZ00121 1406 KADELKKAAAAKKKAD--EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeakkadeaKKKAEEAK 1483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1235 EVDDLSSNIEYLTKNKANAEKlcrtyedqLNEAKSKVDELQRQLADVSTQRARLQTES--GELSRLLEEKESfINQLTRG 1312
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKK--------AAEAKKKADEAKKAEEAKKADEAKKAEEAkkADEAKKAEEKKK-ADELKKA 1554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1313 ----KTSFTQMIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKSELQRSLSKANAEVAQWRTKYET-DA 1387
Cdd:PTZ00121 1555 eelkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEkKK 1634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1388 IQRTEELEEAKKKLAIRLQeaeEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKqrnfdriiAEWKQK 1467
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELK---KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE--------AEEAKK 1703
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1468 YEETQAELEASQKESRslstelfKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSE 1547
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAE-------ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1548 IQAALEEaegALEHEESKTlriqlelnqvKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKME 1627
Cdd:PTZ00121 1777 KEAVIEE---ELDEEDEKR----------RMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQL 1843
|
810
....*....|....*....
gi 1394781870 1628 GDLNEMEIQLSHANRQAAE 1646
Cdd:PTZ00121 1844 EEADAFEKHKFNKNNENGE 1862
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1091-1930 |
8.90e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.04 E-value: 8.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1091 KDFEMNQLNSRIEDQQVLEAQlqKKIKELQARIEELEEELEAERAARAKVEK-QRAEVARELEELSERLEEAGGATAIQL 1169
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAF--GKAEEAKKTETGKAEEARKAEEAKKKAEDaRKAEEARKAEDARKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1170 EMNKK-REAEFLKLRRDLEEATLQHES-TAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEmKMEVDDLSSNIEYLT 1247
Cdd:PTZ00121 1155 EIARKaEDARKAEEARKAEDAKKAEAArKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1248 KNKANAEKLCRTYEDQLNEAKSKVDElqRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQL 1327
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEE--ARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1328 EEETKSKNALAHALQASRhDCDLLREQYEEEVEAKSELQRSLSKANAEVAQWRTKYETDAIQRTEE---LEEAKKKLAIR 1404
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkADAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1405 LQEAEEAVEAAHAKCSSLE-KTKHRLQTEIEDLSIDLERANSAAAAldKKQRNFDRIIAEWKQKYEETQAELEASQKESR 1483
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1484 SLSTELFKLKNAYEESLDNLETLKRENKNLQEEiADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHEE 1563
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADE-AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1564 SKTLRIQLELNqvKADVDRKLAEKDEEFENLRRNHQRAMDSMQATldaeaKARNEAIRLRKKMEGDLNEMEIQLSHANRQ 1643
Cdd:PTZ00121 1548 ADELKKAEELK--KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE-----EARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1644 AAEaqkmvrqlqsqikdlqielddtmrhndDLKEQAAALERRNNLLLAEVEELRaaleQAERGRKLAEQELLEATErvnl 1723
Cdd:PTZ00121 1621 KAE---------------------------ELKKAEEEKKKVEQLKKKEAEEKK----KAEELKKAEEENKIKAAE---- 1665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1724 lhsqntglinQKKKMEADiaqlttevEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQM 1803
Cdd:PTZ00121 1666 ----------EAKKAEED--------KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1804 RLDEAEQIALKGGKKQIQKLEARVRElegeldTEQKKTAEAQKGIRKYE---RRIKELTYQTEEDRKNLARMQDlidkLQ 1880
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKKDE------EEKKKIAHLKKEEEKKAeeiRKEKEAVIEEELDEEDEKRRME----VD 1797
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1394781870 1881 TKVKSYKRQYEEAEQQAN-SNLVKYRKVQHELDDAEERADIAETQVNKLRA 1930
Cdd:PTZ00121 1798 KKIKDIFDNFANIIEGGKeGNLVINDSKEMEDSAIKEVADSKNMQLEEADA 1848
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1081-1915 |
1.32e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 83.24 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1081 KQQLEEKLKKKDFEMNQLNSRI-EDQQVLEAQ---LQKKIKELQARIEELEEELEAERAARAKvEKQRAEVARELEELSE 1156
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLnESNELHEKQkfyLRQSVIDLQTKLQEMQMERDAMADIRRR-ESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1157 RLEEAggATAIQLEMNKKREAEFLKLRRDLeeatLQHESTAAALRkkhadsvaelSEQIDNLQRVKQKLEKEKSEMKMEV 1236
Cdd:pfam15921 152 HELEA--AKCLKEDMLEDSNTQIEQLRKMM----LSHEGVLQEIR----------SILVDFEEASGKKIYEHDSMSTMHF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1237 DDLSSNIeyltknkanaEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRAR-----LQTESGELSRLLEEKESFINQLTR 1311
Cdd:pfam15921 216 RSLGSAI----------SKILRELDTEISYLKGRIFPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1312 GKTSFTQMIEELKRQLE---EETKSKNA--------LAHALQASRHDCDLLREQYEEEVEaksELQRSLSKANAEVAQWR 1380
Cdd:pfam15921 286 KASSARSQANSIQSQLEiiqEQARNQNSmymrqlsdLESTVSQLRSELREAKRMYEDKIE---ELEKQLVLANSELTEAR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1381 TKYETDAiQRTEELEEAKKKLairlqeaeeaveaahakCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDri 1460
Cdd:pfam15921 363 TERDQFS-QESGNLDDQLQKL-----------------LADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELD-- 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1461 iaEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEeiadltdqisMSGKTIHELEKLKKT 1540
Cdd:pfam15921 423 --DRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE----------MLRKVVEELTAKKMT 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1541 LECEK---SEIQAALEEAEGALEHEESktlriqlELNQVKADVDRKLaekdEEFENLRR--NHQRAMDSMQATLDAEAKA 1615
Cdd:pfam15921 491 LESSErtvSDLTASLQEKERAIEATNA-------EITKLRSRVDLKL----QELQHLKNegDHLRNVQTECEALKLQMAE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1616 RNEAIR-LRKKMEgdlNEMEIQLSHAnRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLlaEVE 1694
Cdd:pfam15921 560 KDKVIEiLRQQIE---NMTQLVGQHG-RTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL--ELE 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1695 ELRAALEQAERGRKLAEqelleatervnlLHSQNTGLINQKKKMEADIAQLTTEVEEAVQECRNAEE-----------KA 1763
Cdd:pfam15921 634 KVKLVNAGSERLRAVKD------------IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEemetttnklkmQL 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1764 KKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAE------QIALKGGKKQIQKLEARVRELEGELD-- 1835
Cdd:pfam15921 702 KSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQskiqflEEAMTNANKEKHFLKEEKNKLSQELStv 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1836 -TEQKKTAEAQKGIRKYERRIKEltyqteedrkNLARMQDLIDKLQTKVKSYKRQYEEAEQQAnsnlVKYrKVQHELDDA 1914
Cdd:pfam15921 782 aTEKNKMAGELEVLRSQERRLKE----------KVANMEVALDKASLQFAECQDIIQRQEQES----VRL-KLQHTLDVK 846
|
.
gi 1394781870 1915 E 1915
Cdd:pfam15921 847 E 847
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1085-1927 |
2.25e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.88 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1085 EEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGA 1164
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1165 TAIQLEMNKK----REAEflKLRRDLEEATLQHESTAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEMKMEvdDLS 1240
Cdd:PTZ00121 1174 DAKKAEAARKaeevRKAE--ELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE--EER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1241 SNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELqrqladvstQRARLQTESGELSRLLEEKEsfinqltrgktsftqmI 1320
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADEL---------KKAEEKKKADEAKKAEEKKK----------------A 1304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1321 EELKRQLEEETKSKNALAHALQASRhDCDLLREQYEEEVEAKSELQRSLSKANAEVAQWRTKYETDAIQRTEE---LEEA 1397
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkADAA 1383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1398 KKKLAIRLQEAEEAVEAAHAKCSSLE-KTKHRLQTEIEDLSIDLERANSAAAAldKKQRNFDRIIAEWKQKYEETQAELE 1476
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKAEE 1461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1477 ASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEiADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAE 1556
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE-AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1557 GALEHEESKTLRIQLELNqvKADVDRKLAEKDEEFENLRRNHQRAMDSMQAtldaeAKARNEAIRLRKKMEGDLNEMEIQ 1636
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELK--KAEEKKKAEEAKKAEEDKNMALRKAEEAKKA-----EEARIEEVMKLYEEEKKMKAEEAK 1613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1637 LSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAALEQA----ERGRKLAEQ 1712
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAkkaeEDEKKAAEA 1693
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1713 ELLEATERVNllhsqntglINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKK 1792
Cdd:PTZ00121 1694 LKKEAEEAKK---------AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1793 NMEQTIKDLQmrlDEAEQIALKGGKKqiqKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARM 1872
Cdd:PTZ00121 1765 EEEKKAEEIR---KEKEAVIEEELDE---EDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADS 1838
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 1394781870 1873 QDLIDKLQTKVKSYKRQYEEAEQQANSNLVKYRKVQHELDDAEEraDIAETQVNK 1927
Cdd:PTZ00121 1839 KNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEE--EIEEADEIE 1891
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
838-1523 |
2.34e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.88 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 838 MKLFFKIKPLLRSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERcdlli 917
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKK----- 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 918 KAKiqlEAKVKELTERVEDEEEINSDLTSKKRKLEDE--CAELKKDIDDLEitlAKVEKEKHATENKVKnlIEEMAALDE 995
Cdd:PTZ00121 1337 KAE---EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkkKEEAKKKADAAK---KKAEEKKKADEAKKK--AEEDKKKAD 1408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 996 VIAKLTKEKKALQEAHQQALDDLQAEEdkvntlTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGD-LKLTQESV 1074
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADE------AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAEEA 1482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1075 MDLENDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEK-QRAEVARELEE 1153
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADElKKAEELKKAEE 1562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1154 LSERLEEAGGATAIQLEMNKKREAEFLKLRRDLEEATL-QHESTAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEM 1232
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1233 KMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKS--KVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLT 1310
Cdd:PTZ00121 1643 AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEakKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELK 1722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1311 RGKTSFTQMIEELKRQLEEETK----------SKNALAHALQASRHDCDLLREQY----EEEVEAKSELQRSL------- 1369
Cdd:PTZ00121 1723 KAEEENKIKAEEAKKEAEEDKKkaeeakkdeeEKKKIAHLKKEEEKKAEEIRKEKeaviEEELDEEDEKRRMEvdkkikd 1802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1370 SKANAEVAQWRTKYETDAIQRTEELEEAKKKlairlqeaeeavEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAA 1449
Cdd:PTZ00121 1803 IFDNFANIIEGGKEGNLVINDSKEMEDSAIK------------EVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADF 1870
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394781870 1450 LDKK--QRNFDRIIAEWKQKYEETQAELEasqkesRSLSTELFKLKN--AYEESLDNLETLKRENKNLQEEIADLTDQ 1523
Cdd:PTZ00121 1871 NKEKdlKEDDEEEIEEADEIEKIDKDDIE------REIPNNNMAGKNndIIDDKLDKDEYIKRDAEETREEIIKISKK 1942
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
851-1382 |
2.63e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.03 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 851 AQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQVtmiqEKNDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKVKEL 930
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKE----EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 931 TERVEDEEEInsdltskkRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEa 1010
Cdd:PRK03918 279 EEKVKELKEL--------KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1011 hqqALDDLQAEEDKVNTLTKAKVKLEQ--QVDDLESSLEQEKKIRM--DLERAKRKLEGDLKLTQESVMDLENDKQQLE- 1085
Cdd:PRK03918 350 ---LEKRLEELEERHELYEEAKAKKEEleRLKKRLTGLTPEKLEKEleELEKAKEEIEEEISKITARIGELKKEIKELKk 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1086 --EKLKKKDFEMNQLNSRIEDQQVLE--AQLQKKIKELQARIEELEEELEAERAARAKVEKQRA---EVARELEELSERL 1158
Cdd:PRK03918 427 aiEELKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkesELIKLKELAEQLK 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1159 EEAGGATAIQLEMNKKREAEFLKLRRDLEEATLQHESTAAALRKKHA--DSVAELSEQIDNLQRVKQKLEKEKSEMKME- 1235
Cdd:PRK03918 507 ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkKKLAELEKKLDELEEELAELLKELEELGFEs 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1236 VDDLSSNIEYLTKnkanaeklcrtYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTS 1315
Cdd:PRK03918 587 VEELEERLKELEP-----------FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394781870 1316 FTQ----MIEELKRQLEEETKSKNALAHALQASRH----DCDLLREQYEEEVEAKSELQrSLSKANAEVAQWRTK 1382
Cdd:PRK03918 656 YSEeeyeELREEYLELSRELAGLRAELEELEKRREeikkTLEKLKEELEEREKAKKELE-KLEKALERVEELREK 729
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
942-1662 |
4.92e-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: 81.22 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 942 SDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEviaKLTKEKKALQEAHQqaldDLQAE 1021
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLND---KLKKNKDKINKLNS----DLSKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1022 EDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKDFEMNQLNSR 1101
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1102 IEDQQVLEAQLQKKIKELQARIeeleeeleaeraarakvekqraevareleelserleeaggataiqlEMNKKREAEFLk 1181
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKI----------------------------------------------QKNKSLESQIS- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1182 lrrDLEEATLQHESTAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKsemkmevDDLSSNIEYLTKNKanaeKLCRTYE 1261
Cdd:TIGR04523 222 ---ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK-------KQLSEKQKELEQNN----KKIKELE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1262 DQLNEAKSKVDELQRQLADVSTQRARLQTESGElsRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKSKNALahal 1341
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQKEQDWNKELKSELKNQE--KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK---- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1342 qasrhdcdllreqyEEEVEAKSELQRSLSKANAEvaqwrtkyetdAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSS 1421
Cdd:TIGR04523 362 --------------QRELEEKQNEIEKLKKENQS-----------YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1422 LEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLD 1501
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEK 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1502 NLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHEESKTlriqlelnqvkadvd 1581
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEK--------------- 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1582 rKLAEKDEEFENLRRNhQRAMDSMQATLDAEAKARNEAIR-LRKKMEgdlnEMEIQLSHANRQAAEAQKMVRQLQSQIKD 1660
Cdd:TIGR04523 562 -EIDEKNKEIEELKQT-QKSLKKKQEEKQELIDQKEKEKKdLIKEIE----EKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
..
gi 1394781870 1661 LQ 1662
Cdd:TIGR04523 636 IK 637
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
855-1778 |
1.03e-14 |
|
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: 80.48 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 855 KEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKnDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKVKELTERV 934
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 935 EDEEEINSDLTSKKRKLEDECAELKKDIDdleitlakvekekHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAH--- 1011
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKtel 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1012 --QQALDDLQAEEDKVNTLTKAKVKLEQQ----VDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLE 1085
Cdd:TIGR00606 346 lvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1086 EKLKKKDFEMNQLNSRIEDQQVLeaqLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGAT 1165
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEI---LEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1166 AIQLEmNKKREAEFLKLRRDLEEATLQHESTAAA---------------LRKKHADSVAELSEQIDNLQRVKQ------K 1224
Cdd:TIGR00606 503 VKSLQ-NEKADLDRKLRKLDQEMEQLNHHTTTRTqmemltkdkmdkdeqIRKIKSRHSDELTSLLGYFPNKKQledwlhS 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1225 LEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQL-------------NEAKSKVDELQRQLADVSTQRARLQTE 1291
Cdd:TIGR00606 582 KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLssyedklfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGA 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1292 SGELSRLLE---------------------EKESFINQLTRGKTSFTQMIEELKRQLEEETKSKNALAHALQASRHDCDL 1350
Cdd:TIGR00606 662 TAVYSQFITqltdenqsccpvcqrvfqteaELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1351 LREQYEEEVEAKSELQRSLSKANAEVAQWRTKYETdaiqrteelEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQ 1430
Cdd:TIGR00606 742 KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGT---------IMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQA 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1431 TEIEdlSIDLERA-NSAAAALDKKQRNFDRIIaewkQKYEETQAELEASQKESRSLSTELFKLKN---AYEESLDNLETL 1506
Cdd:TIGR00606 813 AKLQ--GSDLDRTvQQVNQEKQEKQHELDTVV----SKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQF 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1507 KRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAAleeaegalEHEESKtlRIQLELNQVKADVDRKLAE 1586
Cdd:TIGR00606 887 EEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISS--------KETSNK--KAQDKVNDIKEKVKNIHGY 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1587 KDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMeiqlshanRQAAEAQKMV-RQLQSQIKdlqiel 1665
Cdd:TIGR00606 957 MKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLM--------RQDIDTQKIQeRWLQDNLT------ 1022
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1666 ddTMRHNDDLKEqaaaLERRNNLLLAEVEELRaALEQAERGRKLaEQELLEATERVNLLHSQNTGLINQKKKMEADIAQl 1745
Cdd:TIGR00606 1023 --LRKRENELKE----VEEELKQHLKEMGQMQ-VLQMKQEHQKL-EENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE- 1093
|
970 980 990
....*....|....*....|....*....|...
gi 1394781870 1746 tteveeavQECRNAEEKAKKAITDAAMMAEELK 1778
Cdd:TIGR00606 1094 --------PQFRDAEEKYREMMIVMRTTELVNK 1118
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
950-1840 |
1.63e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 79.63 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 950 KLEDECAELKKDIDDLEitlaKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQAlddlQAEEDKVNTLT 1029
Cdd:pfam02463 157 EIEEEAAGSRLKRKKKE----ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKE----KLELEEEYLLY 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1030 KAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKDFEMNQLNSRIEDQQVL- 1108
Cdd:pfam02463 229 LDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERr 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1109 --------------EAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEeaggatAIQLEMNKK 1174
Cdd:pfam02463 309 kvddeeklkesekeKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEE------ELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1175 REAEFLKLRRDLEEATLQHEStaaalrKKHADSVAELSEQIDNLQRVKQKleKEKSEMKMEVDDLSSNIEYLTKNKANAE 1254
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEE------EKEAQLLLELARQLEDLLKEEKK--EELEILEEEEESIELKQGKLTEEKEELE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1255 KLCRTYEDQLNEAKSKVDELQRqlaDVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKSK 1334
Cdd:pfam02463 455 KQELKLLKDELELKKSEDLLKE---TQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1335 NALAHALQASRHD----CDLLREQYEEEVEAKSELQRSLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLAIRLQEAEE 1410
Cdd:pfam02463 532 GDLGVAVENYKVAistaVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1411 AVEAAHAKCSSLEKTKHRLQTEIEDLsidLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEASQKEsrslstelf 1490
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKL---KESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ--------- 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1491 KLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHEESKTLRIQ 1570
Cdd:pfam02463 680 ELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKK 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1571 LELNQVKADVDRKLAEKDEEFENLRRNHQRAmDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKM 1650
Cdd:pfam02463 760 EEKEEEKSELSLKEKELAEEREKTEKLKVEE-EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1651 VRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQntg 1730
Cdd:pfam02463 839 ALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK--- 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1731 lINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKeQDTSAHLERMKKNMEQtikDLQMRLDEAEQ 1810
Cdd:pfam02463 916 -ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNK-RLLLAKEELGKVNLMA---IEEFEEKEERY 990
|
890 900 910
....*....|....*....|....*....|
gi 1394781870 1811 IALKGGKKQIQKLEARVRELEGELDTEQKK 1840
Cdd:pfam02463 991 NKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
922-1332 |
2.09e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 79.33 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 922 QLEAKVKELTERVEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLT 1001
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1002 KEKKALQEAHQQALDDLQAEEDKvntltkaKVKLEQQVDDLESSLEQekkirmdLERAKRKLEGDLKLTQESVMDLENDK 1081
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLKEELKA-------LREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1082 QQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEA 1161
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1162 ggataiqlemnkkrEAEFLKLRRDLEEatlqhestaaaLRKKHADSVAELSEQIDNLQRVKQKLeKEKSEMKMEVddlss 1241
Cdd:TIGR02168 907 --------------ESKRSELRRELEE-----------LREKLAQLELRLEGLEVRIDNLQERL-SEEYSLTLEE----- 955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1242 nieyltknkanAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIE 1321
Cdd:TIGR02168 956 -----------AEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE 1024
|
410
....*....|.
gi 1394781870 1322 ELKRQLEEETK 1332
Cdd:TIGR02168 1025 EIDREARERFK 1035
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
848-1334 |
3.51e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 848 LRSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEEK--QVTMIQEKNDLALQLQAEQDNLADAEERcdlLIKAKIQLEA 925
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkELKELKEKAEEYIKLSEFYEEYLDELRE---IEKRLSRLEE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 926 KVKELTERVEDEEEINsdltSKKRKLEDECAELKKDIDDLEitlakvekEKHATENKVKNLIEEMAALDEVIAKLTKEK- 1004
Cdd:PRK03918 322 EINGIEERIKELEEKE----ERLEELKKKLKELEKRLEELE--------ERHELYEEAKAKKEELERLKKRLTGLTPEKl 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1005 -KALQEAHQQALDdlqaEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGD-----LKLTQESVMDLE 1078
Cdd:PRK03918 390 eKELEELEKAKEE----IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1079 NDKQQLEEKLKKKDFEMNQLNSRIEDQQVL--EAQLQKKIKELQARIeeleeeleaeraarAKVEKQRAEVARELEELSE 1156
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELikLKELAEQLKELEEKL--------------KKYNLEELEKKAEEYEKLK 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1157 RLEEAGGATAIQLEMNKKREAEFLKLRRDLEEATLQHESTAAALRKKHAD----SVAELSEQIDNLQR----------VK 1222
Cdd:PRK03918 532 EKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfeSVEELEERLKELEPfyneylelkdAE 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1223 QKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLcrtyEDQLNEAKSKVDElqrqladvsTQRARLQTESGELSRLLEEK 1302
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEEL----RKELEELEKKYSE---------EEYEELREEYLELSRELAGL 678
|
490 500 510
....*....|....*....|....*....|..
gi 1394781870 1303 ESFINQLTRGKTSFTQMIEELKRQLEEETKSK 1334
Cdd:PRK03918 679 RAELEELEKRREEIKKTLEKLKEELEEREKAK 710
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
854-1666 |
4.24e-14 |
|
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: 78.24 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 854 EKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQ-----------AEQDNLADAEERCDLLIKAKIQ 922
Cdd:pfam15921 102 EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQntvheleaakcLKEDMLEDSNTQIEQLRKMMLS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 923 LEAKVKELTERVEDEEE-------------------INSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEkhaTENKV 983
Cdd:pfam15921 182 HEGVLQEIRSILVDFEEasgkkiyehdsmstmhfrsLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSE---SQNKI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 984 KNL-------IEEMAALDEV-IAKLT-KEKKALQEAH--QQALDDLQAEEDKVNTLTKakvkleQQVDDLESSLEQekkI 1052
Cdd:pfam15921 259 ELLlqqhqdrIEQLISEHEVeITGLTeKASSARSQANsiQSQLEIIQEQARNQNSMYM------RQLSDLESTVSQ---L 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1053 RMDLERAKRKLEGDLKLTQESVMdLENdkQQLEEKLKKKDfEMNQLNSRIEDQ-QVLEAQLQKKIKELQARIEELEEELE 1131
Cdd:pfam15921 330 RSELREAKRMYEDKIEELEKQLV-LAN--SELTEARTERD-QFSQESGNLDDQlQKLLADLHKREKELSLEKEQNKRLWD 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1132 AERAARAKVEKQRAEVAREleelserleeaggataiqlEMNKKREAEFLKLRRDLEEATLQHESTAAALRKKHADSVAEL 1211
Cdd:pfam15921 406 RDTGNSITIDHLRRELDDR-------------------NMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSL 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1212 SEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTE 1291
Cdd:pfam15921 467 TAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNV 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1292 SGElsrlleekesfinqltrgktsftqmIEELKRQLEEETKSknalahalqasrhdCDLLREQYEEEVEAKSELQRSLSK 1371
Cdd:pfam15921 547 QTE-------------------------CEALKLQMAEKDKV--------------IEILRQQIENMTQLVGQHGRTAGA 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1372 ANAEVAQwrtkYETDAIQRTEELEEAKkklaIRLQEAEEAVEAAHAKCSSLEKTKHRLqteiedlsidlerANSAAAALd 1451
Cdd:pfam15921 588 MQVEKAQ----LEKEINDRRLELQEFK----ILKDKKDAKIRELEARVSDLELEKVKL-------------VNAGSERL- 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1452 kkqrnfdRIIAEWKQKYEETQAELEASQKESRSLSTElfklknayeesldnLETLKRENKNLQEEIADLTDQISMSGKTI 1531
Cdd:pfam15921 646 -------RAVKDIKQERDQLLNEVKTSRNELNSLSED--------------YEVLKRNFRNKSEEMETTTNKLKMQLKSA 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1532 H-ELEKLKKTLECEKSEIQAALEEAEGALEHEESKtlRIQLELNQVKADVDRKL---AEKDEEFENLRRNHQRAMDSMQA 1607
Cdd:pfam15921 705 QsELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAK--RGQIDALQSKIQFLEEAmtnANKEKHFLKEEKNKLSQELSTVA 782
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394781870 1608 TLDAEAKARNEAIRLR-KKMEGDLNEMEIQLSHANRQAAEAQKMV-RQLQSQIK-DLQIELD 1666
Cdd:pfam15921 783 TEKNKMAGELEVLRSQeRRLKEKVANMEVALDKASLQFAECQDIIqRQEQESVRlKLQHTLD 844
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1380-1893 |
4.93e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.80 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1380 RTKYETDAIQRTEELE----EAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQT------EIEDLSIDLERANSAAAA 1449
Cdd:PRK03918 177 RIERLEKFIKRTENIEelikEKEKELEEVLREINEISSELPELREELEKLEKEVKEleelkeEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1450 LDKKQRNFDRIIAEWKQKYEETQaELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGK 1529
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1530 TIHELEKLKKtlecEKSEIQAALEEAEG-ALEHEESKTLRIQLElNQVKADVDRKLAEKDEEFENLRRNHQRAMD----- 1603
Cdd:PRK03918 336 KEERLEELKK----KLKELEKRLEELEErHELYEEAKAKKEELE-RLKKRLTGLTPEKLEKELEELEKAKEEIEEeiski 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1604 -SMQATLDAEAKARNEAIRLRKKMEGD----------------LNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELD 1666
Cdd:PRK03918 411 tARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1667 D--TMRHNDDLKEQAAALERRNNLLlaEVEELRAALEQAER-GRKLAEQE-----LLEATERVNLLHSQNTGLINQKKKM 1738
Cdd:PRK03918 491 KesELIKLKELAEQLKELEEKLKKY--NLEELEKKAEEYEKlKEKLIKLKgeiksLKKELEKLEELKKKLAELEKKLDEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1739 EADIAQLTT-----------EVEEAVQECRNAEEK---AKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMR 1804
Cdd:PRK03918 569 EEELAELLKeleelgfesveELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1805 LDEAEQI----ALKGGKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTyQTEEDRKNLARMQDLIDKLQ 1880
Cdd:PRK03918 649 LEELEKKyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE-KAKKELEKLEKALERVEELR 727
|
570
....*....|...
gi 1394781870 1881 TKVKSYKRQYEEA 1893
Cdd:PRK03918 728 EKVKKYKALLKER 740
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1212-1915 |
5.18e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 78.09 E-value: 5.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1212 SEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLaDVSTQRARLQTE 1291
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR-EAQEEQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1292 SGELSRLLEEKESFINQLtrgktsftqmiEELKRQLEEETKSKNALAHalQASRHDCDLLREQYEEEVEAKSELQRSLSK 1371
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVL-----------EETQERINRARKAAPLAAH--IKAVTQIEQQAQRIHTELQSKMRSRAKLLM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1372 ANAEVAQWRTkyetdAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALD 1451
Cdd:TIGR00618 329 KRAAHVKQQS-----SIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1452 KKQRNFDRIIAEwKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISmSGKTI 1531
Cdd:TIGR00618 404 ILQREQATIDTR-TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ-TKEQI 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1532 HELEKLKKTLECEKSEIQAALE-EAEGALEHEESKTLRIQL----------------ELNQVKADVDRKLAEKDEEFENL 1594
Cdd:TIGR00618 482 HLQETRKKAVVLARLLELQEEPcPLCGSCIHPNPARQDIDNpgpltrrmqrgeqtyaQLETSEEDVYHQLTSERKQRASL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1595 RRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDD 1674
Cdd:TIGR00618 562 KEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQEL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1675 LKEQAAALERRNNLLLAEVEE-LRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKM---EADIAQLTTEVE 1750
Cdd:TIGR00618 642 ALKLTALHALQLTLTQERVREhALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLrelETHIEEYDREFN 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1751 EAVQECRNAEEKAKKAITDAAMMAEELKKEQDTS-AHLERMKKNMEQTIKDLQMRLDEAEQIalkggkkqIQKLEARVRE 1829
Cdd:TIGR00618 722 EIENASSSLGSDLAAREDALNQSLKELMHQARTVlKARTEAHFNNNEEVTAALQTGAELSHL--------AAEIQFFNRL 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1830 LEGELDTEQKKTAEAQKGIRKYErriKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQ---YEEAEQQANSNLVKYRK 1906
Cdd:TIGR00618 794 REEDTHLLKTLEAEIGQEIPSDE---DILNLQCETLVQEEEQFLSRLEEKSATLGEITHQllkYEECSKQLAQLTQEQAK 870
|
....*....
gi 1394781870 1907 VQHELDDAE 1915
Cdd:TIGR00618 871 IIQLSDKLN 879
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1182-1879 |
6.48e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.65 E-value: 6.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1182 LRRDLEEATLQHEstaaALR--KKHADSVAELSEQIDNLQRVKQKLEKEKSEMKMEVddLSSNIEYLTKNKANAEKLCRT 1259
Cdd:COG4913 240 AHEALEDAREQIE----LLEpiRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1260 YEDQLNEAKSKVDELQRQLADVSTQR-ARLQTESGELSRLLEEKEsfinqltRGKTSFTQMIEELKRQLEEETKSKNALA 1338
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERE-------RRRARLEALLAALGLPLPASAEEFAALR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1339 HALQASRHDCDLLREQYEEEVeakSELQRSLSKANAEVAQWRTkyETDAIQRT-----EELEEAKKKLAIRLQEAEEAVE 1413
Cdd:COG4913 387 AEAAALLEALEEELEALEEAL---AEAEAALRDLRRELRELEA--EIASLERRksnipARLLALRDALAEALGLDEAELP 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1414 AAhakCSSLE-KTKHRL-QTEIE--------DLSIDLERANSAAAALDkkQRNF-DRIIAEwkqKYEETQAELEASQKES 1482
Cdd:COG4913 462 FV---GELIEvRPEEERwRGAIErvlggfalTLLVPPEHYAAALRWVN--RLHLrGRLVYE---RVRTGLPDPERPRLDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1483 RSLSTELFKLKNAYEESL-------------DNLETLKRENKNLQeeiadLTDQISMSGktiheleklkktlecekseiq 1549
Cdd:COG4913 534 DSLAGKLDFKPHPFRAWLeaelgrrfdyvcvDSPEELRRHPRAIT-----RAGQVKGNG--------------------- 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1550 aaleeaeGALEHEESKTLRIQLELNQvkaDVDRKLAEKDEEFENLRRNHQRAmDSMQATLDAEAKARNEAIRLRKKMEgD 1629
Cdd:COG4913 588 -------TRHEKDDRRRIRSRYVLGF---DNRAKLAALEAELAELEEELAEA-EERLEALEAELDALQERREALQRLA-E 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1630 LNEMEIQLSHANRQAAEAQKM----------VRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAA 1699
Cdd:COG4913 656 YSWDEIDVASAEREIAELEAElerldassddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1700 LEQAERGRKLAEQELLEAtERVNLLHSQNTGLInqKKKMEADIAQLTTEVEEAVQECRNAEEKAKK-------------- 1765
Cdd:COG4913 736 LEAAEDLARLELRALLEE-RFAAALGDAVEREL--RENLEERIDALRARLNRAEEELERAMRAFNRewpaetadldadle 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1766 AITDAAMMAEELkKEQDTSAHLERMK----KNMEQTIKDLQMRLDEAEQIAlkggKKQIQKLEARVRELE-GE-----LD 1835
Cdd:COG4913 813 SLPEYLALLDRL-EEDGLPEYEERFKellnENSIEFVADLLSKLRRAIREI----KERIDPLNDSLKRIPfGPgrylrLE 887
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1394781870 1836 TEQKKTAEaqkgIRKYERRIKELT----YQTEEDR-KNLARMQDLIDKL 1879
Cdd:COG4913 888 ARPRPDPE----VREFRQELRAVTsgasLFDEELSeARFAALKRLIERL 932
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1519-1943 |
8.99e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 77.42 E-value: 8.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1519 DLTDQISMSGKTIHEL-EKLKKTLECEkSEIQAALEEAEGALEHEEsktlRIQLELNQVKADVDRKLAEKD--EEFENLR 1595
Cdd:TIGR02169 143 DVTDFISMSPVERRKIiDEIAGVAEFD-RKKEKALEELEEVEENIE----RLDLIIDEKRQQLERLRREREkaERYQALL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1596 RNHQramdsmqatlDAEAKarneaIRLRKKmegdlNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDL 1675
Cdd:TIGR02169 218 KEKR----------EYEGY-----ELLKEK-----EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1676 KEQAAAL-ERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADI-------AQLTT 1747
Cdd:TIGR02169 278 NKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIeeerkrrDKLTE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1748 EVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDtsaHLERMKKNMEQTIKDLQMRLDEAEQIALKGG--KKQIQKLEA 1825
Cdd:TIGR02169 358 EYAELKEELEDLRAELEEVDKEFAETRDELKDYRE---KLEKLKREINELKRELDRLQEELQRLSEELAdlNAAIAGIEA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1826 RVRELEGELDTEQKKtaeaqkgIRKYERRIKELtyqteedrknlarmqdlidklQTKVKSYKRQYEEAEQqansnlvKYR 1905
Cdd:TIGR02169 435 KINELEEEKEDKALE-------IKKQEWKLEQL---------------------AADLSKYEQELYDLKE-------EYD 479
|
410 420 430
....*....|....*....|....*....|....*...
gi 1394781870 1906 KVQHELDDAEERADIAETQVNKLRARSREVVITSKVLK 1943
Cdd:TIGR02169 480 RVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLK 517
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
997-1949 |
1.09e-13 |
|
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: 77.01 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 997 IAKLTKEKKALQEAHQ------QALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLT 1070
Cdd:TIGR00606 178 IFSATRYIKALETLRQvrqtqgQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEI 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1071 QE---SVMDLENDKQQLEEKLKKKDFEMNQLNS-RIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAE 1146
Cdd:TIGR00606 258 EHnlsKIMKLDNEIKALKSRKKQMEKDNSELELkMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1147 VARELEELSERLEEAGGATAIQLEMNKKREAEFLKLRRDLEEATLQHEstaaalrkkhadsvAELSEQIDNLQRVKQKLE 1226
Cdd:TIGR00606 338 LNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERG--------------PFSERQIKNFHTLVIERQ 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1227 KEKSEMkmevddlssnieyltknkanAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQrarLQTESGELSRLLEEKESFI 1306
Cdd:TIGR00606 404 EDEAKT--------------------AAQLCADLQSKERLKQEQADEIRDEKKGLGRT---IELKKEILEKKQEELKFVI 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1307 NQLTRGKTSFTQMIEelkrQLEEETKSKNALAHALQASRHDCDLLREQYEEEveAKSELQRSLSKANAEVAQWRTKYETd 1386
Cdd:TIGR00606 461 KELQQLEGSSDRILE----LDQELRKAERELSKAEKNSLTETLKKEVKSLQN--EKADLDRKLRKLDQEMEQLNHHTTT- 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1387 aiqRTEELEEAKKKLAIRLQEAEEAVEAAHAKCS---------SLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQ--- 1454
Cdd:TIGR00606 534 ---RTQMEMLTKDKMDKDEQIRKIKSRHSDELTSllgyfpnkkQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKnhi 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1455 RNFDRIIAEWKQKYEET----------QAELEASQKESRSLSTELFKLKNAYEESLDNLETLKREN-------------- 1510
Cdd:TIGR00606 611 NNELESKEEQLSSYEDKlfdvcgsqdeESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcqrvfqte 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1511 KNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQaaleeaeGALEHEESKTLRIQLELNQVKADVDRKLAEKDEE 1590
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEML-------GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1591 FENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMR 1670
Cdd:TIGR00606 764 KNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVS 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1671 HNDDLKEQAAALERRNNLLLAEVEELRAAL----EQAERGRKLAEQELLEATErvnlLHSQNTGLINQKKKMEADIAQLT 1746
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTNELKSEKlqigTNLQRRQQFEEQLVELSTE----VQSLIREIKDAKEQDSPLETFLE 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1747 TEVEEAVQECRNAEEKAKKAITDAAMMAEELKK--------EQDTSAHLERMKKNMEQTIKDLQMRLDEAEQialkggkk 1818
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDDYLKQKETELNTVNAQLEECEK-------- 991
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1819 QIQKLEARVRELEGELDTE--QKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQdlidKLQTKVKSYKRQYEEAEQQ 1896
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIDTQkiQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQ----VLQMKQEHQKLEENIDLIK 1067
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|...
gi 1394781870 1897 ANSNLVKYRKVQHELDDAEERADIAETQVNKLRARSREVVITSKVLKTASLDI 1949
Cdd:TIGR00606 1068 RNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDL 1120
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
980-1808 |
1.23e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 76.60 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 980 ENKVKNLIEEMAALDEVIAKLTKEKKALQEahqqalDDLQAEEDKVNTLTKAKvKLEQQVDDLESSLEQEKKIRMDLERA 1059
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDK------NLNKDEEKINNSNNKIK-ILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1060 KRKLEGDLKLTQESVMDLENDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAK 1139
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1140 VEKQRAEVARELEELSERLEEaggataiqLEMNKKREAEFLKLRRDLEEATLQHESTAAALRKKHADSVAELSEQIDNLQ 1219
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLLSN--------LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1220 RVKQKLEKEKsemkmevDDLSSNIEYLTKNKanaeKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGElsRLL 1299
Cdd:TIGR04523 257 QLKDEQNKIK-------KQLSEKQKELEQNN----KKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQE--KKL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1300 EEKESFINQLTRGKTSFTQMIEELKRQLEEETKSKNALahalqasrhdcdllreqyEEEVEAKSELQRSLSKANAEvaqw 1379
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK------------------QRELEEKQNEIEKLKKENQS---- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1380 rtkyetdAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDR 1459
Cdd:TIGR04523 382 -------YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1460 IIAEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKK 1539
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1540 TLECEKSEIQAALEEAEGALEHEEsktlriqleLNQVKADVDRKLAEKDEEFENLRRNHQramdsmqatldaeakarnea 1619
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKEN---------LEKEIDEKNKEIEELKQTQKSLKKKQE-------------------- 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1620 irlrkkmegdlnemeiqlshanrqaaEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAA 1699
Cdd:TIGR04523 586 --------------------------EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK 639
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1700 LEQAERGRKLAEQELLEATERVNLLHSQNTGLinqkKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEELKK 1779
Cdd:TIGR04523 640 KNKLKQEVKQIKETIKEIRNKWPEIIKKIKES----KTKIDDIIELMKDWLKELSLHYKKYITRMIRIKDLPKLEEKYKE 715
|
810 820
....*....|....*....|....*....
gi 1394781870 1780 EQDTSAHLERMKKNMEQTIKDLQMRLDEA 1808
Cdd:TIGR04523 716 IEKELKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1439-1934 |
1.70e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 76.31 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1439 DLERANSAAAALDKKQRNFDR-IIAEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKrenkNLQEei 1517
Cdd:pfam15921 89 DLQRRLNESNELHEKQKFYLRqSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAK----CLKE-- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1518 adltDQISMSGKTIHELEKLKKTLECEKSEIQAAL---EEAEGALEHEESKTLRIQLElnQVKADVDRKLAEKDEEFENL 1594
Cdd:pfam15921 163 ----DMLEDSNTQIEQLRKMMLSHEGVLQEIRSILvdfEEASGKKIYEHDSMSTMHFR--SLGSAISKILRELDTEISYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1595 RRNHQRAMDSMQAtLDAEAKARNEAI--RLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQielddtmrhn 1672
Cdd:pfam15921 237 KGRIFPVEDQLEA-LKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQ---------- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1673 DDLKEQAAALERRNNLLLAEVEELRAALEQAERgrkLAEQELLEATERVNLLHSQNTglinqkkkmeadiaQLTTEVEEA 1752
Cdd:pfam15921 306 EQARNQNSMYMRQLSDLESTVSQLRSELREAKR---MYEDKIEELEKQLVLANSELT--------------EARTERDQF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1753 VQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQialkggkkQIQKLEARVRELEG 1832
Cdd:pfam15921 369 SQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM--------EVQRLEALLKAMKS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1833 ELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKR----------QYEEAEQQANSNLV 1902
Cdd:pfam15921 441 ECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERtvsdltaslqEKERAIEATNAEIT 520
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1394781870 1903 KYR--------KVQHeLDDAEERADIAETQVNKLRARSRE 1934
Cdd:pfam15921 521 KLRsrvdlklqELQH-LKNEGDHLRNVQTECEALKLQMAE 559
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
32-75 |
3.19e-13 |
|
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: 65.53 E-value: 3.19e-13
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1394781870 32 DGKKRAWIPDEKEAYLEIEIKESSGGKVIVETKDKQTRVVKEDD 75
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDD 44
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1301-1952 |
3.41e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.56 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1301 EKESFINQLTRGKTS-----FTQMIEELKRQLEEETKSKNALAHALQASRhdcdllreqYEEEVEAKSELQRSLSKANAE 1375
Cdd:PTZ00121 1061 EAKAHVGQDEGLKPSykdfdFDAKEDNRADEATEEAFGKAEEAKKTETGK---------AEEARKAEEAKKKAEDARKAE 1131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1376 VAqwRTKYETDAIQRTEELEEAKKKLAIRlqeaeeaVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQr 1455
Cdd:PTZ00121 1132 EA--RKAEDARKAEEARKAEDAKRVEIAR-------KAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARK- 1201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1456 nfdriiAEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELE 1535
Cdd:PTZ00121 1202 ------AEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1536 KLKKTLECEKSEIQAALEEAEGALEHEESKTLRIQLELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKA 1615
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA 1355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1616 RNEAIRLRKKMEGDlnemEIQLSHANRQAAEAQKMVRQlqsqikdlqielddtMRHNDDLKEQAAALERRNNlllaEVEE 1695
Cdd:PTZ00121 1356 ADEAEAAEEKAEAA----EKKKEEAKKKADAAKKKAEE---------------KKKADEAKKKAEEDKKKAD----ELKK 1412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1696 LRAALEQAERGRKLAEqELLEATErvnllhsqntglinQKKKMEAdiAQLTTEVEEAVQECRNAEEKAKKAitDAAMMAE 1775
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAE-EKKKADE--------------AKKKAEE--AKKADEAKKKAEEAKKAEEAKKKA--EEAKKAD 1473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1776 ELKKEQDTSAHLERMKKNMEQTIK---------DLQMRLDEAEQIALKGGKKQIQKLEARVRELEGELDTEQKKTAEAQK 1846
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKkadeakkaaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1847 G--IRKYERRIK-ELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQYEEAEQQANSNlvKYRKVQHELDDAEE--RADIA 1921
Cdd:PTZ00121 1554 AeeLKKAEEKKKaEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE--EAKKAEEAKIKAEElkKAEEE 1631
|
650 660 670
....*....|....*....|....*....|.
gi 1394781870 1922 ETQVNKLRARSREVVITSKVLKTASLDIGVR 1952
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1427-1934 |
6.52e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.57 E-value: 6.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1427 HRLQTEIEDL--SID-LERANSAAAALDKKQRNFDRiiaewkQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNL 1503
Cdd:COG4913 238 ERAHEALEDAreQIElLEPIRELAERYAAARERLAE------LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1504 ETLKRENKNLQEEIADLTDQISMS-GKTIHELEKLKKTLECEKSEIQAALEEAEGALeheesKTLRIQLELNQvkadvdr 1582
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALL-----AALGLPLPASA------- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1583 klaekdEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKmegdlnemeiqlshANRQAAEAQKMVRQLQSQIKDLQ 1662
Cdd:COG4913 380 ------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRD--------------LRRELRELEAEIASLERRKSNIP 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1663 IELDDtMRhnDDLKEQAAALERRNNLL--LAEVEEL----RAALEQAERGRKLA-------EQELLEATERVNLLHSQNT 1729
Cdd:COG4913 440 ARLLA-LR--DALAEALGLDEAELPFVgeLIEVRPEeerwRGAIERVLGGFALTllvppehYAAALRWVNRLHLRGRLVY 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1730 GLINQKKK----MEADIAQLTTEVE-------EAVQE----------CRNAEE--KAKKAITDAAMMAEELKK-EQDTSA 1785
Cdd:COG4913 517 ERVRTGLPdperPRLDPDSLAGKLDfkphpfrAWLEAelgrrfdyvcVDSPEElrRHPRAITRAGQVKGNGTRhEKDDRR 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1786 HLER---MKKNMEQTIKDLQMRLDEAEQiALKGGKKQIQKLEARVRELEGELDTEQK--KTAEAQKGIRKYERRIKELty 1860
Cdd:COG4913 597 RIRSryvLGFDNRAKLAALEAELAELEE-ELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAEL-- 673
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394781870 1861 qtEEDRKNLARMQDLIDKLQTKVKSYKRQYEEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRARSRE 1934
Cdd:COG4913 674 --EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
854-1590 |
6.61e-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: 74.62 E-value: 6.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 854 EKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKVKELTER 933
Cdd:pfam02463 278 EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 934 VEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQ 1013
Cdd:pfam02463 358 EEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1014 ALDDLQA--EEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKK 1091
Cdd:pfam02463 438 SIELKQGklTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1092 DFEMNQLNSRIEDQQVLEAQLQKkiKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGATAIQLEM 1171
Cdd:pfam02463 518 DGVGGRIISAHGRLGDLGVAVEN--YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIA 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1172 NKKREAEFLKLRRDLEEATLQHESTAAALRKKHADSVAELSEQ--IDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKN 1249
Cdd:pfam02463 596 VLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKesAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKEL 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1250 KANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEE 1329
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1330 ETKSKNALAHALQASRHDCDLLREQYEEEVEAKSELQRSLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLAIRLQEAE 1409
Cdd:pfam02463 756 RLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEEL 835
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1410 EAVEAAHAKcsSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEASQKESRSLSTEL 1489
Cdd:pfam02463 836 EELALELKE--EQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLE 913
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1490 F---KLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHEESKT 1566
Cdd:pfam02463 914 EkenEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKD 993
|
730 740
....*....|....*....|....
gi 1394781870 1567 LRIQLELNQVKADVDRKLAEKDEE 1590
Cdd:pfam02463 994 ELEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1034-1717 |
9.86e-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: 9.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1034 KLEQQVDDLESSLEQEKKIRMDLERAKRKLEgdlklTQESVMDLENDKQQLEEKLKKKDFEMNQLNSriedqqvleAQLQ 1113
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIE-----LLEPIRELAERYAAARERLAELEYLRAALRL---------WFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1114 KKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGATAIQLEMN--------KKREAEFLKLRRD 1185
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREierlerelEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1186 LEEATLQHESTA---AALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNK----ANAEKLCR 1258
Cdd:COG4913 368 LAALGLPLPASAeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRD 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1259 TYEDQLNEAKSKV----DELQRQLAD----------VSTQRARLQTESGELSRLLEekesFINQLTRGKTSFTQMIEELK 1324
Cdd:COG4913 448 ALAEALGLDEAELpfvgELIEVRPEEerwrgaiervLGGFALTLLVPPEHYAAALR----WVNRLHLRGRLVYERVRTGL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1325 RQLEEETKSKNALAHALQASRHDC-DLLREQYEEE-----VEAKSELQ---RSLSKAnAEVAQWRTKYETDAIQRTEEL- 1394
Cdd:COG4913 524 PDPERPRLDPDSLAGKLDFKPHPFrAWLEAELGRRfdyvcVDSPEELRrhpRAITRA-GQVKGNGTRHEKDDRRRIRSRy 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1395 ---EEAKKKLAIrlqeaeeaveaahakcssLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIiaewkQKYEET 1471
Cdd:COG4913 603 vlgFDNRAKLAA------------------LEAELAELEEELAEAEERLEALEAELDALQERREALQRL-----AEYSWD 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1472 QAELEASQKESRSLSTELFKLknayEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAA 1551
Cdd:COG4913 660 EIDVASAEREIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1552 LEEAEGALEHEESKTL--------------RIQLELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARN 1617
Cdd:COG4913 736 LEAAEDLARLELRALLeerfaaalgdaverELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLP 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1618 EAIRLRKKMEGD------------LNEMEIQ-LSHANRQAAEAQKMVRQlqsQIKdlqiELDDTMRH---NDDLKEQAAA 1681
Cdd:COG4913 816 EYLALLDRLEEDglpeyeerfkelLNENSIEfVADLLSKLRRAIREIKE---RID----PLNDSLKRipfGPGRYLRLEA 888
|
730 740 750
....*....|....*....|....*....|....*.
gi 1394781870 1682 LERRNnlllAEVEELRAALEQAERGRKLAEQELLEA 1717
Cdd:COG4913 889 RPRPD----PEVREFRQELRAVTSGASLFDEELSEA 920
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
855-1313 |
1.64e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.49 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 855 KEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQD--NLADAEERCDLLIKAKIQLEAKVKELTE 932
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 933 RVEDEEEINSDLTSKKRKLEDECAEL----KKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQ 1008
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1009 EAHQqalddLQAEEDKVNTLTkAKVKLEQQVDDLESSLEQEKKIRM-----------DLERAKRKLEGDLKLTQESVMDL 1077
Cdd:COG4717 241 LEER-----LKEARLLLLIAA-ALLALLGLGGSLLSLILTIAGVLFlvlgllallflLLAREKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1078 ENDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARieeleeeleaeraarakveKQRAEVARELEELSER 1157
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL-------------------EEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1158 LEEAGGATAIQLEMNKKREAEFLKLRRDLEEATLQ-HESTAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEMKMEV 1236
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1237 DDLSSNIEYLTKNKANAEKlcrtyEDQLNEAKSKVDELQR-----QLADVSTQRARLQTESGELSRLLEEKESFINQLTR 1311
Cdd:COG4717 456 AELEAELEQLEEDGELAEL-----LQELEELKAELRELAEewaalKLALELLEEAREEYREERLPPVLERASEYFSRLTD 530
|
..
gi 1394781870 1312 GK 1313
Cdd:COG4717 531 GR 532
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
847-1599 |
1.77e-12 |
|
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: 73.08 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 847 LLRSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKqvtmiqeKNDLALQLQAEQDnlaDAEERCDLLIKAKIQLEAK 926
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGK-------AELLTLRSQLLTL---CTPCMPDTYHERKQVLEKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 927 VKELTERVEDEEEINSDLTSK------KRKLEDECAELKKDIDDLEITLAKVEKEKHATE--NKVKNLIEEMAALDEVIA 998
Cdd:TIGR00618 228 LKHLREALQQTQQSHAYLTQKreaqeeQLKKQQLLKQLRARIEELRAQEAVLEETQERINraRKAAPLAAHIKAVTQIEQ 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 999 KLT------KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQe 1072
Cdd:TIGR00618 308 QAQrihtelQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQ- 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1073 svmDLENDKQQLE---EKLKKKDFEMNQLNSRIEDQQVLEAQL--QKKIKELQARIEELEEELEAERAARAKVEKQRAEV 1147
Cdd:TIGR00618 387 ---QKTTLTQKLQslcKELDILQREQATIDTRTSAFRDLQGQLahAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1148 ARELEELSERLEEAGGATAIQLEMNKKREAEFL----KLRRDLEEATLQHESTAAALRKKHADS---------VAELSEQ 1214
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLlelqEEPCPLCGSCIHPNPARQDIDNPGPLTrrmqrgeqtYAQLETS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1215 IDN----LQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLcRTYEDQLNEAKSKVDELQRQLADVSTQRARLQT 1290
Cdd:TIGR00618 544 EEDvyhqLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL-QNITVRLQDLTEKLSEAEDMLACEQHALLRKLQ 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1291 ESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEetksknalaHALQASRHDCDLLREQYEEEVEAKSELQRSLS 1370
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVR---------EHALSIRVLPKELLASRQLALQKMQSEKEQLT 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1371 KANAEVAQWRTKyetdaiqrTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDlsidlERANSAAAAL 1450
Cdd:TIGR00618 694 YWKEMLAQCQTL--------LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH-----QARTVLKART 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1451 DKKQRNFDRIIAEWK--QKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKR-ENKNLQEEIADLTDQISMS 1527
Cdd:TIGR00618 761 EAHFNNNEEVTAALQtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRLEEK 840
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394781870 1528 GKTIHELEKLKKTLEcEKSEIQAALEEAEGALEHEESKTLRIQLELNQVKADVDRKLAEKDEEFENLRRNHQ 1599
Cdd:TIGR00618 841 SATLGEITHQLLKYE-ECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQ 911
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
918-1148 |
2.17e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 70.95 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 918 KAKIQLEAKVKELTERVEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEmaaldevI 997
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE-------I 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 998 AKLTKEKKALQEAHQQALDDLQaeedKVNTLTKAKVKLEQQ-VDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMD 1076
Cdd:COG4942 93 AELRAELEAQKEELAELLRALY----RLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394781870 1077 LENDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVA 1148
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1252-1912 |
2.62e-12 |
|
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: 72.06 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1252 NAEKLCRTYEDQLNEAkskvDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKtsftqmiEELKRQLEEET 1331
Cdd:pfam05483 72 NSEGLSRLYSKLYKEA----EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFEN-------EKVSLKLEEEI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1332 KSKNALAHALQASRHDCDLLRE--------------QYEEEVEAKSELQRSLSKANAEVAQWRTKYETDAIQRTEELEEA 1397
Cdd:pfam05483 141 QENKDLIKENNATRHLCNLLKEtcarsaektkkyeyEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKED 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1398 KKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRiiaewkqkyeetqaELEA 1477
Cdd:pfam05483 221 HEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDE--------------NLKE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1478 SQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQismSGKTIHELEKLKKTLECEKSEIQAALEEAEG 1557
Cdd:pfam05483 287 LIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEE---KEAQMEELNKAKAAHSFVVTEFEATTCSLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1558 ALEHEESKTLRIQLELNQVKADVDRKLAEKdEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEgdlnemEIQl 1637
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSEL-EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAE------ELK- 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1638 shanrqaAEAQKMVRQLQSQIKDLQielddtmrhndDLKEQAAALERRNNLLLAEVEELRAALEQaergRKLAEQELLEA 1717
Cdd:pfam05483 436 -------GKEQELIFLLQAREKEIH-----------DLEIQLTAIKTSEEHYLKEVEDLKTELEK----EKLKNIELTAH 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1718 TERVNL----LHSQNTGLINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQD-TSAHLERMKK 1792
Cdd:pfam05483 494 CDKLLLenkeLTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDeVKCKLDKSEE 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1793 NMEQTIKDLQMRLDEAEQIALKGG--KKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLA 1870
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKILENKCNnlKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE 653
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1394781870 1871 RMQDLIDK-LQTKVKSYKRQYEEAEqQANSNLVKYRKVQHELD 1912
Cdd:pfam05483 654 EIIDNYQKeIEDKKISEEKLLEEVE-KAKAIADEAVKLQKEID 695
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1223-1814 |
2.77e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1223 QKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEk 1302
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1303 esfinqltrgktsftqmIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYE--EEVEAKSELQRSLSKANAEVAQWR 1380
Cdd:PRK03918 240 -----------------IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1381 TKYEtDAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRI 1460
Cdd:PRK03918 303 EEYL-DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1461 ----IAEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRE-------NKNLQEE-----IADLTDQI 1524
Cdd:PRK03918 382 tgltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcGRELTEEhrkelLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1525 SMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHEESKTLRIQLELNQVKADVDrKLAEKDEEFENLRRNhQRAMDS 1604
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEK-LIKLKG 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1605 MQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAE-AQKMVRQLQSQIKdlqiELDDTMRHNDDLKEQAAALE 1683
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElGFESVEELEERLK----ELEPFYNEYLELKDAEKELE 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1684 RRNNLLLAEVEELRAALEQAERGRKLAEqELLEATERVNLLHSQNT--GLINQKKKMEADIAQLTTEVEEAvqecRNAEE 1761
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLE-ELRKELEELEKKYSEEEyeELREEYLELSRELAGLRAELEEL----EKRRE 690
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1394781870 1762 KAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALK 1814
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALS 743
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1608-1951 |
3.38e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1608 TLDAEAKARNEAIRLRKKME--------GDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQA 1679
Cdd:TIGR02168 204 SLERQAEKAERYKELKAELRelelallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1680 AALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVEEavqecrna 1759
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES-------- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1760 eekakkaitdaamMAEELKKeqdtsahLERMKKNMEQTIKDLQMRLDEAEQiALKGGKKQIQKLEARVRELEGELDTEQK 1839
Cdd:TIGR02168 356 -------------LEAELEE-------LEAELEELESRLEELEEQLETLRS-KVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1840 KTAEAQKGIRKYERRIKELtyQTEEDRKNLARMQDLIDKLQTKVKSYKRQYEEAEQQANSNLVKYRKVQHELDDAEERAD 1919
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
330 340 350
....*....|....*....|....*....|..
gi 1394781870 1920 IAETQVNKLRARSREVVITSKVLKTASLDIGV 1951
Cdd:TIGR02168 493 SLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
849-1406 |
4.31e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.61 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 849 RSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLikakIQLEAKVK 928
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL----ETLEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 929 ELTERVEDEEEINSDLTSKKRKLEDECAELKKDIDDLeitLAKVEKEKHATEnkvknlieemaALDEVIAKLTKEKKALQ 1008
Cdd:PRK02224 262 DLRETIAETEREREELAEEVRDLRERLEELEEERDDL---LAEAGLDDADAE-----------AVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1009 EAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEsslEQEKKIRMDLERAKRKLEGdlklTQESVMDLENDKQQLEEKL 1088
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELR---EEAAELESELEEAREAVED----RREEIEELEEEIEELRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1089 KKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEaeraarakvEKQRAEVARELEELSERLEEAGGATAIQ 1168
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE---------EAEALLEAGKCPECGQPVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1169 lemnkKREAEFLKLRRDLEEATLQHESTAAALRKkhADSVAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTK 1248
Cdd:PRK02224 472 -----EDRERVEELEAELEDLEEEVEEVEERLER--AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1249 NKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRL------LEEKESFINQLTRGKTSFTQMIEE 1322
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIrtllaaIADAEDEIERLREKREALAELNDE 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1323 LKRQLEEETKSKNALAHALQASRHD---CDLLR-EQYEEEV--------EAKSELQRSLSKANAEvaqwrtkyetdaIQR 1390
Cdd:PRK02224 625 RRERLAEKRERKRELEAEFDEARIEearEDKERaEEYLEQVeekldelrEERDDLQAEIGAVENE------------LEE 692
|
570
....*....|....*.
gi 1394781870 1391 TEELEEAKKKLAIRLQ 1406
Cdd:PRK02224 693 LEELRERREALENRVE 708
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
849-1463 |
4.57e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.64 E-value: 4.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 849 RSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKVK 928
Cdd:TIGR02169 372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 929 ELTERVEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDE-------VIAKLT 1001
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLG 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1002 KEKKALQEAHQQAL----------DDLQAEED--------------------KVNTLTKAKVKLEQQVDDLESSLEQEKK 1051
Cdd:TIGR02169 532 SVGERYATAIEVAAgnrlnnvvveDDAVAKEAiellkrrkagratflplnkmRDERRDLSILSEDGVIGFAVDLVEFDPK 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1052 IR-------------MDLERAKR--------KLEGDLkLTQESVMDLENDKQQLEEKLKKKDF-EMNQLNSRIEDQQVLE 1109
Cdd:TIGR02169 612 YEpafkyvfgdtlvvEDIEAARRlmgkyrmvTLEGEL-FEKSGAMTGGSRAPRGGILFSRSEPaELQRLRERLEGLKREL 690
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1110 AQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAggATAIQlEMNKKREAEFLKLRrDLEEA 1189
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL--EEDLS-SLEQEIENVKSELK-ELEAR 766
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1190 TLQHESTAAALRKKHADSVAELS-EQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAK 1268
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1269 SKVDELQRQLADVSTQRARLQTE-----------SGELSRLLEEKESFINQLTRGKtsftQMIEELKRQLEEETKSKNAL 1337
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEEleeleaalrdlESRLGDLKKERDELEAQLRELE----RKIEELEAQIEKKRKRLSEL 922
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1338 AHALQASRHDCDLLREQYEEEVEAKSELqrslskANAEVAQWRTKYETDAIQRTE--------ELEEAKKKLairlqeae 1409
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGEDEEIPEEE------LSLEDVQAELQRVEEEIRALEpvnmlaiqEYEEVLKRL-------- 988
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1394781870 1410 eaveaahakcSSLEKTKHRLQTEIEDL-----SIDLERANSAAAALDKKQRNFDRIIAE 1463
Cdd:TIGR02169 989 ----------DELKEKRAKLEEERKAIlerieEYEKKKREVFMEAFEAINENFNEIFAE 1037
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1085-1708 |
7.04e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.86 E-value: 7.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1085 EEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSerleeaggA 1164
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE--------E 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1165 TAIQLEMNKKREAEFLKLRRDLEEATLQHESTAAALRKKhadsVAELSEQIDNLQRVKQKlEKEKSEMKMEVDDLSSNIE 1244
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE----IEELEEKVKELKELKEK-AEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1245 YLTKNKANAEKLCRTYEDQLNEAKSKVDELQrqladvstqraRLQTESGELSRLLEEKESFINQLTRGKTSFTQMiEELK 1324
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLE-----------ELKKKLKELEKRLEELEERHELYEEAKAKKEEL-ERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1325 RQLEEETKSKnalahalqasrhdcdlLREQYEEEVEAKSELQRSLSKANAEVAQWRTKyETDAIQRTEELEEAKKKLAIr 1404
Cdd:PRK03918 379 KRLTGLTPEK----------------LEKELEELEKAKEEIEEEISKITARIGELKKE-IKELKKAIEELKKAKGKCPV- 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1405 lqeaeeaveaahakCSSLEKTKHRLQ------TEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQ--KYEETQAELE 1476
Cdd:PRK03918 441 --------------CGRELTEEHRKElleeytAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1477 ASQKESRSLSTElfKLKNAYEEsldnLETLKRENKNLQEEIADLTDQIsmsgKTIHELEKLKKTLECEKSEIQAALEEAE 1556
Cdd:PRK03918 507 ELEEKLKKYNLE--ELEKKAEE----YEKLKEKLIKLKGEIKSLKKEL----EKLEELKKKLAELEKKLDELEEELAELL 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1557 GALEHEESKTLR-IQLELNQVKADVDRKLAEKDEEFENLRRnhQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEI 1635
Cdd:PRK03918 577 KELEELGFESVEeLEERLKELEPFYNEYLELKDAEKELERE--EKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394781870 1636 QLS-----HANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNlllaEVEELRAALEQAERGRK 1708
Cdd:PRK03918 655 KYSeeeyeELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK----ELEKLEKALERVEELRE 728
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1466-1685 |
7.91e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.41 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1466 QKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEK 1545
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1546 SEIQAALEEAEGALeHEESKTLRIQLELNQVKA-DVDRKLaekdEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRK 1624
Cdd:COG4942 100 EAQKEELAELLRAL-YRLGRQPPLALLLSPEDFlDAVRRL----QYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394781870 1625 KMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERR 1685
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
912-1661 |
1.38e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 70.00 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 912 RCDLLIKAKIQLEAKVKELTERVEDEEEINSDLTSKKRKLEDECAELKKDI----DDLEITLAKVEKEKHATENKVKNLI 987
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 988 EEMAALDEVIAKLTKEKKALQEAH--QQALDDLQAEEDKVNTLTKAkvkleqqVDDLESSLEQEKKIRMDLERAKRKLEG 1065
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAV-------LEETQERINRARKAAPLAAHIKAVTQI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1066 DLKLtQESVMDLENDKQQLEEKLKKKDFEMNQlNSRIEDQQVLEAQLQKKIKELqaRIEELEEELEAERAARAKVEKQRA 1145
Cdd:TIGR00618 306 EQQA-QRIHTELQSKMRSRAKLLMKRAAHVKQ-QSSIEEQRRLLQTLHSQEIHI--RDAHEVATSIREISCQQHTLTQHI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1146 EVARELEELSERLEEAGGATAIQLEmNKKREAEFLKLRRDLEEATLQHESTAAALRKKHADSVAELSEQIDNLQRVKQKL 1225
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCKELDILQ-REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1226 EKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLAdvstQRARLQTESGELSRLLEEKESF 1305
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN----PARQDIDNPGPLTRRMQRGEQT 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1306 INQL-TRGKTSFTQMIEELKR------QLEEETKSKNALAHALQASRHDCDLLREQYEE---EVEAKSELQRSLSKANAE 1375
Cdd:TIGR00618 537 YAQLeTSEEDVYHQLTSERKQraslkeQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRlqdLTEKLSEAEDMLACEQHA 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1376 vaqwrtkyetdaiqrteelEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEiedLSIDLERANSAAAALDKkqr 1455
Cdd:TIGR00618 617 -------------------LLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT---LTQERVREHALSIRVLP--- 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1456 nfdriiaewKQKYEETQAELEASQKESRSLST---ELFKLKNAYEESLDNLETLKRENKNLQE----EIADLTDQISMSG 1528
Cdd:TIGR00618 672 ---------KELLASRQLALQKMQSEKEQLTYwkeMLAQCQTLLRELETHIEEYDREFNEIENasssLGSDLAAREDALN 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1529 KTIHELEKLKKTLECEKSEIQAALEEAEGALEH---EESKTLRIQLELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSM 1605
Cdd:TIGR00618 743 QSLKELMHQARTVLKARTEAHFNNNEEVTAALQtgaELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQ 822
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1394781870 1606 QATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDL 1661
Cdd:TIGR00618 823 CETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1321-1895 |
1.42e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.07 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1321 EELKRQLEE-ETKSKNALAHALQASRHDCDLLREQYEEEVEAKSElqrSLSKANAEVAQWRTKYEtdaiqRTEELEEAKK 1399
Cdd:PRK02224 190 DQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARE---TRDEADEVLEEHEERRE-----ELETLEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1400 KLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEASQ 1479
Cdd:PRK02224 262 DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1480 KESRSLstelfklknayeesLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGAL 1559
Cdd:PRK02224 342 EEAESL--------------REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1560 EHEESKTLRIQLELNQVKADVDRKLAEKDEEFENLRRNH------------QRAMDSMQATLDAEAKARNEAIRL-RKKM 1626
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgQPVEGSPHVETIEEDRERVEELEAeLEDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1627 EGDLNEMEIQLSHAnRQAAEAQKMVRQLQSQIKDLQIELDDtmrHNDDLKEQAAALERrnnlLLAEVEELRAALEQAERG 1706
Cdd:PRK02224 488 EEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAE---RRETIEEKRERAEE----LRERAAELEAEAEEKREA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1707 RKLAEQELLEATERVNLLHSQNTGLINQKKKMEaDIAQLTTEVEEAVQECRNAEEKAKkaitDAAMMAEELKkeqdtsah 1786
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKRE----ALAELNDERR-------- 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1787 lERMKKNMEQtIKDLQMRLDEAeqiALKGGKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELtyqtEEDR 1866
Cdd:PRK02224 627 -ERLAEKRER-KRELEAEFDEA---RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL----EELR 697
|
570 580
....*....|....*....|....*....
gi 1394781870 1867 KNLARMQDLIDKLQTkvksykrQYEEAEQ 1895
Cdd:PRK02224 698 ERREALENRVEALEA-------LYDEAEE 719
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
849-1400 |
1.70e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 69.75 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 849 RSAQTEKEMATMKEEFQKLKEALEKS----EAKRKELEEKQVTM---IQEKNDLALQLQAE-QDNLADAEERCDLLIKAK 920
Cdd:pfam05483 170 KTKKYEYEREETRQVYMDLNNNIEKMilafEELRVQAENARLEMhfkLKEDHEKIQHLEEEyKKEINDKEKQVSLLLIQI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 921 IQLEAKVKELTERVEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKL 1000
Cdd:pfam05483 250 TEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1001 TKEKKALQEAHQQA--LDDLQAEEDKVNTLTKAKV-KLEQQvdDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDL 1077
Cdd:pfam05483 330 TEEKEAQMEELNKAkaAHSFVVTEFEATTCSLEELlRTEQQ--RLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1078 ENDKQQLEEKLKKKDfEMNQLNSRIED----QQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEE 1153
Cdd:pfam05483 408 EELKKILAEDEKLLD-EKKQFEKIAEElkgkEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLK 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1154 LSERLEEAGGATAIQLEMNKKREAEFLKLRRDLEEATLQHESTAAALrkKHADSVAELSEQI-DNLQRVKQKLEKEKSEM 1232
Cdd:pfam05483 487 NIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERML--KQIENLEEKEMNLrDELESVREEFIQKGDEV 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1233 KMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFIN----Q 1308
Cdd:pfam05483 565 KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNklelE 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1309 LTRGKTSFTQMIEELKRQLEEETKSKNALAHALQASRHDCDllrEQYEEEVEAKSELQRSLSKANAEVAQWRTKYETDAI 1388
Cdd:pfam05483 645 LASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIAD---EAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIE 721
|
570
....*....|..
gi 1394781870 1389 QRTEELEEAKKK 1400
Cdd:pfam05483 722 ERDSELGLYKNK 733
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
855-1546 |
1.91e-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: 69.28 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 855 KEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEkndlalqLQAEQDNLADAEERCDLLIKAKIQLEAKVKELTERV 934
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE-------IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 935 EDEEEINSDLTSKKRKLEDECAELKKDIDD---LEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAH 1011
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKnksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1012 QQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKkirmdleraKRKLEGDLKLTQESVMDLENDKQQLEEKLKKK 1091
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN---------NQKEQDWNKELKSELKNQEKKLEEIQNQISQN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1092 DFEMNQLNSRIEdqqvleaQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEvareleelserleeaggataiqlem 1171
Cdd:TIGR04523 334 NKIISQLNEQIS-------QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS------------------------- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1172 nKKREAEFLKLRRDLEEATLQHESTAAalrkkhadsvAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKA 1251
Cdd:TIGR04523 382 -YKQEIKNLESQINDLESKIQNQEKLN----------QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1252 NAEKlcrtyedQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEET 1331
Cdd:TIGR04523 451 VKEL-------IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLK 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1332 KSKNALahalqasrhdcdllrEQYEEEVEAK-SELQRSLSKANAEVAQWRTKYETDAIQRT-EELEEAKKklairlqeae 1409
Cdd:TIGR04523 524 EKIEKL---------------ESEKKEKESKiSDLEDELNKDDFELKKENLEKEIDEKNKEiEELKQTQK---------- 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1410 eaveaahakcsSLEKTKHRLQTEIEDLSidleransaaaaldKKQRNFDRIIAEWKQKYEETQAELEASQKESRSLSTEL 1489
Cdd:TIGR04523 579 -----------SLKKKQEEKQELIDQKE--------------KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1394781870 1490 FKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKS 1546
Cdd:TIGR04523 634 KNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELS 690
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1299-1931 |
1.97e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.56 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1299 LEEKESFiNQLTRGKTSFTQmIEELKRQLEEETKSKNALAHALQasrhdcdlLREQYEEEVEAKSELQRSLSKANAEVAQ 1378
Cdd:COG4913 218 LEEPDTF-EAADALVEHFDD-LERAHEALEDAREQIELLEPIRE--------LAERYAAARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1379 wrTKYETdAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTE-IEDLSIDLERANSAAAALDKKQRNF 1457
Cdd:COG4913 288 --RRLEL-LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1458 DRIIAEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKREnknLQEEIADLTDQISmsgktihELEKL 1537
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIA-------SLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1538 KKTLEcekSEIQAALEEAEGALEHEESKtLRIQLELNQVKADvdrklaekDEEFEN-----LrrnHQRAMdsmqaTL--- 1609
Cdd:COG4913 435 KSNIP---ARLLALRDALAEALGLDEAE-LPFVGELIEVRPE--------EERWRGaiervL---GGFAL-----TLlvp 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1610 -DAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTmrhnddlkeqaaaLERRNNL 1688
Cdd:COG4913 495 pEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAE-------------LGRRFDY 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1689 LLAE-VEELRA---ALEQA-------ERGRKLAEQELleatERVNLLHSQNTGLINQKkkmEADIAQLTTEVEEA---VQ 1754
Cdd:COG4913 562 VCVDsPEELRRhprAITRAgqvkgngTRHEKDDRRRI----RSRYVLGFDNRAKLAAL---EAELAELEEELAEAeerLE 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1755 ECRNAEEKAKKAITDAAMMAEELKKEQDTSAHlermkknmEQTIKDLQMRLDEAEQialkgGKKQIQKLEARVRELEGEL 1834
Cdd:COG4913 635 ALEAELDALQERREALQRLAEYSWDEIDVASA--------EREIAELEAELERLDA-----SSDDLAALEEQLEELEAEL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1835 DTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTkvKSYKRQYEEAEQQANSNLVKyRKVQHELDDA 1914
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--ALLEERFAAALGDAVERELR-ENLEERIDAL 778
|
650
....*....|....*..
gi 1394781870 1915 EERADIAETQVNKLRAR 1931
Cdd:COG4913 779 RARLNRAEEELERAMRA 795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1213-1891 |
3.40e-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: 68.51 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1213 EQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTES 1292
Cdd:TIGR04523 68 EKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1293 GELSRLLEEKESFINQLTRgktsftqMIEELKRQLEEETKSKNALAHALQASRHDcdLLREQYEEEV-EAKSELQRSLSK 1371
Cdd:TIGR04523 148 KKKEKELEKLNNKYNDLKK-------QKEELENELNLLEKEKLNIQKNIDKIKNK--LLKLELLLSNlKKKIQKNKSLES 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1372 ANAEVAQWRTKYETDAIQRTEELEEAKKKLairlqeaeeaveaahakcsslektkHRLQTEIEDLSIDLERANSAaaaLD 1451
Cdd:TIGR04523 219 QISELKKQNNQLKDNIEKKQQEINEKTTEI-------------------------SNTQTQLNQLKDEQNKIKKQ---LS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1452 KKQrnfdriiaewkQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNleTLKRENKNLQEEIADLTDQISMSGKTI 1531
Cdd:TIGR04523 271 EKQ-----------KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQNQISQNNKII 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1532 HELEKLKKTLECEKSeiqaaleeaegaleHEESKTLRIQLELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLDA 1611
Cdd:TIGR04523 338 SQLNEQISQLKKELT--------------NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1612 EAKARNEAIRLRKKmEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERrnnllla 1691
Cdd:TIGR04523 404 EKLNQQKDEQIKKL-QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR------- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1692 EVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKaitdaa 1771
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK------ 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1772 mMAEELKKEQdtsahLERMKKNMEQTIKDLqmrldeaeqialkggKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKY 1851
Cdd:TIGR04523 550 -DDFELKKEN-----LEKEIDEKNKEIEEL---------------KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEK 608
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1394781870 1852 ERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQYE 1891
Cdd:TIGR04523 609 EKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
848-1458 |
5.30e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 68.28 E-value: 5.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 848 LRSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADaEERCDLLIKAKI-QLEAK 926
Cdd:pfam01576 419 ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLrQLEDE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 927 VKELTERVEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKA 1006
Cdd:pfam01576 498 RNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1007 LQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDD--LESSLEQEKKIRMDLErAKRKLEGDLKLTQEsVMDLENDKQQL 1084
Cdd:pfam01576 578 LQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEekAISARYAEERDRAEAE-AREKETRALSLARA-LEEALEAKEEL 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1085 EEKLKKKDFEMNQLNSRIED--QQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAG 1162
Cdd:pfam01576 656 ERTNKQLRAEMEDLVSSKDDvgKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQA 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1163 gataiQLEMNKKREAEFLKLRRDLE---EATLQHESTAAALRKKHADSVAELSEQIDNLQR-----VKQ--KLEKEKSEM 1232
Cdd:pfam01576 736 -----RDEQGEEKRRQLVKQVRELEaelEDERKQRAQAVAAKKKLELDLKELEAQIDAANKgreeaVKQlkKLQAQMKDL 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1233 KMEVDDL-SSNIEYLTKNKANAEKL-------------CRTYEDQLNEAKSKVDELQRQLADVSTQRA-------RLQTE 1291
Cdd:pfam01576 811 QRELEEArASRDEILAQSKESEKKLknleaellqlqedLAASERARRQAQQERDELADEIASGASGKSalqdekrRLEAR 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1292 SGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKSKNALAHAL-QASRHDCDLLREQYEEEVEAKSELQRSLS 1370
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARqQLERQNKELKAKLQEMEGTVKSKFKSSIA 970
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1371 KANAEVAQWRTKYETDAIQR---TEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAA 1447
Cdd:pfam01576 971 ALEAKIAQLEEQLEQESRERqaaNKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRAN 1050
|
650
....*....|.
gi 1394781870 1448 AALDKKQRNFD 1458
Cdd:pfam01576 1051 AARRKLQRELD 1061
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1441-1919 |
5.43e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.14 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1441 ERANSAAAA----LDKKQRNFDRIIAEWKQKYE----ETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENKN 1512
Cdd:PRK02224 169 ERASDARLGvervLSDQRGSLDQLKAQIEEKEEkdlhERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1513 LQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHeesktLRIQLELNQVKAD-VDRKLAEKDEEF 1591
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDD-----LLAEAGLDDADAEaVEARREELEDRD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1592 ENLRRnhqramDSMQATLDAEAkARNEAIRLRKKMEgDLNEmeiqlshanrQAAEaqkmvrqLQSQIKDLQIELDDTMRH 1671
Cdd:PRK02224 324 EELRD------RLEECRVAAQA-HNEEAESLREDAD-DLEE----------RAEE-------LREEAAELESELEEAREA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1672 NDDLKEQAAALErrnnlllAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLinqkkkmEADIaqltTEVEE 1751
Cdd:PRK02224 379 VEDRREEIEELE-------EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL-------EATL----RTARE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1752 AVQECRNAEEKAK-----KAITDAAMmAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIAlkggkkqiqKLEAR 1826
Cdd:PRK02224 441 RVEEAEALLEAGKcpecgQPVEGSPH-VETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV---------EAEDR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1827 VRELEGELDTEQKKTAEAQKGIrkyerrikeltyqtEEDRKNLARMQDLIDKLQTKVKSYKRQYEEAEQQANSNLVKYRK 1906
Cdd:PRK02224 511 IERLEERREDLEELIAERRETI--------------EEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
490
....*....|...
gi 1394781870 1907 VQHELDDAEERAD 1919
Cdd:PRK02224 577 LNSKLAELKERIE 589
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
911-1542 |
5.53e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 911 ERCDLLIKAKIQLEAKVKELTERVEDEEEINSDLTSKKRKLEDECAELKKDIDDLEIT---LAKVEKEKHATENKVKNLI 987
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 988 EEMAALDEVIAKLTKEKKALQEAHQQaLDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEqekkirmdlerakrKLEGDL 1067
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKE-LKELKEKAEEYIKLSEFYEEYLDELREIEKRLS--------------RLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1068 KLTQESVMDLENDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEV 1147
Cdd:PRK03918 324 NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1148 ARELEELSERLEEAggataiqlemnKKREAEFLKLRRDLEEATLQHESTAAALRKKH-ADSVAELSEQIDNLQRVKQKLE 1226
Cdd:PRK03918 404 EEEISKITARIGEL-----------KKEIKELKKAIEELKKAKGKCPVCGRELTEEHrKELLEEYTAELKRIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1227 KEKSEMK---MEVDDLSSNIEYLTKNKANAEKLcRTYEDQLNeaKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKE 1303
Cdd:PRK03918 473 EKERKLRkelRELEKVLKKESELIKLKELAEQL-KELEEKLK--KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1304 SfINQLTRGKTSFTQMIEELKRQLEEetksknalahalqasrhdcdLLREQYEEEVEAKSELQRslskanaevaqwrtky 1383
Cdd:PRK03918 550 K-LEELKKKLAELEKKLDELEEELAE--------------------LLKELEELGFESVEELEE---------------- 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1384 etdaiqRTEELEEAKKKLaIRLQEAEEAVEaahakcsSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKqrnfdriIAE 1463
Cdd:PRK03918 593 ------RLKELEPFYNEY-LELKDAEKELE-------REEKELKKLEEELDKAFEELAETEKRLEELRKE-------LEE 651
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394781870 1464 WKQKYEETqaELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTdqismsgKTIHELEKLKKTLE 1542
Cdd:PRK03918 652 LEKKYSEE--EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE-------KAKKELEKLEKALE 721
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
854-1675 |
6.23e-11 |
|
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: 68.15 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 854 EKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLadaeERCDLLIKAkIQLEAKVKELTER 933
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHI----RARDSLIQS-LATRLELDGFERG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 934 VEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQ 1013
Cdd:TIGR00606 386 PFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQ 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1014 ALDDLQAEEDKVNTLTKAKVKLE--QQVDDLESSLEQEKKI---RMDLERAKRKLEGDL------KLTQESVMDLENDKQ 1082
Cdd:TIGR00606 466 LEGSSDRILELDQELRKAERELSkaEKNSLTETLKKEVKSLqneKADLDRKLRKLDQEMeqlnhhTTTRTQMEMLTKDKM 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1083 QLEEKLKKKDF----EMNQLNSRIEDQQVLEAQLQKK---IKELQARIEELEEELEAERAARAKVEKQRAEVARELEELS 1155
Cdd:TIGR00606 546 DKDEQIRKIKSrhsdELTSLLGYFPNKKQLEDWLHSKskeINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYE 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1156 ERLEEAGGATAIqlemnkkrEAEFLKLRRDLEEATLQHESTAAAlRKKHADSVAELSEQIDNLQRVKQKLEKEKSEMKME 1235
Cdd:TIGR00606 626 DKLFDVCGSQDE--------ESDLERLKEEIEKSSKQRAMLAGA-TAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEF 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1236 VDDLSSNIEYLTKNKANAEKLCRTYEDQLNE----AKSKVDELQRQLADVSTQRARLQTESGELSRL---LEEKESFIN- 1307
Cdd:TIGR00606 697 ISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLkndIEEQETLLGt 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1308 ---QLTRGKTSFTQ--MIEELKRQLEEETKSKNALAHALQASrhDCDLLREQYEEEVEAKSELQRSLSKA---NAEVAQW 1379
Cdd:TIGR00606 777 impEEESAKVCLTDvtIMERFQMELKDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKielNRKLIQD 854
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1380 RTKYETDAIQRTEELEEAKKKLAIRLQeaeeaveaahaKCSSLEKTKHRLQTEIEDLSIDLeransaaaaldKKQRNFDR 1459
Cdd:TIGR00606 855 QQEQIQHLKSKTNELKSEKLQIGTNLQ-----------RRQQFEEQLVELSTEVQSLIREI-----------KDAKEQDS 912
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1460 IIAEWKQKYEETQAELEASQKESRSLSTelfklknayeeslDNLETLKRENKNLQEEIADLTDQISmSGKtihelEKLKK 1539
Cdd:TIGR00606 913 PLETFLEKDQQEKEELISSKETSNKKAQ-------------DKVNDIKEKVKNIHGYMKDIENKIQ-DGK-----DDYLK 973
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1540 TLECEKSEIQAALEEAEGALE--HEESKTLRIQLELNQVKADV------DRKLAEKDEEFENLRRNHQRAMDSMQAT-LD 1610
Cdd:TIGR00606 974 QKETELNTVNAQLEECEKHQEkiNEDMRLMRQDIDTQKIQERWlqdnltLRKRENELKEVEEELKQHLKEMGQMQVLqMK 1053
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394781870 1611 AEAKARNEAIRLRKKME----GDLNEMEIQLSHANRQAAEAQkmVRQLQSQIKDLQIELDDTMRHNDDL 1675
Cdd:TIGR00606 1054 QEHQKLEENIDLIKRNHvlalGRQKGYEKEIKHFKKELREPQ--FRDAEEKYREMMIVMRTTELVNKDL 1120
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1321-1716 |
6.70e-11 |
|
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: 67.23 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1321 EELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEA----KSELQRSLSKANAEVAQWRtkyetdaiQRTEELEE 1396
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQwerqRRELESRVAELKEELRQSR--------EKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1397 AKKKLAIRLQEAEEAVEAAHAKcssLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEE---TQA 1473
Cdd:pfam07888 102 KYKELSASSEELSEEKDALLAQ---RAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAErkqLQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1474 ELEASQKESRSLSTELFKLKNAYEESLDNLETlkrenknLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALE 1553
Cdd:pfam07888 179 KLQQTEEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASER 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1554 EAEGALEheesktlriqlELNQVKADVDRKLAEKdeefenlrrnHQRAMDSMQATL---DAEAKARNEAIRLRKKMEGDL 1630
Cdd:pfam07888 252 KVEGLGE-----------ELSSMAAQRDRTQAEL----------HQARLQAAQLTLqlaDASLALREGRARWAQERETLQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1631 NEMEIQLSHANRQAAEAQKMVRQLQ---SQIKDLQIELDdtmRHNDDLKEQAAALERrnnlllaEVEELRAALE--QAER 1705
Cdd:pfam07888 311 QSAEADKDRIEKLSAELQRLEERLQeerMEREKLEVELG---REKDCNRVQLSESRR-------ELQELKASLRvaQKEK 380
|
410
....*....|..
gi 1394781870 1706 GRKLAE-QELLE 1716
Cdd:pfam07888 381 EQLQAEkQELLE 392
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1429-1835 |
9.13e-11 |
|
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: 66.64 E-value: 9.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1429 LQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEEtqaeLEASQKESRSLSTELFKLKNA------------- 1495
Cdd:pfam05622 64 LQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEE----LTSLAEEAQALKDEMDILRESsdkvkkleatvet 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1496 YEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQaaleEAEGALEHEESKTLRIQLELNQ 1575
Cdd:pfam05622 140 YKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1576 VKADVDRKLAEKD----------EEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAA 1645
Cdd:pfam05622 216 LEEKLEALQKEKErliierdtlrETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1646 EAQKmvRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAErgrklaeqelleatervnllh 1725
Cdd:pfam05622 296 LGQE--GSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQG--------------------- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1726 SQNTGLINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQT--- 1797
Cdd:pfam05622 353 SKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKAksv 432
|
410 420 430
....*....|....*....|....*....|....*...
gi 1394781870 1798 IKDLQMRLDEAEQIALKGGKKQIQKLEARVRELEGELD 1835
Cdd:pfam05622 433 IKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFE 470
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1262-1715 |
1.16e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1262 DQLNEAKSKVDELQRQLADVSTQRARLQtesgELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEEtksknalahAL 1341
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEKLLQLLPLYQELE---------AL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1342 QASRHDCDLLREQYEEEVEAKSELQRSLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSS 1421
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1422 LEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDR-----IIAEWKQKYEETQAELEASQKESRSLS---TELFKLK 1493
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARLLLLIAaallaLLGLGGSLLSLILTIAGVLFLVLGLLAllfLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1494 NAYEESLDNLETLKRENKNLQEEIADLTDQISMSGK-TIHELEKLKKTLEcEKSEIQAALEEAEGALEHEESKTLRIQLe 1572
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDlSPEELLELLDRIE-ELQELLREAEELEEELQLEELEQEIAAL- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1573 LNQVKADVDRKLAEKDEEFENlRRNHQRAMDSMQATLDAEAKARNEAIRlrkkmEGDLNEMEIQLSHANRQAAEAQKMVR 1652
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLE-----ALDEEELEEELEELEEELEELEEELE 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394781870 1653 QLQSQIKDLQIELDDTMRHN--DDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELL 1715
Cdd:COG4717 450 ELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
872-1553 |
1.20e-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: 67.17 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 872 EKSEAKRKE----LEEKQ-VTMIQEKNDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKVKELTERVEdeeEINSDLTS 946
Cdd:pfam12128 214 PKSRLNRQQvehwIRDIQaIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQ---ETSAELNQ 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 947 KKRKLEDECAELKkdiddleitlAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQALDDLQAE----E 1022
Cdd:pfam12128 291 LLRTLDDQWKEKR----------DELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSElenlE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1023 DKVNTLTKAKVKLEQQVDDLESSLEQEKKI---RMDLERAKRKLEGDLKLTQEsvmdlENDKQQLEEKLKKkdfEMNQLN 1099
Cdd:pfam12128 361 ERLKALTGKHQDVTAKYNRRRSKIKEQNNRdiaGIKDKLAKIREARDRQLAVA-----EDDLQALESELRE---QLEAGK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1100 SRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVAR---ELEELSERLEEAGGATAIQLEMNKKRE 1176
Cdd:pfam12128 433 LEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAanaEVERLQSELRQARKRRDQASEALRQAS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1177 AEFLKLRRDLEEATLQHESTA----AALRKKHAD----------------------SVAELSEQIDNLQRVKQKLEK-EK 1229
Cdd:pfam12128 513 RRLEERQSALDELELQLFPQAgtllHFLRKEAPDweqsigkvispellhrtdldpeVWDGSVGGELNLYGVKLDLKRiDV 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1230 SEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVstqRARLQTESGELSRLLEEKESFINQL 1309
Cdd:pfam12128 593 PEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFA---RTALKNARLDLRRLFDEKQSEKDKK 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1310 TRGKTSFTQMIEELKRQLEEEtksKNALAHALQA-SRHDCDLLREQYEEEVEAKSELQRSLSKANAEVAQWRTKYETDAI 1388
Cdd:pfam12128 670 NKALAERKDSANERLNSLEAQ---LKQLDKKHQAwLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAK 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1389 QRTEELEEAKKKlairlqeaeeaveaAHAKCSSLEKTKHRLQTEIEDLSIDLERA---NSAAAALDKKQR--------NF 1457
Cdd:pfam12128 747 AELKALETWYKR--------------DLASLGVDPDVIAKLKREIRTLERKIERIavrRQEVLRYFDWYQetwlqrrpRL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1458 DRIIAEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADL-----TDQISMS-GKTI 1531
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLkedanSEQAQGSiGERL 892
|
730 740
....*....|....*....|..
gi 1394781870 1532 HELEKLKKTLECEKSEIQAALE 1553
Cdd:pfam12128 893 AQLEDLKLKRDYLSESVKKYVE 914
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1218-1714 |
2.01e-10 |
|
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: 65.92 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1218 LQRVKQKLEKEKSEMK-MEVDDLSSNIEYLTKNKANAEKLCRTyEDQLNEAKSKVDELQRQLADVST------QRARLQT 1290
Cdd:pfam05557 4 LIESKARLSQLQNEKKqMELEHKRARIELEKKASALKRQLDRE-SDRNQELQKRIRLLEKREAEAEEalreqaELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1291 ESGE-LSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKSELQRSL 1369
Cdd:pfam05557 83 KYLEaLNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1370 SKANAEVAQWRT------KYETDAiqrtEELEEAKKKLA--IRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLE 1441
Cdd:pfam05557 163 SSLAEAEQRIKElefeiqSQEQDS----EIVKNSKSELAriPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1442 RansaaaaldkkqrnfdriiaewkqkYEETQAELEASQKESRSLSTELFKLKNAYEESLDNL---ETLKRENKNLQEEIA 1518
Cdd:pfam05557 239 R-------------------------EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLrspEDLSRRIEQLQQREI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1519 DLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHEESKTLRIQlelnqvkadvdRKLAEKDEEFENLRRNH 1598
Cdd:pfam05557 294 VLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ-----------RRVLLLTKERDGYRAIL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1599 QRAMDSMQATLDAEAKARN--EAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKdlqielddTMRHNDDLK 1676
Cdd:pfam05557 363 ESYDKELTMSNYSPQLLERieEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQ--------ALRQQESLA 434
|
490 500 510
....*....|....*....|....*....|....*...
gi 1394781870 1677 EQAAALERRNNLLLaEVEELRAALEQAERGRKLAEQEL 1714
Cdd:pfam05557 435 DPSYSKEEVDSLRR-KLETLELERQRLREQKNELEMEL 471
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
849-1281 |
4.60e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 849 RSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKVK 928
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 929 ELTERVEDEEEINSdltskkrklEDECAELKKDIDDLEITLAKVEKEkhatenkvknliEEMAALDEVIAKLTKEKKALQ 1008
Cdd:PRK02224 437 TARERVEEAEALLE---------AGKCPECGQPVEGSPHVETIEEDR------------ERVEELEAELEDLEEEVEEVE 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1009 EAHQQAlDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKL 1088
Cdd:PRK02224 496 ERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1089 KKKDFEMNQLNSRIEDQQVLEAQLQkKIKELQARIeeleeeleaeraarAKVEKQRAEVAreleelserleeaggataiq 1168
Cdd:PRK02224 575 AELNSKLAELKERIESLERIRTLLA-AIADAEDEI--------------ERLREKREALA-------------------- 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1169 lEMNKKREaEFLKLRRD-------------LEEATLQHESTAAALRKKhADSVAELSEQIDNLQR----VKQKLEkEKSE 1231
Cdd:PRK02224 620 -ELNDERR-ERLAEKRErkreleaefdearIEEAREDKERAEEYLEQV-EEKLDELREERDDLQAeigaVENELE-ELEE 695
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1394781870 1232 MKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSK-VDELQRQLADV 1281
Cdd:PRK02224 696 LRERREALENRVEALEALYDEAEELESMYGDLRAELRQRnVETLERMLNET 746
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
895-1362 |
5.43e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 895 LALQLQAEQDNLADAEERCDLLIKAKIQ-LEAKVKELTERVEDEEEinsdLTSKKRKLEDECAELKKDIDDLEITLAKVE 973
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKeLEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 974 KEKhatenKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDL----ESSLEQE 1049
Cdd:COG4717 123 KLL-----QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1050 KKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLkkkdfEMNQLNSRIEDQQVL--------------------- 1108
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARLLlliaaallallglggsllsli 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1109 -----------------EAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGATAIQLEM 1171
Cdd:COG4717 273 ltiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1172 NKKREAEFLKLRRDLEEATLQhestaAALRKKHADSVAELSEQIDNLQRvKQKLEKEKSEMKMEVDDLSSNIEYL--TKN 1249
Cdd:COG4717 353 LREAEELEEELQLEELEQEIA-----ALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELleALD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1250 KANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQtESGELSRLLEEkesfinqltrgktsftqmIEELKRQLEE 1329
Cdd:COG4717 427 EEELEEELEELEEELEELEEELEELREELAELEAELEQLE-EDGELAELLQE------------------LEELKAELRE 487
|
490 500 510
....*....|....*....|....*....|...
gi 1394781870 1330 ETKSKNALAHALQASRHDCDLLREQYEEEVEAK 1362
Cdd:COG4717 488 LAEEWAALKLALELLEEAREEYREERLPPVLER 520
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1205-1406 |
1.23e-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: 62.47 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1205 ADSVAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQ 1284
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1285 RARLQTESGELSR------------LLEEKESFiNQLTRGKTSFTQMIEELKRQLEEETKSKNALAHALQASRHDCDLLR 1352
Cdd:COG4942 99 LEAQKEELAELLRalyrlgrqpplaLLLSPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1394781870 1353 EQYEEEVEAKSELQRSLSKANAEVAQWRTKYETDAiQRTEELEEAKKKLAIRLQ 1406
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIA 230
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1623-1844 |
1.27e-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: 62.47 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1623 RKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAALE- 1701
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1702 -QAERGRKLAEQELLEATERVNLLHSQN--TGLINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEELK 1778
Cdd:COG4942 102 qKEELAELLRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394781870 1779 KEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQiALKGGKKQIQKLEARVRELEGELDTEQKKTAEA 1844
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAA-ELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1545-1934 |
2.32e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1545 KSEIQAALEEAEGALEHEESKTLRIQL-ELNQVKADVDRKLaekdEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLr 1623
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLnGLESELAELDEEI----ERYEEQREQARETRDEADEVLEEHEERREELETL- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1624 kkmEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAALEQA 1703
Cdd:PRK02224 257 ---EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1704 ERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVE---EAVQECRNAEEKAKKAITDAAmmaEELKKE 1780
Cdd:PRK02224 334 RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEdrrEEIEELEEEIEELRERFGDAP---VDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1781 QDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGgkkqiQKLEARVRELEGELDTEQKKTAEAqkgIRKYERRIKELTY 1860
Cdd:PRK02224 411 EDFLEELREERDELREREAELEATLRTARERVEEA-----EALLEAGKCPECGQPVEGSPHVET---IEEDRERVEELEA 482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394781870 1861 QTEEDRKNLARMQDLIDKLQTKVksykrqyeEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRARSRE 1934
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAEDLV--------EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
852-1542 |
2.43e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 852 QTEKEMATMKEEFQKLKEA---LEKSEAKRK---ELEEKQVTMIQEKNDLA-LQLQAEQDNLADAEERCDLLIKAKIQLE 924
Cdd:COG4913 222 DTFEAADALVEHFDDLERAheaLEDAREQIEllePIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 925 AKVKELTERVEDEEEINSDLTSKKRKLEDECAELK-KDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKE 1003
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1004 KKALQEAHQQALDDLQAEEDKVNT----LTKAKVKLEQQVDDLES---SLEQEKK-IRMDLERAKRKLEGDLKLTQESV- 1074
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAeiaSLERRKSnIPARLLALRDALAEALGLDEAELp 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1075 -----MDLENDKQQLE---EKLkkkdfemnqLNSR-----IEDQQvlEAQLQKKIKELQARieeleeeleaeraarAKVE 1141
Cdd:COG4913 462 fvgelIEVRPEEERWRgaiERV---------LGGFaltllVPPEH--YAAALRWVNRLHLR---------------GRLV 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1142 KQRaeVARELEELSERLEEAGG-ATAIQLEMNKKRE--AEFLKLRRDLE----EATLQHES---TAAALRKK------HA 1205
Cdd:COG4913 516 YER--VRTGLPDPERPRLDPDSlAGKLDFKPHPFRAwlEAELGRRFDYVcvdsPEELRRHPraiTRAGQVKGngtrheKD 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1206 DSVAELSEQI---DNLQRVKQkLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYE--DQLNEAKSKVDELQRQLAD 1280
Cdd:COG4913 594 DRRRIRSRYVlgfDNRAKLAA-LEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAE 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1281 VSTQRARLQTESGELsrlleekesfinqltrgktsftqmiEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVE 1360
Cdd:COG4913 673 LEAELERLDASSDDL-------------------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1361 AKSELQRSLSKANAEVAQWrtkyetdaiqRTEELEEAKKKLAIRlqeaeeaveaahakcSSLEKTKHRLQTEIEDLSIDL 1440
Cdd:COG4913 728 ELDELQDRLEAAEDLARLE----------LRALLEERFAAALGD---------------AVERELRENLEERIDALRARL 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1441 ERANSAAAaldkkqrnfdRIIAEWKQKYEETQAELEASQKESRSLSTELFKLKN----AYEESLdnletLKRENKNLQEE 1516
Cdd:COG4913 783 NRAEEELE----------RAMRAFNREWPAETADLDADLESLPEYLALLDRLEEdglpEYEERF-----KELLNENSIEF 847
|
730 740
....*....|....*....|....*..
gi 1394781870 1517 IADLTDQISMSGKTIHE-LEKLKKTLE 1542
Cdd:COG4913 848 VADLLSKLRRAIREIKErIDPLNDSLK 874
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1178-1858 |
2.97e-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: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1178 EFLKLRRDLEeatlQHESTAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKlc 1257
Cdd:pfam12128 242 EFTKLQQEFN----TLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADA-- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1258 rtyedQLNEAKSKVDELQRQLAdvSTQRARLQTESGELSRL------LEEKESFINQLTRGKTSFTQMIEELKRQLEEET 1331
Cdd:pfam12128 316 -----AVAKDRSELEALEDQHG--AFLDADIETAAADQEQLpswqseLENLEERLKALTGKHQDVTAKYNRRRSKIKEQN 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1332 KSKNA-LAHALQASRHDCDLLREQYEEEVEA-KSELQRSLSKANAEVAQwrtkyetdaiqRTEELEEAKKKLAIRLQEAE 1409
Cdd:pfam12128 389 NRDIAgIKDKLAKIREARDRQLAVAEDDLQAlESELREQLEAGKLEFNE-----------EEYRLKSRLGELKLRLNQAT 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1410 EAVEAAHAKCSSLEKTkHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEASQK----ESRSL 1485
Cdd:pfam12128 458 ATPELLLQLENFDERI-ERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELqlfpQAGTL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1486 STELFKLKNAYEESLDNL---ETLKRENKNLQEEIADLTDQISMSGKTIHeLEKLK-KTLECEKSEIQAALEEAEGALEH 1561
Cdd:pfam12128 537 LHFLRKEAPDWEQSIGKVispELLHRTDLDPEVWDGSVGGELNLYGVKLD-LKRIDvPEWAASEEELRERLDKAEEALQS 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1562 EESKTLRIQLELNQVKADVD---RKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLrkkmegdlnemeiqls 1638
Cdd:pfam12128 616 AREKQAAAEEQLVQANGELEkasREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDS---------------- 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1639 hanrqaaeAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAAleRRNNLLLAEVEELRAALEQAERGrKLAEQELLEAt 1718
Cdd:pfam12128 680 --------ANERLNSLEAQLKQLDKKHQAWLEEQKEQKREART--EKQAYWQVVEGALDAQLALLKAA-IAARRSGAKA- 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1719 eRVNLLHSQNTGLINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDtsaHLERMKKNMEQTI 1798
Cdd:pfam12128 748 -ELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRP---RLATQLSNIERAI 823
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1799 KDLQMRLdeaeqialkggKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKEL 1858
Cdd:pfam12128 824 SELQQQL-----------ARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL 872
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1180-1931 |
3.00e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.67 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1180 LKLRRDLEEAtlqhESTAAALRKKHADSVAELSEQIDNLQRVKQKLE---------------KEKSEM-KMEVDDLSSNI 1243
Cdd:PRK04863 289 LELRRELYTS----RRQLAAEQYRLVEMARELAELNEAESDLEQDYQaasdhlnlvqtalrqQEKIERyQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1244 EYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELS---RLLEEKESFINQLTRGKTSFTQMI 1320
Cdd:PRK04863 365 EEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQqavQALERAKQLCGLPDLTADNAEDWL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1321 EELKRQLEEETKSKNALAHALQASrhdcDLLREQYEE----------EVEAKS------ELQRSLSKANAEVAQ---WRT 1381
Cdd:PRK04863 445 EEFQAKEQEATEELLSLEQKLSVA----QAAHSQFEQayqlvrkiagEVSRSEawdvarELLRRLREQRHLAEQlqqLRM 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1382 KYeTDAIQRTEE-------LEEAKKKLAIRLQEAEEaveaahakcssLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQ 1454
Cdd:PRK04863 521 RL-SELEQRLRQqqraerlLAEFCKRLGKNLDDEDE-----------LEQLQEELEARLESLSESVSEARERRMALRQQL 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1455 RNFDRIIAEWKQK--------------YEETQAELEASQKESRSLSTELFKLKNAYEESlDNLETLKREnknLQEEI--- 1517
Cdd:PRK04863 589 EQLQARIQRLAARapawlaaqdalarlREQSGEEFEDSQDVTEYMQQLLERERELTVER-DELAARKQA---LDEEIerl 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1518 -----------------------ADLTDQIS--------------MSGKTIHELEKLKKTLECE----------KSEIQA 1550
Cdd:PRK04863 665 sqpggsedprlnalaerfggvllSEIYDDVSledapyfsalygpaRHAIVVPDLSDAAEQLAGLedcpedlyliEGDPDS 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1551 ------ALEEAEGALEHEESK-TLRI----------------QLELNQVKAD-VDRKLAEKDEEFENLRRNHQRAMDSMq 1606
Cdd:PRK04863 745 fddsvfSVEELEKAVVVKIADrQWRYsrfpevplfgraarekRIEQLRAEREeLAERYATLSFDVQKLQRLHQAFSRFI- 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1607 atldaeakARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDdlkeQAAALERrn 1686
Cdd:PRK04863 824 --------GSHLAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLP----RLNLLAD-- 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1687 NLLLAEVEELRAALEQAERgrklAEQELleatervnllhSQNTGLINQKKKM-------EADIAQLTTEVEEAVQECRNA 1759
Cdd:PRK04863 890 ETLADRVEEIREQLDEAEE----AKRFV-----------QQHGNALAQLEPIvsvlqsdPEQFEQLKQDYQQAQQTQRDA 954
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1760 EEKAkKAITDAAMMAEELKKEQDTsahlERMKKNMEQTIKdLQMRLDEAEQ------IALKGGKKQIQKLEARVRELEGE 1833
Cdd:PRK04863 955 KQQA-FALTEVVQRRAHFSYEDAA----EMLAKNSDLNEK-LRQRLEQAEQertrarEQLRQAQAQLAQYNQVLASLKSS 1028
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1834 LDTEQKKTAEAqkgirkyERRIKELTYQTEEDRKNLARMQDliDKLQTKVKSYKRQYEEAEQQANSNLVKYRKVQHELDD 1913
Cdd:PRK04863 1029 YDAKRQMLQEL-------KQELQDLGVPADSGAEERARARR--DELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRK 1099
|
890
....*....|....*...
gi 1394781870 1914 AEERADIAETQVNKLRAR 1931
Cdd:PRK04863 1100 LERDYHEMREQVVNAKAG 1117
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1655-1889 |
4.58e-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: 60.55 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1655 QSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINQ 1734
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1735 KKKMEADIAQLTteveeavqecRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQI--A 1812
Cdd:COG4942 99 LEAQKEELAELL----------RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALraE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394781870 1813 LKGGKKQIQKLEARVRELEGELDTEQKktaEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQ 1889
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1085-1846 |
4.82e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 61.66 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1085 EEKLKKKDFEMNQLNSRIEDQQVLEAQlqkKIKELQARIEELEEELEAERAARAK-VEKQRAEVARELEELSERLEEAGG 1163
Cdd:pfam05483 62 QEGLKDSDFENSEGLSRLYSKLYKEAE---KIKKWKVSIEAELKQKENKLQENRKiIEAQRKAIQELQFENEKVSLKLEE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1164 ATAIQLEMNKKREA--EFLKLRRDL----EEATLQHESTAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEMKMEVD 1237
Cdd:pfam05483 139 EIQENKDLIKENNAtrHLCNLLKETcarsAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1238 DLSSNIEYLTKNkanaeklcrtYEDQLNEAKSKVDELQRQLADVSTQRARLQ---TESGELSRLLEEKESF----INQLT 1310
Cdd:pfam05483 219 EDHEKIQHLEEE----------YKKEINDKEKQVSLLLIQITEKENKMKDLTfllEESRDKANQLEEKTKLqdenLKELI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1311 RGKTSFTQMIEELKRQLEEETKSKNALAHALQ-ASRHDCDLLRE---QYEEEVEAKSELQRSLSKANAEVAQWRTKYETD 1386
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiATKTICQLTEEkeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTE 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1387 AiQRTEELEEAKKKLAIRLQeaeeaveaahAKCSSLE---KTKHRLQTEIEDLSIDLERANSaaaaLDKKQRNFDRIIAE 1463
Cdd:pfam05483 369 Q-QRLEKNEDQLKIITMELQ----------KKSSELEemtKFKNNKEVELEELKKILAEDEK----LLDEKKQFEKIAEE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1464 WKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNlqeeiadltdqismsgktihelEKLKKTlec 1543
Cdd:pfam05483 434 LKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK----------------------EKLKNI--- 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1544 ekseiqaaleeaegALEHEESKTLRIQLELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLR 1623
Cdd:pfam05483 489 --------------ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1624 KKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAALEQA 1703
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1704 ERGRKLAEQELLEATERVNLLHSQNTGLINQKK----KMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEELKK 1779
Cdd:pfam05483 635 EIKVNKLELELASAKQKFEEIIDNYQKEIEDKKiseeKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKH 714
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394781870 1780 EQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQIQKLEarvRELEGELDTEQKKTAEAQK 1846
Cdd:pfam05483 715 QYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLK---KQLEIEKEEKEKLKMEAKE 778
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1492-1890 |
5.08e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1492 LKNAYEESLDNLETLK-RENKNLQEEIADLTDQISMSGKTIHELEKLKKTLEcEKSEIQAALEEAEGALEHEESKTLRIQ 1570
Cdd:COG4717 47 LLERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1571 --LELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQ 1648
Cdd:COG4717 126 qlLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1649 KMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEV----------------------------------- 1693
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaallallglggsllsliltiagvlflvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1694 ---------------EELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVEEAVQECRN 1758
Cdd:COG4717 286 lallflllarekaslGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1759 AEEKAKKA----------ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKggkKQIQKLEARVR 1828
Cdd:COG4717 366 EELEQEIAallaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE---EELEELEEELE 442
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394781870 1829 ELEGELDTEQKKTAEAqkgirkyERRIKELtyqteEDRKNLARMQDLIDKLQTKVKSYKRQY 1890
Cdd:COG4717 443 ELEEELEELREELAEL-------EAELEQL-----EEDGELAELLQELEELKAELRELAEEW 492
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1484-1845 |
5.77e-09 |
|
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: 60.47 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1484 SLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISmsgktihELEKLKKTLECEKSEIQAALEEAEGALEHee 1563
Cdd:pfam19220 38 AILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLS-------AAEGELEELVARLAKLEAALREAEAAKEE-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1564 sktLRIQL-ELNQVKADVDRKLAEKDEefenlrrnHQRAMDSMQATLDAEAKARNEAirlrkkmegdLNEMEIQLSHANR 1642
Cdd:pfam19220 109 ---LRIELrDKTAQAEALERQLAAETE--------QNRALEEENKALREEAQAAEKA----------LQRAEGELATARE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1643 QAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLlaeveELRAALEQAERGRKLAEQEL---LEATE 1719
Cdd:pfam19220 168 RLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRAL-----EGQLAAEQAERERAEAQLEEaveAHRAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1720 RvNLLHSQNTGLINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIK 1799
Cdd:pfam19220 243 R-ASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1394781870 1800 DLQMRLD------EAEQIALKGGKKQIQKLEARVRELEGELDTEqKKTAEAQ 1845
Cdd:pfam19220 322 ELEERAEmltkalAAKDAALERAEERIASLSDRIAELTKRFEVE-RAALEQA 372
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
854-1090 |
8.13e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 8.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 854 EKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKVKELTER 933
Cdd:PRK03918 492 ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEE 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 934 VED-EEEINSDLTSKKRKLEDECAELKKdIDDLEITLAKVEKEKHATENKVKNLIEEmaaLDEVIAKLTKEKKALQEAHQ 1012
Cdd:PRK03918 572 LAElLKELEELGFESVEELEERLKELEP-FYNEYLELKDAEKELEREEKELKKLEEE---LDKAFEELAETEKRLEELRK 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1013 QaLDDLQAE--EDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLEN------DKQQL 1084
Cdd:PRK03918 648 E-LEELEKKysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKlekaleRVEEL 726
|
....*.
gi 1394781870 1085 EEKLKK 1090
Cdd:PRK03918 727 REKVKK 732
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1357-1917 |
1.44e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.12 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1357 EEVEAKSELQRSLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLAIRLQEAEEAVEAAhakcsslEKTKHRLQTEIEDl 1436
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFEN-------EKVSLKLEEEIQE- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1437 SIDLERANSAAAALDKKQRNFDRIIAEWKQKYEetqAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRE-NKNLQE 1515
Cdd:pfam05483 143 NKDLIKENNATRHLCNLLKETCARSAEKTKKYE---YEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEmHFKLKE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1516 EIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHEESKTLRIQlELNQVKADVDRKLAEKDE----EF 1591
Cdd:pfam05483 220 DHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE-EKTKLQDENLKELIEKKDhltkEL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1592 ENLRRNHQRAMdSMQATLDAEAKARNEAI-RLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDdtmR 1670
Cdd:pfam05483 299 EDIKMSLQRSM-STQKALEEDLQIATKTIcQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLE---K 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1671 HNDDLKEQAAALERRNNLL----------LAEVEELRAALEQAE-------RGRKLAEQ---------ELLEATER-VNL 1723
Cdd:pfam05483 375 NEDQLKIITMELQKKSSELeemtkfknnkEVELEELKKILAEDEklldekkQFEKIAEElkgkeqeliFLLQAREKeIHD 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1724 LHSQNTGLINQKKKMEADIAQLTTEVE-------EAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ 1796
Cdd:pfam05483 455 LEIQLTAIKTSEEHYLKEVEDLKTELEkeklkniELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1797 TIKDLQmrldeAEQIALKGGKKQIQK-LEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDL 1875
Cdd:pfam05483 535 QIENLE-----EKEMNLRDELESVREeFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1394781870 1876 IDKLQTKVKSYKRQYEEAEQQANSNLVKYRKVQHELDDAEER 1917
Cdd:pfam05483 610 IEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK 651
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1295-1720 |
1.90e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1295 LSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKSKnalaHALQASRHDCDLLREQYEEEVEAKSELQRSLSKANA 1374
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1375 EVAQWrtkyetDAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEktkhRLQTEIEDLSIDLERANSAAAALDKKQ 1454
Cdd:COG4717 124 LLQLL------PLYQELEALEAELAELPERLEELEERLEELRELEEELE----ELEAELAELQEELEELLEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1455 rnfdriIAEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEE-----------IADLTDQ 1523
Cdd:COG4717 194 ------LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallaLLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1524 ISMSGKTIHELEKLKKTLEC--------EKSEIQAALEEAEGALEHEESKtlriQLELNQVKADVDRKLAEKDEEFENLR 1595
Cdd:COG4717 268 LLSLILTIAGVLFLVLGLLAllflllarEKASLGKEAEELQALPALEELE----EEELEELLAALGLPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1596 RNHQRAMDSMQATLDAEAKARNEAIRLRKK---------MEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELD 1666
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAallaeagveDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE 423
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1394781870 1667 DTMRHN-----DDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATER 1720
Cdd:COG4717 424 ALDEEEleeelEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELK 482
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
922-1351 |
2.06e-08 |
|
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: 59.14 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 922 QLEAKVKELTERVEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLT 1001
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1002 KEKKAL---QEAHQQALDDLqaeEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLE 1078
Cdd:pfam07888 115 EEKDALlaqRAAHEARIREL---EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1079 NDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSerl 1158
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRD--- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1159 eeaggataiqlemnkKREAEFLKLRRDLEEATLQHESTAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEM-KMEvd 1237
Cdd:pfam07888 269 ---------------RTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELqRLE-- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1238 dlssniEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADvstQRARLQTESGELSRLLEEKESFInqltrgktsft 1317
Cdd:pfam07888 332 ------ERLQEERMEREKLEVELGREKDCNRVQLSESRRELQE---LKASLRVAQKEKEQLQAEKQELL----------- 391
|
410 420 430
....*....|....*....|....*....|....
gi 1394781870 1318 QMIEELKRQLEEETKSKNALAHALQASRHDCDLL 1351
Cdd:pfam07888 392 EYIRQLEQRLETVADAKWSEAALTSTERPDSPLS 425
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1489-1911 |
3.51e-08 |
|
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: 58.33 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1489 LFKLKNAYEEsLDNLETLKRE--NKNLQEEIADLtDQISMSGKTIHELEKLKKT----LECEKSEIQAALEEAEGALE-H 1561
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELNDkY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1562 EESKTLRIQLELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLR-------KKMEGDLNEME 1634
Cdd:pfam06160 80 RFKKAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRfsygpaiDELEKQLAEIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1635 IQLSH-----ANRQAAEAQKMVRQLQSQIKDLQielddtmrhnDDLKEQAAALERRNNLLLAEVEELRAALEQ-AERGRK 1708
Cdd:pfam06160 160 EEFSQfeeltESGDYLEAREVLEKLEEETDALE----------ELMEDIPPLYEELKTELPDQLEELKEGYREmEEEGYA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1709 LAEQELLEATERVNLLHSQNTGLINQK--KKMEADIAQLTTEVEeAVQECRNAEEKAKKaitdaammaeELKKEQDT-SA 1785
Cdd:pfam06160 230 LEHLNVDKEIQQLEEQLEENLALLENLelDEAEEALEEIEERID-QLYDLLEKEVDAKK----------YVEKNLPEiED 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1786 HLERMKKNMEQTIKDLQM-----RLDEAEQIALKGGKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKElty 1860
Cdd:pfam06160 299 YLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEE--- 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1394781870 1861 qteedrknlarmqdlIDKLQTKVKSYKRQYEEAEQQANSNLVKYRKVQHEL 1911
Cdd:pfam06160 376 ---------------IEEEQEEFKESLQSLRKDELEAREKLDEFKLELREI 411
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
853-1237 |
4.83e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.11 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 853 TEKEMATMKEEFQKLKEALEKseaKRKELEEKQVTMIQEKNDL--------ALQLQAEQD-------NLADAEERCDLLI 917
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSE---KQKELEQNNKKIKELEKQLnqlkseisDLNNQKEQDwnkelksELKNQEKKLEEIQ 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 918 KAKIQLEAKVKELTERVEDEEEINSDLTSKKRKLEDECAE-------LKKDIDDLEITLAKVEKEKHATENKVKNLIEEM 990
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEkqneiekLKKENQSYKQEIKNLESQINDLESKIQNQEKLN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 991 AALDEVIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLT 1070
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1071 QESVMD-------LENDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQ 1143
Cdd:TIGR04523 488 QKELKSkekelkkLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKN 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1144 RAEVARELEELSERLEEaggaTAIQLEMNKKrEAEFLKLRRDLEEATLQHESTAAALRKKHADSvAELSEQIDNLQRVKQ 1223
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQ----EEKQELIDQK-EKEKKDLIKEIEEKEKKISSLEKELEKAKKEN-EKLSSIIKNIKSKKN 641
|
410
....*....|....
gi 1394781870 1224 KLEKEKSEMKMEVD 1237
Cdd:TIGR04523 642 KLKQEVKQIKETIK 655
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1696-1931 |
5.91e-08 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 55.22 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1696 LRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVEEavqecrnAEEKAKKAitdaammae 1775
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEK-------WEEKARLA--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1776 eLKKEQDTSAH--LERmKKNMEQTIKDLQMRLDEAEQIALKgGKKQIQKLEARVRELEGELDT--EQKKTAEAQKGIRKY 1851
Cdd:COG1842 78 -LEKGREDLAReaLER-KAELEAQAEALEAQLAQLEEQVEK-LKEALRQLESKLEELKAKKDTlkARAKAAKAQEKVNEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1852 ERRIkeltyQTEEDRKNLARMQDLIDKLqtkvksykrqyeEAEQQANSNLVKYRKVQHELDDAEERADIaETQVNKLRAR 1931
Cdd:COG1842 155 LSGI-----DSDDATSALERMEEKIEEM------------EARAEAAAELAAGDSLDDELAELEADSEV-EDELAALKAK 216
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1595-1905 |
6.46e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1595 RRNHQRAMDSMQ--ATLDAEAKARNEAI-RLRKKME----GDLNEMEIQLSHANRQaaEAQKMVRQLQSQIKDLQIELdd 1667
Cdd:COG3206 93 RPVLERVVDKLNldEDPLGEEASREAAIeRLRKNLTvepvKGSNVIEISYTSPDPE--LAAAVANALAEAYLEQNLEL-- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1668 tmrhnddlkeQAAALERRNNLLLAEVEELRAALEQAERgrKLA----EQELLEATERVNLLHSQNTGLINQKKKMEADIA 1743
Cdd:COG3206 169 ----------RREEARKALEFLEEQLPELRKELEEAEA--ALEefrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1744 QLTTEVEeAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNMEQTIKDLQMRLDEAEQIAL 1813
Cdd:COG3206 237 EAEARLA-ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRIL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1814 KGGKKQIQKLEARVRELEGELDteqkktaeaqkgirKYERRIKELTyqteEDRKNLARMQDLIDKLQTKVKSYKRQYEEA 1893
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLA--------------QLEARLAELP----ELEAELRRLEREVEVARELYESLLQRLEEA 377
|
330
....*....|..
gi 1394781870 1894 EQQANSNLVKYR 1905
Cdd:COG3206 378 RLAEALTVGNVR 389
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1427-1888 |
7.08e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1427 HRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWK--QKYEETQAELEASQKESRSLSTELfklkNAYEESLDNLE 1504
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERL----EELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1505 TLKRENKNLQEEIADLTDQISMSgkTIHELEKLKKTLEceksEIQAALEEAEGALEheesktlRIQLELNQVKADVDRkL 1584
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLA--TEEELQDLAEELE----ELQQRLAELEEELE-------EAQEELEELEEELEQ-L 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1585 AEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHAnrQAAEAQKMVRQLQSQIKDLQIE 1664
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL--LFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1665 LDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEAtERVNLLHSQNTGLINQKKKMEADIAQ 1744
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEELRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1745 LTTEVEEAVQEcRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMkKNMEQTIKDLQMRLDEAEQialkggkkQIQKLE 1824
Cdd:COG4717 390 ALEQAEEYQEL-KEELEELEEQLEELLGELEELLEALDEEELEEEL-EELEEELEELEEELEELRE--------ELAELE 459
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394781870 1825 ARVRELEGELDTEQKKTAEAQKgirkyERRIKELtyqtEEDRKNLARMQDLIDKLQTKVKSYKR 1888
Cdd:COG4717 460 AELEQLEEDGELAELLQELEEL-----KAELREL----AEEWAALKLALELLEEAREEYREERL 514
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1688-1927 |
8.24e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1688 LLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAI 1767
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1768 TDAAMMAEELKKEQDTSAHLER-MKKNMEQTIKDLQMRLDEAEQIA--LKGGKKQIQKLEARVRELEGELDTEQKKTAEA 1844
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRaLYRLGRQPPLALLLSPEDFLDAVrrLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1845 QKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQYEEAEQQANSNLVKYRKVQHELDDAEERADIAETQ 1924
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 1394781870 1925 VNK 1927
Cdd:COG4942 250 ALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
942-1168 |
9.01e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 9.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 942 SDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQALDDLQ-- 1019
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1020 -AEEDKVNTLTKAK--VKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKkkdfemn 1096
Cdd:COG3883 99 gGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA------- 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394781870 1097 QLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGATAIQ 1168
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1430-1649 |
9.01e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 9.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1430 QTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRE 1509
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1510 NKN------------LQEEIADLTDQISM-------SGKTIHELEKLKKTLECEKSEIQAALEEAEGALEheesktlriq 1570
Cdd:COG3883 95 LYRsggsvsyldvllGSESFSDFLDRLSAlskiadaDADLLEELKADKAELEAKKAELEAKLAELEALKA---------- 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394781870 1571 lELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQAtLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQK 1649
Cdd:COG3883 165 -ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE-LEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
851-1063 |
9.16e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 9.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 851 AQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKVKEL 930
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 931 TERVED------------------EEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAA 992
Cdd:COG4942 103 KEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394781870 993 LDEVIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQ--EKKIRMDLERAKRKL 1063
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAaaERTPAAGFAALKGKL 255
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
848-1064 |
9.31e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 9.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 848 LRSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMiqeknDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKV 927
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 928 KELTERVEDEEEINSDLTSkkrklEDECAELKKDIDDLEITLAkvEKEKHATEN--KVKNLIEEMAALdeviakltkeKK 1005
Cdd:COG3206 243 AALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL----------RA 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1394781870 1006 ALQEAHQQALDDLQAEedkVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLE 1064
Cdd:COG3206 306 QLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
810-1882 |
1.11e-07 |
|
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: 57.37 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 810 QKIISRRDALYTIQWNIRAfnvvknwswmKLFFKIKPLLRSAQT-----EKEMATMKEEFQKLKEALEKSEAKRKELEEK 884
Cdd:TIGR01612 518 DEVPSKNIIGFDIDQNIKA----------KLYKEIEAGLKESYElaknwKKLIHEIKKELEEENEDSIHLEKEIKDLFDK 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 885 QVTMIQEK---NDLALQLQAEQDNLADAEERCDLLIKAKIQLE---AKVKEL--------TERVEDEEEINSDLTSKKRK 950
Cdd:TIGR01612 588 YLEIDDEIiyiNKLKLELKEKIKNISDKNEYIKKAIDLKKIIEnnnAYIDELakispyqvPEHLKNKDKIYSTIKSELSK 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 951 LEDEcaelkkDIDDLEITLAKVEKEkhateNKVKNlIEEMAALDEVIAKLTKEKKALQEAHQQALD-DLQAEEDKVNTLT 1029
Cdd:TIGR01612 668 IYED------DIDALYNELSSIVKE-----NAIDN-TEDKAKLDDLKSKIDKEYDKIQNMETATVElHLSNIENKKNELL 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1030 KAKVKLEQQVddlessleqEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEeKLKKKDFEM-NQLNSRIEDQQVL 1108
Cdd:TIGR01612 736 DIIVEIKKHI---------HGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELN-KYKSKISEIkNHYNDQINIDNIK 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1109 EAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELserleeaggataIQLEMNKKRE--------AEFL 1180
Cdd:TIGR01612 806 DEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKF------------INFENNCKEKidseheqfAELT 873
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1181 -KLRRDLEEATL----QHESTAAALRKKHADSVAELSEQIDNLQRV----------KQKLEKEKSEMKMEVDDLSSNIEY 1245
Cdd:TIGR01612 874 nKIKAEISDDKLndyeKKFNDSKSLINEINKSIEEEYQNINTLKKVdeyikicentKESIEKFHNKQNILKEILNKNIDT 953
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1246 LtKNKANAEKlcrTYEDQL-NEAKSKVDELQRQLADVSTqrARLQTESGELSRLLEEKESFINQlTRGKTSFTQMIEELK 1324
Cdd:TIGR01612 954 I-KESNLIEK---SYKDKFdNTLIDKINELDKAFKDASL--NDYEAKNNELIKYFNDLKANLGK-NKENMLYHQFDEKEK 1026
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1325 RQLEEETKSKNA------LAHALQASRHDcdlLREQYEEEVEAKSEL--QRSLSKANAEVAQWRTKYET----------- 1385
Cdd:TIGR01612 1027 ATNDIEQKIEDAnknipnIEIAIHTSIYN---IIDEIEKEIGKNIELlnKEILEEAEINITNFNEIKEKlkhynfddfgk 1103
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1386 -DAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLS--IDLERANSAAAALDKKQRNFDRIIA 1462
Cdd:TIGR01612 1104 eENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEdvADKAISNDDPEEIEKKIENIVTKID 1183
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1463 EWKQKYEETQAEL-EASQKESRSLSTELFKLKN-AYEESLDNL--ETLKRENKNlqeeiadltdqismSGKTIHELEKLK 1538
Cdd:TIGR01612 1184 KKKNIYDEIKKLLnEIAEIEKDKTSLEEVKGINlSYGKNLGKLflEKIDEEKKK--------------SEHMIKAMEAYI 1249
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1539 KTLEcekseiqaALEEAEGALEHEESKTLRIQLELNQVKADVDrklaeKDEEFENLRRNHQRAMDSMqatldaeakaRNE 1618
Cdd:TIGR01612 1250 EDLD--------EIKEKSPEIENEMGIEMDIKAEMETFNISHD-----DDKDHHIISKKHDENISDI----------REK 1306
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1619 AIRLRKKM--EGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQ--IELDDTMRHNDDLKEQAAALERRNNLLLAEV- 1693
Cdd:TIGR01612 1307 SLKIIEDFseESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYniLKLNKIKKIIDEVKEYTKEIEENNKNIKDELd 1386
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1694 ---------------EELRAALEQAERGRKLAE--QELLEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVEEAVQEC 1756
Cdd:TIGR01612 1387 kseklikkikddinlEECKSKIESTLDDKDIDEciKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKS 1466
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1757 RN-AEEKAKKAITDAAMMAEELKKEQDTS-----------AHLERMKKNMEQTIKDLQMRLDEAEQIALKGG----KKQI 1820
Cdd:TIGR01612 1467 QHiLKIKKDNATNDHDFNINELKEHIDKSkgckdeadknaKAIEKNKELFEQYKKDVTELLNKYSALAIKNKfaktKKDS 1546
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394781870 1821 QKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTK 1882
Cdd:TIGR01612 1547 EIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENK 1608
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
984-1457 |
1.59e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 984 KNLIEEMAALDEVIAKLtKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLE------SSLEQEKKIRMDLE 1057
Cdd:COG4717 64 RKPELNLKELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllqllPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1058 RAKRKLEgDLKLTQESVMDLENDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQ--------LQKKIKELQARIEELEEE 1129
Cdd:COG4717 143 ELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQdlaeeleeLQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1130 LEAERAARAKVEKQRAEVARELEELSERLEEAGGATAIQLEMNKKREAEFLKLRRDLEEATLQHESTAAALRKKHADSVA 1209
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1210 ELSEQIDNLQRvKQKLEKEksEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSkvDELQRQLADVSTQRARLQ 1289
Cdd:COG4717 302 KEAEELQALPA-LEELEEE--ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE--LEEELQLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1290 TESG-----ELSRLLEEKESFINQLTRgktsftqmIEELKRQLEEETKSKNALAHAlqasrHDCDLLREQYEEEVEAKSE 1364
Cdd:COG4717 377 AEAGvedeeELRAALEQAEEYQELKEE--------LEELEEQLEELLGELEELLEA-----LDEEELEEELEELEEELEE 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1365 LQRSLSKANAEVAqwRTKYETDAIQRTEELEEAKKKLAirlqeaeeaveaahakcsslektkhRLQTEIEDLSIDLERAN 1444
Cdd:COG4717 444 LEEELEELREELA--ELEAELEQLEEDGELAELLQELE-------------------------ELKAELRELAEEWAALK 496
|
490
....*....|...
gi 1394781870 1445 SAAAALDKKQRNF 1457
Cdd:COG4717 497 LALELLEEAREEY 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1261-1478 |
2.24e-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: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1261 EDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKS-KNALAH 1339
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1340 ALQASRHDCD--LLREQYEEEVEAKSELQRSLSKANAEVAQwrtkyetDAIQRTEELEEAKKKLAIRLQEAEEAVEAAHA 1417
Cdd:COG4942 113 LYRLGRQPPLalLLSPEDFLDAVRRLQYLKYLAPARREQAE-------ELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394781870 1418 KCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEAS 1478
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
891-1541 |
2.46e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.06 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 891 EKNDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKVKELTERVEDEEEINSDLTSKkrklEDECAELKKDIDDLEITLA 970
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSS----NLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 971 KVEKEKHATENKVKNLIEEMAALDEVIAKLT---KEKKALQEAHQQALDDLQAEEDKVNTLTkakvKLEQQVDDLESSLE 1047
Cdd:PRK01156 215 ITLKEIERLSIEYNNAMDDYNNLKSALNELSsleDMKNRYESEIKTAESDLSMELEKNNYYK----ELEERHMKIINDPV 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1048 QEKKIRMdleRAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKDfEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELE 1127
Cdd:PRK01156 291 YKNRNYI---NDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS-VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYN 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1128 EELEAERAARAKVEKQRAEVARELEELSERLeeagGATAIQLEMNKKREAEflkLRRDLEEatlqhestaaalrkkHADS 1207
Cdd:PRK01156 367 SYLKSIESLKKKIEEYSKNIERMSAFISEIL----KIQEIDPDAIKKELNE---INVKLQD---------------ISSK 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1208 VAELSEQIDNLqrvKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRAR 1287
Cdd:PRK01156 425 VSSLNQRIRAL---RENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVD 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1288 LQTESGEL-SRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKSKNALAhalQASRHDCDLLREQYEEEVEAKSELQ 1366
Cdd:PRK01156 502 LKKRKEYLeSEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKN---RYKSLKLEDLDSKRTSWLNALAVIS 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1367 RSLSKANAEVAQWRTKYETDAIQRTEELEeakkklaIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERansa 1446
Cdd:PRK01156 579 LIDIETNRSRSNEIKKQLNDLESRLQEIE-------IGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEK---- 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1447 aaaLDKKQRNFDRIIAEwKQKYEETQAELEASQKESrslSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISM 1526
Cdd:PRK01156 648 ---LRGKIDNYKKQIAE-IDSIIPDLKEITSRINDI---EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
650
....*....|....*
gi 1394781870 1527 SGKTIHELEKLKKTL 1541
Cdd:PRK01156 721 INETLESMKKIKKAI 735
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
859-1025 |
2.60e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.78 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 859 TMKEEFQKLKEaLEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKVKELTERVE-DE 937
Cdd:COG1579 1 AMPEDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 938 EEINSDLTSKKRK-LEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQALD 1016
Cdd:COG1579 80 EQLGNVRNNKEYEaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
....*....
gi 1394781870 1017 DLQAEEDKV 1025
Cdd:COG1579 160 ELEAEREEL 168
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1485-1943 |
2.62e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.80 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1485 LSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHEES 1564
Cdd:TIGR04523 80 LEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1565 KTLRIQLELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKarneaIRLRKKMEGDLNEMEIQLSHANRQA 1644
Cdd:TIGR04523 160 KYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK-----IQKNKSLESQISELKKQNNQLKDNI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1645 AEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQaaaLERRNNlllaEVEELRAALEQAERGRKLAEQEL--LEATERVN 1722
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ---LSEKQK----ELEQNNKKIKELEKQLNQLKSEIsdLNNQKEQD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1723 LLHSQNTGLINQKKKMEADIAQLTtEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEqdtsahLERMKKNMEQTIKDLQ 1802
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQIS-QNNKIISQLNEQISQLKKELTNSESENSEKQRE------LEEKQNEIEKLKKENQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1803 MRLDEAEQIalkggKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTK 1882
Cdd:TIGR04523 381 SYKQEIKNL-----ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394781870 1883 VKSYKRQYEEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRARSREVVITSKVLK 1943
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT 516
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1627-1846 |
2.67e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1627 EGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAALeqAERG 1706
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL--GERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1707 RKLAEQELLEATERVnLLHSQNTG-LINQ----KKKMEADiAQLTTEVEEAVQECRNAEEKAKKAITDaammAEELKKEq 1781
Cdd:COG3883 93 RALYRSGGSVSYLDV-LLGSESFSdFLDRlsalSKIADAD-ADLLEELKADKAELEAKKAELEAKLAE----LEALKAE- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394781870 1782 dtsahLERMKKNMEQTIKDLQMRLDEAEQialkggkkQIQKLEARVRELEGELDTEQKKTAEAQK 1846
Cdd:COG3883 166 -----LEAAKAELEAQQAEQEALLAQLSA--------EEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
847-1121 |
2.98e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.88 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 847 LLRSAQTEKEMATMKEEFQKLKEALEKSEAKRKEL--EEKQVTMIQEK-----NDLALQLQAEQDNLADAEERCDLLIKA 919
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLldEKKQFEKIAEElkgkeQELIFLLQAREKEIHDLEIQLTAIKTS 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 920 KIQLEAKVKELTERVEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAK 999
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1000 LTKEKKALQEAHQQALDDLQAEEDK-----------VNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKL--EGD 1066
Cdd:pfam05483 546 LRDELESVREEFIQKGDEVKCKLDKseenarsieyeVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALkkKGS 625
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1394781870 1067 LKLTQESVMDLENDKQQLEEKLKKKDFE--MNQLNSRIEDQQVLEAQLQKKIKELQA 1121
Cdd:pfam05483 626 AENKQLNAYEIKVNKLELELASAKQKFEeiIDNYQKEIEDKKISEEKLLEEVEKAKA 682
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1469-1728 |
4.85e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 55.30 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1469 EETQAELEASQKeSRSLSTELFKLKNAYEESL---DNLETLKRENKNLQEEIADLTDQISMSGKtihELEKLKKTLECEK 1545
Cdd:PRK11281 39 ADVQAQLDALNK-QKLLEAEDKLVQQDLEQTLallDKIDRQKEETEQLKQQLAQAPAKLRQAQA---ELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1546 SEIQAALEeaegaLEHEESKTLRIQLELNQVKADvdrkLAEKDEEFENLRRNHQRAmdsmQATLDAeAKARNEAIRLRKK 1625
Cdd:PRK11281 115 RETLSTLS-----LRQLESRLAQTLDQLQNAQND----LAEYNSQLVSLQTQPERA----QAALYA-NSQRLQQIRNLLK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1626 ----MEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRhnDDLKEQAAALERRNNLLLAEVEELRAAL- 1700
Cdd:PRK11281 181 ggkvGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQR--DYLTARIQRLEHQLQLLQEAINSKRLTLs 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1701 ----EQAERGRKLAE------------------QELLEATERVNLLHSQN 1728
Cdd:PRK11281 259 ektvQEAQSQDEAARiqanplvaqeleinlqlsQRLLKATEKLNTLTQQN 308
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
656-683 |
5.61e-07 |
|
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: 51.58 E-value: 5.61e-07
10 20
....*....|....*....|....*...
gi 1394781870 656 SQLHKENLNKLMTNLRATQPHFVRCIIP 683
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1038-1657 |
7.20e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.52 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1038 QVDDLESSLEQEKKIRMD-------LERAKRKLEGDLKLTQESVMDLENdkqqLEEKLKKKDFEMNQLNSRIEDQQVLEA 1110
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDeileinsLERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1111 QLQKKIKELQARIEELEEEL----------EAERAARAKVEKQRAEVARELEELSERLEEAGGATAIQLEM-------NK 1173
Cdd:PRK01156 215 ITLKEIERLSIEYNNAMDDYnnlksalnelSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIindpvykNR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1174 KREAEFLKLRRDLEEATLQHESTAAALRKKHadsvaELSEQIDNLQRVKQKLEKEKSEMkmevDDLSSNIEYLTKNKANA 1253
Cdd:PRK01156 295 NYINDYFKYKNDIENKKQILSNIDAEINKYH-----AIIKKLSVLQKDYNDYIKKKSRY----DDLNNQILELEGYEMDY 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1254 EKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKS 1333
Cdd:PRK01156 366 NSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRN 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1334 KNALAHALQASRHDCDLLREQYEEEVEAKSElqrSLSKANAEVaqwrTKYETDAIQRTEELEEAKKKLAIRLQEAEEAVE 1413
Cdd:PRK01156 446 MEMLNGQSVCPVCGTTLGEEKSNHIINHYNE---KKSRLEEKI----REIEIEVKDIDEKIVDLKKRKEYLESEEINKSI 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1414 AAHAKCSSLEktkhrlqTEIEDLSIDLER---ANSAAAALDKKQRNFDriIAEWKQKYEE--------TQAELEASQKES 1482
Cdd:PRK01156 519 NEYNKIESAR-------ADLEDIKIKINElkdKHDKYEEIKNRYKSLK--LEDLDSKRTSwlnalaviSLIDIETNRSRS 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1483 RSLSTELFKLKNAYEESLDNLETLKRENKN----LQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIqAALEEAEGA 1558
Cdd:PRK01156 590 NEIKKQLNDLESRLQEIEIGFPDDKSYIDKsireIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQI-AEIDSIIPD 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1559 LEHEESKTLRIQLELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLDaeakaRNEAIRLRKKME---GDLNEMEI 1635
Cdd:PRK01156 669 LKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIND-----INETLESMKKIKkaiGDLKRLRE 743
|
650 660
....*....|....*....|..
gi 1394781870 1636 QLSHANRQAaeaqkMVRQLQSQ 1657
Cdd:PRK01156 744 AFDKSGVPA-----MIRKSASQ 760
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1502-1934 |
7.49e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1502 NLETLKRENKNLQE-------EIADLTDQISMSG-----------------KTIHELEKLKKTLECEKSEIQAALEEAEG 1557
Cdd:PRK03918 156 GLDDYENAYKNLGEvikeikrRIERLEKFIKRTEnieelikekekeleevlREINEISSELPELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1558 ALEHEESKTLRIQLELNQVKA------DVDRKLAEKDEEFENLRRNHQRAMDsmqatLDAEAKARNEAIRLRKKMEGDLN 1631
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKleekirELEERIEELKKEIEELEEKVKELKE-----LKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1632 EMEIQLSHANRQAAEAQKMVRQLQS---QIKDLQIELDDTMRHNDDLKEQAAALER-----------RNNLLLAEVEELR 1697
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEERHELYEEakakkeelerlKKRLTGLTPEKLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1698 AALEQAERGRKLAEQELLEATERVNLLHSQNTGL---INQKKKM------------EADIAQLTTEVEEAVQECRNAEEK 1762
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELkkaIEELKKAkgkcpvcgreltEEHRKELLEEYTAELKRIEKELKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1763 AKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQtIKDLQMRLDEAEQIALKGGKKQIQKLEARVRELEGE---LDTEQK 1839
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEiksLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1840 KTAEAQKGIRKYERRIKELtyqtEEDRKNLARMQ-----DLIDKLQTKVKSYKRQYEE------AEQQANSNLVKYRKVQ 1908
Cdd:PRK03918 550 KLEELKKKLAELEKKLDEL----EEELAELLKELeelgfESVEELEERLKELEPFYNEylelkdAEKELEREEKELKKLE 625
|
490 500
....*....|....*....|....*.
gi 1394781870 1909 HELDDAEERADIAETQVNKLRARSRE 1934
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEE 651
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
862-1090 |
8.45e-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: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 862 EEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKVKELTERVEdeeein 941
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 942 sdltskkrKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQALDDLQAE 1021
Cdd:COG4942 94 --------ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394781870 1022 EDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRmdlERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKK 1090
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
937-1367 |
8.96e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 937 EEEINSDLTSKKRKLEDECAELKKDIDDLEiTLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALqEAHQQALD 1016
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1017 DLQAEEDKVNTLTKakvkLEQQVDDLESSLEQEKKIRMDLERAKRKLEgdlKLTQESVMDLENDKQQLEEKLKKKDFEMN 1096
Cdd:COG4717 130 LYQELEALEAELAE----LPERLEELEERLEELRELEEELEELEAELA---ELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1097 QLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQR--------AEVARELEELSERLEEAGGATAIQ 1168
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaalLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1169 LEM----------------NKKREAEFLKLRRDLEEATLQHESTAAAL-RKKHADSVAELSEQIDNLQRVKQKLEKEKSE 1231
Cdd:COG4717 283 LGLlallflllarekaslgKEAEELQALPALEELEEEELEELLAALGLpPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1232 MKMEvddlssniEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESfiNQLTR 1311
Cdd:COG4717 363 LQLE--------ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEE 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1394781870 1312 GKTSFTQMIEELKRQLEEETKSKNALAHALQASRHDcDLLREQYEEEVEAKSELQR 1367
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELRE 487
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1192-1897 |
9.58e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 54.04 E-value: 9.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1192 QHESTAAALRK--KHADSVAELS-EQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEklcrtyedQLNEAK 1268
Cdd:PRK10246 192 QHKSARTELEKlqAQASGVALLTpEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQ--------EASRRQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1269 SKVDELQRQLADVSTQRARLQTesGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKSKNALAHALQasrhdc 1348
Cdd:PRK10246 264 QALQQALAAEEKAQPQLAALSL--AQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAA------ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1349 dllrEQYEEEVEAKSELQRSLSKA------NAEVAQWR---TKYETDAIQR---TEELEEAKKKLAirlqeaeeaveaah 1416
Cdd:PRK10246 336 ----KQSAELQAQQQSLNTWLAEHdrfrqwNNELAGWRaqfSQQTSDREQLrqwQQQLTHAEQKLN-------------- 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1417 akcsslektkhrlqtEIEDLSIDLErANSAAAALDK--KQRNFDRIIAEWKQKYEETQAELEASQKESRSLSTELFKlkn 1494
Cdd:PRK10246 398 ---------------ALPAITLTLT-ADEVAAALAQhaEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQ--- 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1495 aYEESLdnleTLKREN-KNLQEEIADLtdqismsgKTIHELEKLKKTLECEKSEIQAALE------------EAEGALEH 1561
Cdd:PRK10246 459 -RNAAL----NEMRQRyKEKTQQLADV--------KTICEQEARIKDLEAQRAQLQAGQPcplcgstshpavEAYQALEP 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1562 EESKTLRIQLE-------------LNQVKAdVDRKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEG 1628
Cdd:PRK10246 526 GVNQSRLDALEkevkklgeegaalRGQLDA-LTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1629 DlNEMEIQLSHANR------QAAEAQKMVRQLQSQIKDLQIELDDTMRH-------NDD-----------------LKEQ 1678
Cdd:PRK10246 605 Q-EEHERQLRLLSQrhelqgQIAAHNQQIIQYQQQIEQRQQQLLTALAGyaltlpqEDEeaswlatrqqeaqswqqRQNE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1679 AAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVEEAVQECRN 1758
Cdd:PRK10246 684 LTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVF 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1759 AEEKAKKaitdAAMMAEElkkeqdTSAHLERMKKNMEQTIKDLQMRLDEAEQialkggkKQIQKLEARVRELEGELDTEQ 1838
Cdd:PRK10246 764 DDQQAFL----AALLDEE------TLTQLEQLKQNLENQRQQAQTLVTQTAQ-------ALAQHQQHRPDGLDLTVTVEQ 826
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394781870 1839 KKTAEAQ--KGIRKYERRIKELTYQTEEDRKNLARMQDLIdklqtkvksykRQYEEAEQQA 1897
Cdd:PRK10246 827 IQQELAQlaQQLRENTTRQGEIRQQLKQDADNRQQQQALM-----------QQIAQATQQV 876
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1071-1287 |
1.05e-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: 53.23 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1071 QESVMDLENDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARE 1150
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1151 LEELSERLEE-------AGGATAIQLEMNKKREAEFLKLRRDLEEATLQHESTAAALRKKhadsVAELSEQIDNLQRVKQ 1223
Cdd:COG4942 99 LEAQKEELAEllralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394781870 1224 KLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRAR 1287
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1064-1304 |
1.09e-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: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1064 EGDLKLTQESVMDLENDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEeleeeleaerAARAKVEKQ 1143
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA----------EAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1144 RAEVAREleelserleeaggATAIQLEMNKKREAEFLKLRRDLEEAtLQHESTAAALRKKHADSVAELSEQIDNLQRVKQ 1223
Cdd:COG3883 85 REELGER-------------ARALYRSGGSVSYLDVLLGSESFSDF-LDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1224 KLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKE 1303
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
.
gi 1394781870 1304 S 1304
Cdd:COG3883 231 A 231
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1426-1782 |
1.10e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.97 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1426 KHRLQTEIEDLSIDLERANSAAAALDKKQRNFDR---IIAEWKQKYEETQAELEASQKESRslstelfklknayeesldn 1502
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEER------------------- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1503 letlKRENKNLQEEiadltdQISMSGKTIHELEKLKKTLECEKSEIQAALEEAegaleheesKTLRIQLELNQvkadvdR 1582
Cdd:pfam17380 359 ----KRELERIRQE------EIAMEISRMRELERLQMERQQKNERVRQELEAA---------RKVKILEEERQ------R 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1583 KLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRkkmegdlnEMEIQlshanrqaaEAQKMVRQLQSQIKDLQ 1662
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE--------EQERQ---------QQVERLRQQEEERKRKK 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1663 IELDDTMRhnddlkEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEatervnllhsQNTGLINQKKKMEADI 1742
Cdd:pfam17380 477 LELEKEKR------DRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE----------RQKAIYEEERRREAEE 540
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1394781870 1743 AQLTtevEEAVQECRNAEEKAKKAITDAAMMaEELKKEQD 1782
Cdd:pfam17380 541 ERRK---QQEMEERRRIQEQMRKATEERSRL-EAMERERE 576
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
881-1496 |
1.22e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 881 LEEKQVTmiqeknDLALQLQAEQDNLADAEERcdlLIKAKIQLEAkvkeLTERVEDEEEINsDLTSKKRKLEDECAELKK 960
Cdd:COG4913 218 LEEPDTF------EAADALVEHFDDLERAHEA---LEDAREQIEL----LEPIRELAERYA-AARERLAELEYLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 961 DIDDLEITLAKVEKEKHATEnkVKNLIEEMAALDEVIAKLTKEKKALQEAHQQAldDLQAEEDkvntltkakvkLEQQVD 1040
Cdd:COG4913 284 WFAQRRLELLEAELEELRAE--LARLEAELERLEARLDALREELDELEAQIRGN--GGDRLEQ-----------LEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1041 DLESSLEQEKKIRMDLERAKRKLEGDLKLTQEsvmDLENDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQ 1120
Cdd:COG4913 349 RLERELEERERRRARLEALLAALGLPLPASAE---EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1121 ARIEeleeeleaeraarakvekqraevareleelserleeaggataiQLEMNKKR-EAEFLKLRRDLEEATLQHES---- 1195
Cdd:COG4913 426 AEIA-------------------------------------------SLERRKSNiPARLLALRDALAEALGLDEAelpf 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1196 ---------------TAA--ALR---------KKHADSVAELSEQID-----NLQRVKQKLEKEKSE--------MKMEV 1236
Cdd:COG4913 463 vgelievrpeeerwrGAIerVLGgfaltllvpPEHYAAALRWVNRLHlrgrlVYERVRTGLPDPERPrldpdslaGKLDF 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1237 DD--LSSNIEYLTKNKANAEKlCRTyEDQLNEAKSKVdELQRQLADvSTQRARLQTESGELSRL---------LEEKESF 1305
Cdd:COG4913 543 KPhpFRAWLEAELGRRFDYVC-VDS-PEELRRHPRAI-TRAGQVKG-NGTRHEKDDRRRIRSRYvlgfdnrakLAALEAE 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1306 INQLTRGKTSFTQMIEELKRQLEEETKSKNALAHALQASRHDCDLlrEQYEEEVEAKSELQRSLSKANAEVaqwrtkyet 1385
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV--ASAEREIAELEAELERLDASSDDL--------- 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1386 daiqrtEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAA-----AALDKKQRNFDRI 1460
Cdd:COG4913 688 ------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelrALLEERFAAALGD 761
|
650 660 670
....*....|....*....|....*....|....*.
gi 1394781870 1461 IAEwKQKYEETQAELEASQKESRSLSTELFKLKNAY 1496
Cdd:COG4913 762 AVE-RELRENLEERIDALRARLNRAEEELERAMRAF 796
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1105-1345 |
1.50e-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: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1105 QQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELeelserleeagGATAIQLemnKKREAEFLKLRR 1184
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-----------AALARRI---RALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1185 DLEEATLQhestAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQL 1264
Cdd:COG4942 84 ELAELEKE----IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1265 NEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKSKNALAHALQAS 1344
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
.
gi 1394781870 1345 R 1345
Cdd:COG4942 240 A 240
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1469-1935 |
2.02e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.90 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1469 EETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGktihelekLKKTLECEKSEI 1548
Cdd:pfam10174 112 ELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLQSKG--------LPKKSGEEDWER 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1549 QAALEEAEGALEHEESKTLRIQLELNQVKADVDRK----------------LAEKDEEFENLRRNHQRAMDSMQATldae 1612
Cdd:pfam10174 184 TRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRnqlqpdpaktkalqtvIEMKDTKISSLERNIRDLEDEVQML---- 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1613 akaRNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQ---SQIKDLQIELD-------DTMRHNDDLKEQAAAL 1682
Cdd:pfam10174 260 ---KTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSkkeSELLALQTKLEtltnqnsDCKQHIEVLKESLTAK 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1683 ERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERvnllHSQNTGLINQKKKM----EADIAQLTTEVEEAVQECRN 1758
Cdd:pfam10174 337 EQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEE----KSTLAGEIRDLKDMldvkERKINVLQKKIENLQEQLRD 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1759 AE-------EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNM-EQTIKDLQMRLDEAEQIalkggKKQIQKLEARVREL 1830
Cdd:pfam10174 413 KDkqlaglkERVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESL-----KKENKDLKEKVSAL 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1831 EGEL--------DTEQKKTAEAQKGIRKyERRIKELTYQTEEDRKNLARMQDLIDKLQtkvksykrQYEEAEQQANSNLV 1902
Cdd:pfam10174 488 QPELtekessliDLKEHASSLASSGLKK-DSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEIND 558
|
490 500 510
....*....|....*....|....*....|...
gi 1394781870 1903 KYRKVQHELDDAEERADIAETQVNKLRARSREV 1935
Cdd:pfam10174 559 RIRLLEQEVARYKEESGKAQAEVERLLGILREV 591
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
860-1114 |
2.04e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.90 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 860 MKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLikakiqlEAKVKELTERVEDEEE 939
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL-------QTEVDALRLRLEEKES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 940 INSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQA----- 1014
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTdtalt 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1015 -LDDLQAEEDKV-NTLTKAKVKLEQQVDDLESSLEQEKKirmDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKD 1092
Cdd:pfam10174 440 tLEEALSEKERIiERLKEQREREDRERLEELESLKKENK---DLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKD 516
|
250 260
....*....|....*....|....*.
gi 1394781870 1093 FEMNQLN----SRIEDQQVLEAQLQK 1114
Cdd:pfam10174 517 SKLKSLEiaveQKKEECSKLENQLKK 542
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1621-1771 |
2.18e-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: 51.08 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1621 RLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALerRNNlllAEVEELRAAL 1700
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV--RNN---KEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394781870 1701 EQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAA 1771
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1729-1935 |
2.29e-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: 51.26 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1729 TGLINQKKKMEADIAQLTTEVEEAVQECRNAEEK---AKKAITDAAMMAEEL-KKEQDTSAHLERMKKNMEQTIKDLQMR 1804
Cdd:pfam06008 8 TGALPAPYKINYNLENLTKQLQEYLSPENAHKIQieiLEKELSSLAQETEELqKKATQTLAKAQQVNAESERTLGHAKEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1805 LDEAEQIAlkggkKQIQKLEARVRELEGELD-----TEQKKTAEAQKGIRkyERRIKELTYQTEEDRKNLARMQDLIDKL 1879
Cdd:pfam06008 88 AEAIKNLI-----DNIKEINEKVATLGENDFalpssDLSRMLAEAQRMLG--EIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1394781870 1880 QTKVKSYKRQYEEAEQQANSNLVKYrkvQHELDDAEERADIAETQVNKLRARSREV 1935
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEY---EAKLSDLRELLREAAAKTRDANRLNLAN 213
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1082-1555 |
2.71e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1082 QQLEEKLKKKDFEMNQLNSRIEDQQVLEAQ---LQKKIKELQARIEELEEELEAERAARaKVEKQRAEVARELEelserl 1158
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEEleeLEAELEELREELEKLEKLLQLLPLYQ-ELEALEAELAELPE------ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1159 eeaggataiQLEMNKKREAEFLKLRRDLEEATLQHESTAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEMKMEVDD 1238
Cdd:COG4717 147 ---------RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1239 LSSNIEYLTKNKANAEKlcrtyEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKES----------FINQ 1308
Cdd:COG4717 218 AQEELEELEEELEQLEN-----ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlgllalLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1309 LTRGKTSFTQMIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEAKSELQRSLSKANAEVAQWRTkyetdai 1388
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL------- 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1389 qrtEELEEAKKKLAIRLQEAeeaveaahakcsslektkhrlqteiedlsiDLERANSAAAALDKKQrnfdriiaEWKQKY 1468
Cdd:COG4717 366 ---EELEQEIAALLAEAGVE------------------------------DEEELRAALEQAEEYQ--------ELKEEL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1469 EETQAELEASQKESRSLSTELFK--LKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTiHELEKLKKTLECEKS 1546
Cdd:COG4717 405 EELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKA 483
|
....*....
gi 1394781870 1547 EIQAALEEA 1555
Cdd:COG4717 484 ELRELAEEW 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
898-1217 |
3.53e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 898 QLQAEQDNLADAEERCDLLIKAKIQLEAKVKELTERVE--------DEEEINSdltskkRKLEDECAELKKDIDDLE--- 966
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREalqrlaeySWDEIDV------ASAEREIAELEAELERLDass 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 967 ITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAkvKLEQQVDDLESSl 1046
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAAALGD- 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1047 EQEKKIRMDLERAKRKLEGdlkltqesvmDLENDKQQLEEKLK--KKDFEMNQLNSR--IEDQQVLEAQLQK----KIKE 1118
Cdd:COG4913 762 AVERELRENLEERIDALRA----------RLNRAEEELERAMRafNREWPAETADLDadLESLPEYLALLDRleedGLPE 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1119 LQARIEELEEELEAERAA--RAKVEKQRAEVARELEE--LSERLEEAGGATAIQLEMNKKREAEFLKLRRDLEEATLQHE 1194
Cdd:COG4913 832 YEERFKELLNENSIEFVAdlLSKLRRAIREIKERIDPlnDSLKRIPFGPGRYLRLEARPRPDPEVREFRQELRAVTSGAS 911
|
330 340
....*....|....*....|...
gi 1394781870 1195 STAAALRKKHADSVAELSEQIDN 1217
Cdd:COG4913 912 LFDEELSEARFAALKRLIERLRS 934
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
889-1094 |
3.75e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.94 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 889 IQEKNDLALQLQAEQdNLADAEERCDLLIKAKIQLEAKVKELTERVEDEEEINSDLTSKKRKLEDECAELKKDIDdleiT 968
Cdd:PHA02562 199 TYNKNIEEQRKKNGE-NIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE----Q 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 969 LAKVEK--EKHATENKVKNLIEEMaalDEVIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEqqvdDLESSL 1046
Cdd:PHA02562 274 FQKVIKmyEKGGVCPTCTQQISEG---PDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLL----ELKNKI 346
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1394781870 1047 EQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKDFE 1094
Cdd:PHA02562 347 STNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1507-1891 |
5.36e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.66 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1507 KRENKNLQEEIADLTDQ--ISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHEESKTLRIQLELNQVKADVDRKL 1584
Cdd:pfam17380 239 RKESFNLAEDVTTMTPEytVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1585 AEKdEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRL--RKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQikDLQ 1662
Cdd:pfam17380 319 EEA-EKARQAEMDRQAAIYAEQERMAMERERELERIRQeeRKRELERIRQEEIAMEISRMRELERLQMERQQKNE--RVR 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1663 IELDDTMRHNDDLKEQaaalERRNNLLLAEVEELRAALEQA-ERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEAD 1741
Cdd:pfam17380 396 QELEAARKVKILEEER----QRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1742 IAQLTTEVEEAVQECRNAEEKAKKaitdaaMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEaeqialkggkkqiq 1821
Cdd:pfam17380 472 RKRKKLELEKEKRDRKRAEEQRRK------ILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYE-------------- 531
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1822 klEARVRELEGELDTEQKKtaeaqkgirKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQYE 1891
Cdd:pfam17380 532 --EERRREAEEERRKQQEM---------EERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1560-1935 |
6.86e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1560 EHEESKTLRIQLELNQVKADVDRKLAEKDEEFENLRRN---HQRAMDSMQATLDAeAKAR----NEAIRLRKKME---GD 1629
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARElaeLNEAESDLEQDYQA-ASDHlnlvQTALRQQEKIEryqAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1630 LNEMEIQLshanrqaaEAQKMVRQLQSQIKD-LQIELDDTMRHNDDLKEQaaalerrnnllLAEVEElraALEQAERgRK 1708
Cdd:PRK04863 357 LEELEERL--------EEQNEVVEEADEQQEeNEARAEAAEEEVDELKSQ-----------LADYQQ---ALDVQQT-RA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1709 LAEQELLEATERVNLLhSQNTGLinQKKKMEADIAQLTTEVEEAVQECRNAEEK-----AKKAITDAAM-----MAEELK 1778
Cdd:PRK04863 414 IQYQQAVQALERAKQL-CGLPDL--TADNAEDWLEEFQAKEQEATEELLSLEQKlsvaqAAHSQFEQAYqlvrkIAGEVS 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1779 KEQDTSAHLERMKKNMEQTIKD-----LQMRLDEAEQialkgGKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYER 1853
Cdd:PRK04863 491 RSEAWDVARELLRRLREQRHLAeqlqqLRMRLSELEQ-----RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEA 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1854 RIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQyEEAEQQANSNLVKYRKVQHE-LDDAEERADIAETQVNKLRARS 1932
Cdd:PRK04863 566 RLESLSESVSEARERRMALRQQLEQLQARIQRLAAR-APAWLAAQDALARLREQSGEeFEDSQDVTEYMQQLLERERELT 644
|
...
gi 1394781870 1933 REV 1935
Cdd:PRK04863 645 VER 647
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1462-1859 |
7.42e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.66 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1462 AEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKtihELEKLKKTL 1541
Cdd:pfam07888 44 AELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE---ELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1542 ECEKSEIQAALEEAEGALEHEESKTLRIQLELNQVKADVDRKLAEKDEEfENLRRNHQRAMDSMQATLDAEAK----ARN 1617
Cdd:pfam07888 121 LAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE-EAERKQLQAKLQQTEEELRSLSKefqeLRN 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1618 ---EAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSqikdLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVE 1694
Cdd:pfam07888 200 slaQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRS----LQERLNASERKVEGLGEELSSMAAQRDRTQAELH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1695 ELRaaLEQAERGRKLAEQELLEATERVNLlHSQNTGLINQKKKMEADIAQLTTEV---EEAVQECRNAEEKAKKaitdaa 1771
Cdd:pfam07888 276 QAR--LQAAQLTLQLADASLALREGRARW-AQERETLQQSAEADKDRIEKLSAELqrlEERLQEERMEREKLEV------ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1772 mmaeELKKEQDTSahlermkknmeqtikdlqmrldeaeQIALKGGKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKY 1851
Cdd:pfam07888 347 ----ELGREKDCN-------------------------RVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQL 397
|
....*...
gi 1394781870 1852 ERRIKELT 1859
Cdd:pfam07888 398 EQRLETVA 405
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
854-983 |
7.74e-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: 49.15 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 854 EKEMATMKEEFQKLKEALEKSEAKRKELEEKqvtmIQEKNDLALQLQAEQDNLADAEE------RCDLLIKAKIQLEAKV 927
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELE----IEEVEARIKKYEEQLGNVRNNKEyealqkEIESLKRRISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 928 KELTERVEDEE----EINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKV 983
Cdd:COG1579 113 LELMERIEELEeelaELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1197-1955 |
8.13e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.11 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1197 AAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNK---ANAEKLCRtYEDQLNEAKSKVDE 1273
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQtalRQQEKIER-YQEDLEELTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1274 LQRQLADVSTQRARLqtesgelsrlleekesfinqltrgktsftqmiEELKRQLEEETKS-KNALAHALQAsrhdCDLLR 1352
Cdd:COG3096 366 QEEVVEEAAEQLAEA--------------------------------EARLEAAEEEVDSlKSQLADYQQA----LDVQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1353 E---QYEEEVEAKSELQR-----SLSKANAEvaQWRTKYETDAIQRTEELEEAKKKLAIrlqeaeeaveaahakcSSLEK 1424
Cdd:COG3096 410 TraiQYQQAVQALEKARAlcglpDLTPENAE--DYLAAFRAKEQQATEEVLELEQKLSV----------------ADAAR 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1425 TKHR----LQTEIEDlSIDLERANSAAAALDKKQRNFdRIIAEWKQKYEETQAELE---ASQKESRSLSTELFKLKNAYE 1497
Cdd:COG3096 472 RQFEkayeLVCKIAG-EVERSQAWQTARELLRRYRSQ-QALAQRLQQLRAQLAELEqrlRQQQNAERLLEEFCQRIGQQL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1498 ESLDNLETLKREnknLQEEIADLTDQISMSGKtiheleklkktlecEKSEIQAALEEAEgALEHEESKTLRIQLELNQVK 1577
Cdd:COG3096 550 DAAEELEELLAE---LEAQLEELEEQAAEAVE--------------QRSELRQQLEQLR-ARIKELAARAPAWLAAQDAL 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1578 AdvdrKLAEK-DEEFENLrrnhQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEiQLSHANrqAAEAQKMVR---- 1652
Cdd:COG3096 612 E----RLREQsGEALADS----QEVTAAMQQLLEREREATVERDELAARKQALESQIE-RLSQPG--GAEDPRLLAlaer 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1653 ---QLQSQIKDlQIELDDT---------MRHN---DDLKEQAAALERR----NNLLLAE------------VEEL----- 1696
Cdd:COG3096 681 lggVLLSEIYD-DVTLEDApyfsalygpARHAivvPDLSAVKEQLAGLedcpEDLYLIEgdpdsfddsvfdAEELedavv 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1697 --------------------RAALEQaeRGRKLAEQ--ELLE--ATERVNL-----LHSQNTGLINQKKKM------EAD 1741
Cdd:COG3096 760 vklsdrqwrysrfpevplfgRAAREK--RLEELRAErdELAEqyAKASFDVqklqrLHQAFSQFVGGHLAVafapdpEAE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1742 IAQLT---TEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLErmKKNMEQTIKDLQMRLDEAEQ----IALK 1814
Cdd:COG3096 838 LAALRqrrSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLA--DETLADRLEELREELDAAQEaqafIQQH 915
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1815 GgkKQIQKLEARVRELEG---ELDTEQKKTAEAQKGIRKYERRIKELT----------YQTEEDRknLARMQDLIDKLqt 1881
Cdd:COG3096 916 G--KALAQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALSevvqrrphfsYEDAVGL--LGENSDLNEKL-- 989
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394781870 1882 kvksyKRQYEEAEQQANSNLVKYRKVQHELDDAeeradiaeTQV-NKLRARSREVVITSKVLKTASLDIGVRLPD 1955
Cdd:COG3096 990 -----RARLEQAEEARREAREQLRQAQAQYSQY--------NQVlASLKSSRDAKQQTLQELEQELEELGVQADA 1051
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
953-1202 |
8.45e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 953 DECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQeahqqalDDLQAEEDKVNTLTKAK 1032
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE-------QELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1033 VKLEQQVDDLESSLEQekkiRMD-LERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQ 1111
Cdd:COG4942 93 AELRAELEAQKEELAE----LLRaLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1112 LQKKIKELQARIEELEEELEaeraaraKVEKQRAEVARELEELSERLEEAGGATAIQLEMNKKREAEFLKLRRDLEEATL 1191
Cdd:COG4942 169 LEAERAELEALLAELEEERA-------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
250
....*....|.
gi 1394781870 1192 QHESTAAALRK 1202
Cdd:COG4942 242 RTPAAGFAALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
982-1281 |
9.72e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 982 KVKNLIEEMAALDEVIAKLTKEKKALQEAHQ---------QALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSleqekki 1052
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDalqerrealQRLAEYSWDEIDVASAEREIAELEAELERLDAS------- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1053 RMDLERAKRKLEgdlkltqesvmDLENDKQQLEEKLKKKDFEMNQLNSRIEdqqvleaQLQKKIKELQARIEELEEELEA 1132
Cdd:COG4913 684 SDDLAALEEQLE-----------ELEAELEELEEELDELKGEIGRLEKELE-------QAEEELDELQDRLEAAEDLARL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1133 ERAARakVEKQRAEVARELEELSERLEEAGGATAIQLEMNkkreaeflKLRRDLEEATLQHESTAAALRKKHADSVAELS 1212
Cdd:COG4913 746 ELRAL--LEERFAAALGDAVERELRENLEERIDALRARLN--------RAEEELERAMRAFNREWPAETADLDADLESLP 815
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394781870 1213 EQIDNLQRVKQ-KLEKEKSEMKmevddlssniEYLTKN-KANAEKLCRTYEDQLNEAKSKVDELQRQLADV 1281
Cdd:COG4913 816 EYLALLDRLEEdGLPEYEERFK----------ELLNENsIEFVADLLSKLRRAIREIKERIDPLNDSLKRI 876
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
847-1089 |
9.80e-06 |
|
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: 50.06 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 847 LLRSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEEK---------QVTMIQEKNDLALQLQAEQDNLADAEERCDLLI 917
Cdd:pfam15742 99 VLKQAQSIKSQNSLQEKLAQEKSRVADAEEKILELQQKlehahkvclTDTCILEKKQLEERIKEASENEAKLKQQYQEEQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 918 KAKIQLEAKVKELTERVedeeeinSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEemaaLDEVI 997
Cdd:pfam15742 179 QKRKLLDQNVNELQQQV-------RSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQE----LSEKL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 998 AKLTKEKKALQEAHQQALDDLQAEEDKVNtltkakvkleqqvddlESSLEQEKKIRmdleRAKRKLEGDLKLTQESVMDL 1077
Cdd:pfam15742 248 SSLQQEKEALQEELQQVLKQLDVHVRKYN----------------EKHHHHKAKLR----RAKDRLVHEVEQRDERIKQL 307
|
250
....*....|....*
gi 1394781870 1078 END---KQQLEEKLK 1089
Cdd:pfam15742 308 ENEigiLQQQSEKEK 322
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1420-1665 |
9.97e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1420 SSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEASQKESRSLSTElfklknayees 1499
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE----------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1500 ldnLETLKRENKNLQEEIADLTDQISMSGKTiheleklkktleceksEIQAALEEAEGALEHEesKTLRIQLELNQVKAD 1579
Cdd:COG4942 92 ---IAELRAELEAQKEELAELLRALYRLGRQ----------------PPLALLLSPEDFLDAV--RRLQYLKYLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1580 VDRKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIK 1659
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
....*.
gi 1394781870 1660 DLQIEL 1665
Cdd:COG4942 231 RLEAEA 236
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1179-1736 |
1.02e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1179 FLKLRRDLEEATLQHESTAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYlTKNKANA-EKLC 1257
Cdd:pfam05483 199 FEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEE-SRDKANQlEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1258 RTYEDQLNEAKSKVDELQRQLAD--------VSTQRA---RLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKR- 1325
Cdd:pfam05483 278 KLQDENLKELIEKKDHLTKELEDikmslqrsMSTQKAleeDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEAt 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1326 --QLEEETKSKNalaHALQASRHDCDLLREQYEEEVEAKSELQRSLSKANAEVAQWRT--------KYETDAIQR-TEEL 1394
Cdd:pfam05483 358 tcSLEELLRTEQ---QRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKilaedeklLDEKKQFEKiAEEL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1395 EEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKkqrNFDRIIAEWKQKYEET--- 1471
Cdd:pfam05483 435 KGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA---HCDKLLLENKELTQEAsdm 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1472 -------QAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIH----ELEKLKKT 1540
Cdd:pfam05483 512 tlelkkhQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEyevlKKEKQMKI 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1541 LECEKSEIQAALEEAEGALE--HEESKTLR-------IQLELNQVKAD-VDRKLAEKDEEFENLRRNHQRAMD----SMQ 1606
Cdd:pfam05483 592 LENKCNNLKKQIENKNKNIEelHQENKALKkkgsaenKQLNAYEIKVNkLELELASAKQKFEEIIDNYQKEIEdkkiSEE 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1607 ATLDAEAKAR---NEAIRLRKkmegdlnEMEIQLSHA-NRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAAL 1682
Cdd:pfam05483 672 KLLEEVEKAKaiaDEAVKLQK-------EIDKRCQHKiAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAAL 744
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1394781870 1683 ERRNNLLLAEVEELRAALEqAERgrklaeqellEATERVNLLHSQNTGLINQKK 1736
Cdd:pfam05483 745 EIELSNIKAELLSLKKQLE-IEK----------EEKEKLKMEAKENTAILKDKK 787
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
903-1121 |
1.11e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 903 QDNLADAEERCDLLIKAKIQLEAKVKELTERVEDeeeinsdLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENK 982
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEE-------LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 983 VKNLIEEMAALDEVIAKLTkekkALQEAH--------QQALDDL-QAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIR 1053
Cdd:COG3883 88 LGERARALYRSGGSVSYLD----VLLGSEsfsdfldrLSALSKIaDADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394781870 1054 MDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQA 1121
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1306-1883 |
1.14e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.67 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1306 INQLTRGKTSFTQMIEELKrqleEETKSKNALAHALQASRHDCDLLREQYEEEVEAKSELQRSLSKANAEVAQWRTKYE- 1384
Cdd:PRK01156 161 INSLERNYDKLKDVIDMLR----AEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNn 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1385 -TDAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQtEIEDLSIDLERANSAAAALDKKQrnfdriIAE 1463
Cdd:PRK01156 237 lKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHM-KIINDPVYKNRNYINDYFKYKND------IEN 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1464 WKQKYEETQAELEASQKESRSLStELFKLKNAYEEsldnletLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLEC 1543
Cdd:PRK01156 310 KKQILSNIDAEINKYHAIIKKLS-VLQKDYNDYIK-------KKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1544 EKSEIQAALEEAEGALEHEESKTLRIQLELNQVKADVDR---KLAEKDEEFENLRRNHQRAMDSMqATLDAEAKARNEAI 1620
Cdd:PRK01156 382 YSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDissKVSSLNQRIRALRENLDELSRNM-EMLNGQSVCPVCGT 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1621 RLRKKMEGDLNEmeiqlsHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDL-KEQAAALERRNNLLlaevEELRAA 1699
Cdd:PRK01156 461 TLGEEKSNHIIN------HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLeSEEINKSINEYNKI----ESARAD 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1700 LEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVEeaVQECRNAEEKAKKAITDAAMMAEELKK 1779
Cdd:PRK01156 531 LEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLID--IETNRSRSNEIKKQLNDLESRLQEIEI 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1780 E-QDTSAHLERMKKNMEQTIKDLQMRLDEAEqiALKGGKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKEL 1858
Cdd:PRK01156 609 GfPDDKSYIDKSIREIENEANNLNNKYNEIQ--ENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKS 686
|
570 580
....*....|....*....|....*
gi 1394781870 1859 TYQTEEDRKNLARMQDLIDKLQTKV 1883
Cdd:PRK01156 687 RKALDDAKANRARLESTIEILRTRI 711
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1176-1338 |
1.20e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1176 EAEFLKLRRDLEEATLQHESTAAALRKKHADsVAELSEQIDNLQrvkQKLEKEKSEMKMEV------------------- 1236
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAEIAEAE---AEIEERREELGERAralyrsggsvsyldvllgs 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1237 ---DDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGK 1313
Cdd:COG3883 112 esfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
170 180
....*....|....*....|....*
gi 1394781870 1314 TSFTQMIEELKRQLEEETKSKNALA 1338
Cdd:COG3883 192 AAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1469-1825 |
1.45e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.96 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1469 EETQAELEASQKESRSLSTELFKLKNAYEESLD-NLETLKRENKNLQEEIADLTDQISMSGKTiHELEKLKKTLECEKse 1547
Cdd:COG5185 249 AQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNeNANNLIKQFENTKEKIAEYTKSIDIKKAT-ESLEEQLAAAEAEQ-- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1548 iqaaleEAEGALEHEESKTLRIQLELNQVKADVDRKLAEKDEEFENLRRNHQRAmdsmqatlDAEAKARNEAIRLRKKME 1627
Cdd:COG5185 326 ------ELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELS--------KSSEELDSFKDTIESTKE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1628 GDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELraALEQAERGR 1707
Cdd:COG5185 392 SLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEE--SQSRLEEAY 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1708 KLAEQELLEATERVNLLHSQntgLINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKE------Q 1781
Cdd:COG5185 470 DEINRSVRSKKEDLNEELTQ---IESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILalenliP 546
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1394781870 1782 DTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQIQKLEA 1825
Cdd:COG5185 547 ASELIQASNAKTDGQAANLRTAVIDELTQYLSTIESQQAREDPI 590
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
850-1038 |
1.54e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 850 SAQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERcdlLIKAKIQLEAKVKE 929
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 930 LTERV------------------------------------EDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVE 973
Cdd:COG3883 88 LGERAralyrsggsvsyldvllgsesfsdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394781870 974 KEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQ 1038
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1459-1664 |
1.78e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1459 RIIAEWKQKYEETQAEL--EASQKESRSLSTELFKLKNAYEESLDNLETLKRENK--NLQEEIADLTDQISMSGKTIHEL 1534
Cdd:COG3206 152 AVANALAEAYLEQNLELrrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1535 EKLKKTLECEKSEIQAALEEAEGAL----EHEESKTLRIQL-ELNQVKADVDRKLAEK-------DEEFENLRRNHQRAM 1602
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALpellQSPVIQQLRAQLaELEAELAELSARYTPNhpdvialRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1603 DSMQATLDAE---AKARNEAIR-----LRKKMEgDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIE 1664
Cdd:COG3206 312 QRILASLEAEleaLQAREASLQaqlaqLEARLA-ELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
861-1329 |
1.80e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 49.74 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 861 KEEFQKLKEALEKSEAKRKELEEKQVTMIQEKndlalqLQAEQDNLADAEERCDLLIKAKIQLEAKVKELTERVEDEEEI 940
Cdd:pfam05557 50 NQELQKRIRLLEKREAEAEEALREQAELNRLK------KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 941 NSDLTSKKRKLED---ECAELKKDIDDLEI---TLAKVEKEKHATENKVKNLIEEMA--ALDEVIAKLTKEKKALQEAHQ 1012
Cdd:pfam05557 124 ELELQSTNSELEElqeRLDLLKAKASEAEQlrqNLEKQQSSLAEAEQRIKELEFEIQsqEQDSEIVKNSKSELARIPELE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1013 QALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIR---MDLERAKRKLEGDLK----------LTQESVMDLEN 1079
Cdd:pfam05557 204 KELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYReeaATLELEKEKLEQELQswvklaqdtgLNLRSPEDLSR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1080 DKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVAR---------- 1149
Cdd:pfam05557 284 RIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKerdgyraile 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1150 -------ELEELSERLEEAGGATAIQLEMNKKREAEFLKLRRDLEEATLQHESTAAALR----KKHADSVAELS---EQI 1215
Cdd:pfam05557 364 sydkeltMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERelqaLRQQESLADPSyskEEV 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1216 DNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAkSKVDELQRQLADvstqraRLQTESGEL 1295
Cdd:pfam05557 444 DSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPA-AEAYQQRKNQLE------KLQAEIERL 516
|
490 500 510
....*....|....*....|....*....|....*...
gi 1394781870 1296 SRLLEEKESFINQLTRGKTSFTQMIE----ELKRQLEE 1329
Cdd:pfam05557 517 KRLLKKLEDDLEQVLRLPETTSTMNFkevlDLRKELES 554
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
740-1094 |
1.82e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.90 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 740 DDKFVDSRKATEKLLSSLDLDHTQFKFGHtkvFFKAGLLGHLEEMRDERLAKILTMLQARIRGrLMRIEyqKIISRRDAL 819
Cdd:PLN02939 95 DDHNRASMQRDEAIAAIDNEQQTNSKDGE---QLSDFQLEDLVGMIQNAEKNILLLNQARLQA-LEDLE--KILTEKEAL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 820 YTiQWNIRAFNVVKNWSWMKLffkikpllrSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEE---KQVTMIQEKN--- 893
Cdd:PLN02939 169 QG-KINILEMRLSETDARIKL---------AAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHslsKELDVLKEENmll 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 894 -DLALQLQAEQDNLADAEERCDLLIKAKIQLEAKVKELTERVEDEEEINSDLTSkkrkLEDECaeLKKDIDDLEITLAKv 972
Cdd:PLN02939 239 kDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSP----LQYDC--WWEKVENLQDLLDR- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 973 ekekhaTENKVKNLIEEMAALDEVIAKLTKEKKALQEAhqqalddlqaeedKVNTLTKAKVKLEQQvddlessleQEKKI 1052
Cdd:PLN02939 312 ------ATNQVEKAALVLDQNQDLRDKVDKLEASLKEA-------------NVSKFSSYKVELLQQ---------KLKLL 363
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1394781870 1053 RMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKDFE 1094
Cdd:PLN02939 364 EERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
963-1311 |
1.84e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 49.84 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 963 DDLEITLAKVEKEKHATENKVKNLIEEMA----ALDEVIAKLTKEKKALQEAH---QQALDDLQAEEDKVN-TLTKAKVK 1034
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVqangELEKASREETFARTALKNARldlRRLFDEKQSEKDKKNkALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1035 LEQQVDDLESSLEQ-EKKIRMDLERAKRKLegdlkltQESVMDLENDKQQLEEKLKkkdfemNQLNSRIEDQQVLEAQLQ 1113
Cdd:pfam12128 680 ANERLNSLEAQLKQlDKKHQAWLEEQKEQK-------REARTEKQAYWQVVEGALD------AQLALLKAAIAARRSGAK 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1114 KKIKELQARIEELEEELEAERAARAKVEKQRAEVAReleelserleeaggataiQLEMNKKREAEFLKLRRDLEEATLQH 1193
Cdd:pfam12128 747 AELKALETWYKRDLASLGVDPDVIAKLKREIRTLER------------------KIERIAVRRQEVLRYFDWYQETWLQR 808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1194 ESTAAALRKKHADSVAELSEQIDNLQ----RVKQKLEKEKSEMKMEVDDLSSNieyLTKNKANAEKLCRTYEDQ-LNEAK 1268
Cdd:pfam12128 809 RPRLATQLSNIERAISELQQQLARLIadtkLRRAKLEMERKASEKQQVRLSEN---LRGLRCEMSKLATLKEDAnSEQAQ 885
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1394781870 1269 SKVDELQRQLADVSTQRARLqteSGELSRLLEEKESFINQLTR 1311
Cdd:pfam12128 886 GSIGERLAQLEDLKLKRDYL---SESVKKYVEHFKNVIADHSG 925
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1046-1542 |
1.89e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1046 LEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKDFEMNQLNSRIEdqqvlEAQLQKKIKELQARIEE 1125
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE-----LEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1126 LeeeleaeraarakvekqraevareleelserleeaggataiqlemnKKREAEFLKLRRDLEEATLQHESTAAALRKKHA 1205
Cdd:COG4717 151 L----------------------------------------------EERLEELRELEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1206 DSVAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKlcrtyEDQLNEAKSKVDELQRQLADVSTQR 1285
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-----ELEAAALEERLKEARLLLLIAAALL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1286 ARLQTESGELSRLLEEKES----------FINQLTRGKTSFTQMIEELKRQLEEETKSKNALAHALQASRHDCDLLREQY 1355
Cdd:COG4717 260 ALLGLGGSLLSLILTIAGVlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1356 EEEVEAKSELQRSLSKANAEVAQWrtkyetdaiqRTEELEEAKKKLairLQEAEEAVEAAHAKCSSLEKTKHRLQTEIED 1435
Cdd:COG4717 340 LELLDRIEELQELLREAEELEEEL----------QLEELEQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEELEE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1436 LSIDLERANSAAAALdkkQRNFDRiiAEWKQKYEETQAELEASQKESRSLSTELFKLKNAYE--ESLDNLETLKRENKNL 1513
Cdd:COG4717 407 LEEQLEELLGELEEL---LEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEqlEEDGELAELLQELEEL 481
|
490 500
....*....|....*....|....*....
gi 1394781870 1514 QEEIADLTDQISMSGKTIHELEKLKKTLE 1542
Cdd:COG4717 482 KAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1787-1908 |
2.22e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.81 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1787 LERMKK-NMEQTIKDLQMRLDEAE------QIALKGGKKQIQKLEARVRELEGELDTEQKKTAEAQkgirkyeRRIKELT 1859
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEaersrlQALLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1394781870 1860 YQTEEDRKNLARMQDLIDKLQTKVKSYKRQYEEAEQQANSNLVkyRKVQ 1908
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALA--QRVQ 190
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1307-1802 |
2.33e-05 |
|
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: 49.57 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1307 NQLTRGKTSFTQMIEELKRQLEEETKSKNA---LAHALQASRHdcdllreqYEEEVEAKSELQRSLSKANAEvaQWRTKY 1383
Cdd:COG3096 241 NRMTLEAIRVTQSDRDLFKHLITEATNYVAadyMRHANERREL--------SERALELRRELFGARRQLAEE--QYRLVE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1384 ETDAIqrtEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRlQTEIEDLSIDLERANSaaaaldkkqrnfdrIIAE 1463
Cdd:COG3096 311 MAREL---EELSARESDLEQDYQAASDHLNLVQTALRQQEKIERY-QEDLEELTERLEEQEE--------------VVEE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1464 WKQKYEETQAELEASQKESRSLSTELFKlknaYEESLDNLETlkrenKNLQEEIAdltdqismsgktIHELEKLKKTLEC 1543
Cdd:COG3096 373 AAEQLAEAEARLEAAEEEVDSLKSQLAD----YQQALDVQQT-----RAIQYQQA------------VQALEKARALCGL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1544 EKSEIQAALEEAEGALEHEESKTLRIqLELNQVKADVDRKLAEKDEEFENLrrnhqRAMDSMQATLDAEAKARnEAIRL- 1622
Cdd:COG3096 432 PDLTPENAEDYLAAFRAKEQQATEEV-LELEQKLSVADAARRQFEKAYELV-----CKIAGEVERSQAWQTAR-ELLRRy 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1623 --RKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDtmrhNDDLKEQAAALErrnnlllAEVEELRAAL 1700
Cdd:COG3096 505 rsQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA----AEELEELLAELE-------AQLEELEEQA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1701 EQAERGRKLAEQELLEATERVNLLHSQNTGLInqkkKMEADIAQLTTEVEEAVQECRnaeekakkAITDAamMAEELKKE 1780
Cdd:COG3096 574 AEAVEQRSELRQQLEQLRARIKELAARAPAWL----AAQDALERLREQSGEALADSQ--------EVTAA--MQQLLERE 639
|
490 500
....*....|....*....|....*
gi 1394781870 1781 QDTSA---HLERMKKNMEQTIKDLQ 1802
Cdd:COG3096 640 REATVerdELAARKQALESQIERLS 664
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1170-1934 |
2.79e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 49.66 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1170 EMNKKREAEFLKLRrDLEEATLQ-HESTAAALRKKHADSVAELSEQIDNlqRVKQKLEKEKSEMKMEVDDLSSNIEYLTK 1248
Cdd:TIGR01612 700 DLKSKIDKEYDKIQ-NMETATVElHLSNIENKKNELLDIIVEIKKHIHG--EINKDLNKILEDFKNKEKELSNKINDYAK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1249 nkanaeklcrtYEDQLNEAKSKVDELQRQLADvstQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLE 1328
Cdd:TIGR01612 777 -----------EKDELNKYKSKISEIKNHYND---QINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKD 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1329 EETKSKNALAHALQASRHDCDLLREQYEEEVeakSELQRSLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLAIRLQEA 1408
Cdd:TIGR01612 843 DFLNKVDKFINFENNCKEKIDSEHEQFAELT---NKIKAEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKV 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1409 EEAVEAAHAKCSSLEK--TKHRLQTEIEDLSID-LERANSaaaaLDKKQRN-FDRIIAEWKQKYEETQAELEASQKESRs 1484
Cdd:TIGR01612 920 DEYIKICENTKESIEKfhNKQNILKEILNKNIDtIKESNL----IEKSYKDkFDNTLIDKINELDKAFKDASLNDYEAK- 994
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1485 lSTELFKLKNAYEESL---------DNLETLKRENKNLQEEIADLTDQISMSGKTIH--------ELEKL-KKTLECEKS 1546
Cdd:TIGR01612 995 -NNELIKYFNDLKANLgknkenmlyHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHtsiyniidEIEKEiGKNIELLNK 1073
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1547 EIqaaLEEAEGALEHeesktlriqleLNQVKADVDRKLAEKDEEFENLRRNhqramdsmqatlDAEAKARNEAIRLRKKM 1626
Cdd:TIGR01612 1074 EI---LEEAEINITN-----------FNEIKEKLKHYNFDDFGKEENIKYA------------DEINKIKDDIKNLDQKI 1127
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1627 EGDLNEMEiqlshanRQAAEAQKMVRQLQSQIKDLQiELDDTMRHNDDLKEqaaaLERRNNLLLAEV-------EELRAA 1699
Cdd:TIGR01612 1128 DHHIKALE-------EIKKKSENYIDEIKAQINDLE-DVADKAISNDDPEE----IEKKIENIVTKIdkkkniyDEIKKL 1195
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1700 LEQAERGRKlaEQELLEATERVNLLHSQNTGL-----INQKKK--------MEADIAQLtTEVEEAVQECRNaeEKAKKA 1766
Cdd:TIGR01612 1196 LNEIAEIEK--DKTSLEEVKGINLSYGKNLGKlflekIDEEKKksehmikaMEAYIEDL-DEIKEKSPEIEN--EMGIEM 1270
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1767 ITDAAMMAEELKKEQDTSAHLerMKKNMEQTIKD-----LQMRLDEAEQIALKGGKKQIQKLEARVRELEGELDTEQKKT 1841
Cdd:TIGR01612 1271 DIKAEMETFNISHDDDKDHHI--ISKKHDENISDireksLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEI 1348
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1842 AEAQ-----KGIRKYERRIKELTYQTEEDRKNLarmQDLIDKLQTKVKSYKRqyeeaeqqaNSNLVKYR-KVQHELDDAE 1915
Cdd:TIGR01612 1349 ANIYnilklNKIKKIIDEVKEYTKEIEENNKNI---KDELDKSEKLIKKIKD---------DINLEECKsKIESTLDDKD 1416
|
810
....*....|....*....
gi 1394781870 1916 ERADIAETQVNKLRARSRE 1934
Cdd:TIGR01612 1417 IDECIKKIKELKNHILSEE 1435
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1497-1707 |
2.85e-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: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1497 EESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHEESKtLRIQLELNQV 1576
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE-LGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1577 KADVDRKL-----AEKDEEFenLRRNH--QRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQK 1649
Cdd:COG3883 98 SGGSVSYLdvllgSESFSDF--LDRLSalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1394781870 1650 MVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGR 1707
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
841-1295 |
3.83e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.68 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 841 FFKIKPLLRSAQ-----TEKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEkndlalqLQAEQDNLADAEErcdl 915
Cdd:PRK04778 100 FRKAKHEINEIEslldlIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKS-------LLANRFSFGPALD---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 916 likakiQLEAKVKELTERVEDEEEINSD---LTSKK--RKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKN----L 986
Cdd:PRK04778 169 ------ELEKQLENLEEEFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 987 IEEMAALDEViaKLTKEKKALQEAHQQALDDLQAEEdkvntLTKAKVKLEQ---QVDDLESSLEQEKKIRMDLERAKRKL 1063
Cdd:PRK04778 243 VEEGYHLDHL--DIEKEIQDLKEQIDENLALLEELD-----LDEAEEKNEEiqeRIDQLYDILEREVKARKYVEKNSDTL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1064 EGDLKLTQEsvmdlENDKQQLEEKLKKKDFEMNqlNSRIEDQQvleaQLQKKIKELQARIeeleeeleaeRAARAKVEKQ 1143
Cdd:PRK04778 316 PDFLEHAKE-----QNKELKEEIDRVKQSYTLN--ESELESVR----QLEKQLESLEKQY----------DEITERIAEQ 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1144 RAEvareleelserleeaggATAIQlemnkkreAEFLKLRRDLEEATLQHES---TAAALRKkhADSVAElseqiDNLQR 1220
Cdd:PRK04778 375 EIA-----------------YSELQ--------EELEEILKQLEEIEKEQEKlseMLQGLRK--DELEAR-----EKLER 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1221 VKQKLEKEKSEMKmevddlSSN--------IEYLTKNKANAEKLcrtyEDQLNEAKSKVDELQRQLADVSTQRARLQTES 1292
Cdd:PRK04778 423 YRNKLHEIKRYLE------KSNlpglpedyLEMFFEVSDEIEAL----AEELEEKPINMEAVNRLLEEATEDVETLEEET 492
|
...
gi 1394781870 1293 GEL 1295
Cdd:PRK04778 493 EEL 495
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1493-1911 |
3.90e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.68 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1493 KNAYEEsLDNLETLKRE--NKNLQEEIADLtDQISMSGKTIHELEKLKK---TLECEK-SEIQAALEEAEGALEheESKT 1566
Cdd:PRK04778 25 KRNYKR-IDELEERKQEleNLPVNDELEKV-KKLNLTGQSEEKFEEWRQkwdEIVTNSlPDIEEQLFEAEELND--KFRF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1567 LRIQLELNQVKADVDrkLAEKD-----EEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLR-------KKMEGDLNEME 1634
Cdd:PRK04778 101 RKAKHEINEIESLLD--LIEEDieqilEELQELLESEEKNREEVEQLKDLYRELRKSLLANRfsfgpalDELEKQLENLE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1635 IQLSHANRQAA-----EAQKMVRQLQSQIKDLQielddtmrhnDDLKEQAAALERRNNLLLAEVEELRAALEQ-AERGRK 1708
Cdd:PRK04778 179 EEFSQFVELTEsgdyvEAREILDQLEEELAALE----------QIMEEIPELLKELQTELPDQLQELKAGYRElVEEGYH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1709 LAEQELLEATERVNllhsqntgliNQKKKMEADIAQLttEVEEAVQECRNAEE-------------KAKKaitdaammae 1775
Cdd:PRK04778 249 LDHLDIEKEIQDLK----------EQIDENLALLEEL--DLDEAEEKNEEIQEridqlydilerevKARK---------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1776 ELKKEQDT-SAHLERMKKNMEQTIKDLQM-----RLDEAEQIALKGGKKQIQKLEARVRELEGELDTEQKKTAEAQKgir 1849
Cdd:PRK04778 307 YVEKNSDTlPDFLEHAKEQNKELKEEIDRvkqsyTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQE--- 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394781870 1850 kyerrikeltyQTEEDRKNLARMQDLIDKLQTKVKSykrqYEEAEQQANSNLVKYRKVQHEL 1911
Cdd:PRK04778 384 -----------ELEEILKQLEEIEKEQEKLSEMLQG----LRKDELEAREKLERYRNKLHEI 430
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
773-1118 |
3.91e-05 |
|
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: 48.79 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 773 FKAGLLGHLEEMRDERLAKILTMLQ-ARIRGRLMRIEYQK--IISRRDALytIQWNIRAFNVVKNWSWMKLFF----KIK 845
Cdd:pfam15818 5 FKTSLLEALEELRMRREAETQYEEQiGKIIVETQELKWQKetLQNQKETL--AKQHKEAMAVFKKQLQMKMCAleeeKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 846 PLLRSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLIKAKIQLEA 925
Cdd:pfam15818 83 YQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLHLLAKEDHHKQLNEIEKYYATITGQFGLVKENHGKLEQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 926 KVKELTErvedeeeINSDLTSKKRKLEDECAELKKDIDDLEITLAKVE---KEKHATEN--------KVKNLIEEMAALD 994
Cdd:pfam15818 163 NVQEAIQ-------LNKRLSALNKKQESEICSLKKELKKVTSDLIKSKvtcQYKMGEENinltikeqKFQELQERLNMEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 995 EVIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEqqvddleSSLEQEKKIRMDLERAKRKLEGDLKLTQESV 1074
Cdd:pfam15818 236 ELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEME-------AELKALKENNQTLERDNELQREKVKENEEKF 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1394781870 1075 MDLENDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKE 1118
Cdd:pfam15818 309 LNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQE 352
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1271-1544 |
4.09e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.99 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1271 VDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKSKNALAHALQASRHDCDL 1350
Cdd:pfam00038 56 IEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAF 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1351 LREQYEEEVeakSELQRSLSKANAEVaqwrtkyETDAIqRTEELEEAKKKlaIRLQEAEEAVEaahakcsSLEKTKHRLQ 1430
Cdd:pfam00038 136 LKKNHEEEV---RELQAQVSDTQVNV-------EMDAA-RKLDLTSALAE--IRAQYEEIAAK-------NREEAEEWYQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1431 TEIEDLSIDLERaNSAAAALDKKQrnfdriIAEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNletLKREN 1510
Cdd:pfam00038 196 SKLEELQQAAAR-NGDALRSAKEE------ITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLAD---YQELI 265
|
250 260 270
....*....|....*....|....*....|....
gi 1394781870 1511 KNLQEEIADLTDQISMSGKTIHELEKLKKTLECE 1544
Cdd:pfam00038 266 SELEAELQETRQEMARQLREYQELLNVKLALDIE 299
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1758-1943 |
4.50e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1758 NAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEqIALKGGKKQIQKLEARVRELE---GEL 1834
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEIS-SELPELREELEKLEKEVKELEelkEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1835 DTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLqTKVKSYKRQYEEAEQQANSNLVKYRKVQHELDDA 1914
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170 180
....*....|....*....|....*....
gi 1394781870 1915 EERADIAETQVNKLRARSREVVITSKVLK 1943
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLK 348
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1694-1934 |
4.53e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1694 EELRAALEQA-------ERgRKLAEQELLEATE---RVNLLHsqntglinqkKKMEADIAQLTTEVEEAV--QECRNAEE 1761
Cdd:TIGR02168 155 EERRAIFEEAagiskykER-RKETERKLERTREnldRLEDIL----------NELERQLKSLERQAEKAEryKELKAELR 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1762 KAKKAItdAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQMRLDEAEQialkggkkQIQKLEARVRELEGELDTEQKKT 1841
Cdd:TIGR02168 224 ELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEELRLEVSELEEEIEELQKEL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1842 AEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLI-------DKLQTKVKSYKRQYEEAEQQANSNLVKYRKVQHELDDA 1914
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLeelesklDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
250 260
....*....|....*....|
gi 1394781870 1915 EERADIAETQVNKLRARSRE 1934
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQ 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1387-1619 |
4.56e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1387 AIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQ 1466
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1467 KYEETQAELE----ASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLE 1542
Cdd:COG4942 98 ELEAQKEELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1543 CEKSEIQ---AALEEAegaleheesktlriQLELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEA 1619
Cdd:COG4942 178 ALLAELEeerAALEAL--------------KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
855-1021 |
4.73e-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: 46.84 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 855 KEMATMKEEFQKLKEALEKSEAKRKELEEkqvtmiqEKNDLALQLQAEQDNLADAEERCDLLIKAKiQLEAKVKELTerv 934
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEK-------EIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQKEIE--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 935 edeeeinsDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKhatENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQA 1014
Cdd:COG1579 100 --------SLKRRISDLEDEILELMERIEELEEELAELEAEL---AELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
....*..
gi 1394781870 1015 LDDLQAE 1021
Cdd:COG1579 169 AAKIPPE 175
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1757-1898 |
4.74e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1757 RNAEEKAKKAITDAAMMAEELKKEQDTSA---------HLERMKKNMEQTIKDLQMRLDEAEQIaLKGGKKQIQKLEARV 1827
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAkeeihklrnEFEKELRERRNELQKLEKRLLQKEEN-LDRKLELLEKREEEL 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394781870 1828 RELEGELDTEQ----KKTAEAQKGIRKYERRIKELTYQTEEDRKNLArMQDLIDKLQTKVKSYKRQYE-EAEQQAN 1898
Cdd:PRK12704 113 EKKEKELEQKQqeleKKEEELEELIEEQLQELERISGLTAEEAKEIL-LEKVEEEARHEAAVLIKEIEeEAKEEAD 187
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
950-1560 |
4.81e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.89 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 950 KLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLT---------KEKKALQEAHQQALDDLQA 1020
Cdd:TIGR01612 1108 KYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVAdkaisnddpEEIEKKIENIVTKIDKKKN 1187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1021 EEDKVNTLTKAKVKLEQQvddlESSLEQEKKIRMD------------LERAKRKLEGDLKLTQESVMDLENDKQQLEEKL 1088
Cdd:TIGR01612 1188 IYDEIKKLLNEIAEIEKD----KTSLEEVKGINLSygknlgklflekIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIE 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1089 KKKDFEM---------NQLNSRIEDQQVLEAQLQKKIKELQARieeleeeleaeraarakvekqraevareleelserle 1159
Cdd:TIGR01612 1264 NEMGIEMdikaemetfNISHDDDKDHHIISKKHDENISDIREK------------------------------------- 1306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1160 eaggatAIQLEMNKKREAEFLKLRRDLEEATLQHEstaaalrkKHADSVAELSEQIDNLQRVkQKLEKEKSEMKmEVDDL 1239
Cdd:TIGR01612 1307 ------SLKIIEDFSEESDINDIKKELQKNLLDAQ--------KHNSDINLYLNEIANIYNI-LKLNKIKKIID-EVKEY 1370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1240 SSNIEYLTKN----KANAEKLCRTYEDQLN--EAKSKVD------ELQRQLADVSTQRARLQTESGELS----------- 1296
Cdd:TIGR01612 1371 TKEIEENNKNikdeLDKSEKLIKKIKDDINleECKSKIEstlddkDIDECIKKIKELKNHILSEESNIDtyfknadenne 1450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1297 ---------RLLEEKESFI--NQLTRGKTSFTQMIEELKRQLEEETKSKNALAHALQASRHDCDLLrEQYEEEVeakSEL 1365
Cdd:TIGR01612 1451 nvlllfkniEMADNKSQHIlkIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELF-EQYKKDV---TEL 1526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1366 QRSLSKANAEVAQWRTKYETDAIqrTEELEEAKKKLAIRLQeaeeaveAAHAKCSSLEKTKHRlqteIEDLSIDLERANS 1445
Cdd:TIGR01612 1527 LNKYSALAIKNKFAKTKKDSEII--IKEIKDAHKKFILEAE-------KSEQKIKEIKKEKFR----IEDDAAKNDKSNK 1593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1446 AAAALDKKQRNFDR---IIAEWKQKYEETQAELEASQKESRSLS-----TELFKLKNAYEESLDNLETLKRENKNLQEEI 1517
Cdd:TIGR01612 1594 AAIDIQLSLENFENkflKISDIKKKINDCLKETESIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQKKNIEDKK 1673
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1394781870 1518 ADLtDQISMSGKTIHE-------------LEKLKKTLECEKSEIQAALEEAEGALE 1560
Cdd:TIGR01612 1674 KEL-DELDSEIEKIEIdvdqhkknyeigiIEKIKEIAIANKEEIESIKELIEPTIE 1728
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
929-1344 |
5.83e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 47.75 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 929 ELTERVEDEEEINSDLTSKKRKLEDECAEL---KKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKK 1005
Cdd:pfam19220 14 EMADRLEDLRSLKADFSQLIEPIEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1006 ALQEAHQQAldDLQAEEDKVNTLTKakvklEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLE 1085
Cdd:pfam19220 94 KLEAALREA--EAAKEELRIELRDK-----TAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1086 EKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKEL--QARIEELEEELEAERAARAKVEKQRAEVAReleelserleeagg 1163
Cdd:pfam19220 167 ERLALLEQENRRLQALSEEQAAELAELTRRLAELetQLDATRARLRALEGQLAAEQAERERAEAQL-------------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1164 ataiqlemnkkreaeflklrrDLEEATLQHESTAAALRKKHADSVAELSEQIdnLQRVKQKLeKEKSEMKMEVDdlssni 1243
Cdd:pfam19220 233 ---------------------EEAVEAHRAERASLRMKLEALTARAAATEQL--LAEARNQL-RDRDEAIRAAE------ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1244 eyltKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEEL 1323
Cdd:pfam19220 283 ----RRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAEL 358
|
410 420
....*....|....*....|.
gi 1394781870 1324 KRQLEEETKSKNALAHALQAS 1344
Cdd:pfam19220 359 TKRFEVERAALEQANRRLKEE 379
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
852-1065 |
6.12e-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: 47.97 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 852 QTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQvtmiQEKNDLALQLQAEQDNLADAEERCDLLIKakiQLEAKVKELT 931
Cdd:pfam07888 70 QWERQRRELESRVAELKEELRQSREKHEELEEKY----KELSASSEELSEEKDALLAQRAAHEARIR---ELEEDIKTLT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 932 ERVEDEEeinSDLTSKKRKLEDECAELKKDiddleitlakvEKEKHATENKVKNLIEEMaaldeviAKLTKEKKALQEAH 1011
Cdd:pfam07888 143 QRVLERE---TELERMKERAKKAGAQRKEE-----------EAERKQLQAKLQQTEEEL-------RSLSKEFQELRNSL 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1394781870 1012 QQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEG 1065
Cdd:pfam07888 202 AQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG 255
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1617-1934 |
6.81e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.97 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1617 NEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNddlKEQAAALERRNNL------LL 1690
Cdd:PLN02939 93 SDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLN---QARLQALEDLEKIltekeaLQ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1691 AEVEELRAALEQAERGRKLAEQELLeateRVNLLHSQntgLINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDA 1770
Cdd:PLN02939 170 GKINILEMRLSETDARIKLAAQEKI----HVEILEEQ---LEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDI 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1771 AMMAEELKKEQDTS---AHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQIQKLEARVRELEGELDTEQKKTAEAQ-- 1845
Cdd:PLN02939 243 QFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAAlv 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1846 -KGIRKYERRIKELTYQTEEdrKNLARMQ-DLIDKLQTKVKSYKRQYEEAEQQANSNLVKYRkvqhelDDAEERADIAET 1923
Cdd:PLN02939 323 lDQNQDLRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKLLEERLQASDHEIHSYIQLYQ------ESIKEFQDTLSK 394
|
330
....*....|.
gi 1394781870 1924 QVNKLRARSRE 1934
Cdd:PLN02939 395 LKEESKKRSLE 405
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
862-1093 |
7.15e-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: 47.84 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 862 EEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEErCDLLIKAKIQLEAKVKELTERVEDeeeIN 941
Cdd:pfam18971 610 DEVKKAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKDE-IFALINKEANRDARAIAYTQNLKG---IK 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 942 SDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQALDDLqae 1021
Cdd:pfam18971 686 RELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGINPEWISKVENLNAALNEFKNGKNKDF--- 762
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394781870 1022 edkvNTLTKAKVKLEQQVDDLESSLEQEKKI-RMDLERAKRKLEGDLKLTQESVMDLEN-DKQQLEEKLKK-KDF 1093
Cdd:pfam18971 763 ----SKVTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKNfSKEQLAQQAQKnEDF 833
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1634-1915 |
7.24e-05 |
|
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: 47.70 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1634 EIQLSHANRQAAEAQKMVRQLQSQIK--------DLQIELDDTMRhnDDLKEQAAALERRNNLLLAEV-EELRAALEQAE 1704
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDkrkhtqnvALNKKLSDIKT--EYLYELNVLKEKSEAELTSKTkKELDAAFEQFK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1705 RGRKLAEQELLEATERVNLLHSQNTGL---------INQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAE 1775
Cdd:NF033838 132 KDTLEPGKKVAEATKKVEEAEKKAKDQkeedrrnypTNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQAKA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1776 ELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKG--GKKQIQKLEARV-RELEGELDTE--------------- 1837
Cdd:NF033838 212 KVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKnvATSEQDKPKRRAkRGVLGEPATPdkkendakssdssvg 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1838 -----------QKKTAEAQKGIRKYERRIKEltyQTEEDRKNLA--RMQDL---IDKLQTKVKSYKRQY--EEAEQQANS 1899
Cdd:NF033838 292 eetlpspslkpEKKVAEAEKKVEEAKKKAKD---QKEEDRRNYPtnTYKTLeleIAESDVKVKEAELELvkEEAKEPRNE 368
|
330
....*....|....*.
gi 1394781870 1900 NLVKYRKVQHELDDAE 1915
Cdd:NF033838 369 EKIKQAKAKVESKKAE 384
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
977-1231 |
7.55e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 977 HATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDL 1056
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1057 ERAKRKLEGDLKlTQESVMDLENDKQQLEEKLKKKDFemNQLNSRIEDQQVLEAQLQKKIKEL---QARIEELEEEleae 1133
Cdd:COG4942 96 RAELEAQKEELA-ELLRALYRLGRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELradLAELAALRAE---- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1134 raarakVEKQRAEVareleelserleeaggataiqlemnKKREAEFLKLRRDLEEATLQHESTAAALRKK---HADSVAE 1210
Cdd:COG4942 169 ------LEAERAEL-------------------------EALLAELEEERAALEALKAERQKLLARLEKElaeLAAELAE 217
|
250 260
....*....|....*....|.
gi 1394781870 1211 LSEQIDNLQRVKQKLEKEKSE 1231
Cdd:COG4942 218 LQQEAEELEALIARLEAEAAA 238
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
898-1105 |
7.70e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 47.38 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 898 QLQAEQDNLADAEercdlliKAKIQLEAKVKELTERVEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKH 977
Cdd:PRK11637 48 QLKSIQQDIAAKE-------KSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 978 ATEnkvKNLIEEMAAldeviAKLTKEKKALQ-----EAHQQALDDL-------QAEEDKVNTLTKAKVKLEQQVDDLESS 1045
Cdd:PRK11637 121 AQE---RLLAAQLDA-----AFRQGEHTGLQlilsgEESQRGERILayfgylnQARQETIAELKQTREELAAQKAELEEK 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394781870 1046 LEQEKKIRMDLERAKRKLEGDLKLTQESVMDLEN----DKQQLEeklkkkdfEMNQLNSRIEDQ 1105
Cdd:PRK11637 193 QSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESslqkDQQQLS--------ELRANESRLRDS 248
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1558-1696 |
7.90e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.27 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1558 ALEHEESKTLRIQLELNQVKADVDRKLAEKDEefenlrrnhqramdsMQATLDAEAKARNEAIRLRKKMEGDLNEmEIQL 1637
Cdd:PRK09039 68 LLSLERQGNQDLQDSVANLRASLSAAEAERSR---------------LQALLAELAGAGAAAEGRAGELAQELDS-EKQV 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394781870 1638 SH-ANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLA-EVEEL 1696
Cdd:PRK09039 132 SArALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAqRVQEL 192
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
849-1006 |
8.78e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 8.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 849 RSAQTEKEMATM--KEEFQKLKEALEK-SEAKRKELEEKQVTMIQEKNdlalQLQAEQDNLADAEERcdlLIKAKIQLEA 925
Cdd:PRK12704 49 KEAEAIKKEALLeaKEEIHKLRNEFEKeLRERRNELQKLEKRLLQKEE----NLDRKLELLEKREEE---LEKKEKELEQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 926 KVKELTERvedEEEINSDLTSKKRKLEdECAELKKDiDDLEITLAKVEKE-KHATENKVKNLIEEmaaldeviAKLTKEK 1004
Cdd:PRK12704 122 KQQELEKK---EEELEELIEEQLQELE-RISGLTAE-EAKEILLEKVEEEaRHEAAVLIKEIEEE--------AKEEADK 188
|
..
gi 1394781870 1005 KA 1006
Cdd:PRK12704 189 KA 190
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
847-1121 |
1.02e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 847 LLRSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLIKakiQLEAK 926
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLN---EVKTS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 927 VKELTERVEDEEEInsdltskKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNlieeMAALDEVIAKLTKEKKA 1006
Cdd:pfam15921 666 RNELNSLSEDYEVL-------KRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS----MEGSDGHAMKVAMGMQK 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1007 LQEAHQQALDDLQAE----EDKVNTLTKAKVKLEQQVDDLESSLEQekkirmdLERAKRKLEGDLKLTQESVMDLENDKQ 1082
Cdd:pfam15921 735 QITAKRGQIDALQSKiqflEEAMTNANKEKHFLKEEKNKLSQELST-------VATEKNKMAGELEVLRSQERRLKEKVA 807
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1394781870 1083 QLEEKLKKKDFEMNQLNSRIEDQQV----LEAQLQKKIKELQA 1121
Cdd:pfam15921 808 NMEVALDKASLQFAECQDIIQRQEQesvrLKLQHTLDVKELQG 850
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1461-1930 |
1.03e-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: 47.43 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1461 IAEWKQKYEETQAELEASQKESRSlstELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKT 1540
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKR---ARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1541 LECEKSEIQAALEEAEGALE--HEESKTLRIQL-ELNQVKADVDRKLAEKDEEFENLRRNHQramdsMQATLDAEAKARN 1617
Cdd:pfam05557 81 KKKYLEALNKKLNEKESQLAdaREVISCLKNELsELRRQIQRAELELQSTNSELEELQERLD-----LLKAKASEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1618 EAI----RLRKKMEGDLNEMEIQLSHANRQAAEAQKMvRQLQSQIKDLQIELDDTMRHNDDLKEqaaaLERRNNLLLAEV 1693
Cdd:pfam05557 156 QNLekqqSSLAEAEQRIKELEFEIQSQEQDSEIVKNS-KSELARIPELEKELERLREHNKHLNE----NIENKLLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1694 EELRAALEQAERGRKLA----------EQELLE-----------------ATERVNLLHSQNTGLINQKKKMEADIAQLT 1746
Cdd:pfam05557 231 EDLKRKLEREEKYREEAatlelekeklEQELQSwvklaqdtglnlrspedLSRRIEQLQQREIVLKEENSSLTSSARQLE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1747 TEVEEAVQECRNAEEKakkaITDAAMMAEELK--------------KEQD-TSAHLERMKK--NMEQTIKDLQMRLDEAE 1809
Cdd:pfam05557 311 KARRELEQELAQYLKK----IEDLNKKLKRHKalvrrlqrrvllltKERDgYRAILESYDKelTMSNYSPQLLERIEEAE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1810 QIALKGgKKQIQKLEARVRELEGELDT--EQKKTAEAQKGIRKYERRIKELTYQTEED---RKNLARMQDLIDKLQTKVK 1884
Cdd:pfam05557 387 DMTQKM-QAHNEEMEAQLSVAEEELGGykQQAQTLERELQALRQQESLADPSYSKEEVdslRRKLETLELERQRLREQKN 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1394781870 1885 SYKRQYEEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRA 1930
Cdd:pfam05557 466 ELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQA 511
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1667-1968 |
1.13e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 47.62 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1667 DTMRHNDDLKEQAAALERRNN--------LLLAEVEELRAALEQaergrkLAEQELLEATERVNLLHSQNTglinqkkkM 1738
Cdd:PLN03188 961 EVLRTKIELKRVQDELEHYRNfydmgereVLLEEIQDLRSQLQY------YIDSSLPSARKRNSLLKLTYS--------C 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1739 EADIAQLTTEVEEAVQECrnAEEKAKK-------AITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQI 1811
Cdd:PLN03188 1027 EPSQAPPLNTIPESTDES--PEKKLEQerlrwteAESKWISLAEELRTELDASRALAEKQKHELDTEKRCAEELKEAMQM 1104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1812 ALKGGKKQIQK----------LEARVRELEGELDTEQKktAEAQKGIRKYERR--------IKELTYQTEEDRKNLarmQ 1873
Cdd:PLN03188 1105 AMEGHARMLEQyadleekhiqLLARHRRIQEGIDDVKK--AAARAGVRGAESKfinalaaeISALKVEREKERRYL---R 1179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1874 DLIDKLQTKVksykRQYEEAEQQANSNLVKYRKVQHELDDAEERADIAE-------TQVNKLRARSREVVITSKVLKTAS 1946
Cdd:PLN03188 1180 DENKSLQAQL----RDTAEAVQAAGELLVRLKEAEEALTVAQKRAMDAEqeaaeayKQIDKLKRKHENEISTLNQLVAES 1255
|
330 340
....*....|....*....|....
gi 1394781870 1947 ldigvRLPD--ISSVVNTSSDGKY 1968
Cdd:PLN03188 1256 -----RLPKeaIRPACNDDCMAKY 1274
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1428-1598 |
1.31e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1428 RLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEA--SQKESRSLSTElfklknayeesldnLET 1505
Cdd:COG1579 35 ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKE--------------IES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1506 LKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHEESKtlrIQLELNQVKADVDRKLA 1585
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE---LEAEREELAAKIPPELL 177
|
170
....*....|...
gi 1394781870 1586 EKdeeFENLRRNH 1598
Cdd:COG1579 178 AL---YERIRKRK 187
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1208-1403 |
1.32e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1208 VAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRar 1287
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1288 lqtesgELSRLLEEKESfinqLTRGKTSFTQMIEELKRQLEEETKSKNALAHALQASRHDCDLLREQYEEEVEaksELQR 1367
Cdd:COG1579 90 ------EYEALQKEIES----LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA---ELEA 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1394781870 1368 SLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLAI 1403
Cdd:COG1579 157 ELEELEAEREELAAKIPPELLALYERIRKRKNGLAV 192
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1761-1933 |
1.36e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1761 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIalkggkKQIQKLEARVRELEGELDTEQKK 1840
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1841 TAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTK----VKSYKRQYEEAEQQANSNLVKYRKVQHELDDAEE 1916
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAteeeLQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170
....*....|....*..
gi 1394781870 1917 RADIAETQVNKLRARSR 1933
Cdd:COG4717 228 ELEQLENELEAAALEER 244
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
847-1010 |
1.41e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 847 LLRSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKndlALQLQAEQDNLADAEERCDLLIKAKIQLEAK 926
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE---LEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 927 VKELTERVEDEEEinsdltskkrkLEDECAELKKDIDDL-------EITLAKVEKEKHATENKVKNLIEEMAALDEVIAK 999
Cdd:COG1196 752 ALEELPEPPDLEE-----------LERELERLEREIEALgpvnllaIEEYEELEERYDFLSEQREDLEEARETLEEAIEE 820
|
170
....*....|..
gi 1394781870 1000 LTKEKK-ALQEA 1010
Cdd:COG1196 821 IDRETReRFLET 832
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1775-1935 |
1.46e-04 |
|
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: 46.97 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1775 EELKKEQDTSAHLERMK---KNMEQTIKDLQMRLDEAEQ-IALKGGKKQIQK--LEARVRELEGELDTEQKKTAEAQKGI 1848
Cdd:TIGR02168 176 ETERKLERTRENLDRLEdilNELERQLKSLERQAEKAERyKELKAELRELELalLVLRLEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1849 RKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQYEEAEQQ-------ANSNLVKYRKVQHELDDAEERADIA 1921
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerLANLERQLEELEAQLEELESKLDEL 335
|
170
....*....|....
gi 1394781870 1922 ETQVNKLRARSREV 1935
Cdd:TIGR02168 336 AEELAELEEKLEEL 349
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1710-1899 |
1.61e-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: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1710 AEQELLEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT-SAHLE 1788
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1789 RMKKNMEQT-----------IKDLQMRLDEAEQIAlKGGKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKE 1857
Cdd:COG3883 94 ALYRSGGSVsyldvllgsesFSDFLDRLSALSKIA-DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1394781870 1858 LTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQYEEAEQQANS 1899
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1261-1488 |
1.95e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1261 EDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKSKNALAHA 1340
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1341 LQASRHDCDLLreqyEEEVEAKS--------ELQRSLSKANAEVAQwrtkyetDAIQRTEELEEAKKKLAIRLQEAEEAV 1412
Cdd:COG3883 95 LYRSGGSVSYL----DVLLGSESfsdfldrlSALSKIADADADLLE-------ELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394781870 1413 EAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEASQKESRSLSTE 1488
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1440-1617 |
2.37e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1440 LERANSAAAALDKKqrnfdrIIAEWKQKYEETQAELEasqKESRSLSTELFKLKNA---YEESLDN-LETLKRENKNLQE 1515
Cdd:PRK12704 44 LEEAKKEAEAIKKE------ALLEAKEEIHKLRNEFE---KELRERRNELQKLEKRllqKEENLDRkLELLEKREEELEK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1516 EIADLTdqismsgKTIHELEKLKKTLECEKSEIQAALEEAEGaLEHEESKtlriQLELNQVKADVDRKLAEKDEEFENlr 1595
Cdd:PRK12704 115 KEKELE-------QKQQELEKKEEELEELIEEQLQELERISG-LTAEEAK----EILLEKVEEEARHEAAVLIKEIEE-- 180
|
170 180
....*....|....*....|..
gi 1394781870 1596 rnhqramdsmQATLDAEAKARN 1617
Cdd:PRK12704 181 ----------EAKEEADKKAKE 192
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
967-1214 |
2.45e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 967 ITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSL 1046
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1047 EqekkirmdlERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEEL 1126
Cdd:COG3883 89 G---------ERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1127 EEELEAERAARAKVEKQRAEVARELEELSERLEEAGGATAIQLEMNKKREAEFLKLRRDLEEATLQHESTAAALRKKHAD 1206
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
....*...
gi 1394781870 1207 SVAELSEQ 1214
Cdd:COG3883 240 AAAAASAA 247
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1221-1657 |
2.48e-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: 46.35 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1221 VKQKLEKEKSEMKMevddLSSNIEYLTknkanaeklcrtyeDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLE 1300
Cdd:pfam10174 294 LKQELSKKESELLA----LQTKLETLT--------------NQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1301 EKESFINQ-------LTRGKTSFTQMIEELKRQLEEETKSKNALA---HALQASRHDCDLLREQYEEEVE---------- 1360
Cdd:pfam10174 356 EKESFLNKktkqlqdLTEEKSTLAGEIRDLKDMLDVKERKINVLQkkiENLQEQLRDKDKQLAGLKERVKslqtdssntd 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1361 -AKSELQRSLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSID 1439
Cdd:pfam10174 436 tALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKK 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1440 LERANSAAAALDKKQRNFDRIIAEWKQKYEETQAE---------LEASQKESRSLSTELFKLKNAYEESLDNLETLKREN 1510
Cdd:pfam10174 516 DSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVrtnpeindrIRLLEQEVARYKEESGKAQAEVERLLGILREVENEK 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1511 KNLQEEIADLTDQISMSGKTIHELEKLKKTLECE-KSEIQAALEEAEGALEHEESKTLRIQLE-----LNQVKADVD--- 1581
Cdd:pfam10174 596 NDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEmKKKGAQLLEEARRREDNLADNSQQLQLEelmgaLEKTRQELDatk 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1582 -------RKLAEKDEEFENLRRNHQRAMDSMqatLDAEAKARNEAIRlrkkmEGDLNEMEIQLSHANRQAA--------- 1645
Cdd:pfam10174 676 arlsstqQSLAEKDGHLTNLRAERRKQLEEI---LEMKQEALLAAIS-----EKDANIALLELSSSKKKKTqeevmalkr 747
|
490
....*....|..
gi 1394781870 1646 EAQKMVRQLQSQ 1657
Cdd:pfam10174 748 EKDRLVHQLKQQ 759
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
849-1332 |
2.67e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 849 RSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTmiqekndlALQLQAEQDNLADAEERCDLLIKAKIQLEAKVK 928
Cdd:TIGR00606 592 RLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD--------VCGSQDEESDLERLKEEIEKSSKQRAMLAGATA 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 929 ELTERVEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNL---IEEMAALDEV----IAKLT 1001
Cdd:TIGR00606 664 VYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKekrRDEMLGLAPGrqsiIDLKE 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1002 KEKKALQEAHQQALDDLQAEEDKVN---TLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESvmDLE 1078
Cdd:TIGR00606 744 KEIPELRNKLQKVNRDIQRLKNDIEeqeTLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGS--DLD 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1079 NDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARakveKQRAEVARELEELSERL 1158
Cdd:TIGR00606 822 RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNL----QRRQQFEEQLVELSTEV 897
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1159 EEAGGATAIQLEMNKKREAEFLKLRRDLEEATLQHESTaaalRKKHADSVAELSEQIDNL--------QRVKQKLEKEKS 1230
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETS----NKKAQDKVNDIKEKVKNIhgymkdieNKIQDGKDDYLK 973
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1231 EMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLAdvstqRARLQTESGELSRLLEEKESFINQ-- 1308
Cdd:TIGR00606 974 QKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLT-----LRKRENELKEVEEELKQHLKEMGQmq 1048
|
490 500
....*....|....*....|....
gi 1394781870 1309 LTRGKTSFTQMIEELKRQLEEETK 1332
Cdd:TIGR00606 1049 VLQMKQEHQKLEENIDLIKRNHVL 1072
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1677-1945 |
2.90e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1677 EQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSqntglinQKKKMEADIAQLTTEVEEaVQEC 1756
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISS-------ELPELREELEKLEKEVKE-LEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1757 RNAEEKAKKaitdaammaeELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIAlkGGKKQIQKLEARVRELEGELDT 1836
Cdd:PRK03918 237 KEEIEELEK----------ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV--KELKELKEKAEEYIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1837 EQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQ------TKVKSYKRQYEEAEQ-QANSNLVKYR---- 1905
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKelekrlEELEERHELYEEAKAkKEELERLKKRltgl 384
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1394781870 1906 ---KVQHELDDAEERADIAETQVNKLRARSREVVITSKVLKTA 1945
Cdd:PRK03918 385 tpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1684-1934 |
2.90e-04 |
|
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: 45.94 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1684 RRNNLLLAEVEELRAALE---QAERGRKLAEQELLEATERVNLLHSQ---NTGLINQKKKMEADIAQLTTEVEEAVQEcr 1757
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKErqqKAESELKELEKKHQQLCEEKNALQEQlqaETELCAEAEEMRARLAARKQELEEILHE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1758 naeekakkaitdaamMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAE---------QIALKGGKKQIQK------ 1822
Cdd:pfam01576 80 ---------------LESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEaarqklqleKVTTEAKIKKLEEdillle 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1823 ------------LEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQY 1890
Cdd:pfam01576 145 dqnsklskerklLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQI 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1394781870 1891 EEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRARSRE 1934
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE 268
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
862-1703 |
2.98e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 862 EEFQKLKEALEKSEAKRKELEEkQVTMIQEKNDLAlqlQAEQDN----LADAEERCDLLIKAKIQLEAKVKELtervede 937
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADE-QQEENEARAEAA---EEEVDElksqLADYQQALDVQQTRAIQYQQAVQAL------- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 938 EEINS-----DLTSKKrkLEDECAELKKDIDdlEITLAKVEKEKHATENKVKNLIEEMAAldEVIAKLTKEKKAlQEAHQ 1012
Cdd:PRK04863 424 ERAKQlcglpDLTADN--AEDWLEEFQAKEQ--EATEELLSLEQKLSVAQAAHSQFEQAY--QLVRKIAGEVSR-SEAWD 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1013 QALDDL-QAEEDKVntLTKAKVKLEQQVDDLESSLEQEKkirmDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKkk 1091
Cdd:PRK04863 497 VARELLrRLREQRH--LAEQLQQLRMRLSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLE-- 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1092 dfemnQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEeaggatAIQLEM 1171
Cdd:PRK04863 569 -----SLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTE------YMQQLL 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1172 NKKREAEFLKL-----RRDLEE--ATLQHESTAAALRKKH-AD-----SVAELSEQI---------------------DN 1217
Cdd:PRK04863 638 ERERELTVERDelaarKQALDEeiERLSQPGGSEDPRLNAlAErfggvLLSEIYDDVsledapyfsalygparhaivvPD 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1218 LQRVKQKLEKEksemkmevDDLSSNIeYLTKNKAnaeklcrtyeDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSR 1297
Cdd:PRK04863 718 LSDAAEQLAGL--------EDCPEDL-YLIEGDP----------DSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEVPL 778
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1298 LleekesfinqltrGKTSFTQMIEELKRQLEEETksknalahalqasrhdcdllrEQYEEEVEAKSELQRSLSKANAEVA 1377
Cdd:PRK04863 779 F-------------GRAAREKRIEQLRAEREELA---------------------ERYATLSFDVQKLQRLHQAFSRFIG 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1378 -------QWRTKYETDAI-QRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHR--------LQTEIEDLSIDLE 1441
Cdd:PRK04863 825 shlavafEADPEAELRQLnRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRlnlladetLADRVEEIREQLD 904
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1442 RANSAAAALDKKQRNFDRI-------------IAEWKQKYEETQAELEASQKESRSLsTELFKLKN--AYEESLDNLetl 1506
Cdd:PRK04863 905 EAEEAKRFVQQHGNALAQLepivsvlqsdpeqFEQLKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAhfSYEDAAEML--- 980
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1507 krenknlqEEIADLTDQISmsgktihelEKLKKtLECEKSEIQAALEEAEGALEheesktlriqlELNQVkadvdrkLAE 1586
Cdd:PRK04863 981 --------AKNSDLNEKLR---------QRLEQ-AEQERTRAREQLRQAQAQLA-----------QYNQV-------LAS 1024
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1587 KDEEFENLRRNHQRAMDSMQ-----ATLDAEAKAR------NEAIRL----RKKMEGDLNEMEIQLSHANRQAAEAQKMV 1651
Cdd:PRK04863 1025 LKSSYDAKRQMLQELKQELQdlgvpADSGAEERARarrdelHARLSAnrsrRNQLEKQLTFCEAEMDNLTKKLRKLERDY 1104
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 1394781870 1652 RQLQSQIKDLQIELDDTMR---HNDDLKEqaaaLERRnNLLLAEVEELRAALEQA 1703
Cdd:PRK04863 1105 HEMREQVVNAKAGWCAVLRlvkDNGVERR----LHRR-ELAYLSADELRSMSDKA 1154
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
847-1104 |
3.35e-04 |
|
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: 45.94 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 847 LLRSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEekqvtmiQEKNDLalqlqaeQDNLADAEERCDLLIKAKIQLEAK 926
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQ-------QERDEL-------ADEIASGASGKSALQDEKRRLEAR 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 927 VKELTERVEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLieemaaldeviakltkeKKA 1006
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKEL-----------------KAK 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1007 LQEahqqalddlqaEEDKVNTLTKAKVK-LEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLE 1085
Cdd:pfam01576 954 LQE-----------MEGTVKSKFKSSIAaLEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYK 1022
|
250
....*....|....*....
gi 1394781870 1086 EKLKKKDFEMNQLNSRIED 1104
Cdd:pfam01576 1023 DQAEKGNSRMKQLKRQLEE 1041
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1570-1829 |
3.74e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.59 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1570 QLELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARneairlRKKMEGDLNEMEIQL-SHANRQAAEAQ 1648
Cdd:NF041483 82 QIQADQLRADAERELRDARAQTQRILQEHAEHQARLQAELHTEAVQR------RQQLDQELAERRQTVeSHVNENVAWAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1649 KMVRQLQSQIKDL----QIELDDTMRHNDDLKEQAAALERRNnlLLAEVEELRAALEQ--------AERGRKLAEQELLE 1716
Cdd:NF041483 156 QLRARTESQARRLldesRAEAEQALAAARAEAERLAEEARQR--LGSEAESARAEAEAilrrarkdAERLLNAASTQAQE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1717 ATERVNLLHSQNTGLINQKKKMEADIA----QLTTEVEEAVQECRNAEEKAKKAITDAA---MMAEELKKEQDTSAHLER 1789
Cdd:NF041483 234 ATDHAEQLRSSTAAESDQARRQAAELSraaeQRMQEAEEALREARAEAEKVVAEAKEAAakqLASAESANEQRTRTAKEE 313
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1394781870 1790 MKKNMEQTIKDLQMRLDEAEQiALKGGKKQIQKLEARVRE 1829
Cdd:NF041483 314 IARLVGEATKEAEALKAEAEQ-ALADARAEAEKLVAEAAE 352
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1516-1840 |
3.81e-04 |
|
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: 45.40 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1516 EIADLTDQISMSGKTIHELEKLKKTLECEK----SEIQAALEEAEGALEHEESKTLRIQLELNQVKA---DVDRKLAEKD 1588
Cdd:pfam05667 276 DLAELLSSFSGSSTTDTGLTKGSRFTHTEKlqftNEAPAATSSPPTKVETEEELQQQREEELEELQEqleDLESSIQELE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1589 EEFENLRRNHQRAMDSMQaTLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDT 1668
Cdd:pfam05667 356 KEIKKLESSIKQVEEELE-ELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1669 MRhndDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQ---ELLEATERVN--LLHSQNTGLINQK----KKME 1739
Cdd:pfam05667 435 YR---ALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEElykQLVAEYERLPkdVSRSAYTRRILEIvkniKKQK 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1740 ADIAQLTTEVEEAVQECRNAEEKAKK--AITDAaMMAEELKKEQDTSA---HLERMKKNMEQTIKDLQmrldeaeqialK 1814
Cdd:pfam05667 512 EEITKILSDTKSLQKEINSLTGKLDRtfTVTDE-LVFKDAKKDESVRKaykYLAALHENCEQLIQTVE-----------E 579
|
330 340
....*....|....*....|....*.
gi 1394781870 1815 GGKKQIQklearVRELEGELDTEQKK 1840
Cdd:pfam05667 580 TGTIMRE-----IRDLEEQIETESGK 600
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
977-1378 |
4.34e-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: 45.39 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 977 HATENKVKNLIEEMAALDEViakLTKEKKALQEAHQQALDDLQAEEDK---------VNTLTKAKVKLEQQVDDLESSLE 1047
Cdd:NF033838 36 HAEEVRGGNNPTVTSSGNES---QKEHAKEVESHLEKILSEIQKSLDKrkhtqnvalNKKLSDIKTEYLYELNVLKEKSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1048 QE--KKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKDfEMNQLNSRIEDQQVLEAQLQKKIKELQARIEE 1125
Cdd:NF033838 113 AEltSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQK-EEDRRNYPTNTYKTLELEIAESDVEVKKAELE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1126 LEEELEAERAARAKVEKQRAEVareleelserleEAGGATAIQLEmnkkreaeflKLRRDLEEATLQHESTAAALRKKHA 1205
Cdd:NF033838 192 LVKEEAKEPRDEEKIKQAKAKV------------ESKKAEATRLE----------KIKTDREKAEEEAKRRADAKLKEAV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1206 DSVAELSEQIDNLQRVKQKLEKE-----KSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKV----DELQR 1276
Cdd:NF033838 250 EKNVATSEQDKPKRRAKRGVLGEpatpdKKENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAkdqkEEDRR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1277 QLADVSTQRARLQ-TES------GELSRLLEEKESFINqltrgktsftqmiEELKRQLEEETKSKNALAHALQASRHDcd 1349
Cdd:NF033838 330 NYPTNTYKTLELEiAESdvkvkeAELELVKEEAKEPRN-------------EEKIKQAKAKVESKKAEATRLEKIKTD-- 394
|
410 420
....*....|....*....|....*....
gi 1394781870 1350 llREQYEEEVEAKSELQRSLSKANAEVAQ 1378
Cdd:NF033838 395 --RKKAEEEAKRKAAEEDKVKEKPAEQPQ 421
|
|
| HemX |
COG2959 |
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis ... |
1626-1745 |
4.64e-04 |
|
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis HemX, COG0755, no evidence of involvement in heme biosynthesis) [General function prediction only];
Pssm-ID: 442199 [Multi-domain] Cd Length: 361 Bit Score: 44.57 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1626 MEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLKEQAAALE---------RRNNLLLAEVEEL 1696
Cdd:COG2959 58 QQAELAQLAQQLAALQQQAQELRALAQQLQELLQQLAARLAQLEQRLAELQQQLAALQqllqslsgsSRDDWLLAEAEYL 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1394781870 1697 -RAALEQAERGR--KLAEQELLEATERvnLLHSQNTGLINQKKKMEADIAQL 1745
Cdd:COG2959 138 lRLAGQQLQLEGdvKTALAALQSADAR--LARLNDPSLLPVRRAIARDIARL 187
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
861-1123 |
4.86e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 861 KEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLikakiqLEAKVKELTERVEDEEEI 940
Cdd:COG5185 210 SETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDL------RLEKLGENAESSKRLNEN 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 941 NSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENkvKNLIEEMAALDEVIAKLTKEKKALQEAHQQALDDLQA 1020
Cdd:COG5185 284 ANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAE--QELEESKRETETGIQNLTAEIEQGQESLTENLEAIKE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1021 EEDKVNTltkakvklEQQVDDLESSLEQEKKirmDLERAKRKLEGDLKLTQESVMDLendKQQLEEKLKKKDFEMNQLNS 1100
Cdd:COG5185 362 EIENIVG--------EVELSKSSEELDSFKD---TIESTKESLDEIPQNQRGYAQEI---LATLEDTLKAADRQIEELQR 427
|
250 260
....*....|....*....|...
gi 1394781870 1101 RIEDQQVLEAQLQKKIKELQARI 1123
Cdd:COG5185 428 QIEQATSSNEEVSKLLNELISEL 450
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1174-1524 |
5.10e-04 |
|
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: 45.28 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1174 KREAEFLKLRRDLEEATLQHESTAAalRKKHADSVAELSEQIDNLQRVKQKLEKEKSEMkmeVDDLSSNIEYLTKNKANA 1253
Cdd:pfam15964 373 EKELASQQEKRAQEKEALRKEMKKE--REELGATMLALSQNVAQLEAQVEKVTREKNSL---VSQLEEAQKQLASQEMDV 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1254 EKLCRTYEDQLNEAKSKVDELQRQLADVSTQrarlqtesgeLSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKS 1333
Cdd:pfam15964 448 TKVCGEMRYQLNQTKMKKDEAEKEHREYRTK----------TGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREE 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1334 KNALAHALQASRHDCDLLREQyeeeveaKSELQRSLS---KANAEVAQWRTKYETDAIQRTE-ELEEAKKKLAIRLQEAE 1409
Cdd:pfam15964 518 CLKLTELLGESEHQLHLTRLE-------KESIQQSFSneaKAQALQAQQREQELTQKMQQMEaQHDKTVNEQYSLLTSQN 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1410 EAVEAAHAKC----SSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEASQKESRSL 1485
Cdd:pfam15964 591 TFIAKLKEECctlaKKLEEITQKSRSEVEQLSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQLDKHCQAT 670
|
330 340 350
....*....|....*....|....*....|....*....
gi 1394781870 1486 STELFKLKNAYEEsldnletLKRENKNLQEEIADLTDQI 1524
Cdd:pfam15964 671 AQQLVQLLSKQNQ-------LFKERQNLTEEVQSLRSQV 702
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1656-1922 |
5.76e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1656 SQIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAAL-EQAERGRKLAEQeLLEATERVNLLHSQNTGLINQ 1734
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRdELNAQVKELREE-AQELREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1735 KKKMEADIAQLTTEVEEAVQEcRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALK 1814
Cdd:COG1340 80 RDELNEKLNELREELDELRKE-LAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1815 ggKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQYEEAE 1894
Cdd:COG1340 159 --NEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
250 260
....*....|....*....|....*...
gi 1394781870 1895 QQANSNLVKYRKVQHELDDAEERADIAE 1922
Cdd:COG1340 237 KELRELRKELKKLRKKQRALKREKEKEE 264
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1195-1586 |
6.05e-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: 45.00 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1195 STAAALRKKHADSVAELSEQIdnLQRVKQKLEKEKSEMKMEVDDLSSNI--EYLTKNKANAEKlcrTYEDQLNEAKSKVD 1272
Cdd:NF033838 50 SSGNESQKEHAKEVESHLEKI--LSEIQKSLDKRKHTQNVALNKKLSDIktEYLYELNVLKEK---SEAELTSKTKKELD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1273 ELQRQLadvSTQRARLQTESGELSRLLEEKEsfinqltrgktsftqmiEELKRQLEEETKSKNALAHAlqasrhdcDLLR 1352
Cdd:NF033838 125 AAFEQF---KKDTLEPGKKVAEATKKVEEAE-----------------KKAKDQKEEDRRNYPTNTYK--------TLEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1353 EQYEEEVE-AKSELQrsLSKANAEVAQwrtkyETDAIQRTEELEEAKKKLAIRLQEAEEAVEAAHakcsslEKTKHRLQT 1431
Cdd:NF033838 177 EIAESDVEvKKAELE--LVKEEAKEPR-----DEEKIKQAKAKVESKKAEATRLEKIKTDREKAE------EEAKRRADA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1432 EIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKyeETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENK 1511
Cdd:NF033838 244 KLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKK--ENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAK 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394781870 1512 NLQEEiadltDQISMSGKTIheleklkKTLECEKSEIQAALEEAEGALEHEESKTLRIQLELNQVKADVDRKLAE 1586
Cdd:NF033838 322 DQKEE-----DRRNYPTNTY-------KTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAE 384
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
926-1123 |
6.59e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 926 KVKELTERVEDEEEINSdlTSKKRKLEDECAELKKDIDDLEITLAKVEKEkhatenkVKNLIEEMAALDEVIAKLTKEKK 1005
Cdd:PRK05771 54 KLSEALDKLRSYLPKLN--PLREEKKKVSVKSLEELIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1006 ALQEAHqqALD-DLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKkirmdLERAKRKLEGDLKLtqesVMDLENDKQQL 1084
Cdd:PRK05771 125 RLEPWG--NFDlDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVEN-----VEYISTDKGYVYVV----VVVLKELSDEV 193
|
170 180 190
....*....|....*....|....*....|....*....
gi 1394781870 1085 EEKLKKKDFEMNQLNSRIEDQQVLEaQLQKKIKELQARI 1123
Cdd:PRK05771 194 EEELKKLGFERLELEEEGTPSELIR-EIKEELEEIEKER 231
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1265-1373 |
6.79e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1265 NEAKSKVDELQRQL----ADVSTQRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKS--KNALA 1338
Cdd:PRK00409 505 EEAKKLIGEDKEKLneliASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQaiKEAKK 584
|
90 100 110
....*....|....*....|....*....|....*.
gi 1394781870 1339 HALQASRHDCDLLREQYEEEVEAK-SELQRSLSKAN 1373
Cdd:PRK00409 585 EADEIIKELRQLQKGGYASVKAHElIEARKRLNKAN 620
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1469-1715 |
6.97e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.76 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1469 EETQAELEASQKESRS-LSTELFKLKNAYEESLDNL----ETLKRENKNLQEEIADLTDqismsgktihELEKLKKTLEC 1543
Cdd:pfam00038 24 EQQNKLLETKISELRQkKGAEPSRLYSLYEKEIEDLrrqlDTLTVERARLQLELDNLRL----------AAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1544 EKSEIQAALEEAEGaleheesktLRIQL-ELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLD------------ 1610
Cdd:pfam00038 94 ELNLRTSAENDLVG---------LRKDLdEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdtqvnvemdaar 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1611 --------AEAKARNEAIRLRKKMEGDlNEMEIQLSHANRQAAEAQKMVRQLQSQIKD-------LQIELDDTMRHNDDL 1675
Cdd:pfam00038 165 kldltsalAEIRAQYEEIAAKNREEAE-EWYQSKLEELQQAAARNGDALRSAKEEITElrrtiqsLEIELQSLKKQKASL 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1394781870 1676 KEQAAALERRNNLLLAEVEELRAALEQA------ERGRKLAE-QELL 1715
Cdd:pfam00038 244 ERQLAETEERYELQLADYQELISELEAElqetrqEMARQLREyQELL 290
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1582-1930 |
7.03e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1582 RKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDL 1661
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1662 QIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEAD 1741
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1742 IAQLTTEVEEAVQEcrNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQIQ 1821
Cdd:COG4372 166 LAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1822 KLEARVRELEGELD-TEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQYEEAEQQANSN 1900
Cdd:COG4372 244 LEEDKEELLEEVILkEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330 340 350
....*....|....*....|....*....|
gi 1394781870 1901 LVKYRKVQHELDDAEERADIAETQVNKLRA 1930
Cdd:COG4372 324 LAKKLELALAILLAELADLLQLLLVGLLDN 353
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
833-1248 |
7.08e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 44.75 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 833 KNWSWMKLFFKIKPLLRSA-----QTEKEMATMKEEFQKLK-EALEKSEAKRKELEEkqvtmiQEKNDLALQLQAEQDNL 906
Cdd:pfam09731 28 KDDNFRDFFEEYIPYGEEVvlyalGEDPPLAPKPKTFRPLQpSVVSAVTGESKEPKE------EKKQVKIPRQSGVSSEV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 907 ADAE-ERCDLLIKAKIQLEAKVKELTERvedEEEINSDLTSKKRKLEDECAELKKDiddleitlakvekEKHATENKVKN 985
Cdd:pfam09731 102 AEEEkEATKDAAEAKAQLPKSEQEKEKA---LEEVLKEAISKAESATAVAKEAKDD-------------AIQAVKAHTDS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 986 LIEEMAalDEVIAKLTKEKKALQEAHQQALDDLQAEED-KVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLE 1064
Cdd:pfam09731 166 LKEASD--TAEISREKATDSALQKAEALAEKLKEVINLaKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1065 GDLKLTQESVMDLENDKQQLEEKL--------KKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARieeleeeleAERAA 1136
Cdd:pfam09731 244 LVDQYKELVASERIVFQQELVSIFpdiipvlkEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKR---------EEKHI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1137 RAKVEKQRAEVARELEELSERLEEAGGATAIQLEmnKKREAEFLKLRRDLEE---ATLQHESTAAALRKKHADSVAELSE 1213
Cdd:pfam09731 315 ERALEKQKEELDKLAEELSARLEEVRAADEAQLR--LEFEREREEIRESYEEklrTELERQAEAHEEHLKDVLVEQEIEL 392
|
410 420 430
....*....|....*....|....*....|....*
gi 1394781870 1214 QIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTK 1248
Cdd:pfam09731 393 QREFLQDIKEKVEEERAGRLLKLNELLANLKGLEK 427
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1694-1936 |
7.25e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1694 EELRAALEQA-------ERgRKLAEQELlEATE----RVNLLHSQntgLINQKKKMEadiaqlttevEEAvqecrnaeEK 1762
Cdd:COG1196 155 EERRAIIEEAagiskykER-KEEAERKL-EATEenleRLEDILGE---LERQLEPLE----------RQA--------EK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1763 AKKAItdaammaeELKKEQDTSAHLERMKKnmeqtIKDLQMRLDEAEQiALKGGKKQIQKLEARVRELEGELDTEQKKTA 1842
Cdd:COG1196 212 AERYR--------ELKEELKELEAELLLLK-----LRELEAELEELEA-ELEELEAELEELEAELAELEAELEELRLELE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1843 EAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQYEEAEQQANSNLVKYRKVQHELDDAEERADIAE 1922
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
250
....*....|....
gi 1394781870 1923 TQVNKLRARSREVV 1936
Cdd:COG1196 358 AELAEAEEALLEAE 371
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
910-1072 |
7.53e-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: 43.85 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 910 EERCDLLIKAKIQLEakvKELTERVEDEEEINSDLTskkrKLEDECAELKKDIDDLEitlAKVEKEKHATENKVKNLIEE 989
Cdd:smart00787 136 EWRMKLLEGLKEGLD---ENLEGLKEDYKLLMKELE----LLNSIKPKLRDRKDALE---EELRQLKQLEDELEDCDPTE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 990 MAALDEVIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLErakRKLEGDLKL 1069
Cdd:smart00787 206 LDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEI---EKLKEQLKL 282
|
...
gi 1394781870 1070 TQE 1072
Cdd:smart00787 283 LQS 285
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
862-1091 |
7.64e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 862 EEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKVKELtERVEDEEEIN 941
Cdd:COG1340 50 AQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEI-ERLEWRQQTE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 942 SDLTSKKRKLEDECAELKKDIDDleitlAKVEKEKHateNKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQALDDLQAE 1021
Cdd:COG1340 129 VLSPEEEKELVEKIKELEKELEK-----AKKALEKN---EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIEL 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394781870 1022 EDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLK---------LTQESVMDLENDKQQLEEKLKKK 1091
Cdd:COG1340 201 YKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKklrkkqralKREKEKEELEEKAEEIFEKLKKG 279
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1583-1770 |
7.96e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1583 KLAEKDEEFENLRRNHQRAMDSMQAtlDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQaaeaqkmVRQLQSQIKDLQ 1662
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKEAEAIKK--EALLEAKEEIHKLRNEFEKELRERRNELQKLEKR-------LLQKEENLDRKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1663 IELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRA-ALEQAERGRKL----AEQELLEATErvnllhsqntglinqkKK 1737
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEeQLQELERISGLtaeeAKEILLEKVE----------------EE 166
|
170 180 190
....*....|....*....|....*....|...
gi 1394781870 1738 MEADIAQLTTEVEEAVQEcrNAEEKAKKAITDA 1770
Cdd:PRK12704 167 ARHEAAVLIKEIEEEAKE--EADKKAKEILAQA 197
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1009-1147 |
8.19e-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: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1009 EAHQQALDDLQAEEDKVNTLTKAK-------VKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQEsvmDLENDK 1081
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLkelpaelAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYE 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394781870 1082 QQLEEKLKKKdfEMNQLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAARAKVEKQRAEV 1147
Cdd:COG1579 80 EQLGNVRNNK--EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1775-1906 |
8.27e-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: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1775 EELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQiALKGGKKQIQKLEARVRELEG--ELDTEQKKTAEAQKGIRKYE 1852
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLEL-EIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESLKRRISDLE 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1394781870 1853 RRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQYEEAEQQANSNLVKYRK 1906
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
922-1090 |
8.57e-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: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 922 QLEAKVKELTERVEDeeeinsdLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAAldeviAKLT 1001
Cdd:COG1579 21 RLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-----VRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1002 KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKirmDLERAKRKLEGDLKLTQESVMDLENDK 1081
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAER 165
|
....*....
gi 1394781870 1082 QQLEEKLKK 1090
Cdd:COG1579 166 EELAAKIPP 174
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1265-1914 |
8.69e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1265 NEAKSKVDE---LQRQLADVSTQRARLQTESGELSRLLEEkesfinqLTRGKTSFTQMIEELKRQLEeetKSKNALAHAL 1341
Cdd:PRK04863 279 NERRVHLEEaleLRRELYTSRRQLAAEQYRLVEMARELAE-------LNEAESDLEQDYQAASDHLN---LVQTALRQQE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1342 QASRHDCDL--LREQYEEEVEA-------KSELQRSLSKANAEVAQWRTKYeTDAIQRTEELEeakkKLAIRLQEAEEAV 1412
Cdd:PRK04863 349 KIERYQADLeeLEERLEEQNEVveeadeqQEENEARAEAAEEEVDELKSQL-ADYQQALDVQQ----TRAIQYQQAVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1413 EAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEWKQKYEETQA-----ELEASQKESRSLST 1487
Cdd:PRK04863 424 ERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagevSRSEAWDVARELLR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1488 ELFKLKN------AYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAegaleH 1561
Cdd:PRK04863 504 RLREQRHlaeqlqQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEA-----R 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1562 EESKTLRIQLElnQVKADVDR-------------KLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEG 1628
Cdd:PRK04863 579 ERRMALRQQLE--QLQARIQRlaarapawlaaqdALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQA 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1629 DLNEMEiQLShaNRQAAEAQKMVR-------QLQSQIKDlQIELDDT---------MRH----ND--DLKEQAAALER-R 1685
Cdd:PRK04863 657 LDEEIE-RLS--QPGGSEDPRLNAlaerfggVLLSEIYD-DVSLEDApyfsalygpARHaivvPDlsDAAEQLAGLEDcP 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1686 NNLLLAE------------VEEL-------------------------RAA----LEQAERGRKLAEQELLEATERVNL- 1723
Cdd:PRK04863 733 EDLYLIEgdpdsfddsvfsVEELekavvvkiadrqwrysrfpevplfgRAArekrIEQLRAEREELAERYATLSFDVQKl 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1724 --LHSQNTGLINQKKKM------EADIAQLTT---EVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERmkK 1792
Cdd:PRK04863 813 qrLHQAFSRFIGSHLAVafeadpEAELRQLNRrrvELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD--E 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1793 NMEQTIKDLQMRLDEAEQ----IALKGGK-KQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTY------- 1860
Cdd:PRK04863 891 TLADRVEEIREQLDEAEEakrfVQQHGNAlAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrah 970
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1394781870 1861 -QTEEDRKNLARMQDLIDKLQTKVKSYKRQYEEAEQ---QANSNLVKYRKVQHELDDA 1914
Cdd:PRK04863 971 fSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREqlrQAQAQLAQYNQVLASLKSS 1028
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
835-1045 |
8.97e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 8.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 835 WSWMKLFFKIKPLLRSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAE---E 911
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEleqE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 912 RCDLLIKAKIQLEAKVKELTERVEDEEEINSDLTSKKRKLEDECAELKK-----DIDDLEITLAKVEKEKHATENKVKNL 986
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllealDEEELEEELEELEEELEELEEELEEL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394781870 987 IEEMAALDEVIAKLTKEKK--ALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESS 1045
Cdd:COG4717 452 REELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1191-1406 |
9.26e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1191 LQHESTAAALRKKHADSvAELSEQIDNLQRVKQKLEKEKSE-MKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKS 1269
Cdd:PRK05771 36 LKEELSNERLRKLRSLL-TKLSEALDKLRSYLPKLNPLREEkKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELEN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1270 KVDELQRQLADVStqraRLQTESGELSRLLEEK--ESFINQLTRGKTSFTQMIEELKRQLEEETKSKNALAHALQASRH- 1346
Cdd:PRK05771 115 EIKELEQEIERLE----PWGNFDLDLSLLLGFKyvSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKELs 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394781870 1347 ------------------DCDLLREQYEEEVEAKSELQRSLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLAIRLQ 1406
Cdd:PRK05771 191 deveeelkklgferleleEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSK 268
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1639-1899 |
9.44e-04 |
|
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: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1639 HANRQAAEAQKMVRQLQSQIKDLQIELDDtmrhnddLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEAT 1718
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDA-------LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1719 ERVN--LLHSQNTGlinqkkkmeadiaQLTTEVEeavqecrnaeekakkAITDAAMMAEELKKEQDTSAHLERMKKNMEQ 1796
Cdd:COG3883 86 EELGerARALYRSG-------------GSVSYLD---------------VLLGSESFSDFLDRLSALSKIADADADLLEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1797 tIKDLQMRLDEAEQIAlkggKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLI 1876
Cdd:COG3883 138 -LKADKAELEAKKAEL----EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
250 260
....*....|....*....|...
gi 1394781870 1877 DKLQTKVKSYKRQYEEAEQQANS 1899
Cdd:COG3883 213 AAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1636-1840 |
9.57e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.09 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1636 QLSHANRQAAEAQKMVRQLQSQIKDLQIELDdtmRHNDDLKEQaaalerrnnllLAEVEELRAALEQAERGRKLAEQELL 1715
Cdd:pfam00261 23 KLEEAEKRAEKAEAEVAALNRRIQLLEEELE---RTEERLAEA-----------LEKLEEAEKAADESERGRKVLENRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1716 EATERVNLLHSQntglINQKKKMEADIAQLTTEVEEAV----QECRNAEEKAKKAITDAAMMAEELKK--------EQDT 1783
Cdd:pfam00261 89 KDEEKMEILEAQ----LKEAKEIAEEADRKYEEVARKLvvveGDLERAEERAELAESKIVELEEELKVvgnnlkslEASE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1394781870 1784 SAHLERMKKNMEQtIKDLQMRLDEAEQIALKgGKKQIQKLEARVRELEGELDTEQKK 1840
Cdd:pfam00261 165 EKASEREDKYEEQ-IRFLTEKLKEAETRAEF-AERSVQKLEKEVDRLEDELEAEKEK 219
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
875-1122 |
1.11e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 875 EAKRKELEEKQVTmiqEKNDLALQLQAEqdnLADAEERCDLLIKAKIQLEAKVKELTERVEDEEEINSDLTSKKRKLEDE 954
Cdd:pfam00038 31 ETKISELRQKKGA---EPSRLYSLYEKE---IEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAEND 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 955 CAELKKDIDDLeiTLAKVEkekhaTENKVKNLIEEMAALDEViakLTKEKKALQEAHQQalDDLQAEEDKVNT--LTKAK 1032
Cdd:pfam00038 105 LVGLRKDLDEA--TLARVD-----LEAKIESLKEELAFLKKN---HEEEVRELQAQVSD--TQVNVEMDAARKldLTSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1033 VKLEQQVDdlesslEQEKKIRMDLERA-KRKLEgdlKLTQESVMDLEnDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQ 1111
Cdd:pfam00038 173 AEIRAQYE------EIAAKNREEAEEWyQSKLE---ELQQAAARNGD-ALRSAKEEITELRRTIQSLEIELQSLKKQKAS 242
|
250
....*....|.
gi 1394781870 1112 LQKKIKELQAR 1122
Cdd:pfam00038 243 LERQLAETEER 253
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1183-1715 |
1.13e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.97 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1183 RRDLEEATLQHESTAAALRKKHADSVAELSEQIDNLQRVKQKLE-------KEKSEMKMEVD----DLSSNIEYLTKNKA 1251
Cdd:pfam07111 139 QRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkrageaKQLAEAQKEAEllrkQLSKTQEELEAQVT 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1252 NAEKLcRTY--EDQLNEAKSKVDELQRQ-----LADVSTQRARLQT------------------ESGELSRLLEEKESFI 1306
Cdd:pfam07111 219 LVESL-RKYvgEQVPPEVHSQTWELERQelldtMQHLQEDRADLQAtvellqvrvqslthmlalQEEELTRKIQPSDSLE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1307 NQLTRGKTSFTQMIEELKRQLEEETKSKNaLAH--ALQASRHDCDLLREQYEEEVEAKSELQRSLSKANAEVAQWRTKYE 1384
Cdd:pfam07111 298 PEFPKKCRSLLNRWREKVFALMVQLKAQD-LEHrdSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAK 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1385 TDAIqrteELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDRIIAEW 1464
Cdd:pfam07111 377 GLQM----ELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLM 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1465 KQKYEETQAELEASQKESRSLSTElfklknayeesldnlETLKRENKNLQEEIADLTDQISMSGKTI-HELEKLKKTLEC 1543
Cdd:pfam07111 453 ARKVALAQLRQESCPPPPPAPPVD---------------ADLSLELEQLREERNRLDAELQLSAHLIqQEVGRAREQGEA 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1544 EKSEIQAALEEAEGALEHEESKTLRIQLELNQVKadvdRKLAEKDEEFENLRRNHQRAMDSMQATLdaEAKARNEAIRLR 1623
Cdd:pfam07111 518 ERQQLSEVAQQLEQELQRAQESLASVGQQLEVAR----QGQQESTEEAASLRQELTQQQEIYGQAL--QEKVAEVETRLR 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1624 KKmegdLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDL-KEQAAALERRNNLLLAEVEELRAALEQ 1702
Cdd:pfam07111 592 EQ----LSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEArKEEGQRLARRVQELERDKNLMLATLQQ 667
|
570
....*....|...
gi 1394781870 1703 AERGRKLAEQELL 1715
Cdd:pfam07111 668 EGLLSRYKQQRLL 680
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1028-1123 |
1.31e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1028 LTKAKVKLEQQVDDLESSLEQEKK-----IRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKDFEMNQLNSRI 1102
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIKKealleAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEEL 112
|
90 100
....*....|....*....|.
gi 1394781870 1103 EDQQVLEAQLQKKIKELQARI 1123
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEEL 133
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
854-1061 |
1.41e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 854 EKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLaDAEERCDLLIKAKIQLEAKVKELTER 933
Cdd:PRK01156 528 RADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLI-DIETNRSRSNEIKKQLNDLESRLQEI 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 934 VEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKekhaTENKVKNLIEEMAALDEVIAKLTK----------E 1003
Cdd:PRK01156 607 EIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEK----LRGKIDNYKKQIAEIDSIIPDLKEitsrindiedN 682
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1394781870 1004 KKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRMDLERAKR 1061
Cdd:PRK01156 683 LKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLKR 740
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1198-1361 |
1.47e-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: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1198 AALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANaeklcrtYEDQLNEAKS--KVDELQ 1275
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-------YEEQLGNVRNnkEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1276 RQLADVSTQRARLQTESGELSRLLEEKESFINQLtrgktsfTQMIEELKRQLEEETKSKNALAHALQASRHDCDLLREQY 1355
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
....*.
gi 1394781870 1356 EEEVEA 1361
Cdd:COG1579 169 AAKIPP 174
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
953-1074 |
1.48e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 953 DE-CAELK-------KDIDDLEITLAKVEKEKHATENkvknliEEMAALDEVIAKLTKEKKALQEAHQQALDDLQAEEDK 1024
Cdd:COG0542 396 DEaAARVRmeidskpEELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKEL 469
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1025 VNTLTKAKVKLEQQVDDLESSLEQekkirmdLERAKRKLEGDLKLTQESV 1074
Cdd:COG0542 470 IEEIQELKEELEQRYGKIPELEKE-------LAELEEELAELAPLLREEV 512
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
981-1847 |
1.49e-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: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 981 NKVKNLIEEMAALDEV---IAKLTKEKKALQEAHQQALDDLQaeedKVNTLTKAKVKLEQQVDDLESsleqekkirmdle 1057
Cdd:COG3096 296 GARRQLAEEQYRLVEMareLEELSARESDLEQDYQAASDHLN----LVQTALRQQEKIERYQEDLEE------------- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1058 rakrkLEGDLKLTQESVMDLENDKQQLEEKLKKKDFEMNQLNSRIED-QQVLEAQLQKKIKELQARieeleeeleaeraa 1136
Cdd:COG3096 359 -----LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADyQQALDVQQTRAIQYQQAV-------------- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1137 rakvekQRAEVARELEelserleeagGATAIQLEMNKKREAEFlklRRDLEEATL------QHESTAAALRKKHaDSVAE 1210
Cdd:COG3096 420 ------QALEKARALC----------GLPDLTPENAEDYLAAF---RAKEQQATEevleleQKLSVADAARRQF-EKAYE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1211 LSEQI-------DNLQRVKQKLEkEKSEMKMEVDDLSSnieyLTKNKANAEKLcrtyEDQLNEAKSKVDELQRQLADVST 1283
Cdd:COG3096 480 LVCKIageversQAWQTARELLR-RYRSQQALAQRLQQ----LRAQLAELEQR----LRQQQNAERLLEEFCQRIGQQLD 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1284 QRARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIEELKRQLEEETKSKNALAHALQASRHdcdlLREQYEEEVEAKS 1363
Cdd:COG3096 551 AAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALER----LREQSGEALADSQ 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1364 ELQrslskanaEVAQWRTKYETDAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSL-EKTKHRLQTEI-EDLSI--- 1438
Cdd:COG3096 627 EVT--------AAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRLLALaERLGGVLLSEIyDDVTLeda 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1439 -----------------DLERANSAAAALDKK-------QRNFDRIIAEWKQKYEETQAEL-EASQKE---SRSLSTELF 1490
Cdd:COG3096 699 pyfsalygparhaivvpDLSAVKEQLAGLEDCpedlyliEGDPDSFDDSVFDAEELEDAVVvKLSDRQwrySRFPEVPLF 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1491 KLKnAYEEsldNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTL---------ECEKSEIQAALEEAEGALEH 1561
Cdd:COG3096 779 GRA-AREK---RLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHlavafapdpEAELAALRQRRSELERELAQ 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1562 EESKTLRIQLELNQVKadvdrklaekdEEFENLRRNHQRAMdsmqATLDAEAKARNEAirLRKKMEgDLNEMEIQLSHAN 1641
Cdd:COG3096 855 HRAQEQQLRQQLDQLK-----------EQLQLLNKLLPQAN----LLADETLADRLEE--LREELD-AAQEAQAFIQQHG 916
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1642 RQAAEAQKMVRQLQS---QIKDLQIELDDTMRHNDDLKEQAAAL----ERRNNL-------LLAE----VEELRAALEQA 1703
Cdd:COG3096 917 KALAQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALsevvQRRPHFsyedavgLLGEnsdlNEKLRARLEQA 996
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1704 ERGRKLAEQELLEATERvnllHSQNTglinqkkkmeADIAQLTTEVEEAVQECRNAEEKAK----KAITDAAMMAEELKK 1779
Cdd:COG3096 997 EEARREAREQLRQAQAQ----YSQYN----------QVLASLKSSRDAKQQTLQELEQELEelgvQADAEAEERARIRRD 1062
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394781870 1780 EQDTSAHLERMKKNmeQTIKDLQMRldEAEqialkggkkqIQKLEARVRELEGELDTEQKKTAEAQKG 1847
Cdd:COG3096 1063 ELHEELSQNRSRRS--QLEKQLTRC--EAE----------MDSLQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1418-1575 |
1.51e-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: 42.70 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1418 KCSSLEKTKHRLQTEIEDLSIDLERansaaaaLDKKQRNFDRIIAEWKQKYEETQAELEASQKESRSL----STELFKLK 1493
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKL-------LMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELedcdPTELDRAK 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1494 NAyeesldnLETLKRENKNLQEEIADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHEESKtLRIQLEL 1573
Cdd:smart00787 211 EK-------LKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEK-LKEQLKL 282
|
..
gi 1394781870 1574 NQ 1575
Cdd:smart00787 283 LQ 284
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
851-1302 |
1.55e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.59 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 851 AQTEKEMATMKEEFQKLKEALEKS----EAKRKELEEKQVTMIQ------EKNDLALQLQAEQDNLADAEERCDLLiKAK 920
Cdd:pfam07111 193 AEAQKEAELLRKQLSKTQEELEAQvtlvESLRKYVGEQVPPEVHsqtwelERQELLDTMQHLQEDRADLQATVELL-QVR 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 921 IQ-----LEAKVKELTERVEDEEEINSDLTSKKRKLedecaeLKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDE 995
Cdd:pfam07111 272 VQslthmLALQEEELTRKIQPSDSLEPEFPKKCRSL------LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 996 VIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLT-------KAKVKLEQQVDDLEsslEQEKKIRMDLERAKRKLEGDLK 1068
Cdd:pfam07111 346 QVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQmelsraqEARRRQQQQTASAE---EQLKFVVNAMSSTQIWLETTMT 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1069 LTQESVMDLENDKQQLEEKLKKK----------------------------------DFEMNQLNsriEDQQVLEAQLQK 1114
Cdd:pfam07111 423 RVEQAVARIPSLSNRLSYAVRKVhtikglmarkvalaqlrqescpppppappvdadlSLELEQLR---EERNRLDAELQL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1115 KIKELQARIEELEEELeaeraaraKVEKQR-AEVARELEELSERLEEAGGATAIQLEMNKKREAEFLKLRRDL-EEATLQ 1192
Cdd:pfam07111 500 SAHLIQQEVGRAREQG--------EAERQQlSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLrQELTQQ 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1193 HESTAAALRKKHADSVAELSEQIDNLQRvkqKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKS--- 1269
Cdd:pfam07111 572 QEIYGQALQEKVAEVETRLREQLSDTKR---RLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEGQrla 648
|
490 500 510
....*....|....*....|....*....|....
gi 1394781870 1270 -KVDELQRqlaDVSTQRARLQTEsGELSRLLEEK 1302
Cdd:pfam07111 649 rRVQELER---DKNLMLATLQQE-GLLSRYKQQR 678
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1422-1704 |
1.59e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1422 LEKTKHRLQTEIEDLsIDLERANSAA-AALDKKQRNFDRIIAEWKQKYEETQAELEASQKESRSLSTELFKLKNA--YEE 1498
Cdd:PRK04778 117 IEEDIEQILEELQEL-LESEEKNREEvEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQFVELTESgdYVE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1499 SLDNLETLKRENKNLQEEIADLTDQismsgktiheLEKLKKTLECEKSEIQAA---LEEAEGALEHEEsktlrIQLELNQ 1575
Cdd:PRK04778 196 AREILDQLEEELAALEQIMEEIPEL----------LKELQTELPDQLQELKAGyreLVEEGYHLDHLD-----IEKEIQD 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1576 VKADVDRKLAE----KDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQ----------LSHAN 1641
Cdd:PRK04778 261 LKEQIDENLALleelDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQnkelkeeidrVKQSY 340
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394781870 1642 RQAAEAQKMVRQLQSQIKDLQIELDDtmrHNDDLKEQAAALerrnNLLLAEVEELRAALEQAE 1704
Cdd:PRK04778 341 TLNESELESVRQLEKQLESLEKQYDE---ITERIAEQEIAY----SELQEELEEILKQLEEIE 396
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
988-1560 |
1.60e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.64 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 988 EEMAALDEVIAKLTKEKKAL---QEAHQQAL------DDLQAEEDKVNT-LTKAKVKLEQQVDDLEssleqekkiRMDLE 1057
Cdd:PRK10246 216 EQVQSLTASLQVLTDEEKQLltaQQQQQQSLnwltrlDELQQEASRRQQaLQQALAAEEKAQPQLA---------ALSLA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1058 RAKRKLEGDLKLTQESVMDLENDKQQLEEklkkkdfemnqLNSRIEDQQVLEAQLQKKIKELQARIEELEEELEAERAAR 1137
Cdd:PRK10246 287 QPARQLRPHWERIQEQSAALAHTRQQIEE-----------VNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEH 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1138 AKVEKQRAEVARELEELSERLEEAggataIQLEMNKKREAEFLKLRRDLEEA--TLQHESTAAALrKKHADSVAeLSEQI 1215
Cdd:PRK10246 356 DRFRQWNNELAGWRAQFSQQTSDR-----EQLRQWQQQLTHAEQKLNALPAItlTLTADEVAAAL-AQHAEQRP-LRQRL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1216 DNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSkVDELQRQLADVSTQRARLQteSGEL 1295
Cdd:PRK10246 429 VALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKT-ICEQEARIKDLEAQRAQLQ--AGQP 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1296 SRLLEEKE-SFINQLTRGKTSFTQmieelkRQLEEETKSKNALAHALQASRHDCDLLREQYEEEveaKSELQRSLSKANA 1374
Cdd:PRK10246 506 CPLCGSTShPAVEAYQALEPGVNQ------SRLDALEKEVKKLGEEGAALRGQLDALTKQLQRD---ESEAQSLRQEEQA 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1375 EVAQWRTKYETDAIQRT------------EELEEAKKKLAIR--LQEAEEAVEAAHAKCSS-LEKTKHRLQTEIEDLSID 1439
Cdd:PRK10246 577 LTQQWQAVCASLNITLQpqddiqpwldaqEEHERQLRLLSQRheLQGQIAAHNQQIIQYQQqIEQRQQQLLTALAGYALT 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1440 LERANSAAAALDKKQRNFDRiiaeWKQKYEEtQAELEASQKESRSLSTELFKLKNAYEE----SLDNLETLKRENKNLQE 1515
Cdd:PRK10246 657 LPQEDEEASWLATRQQEAQS----WQQRQNE-LTALQNRIQQLTPLLETLPQSDDLPHSeetvALDNWRQVHEQCLSLHS 731
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394781870 1516 EIADLTDQIS--------------------------------MSGKTIHELEKLKKTLECEKSEIQAALEEAEGALE 1560
Cdd:PRK10246 732 QLQTLQQQDVleaqrlqkaqaqfdtalqasvfddqqaflaalLDEETLTQLEQLKQNLENQRQQAQTLVTQTAQALA 808
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
969-1102 |
1.66e-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: 41.15 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 969 LAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQ 1048
Cdd:pfam11559 16 FLRSGLLFDTAEGVEENIARIINVIYELLQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAK 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1394781870 1049 EKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKDFEMNQLNSRI 1102
Cdd:pfam11559 96 ERQLEKKLKTLEQKLKNEKEELQRLKNALQQIKTQFAHEVKKRDREIEKLKERL 149
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
851-1404 |
1.78e-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: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 851 AQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQvtmIQEKNDLALQLQAEQDNLAdaeercDLLIKAKIQLEAKVKEL 930
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGNGGDRLEQLERE---IERLERELEERERRRARLE------ALLAALGLPLPASAEEF 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 931 TERVEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEK------ 1004
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDeaelpf 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1005 -------KALQEA---------HQQALD------DLQAEEDKVNTLtkakvKLEQQVDDLESSLEQEKKIRMDLER---- 1058
Cdd:COG4913 463 vgelievRPEEERwrgaiervlGGFALTllvppeHYAAALRWVNRL-----HLRGRLVYERVRTGLPDPERPRLDPdsla 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1059 -------------AKRKLEGDLKLTQ-ESVMDLENDKQQL-EEKLKKKDFEMNQLN--SRIEDQQVLEAQLQKKIKELQA 1121
Cdd:COG4913 538 gkldfkphpfrawLEAELGRRFDYVCvDSPEELRRHPRAItRAGQVKGNGTRHEKDdrRRIRSRYVLGFDNRAKLAALEA 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1122 RIEELEEELEAERAARAKVEKQRAEVARELeelserleeaggATAIQLEMNKKREAEFLKLRRDLEEATLQHEstaaALR 1201
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERR------------EALQRLAEYSWDEIDVASAEREIAELEAELE----RLD 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1202 KKHADsVAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEyltknkaNAEKLCRTYEDQLNEAKSKVDELQRQLADv 1281
Cdd:COG4913 682 ASSDD-LAALEEQLEELEAELEELEEELDELKGEIGRLEKELE-------QAEEELDELQDRLEAAEDLARLELRALLE- 752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1282 stqrARLQTESGElsrlleekesfinqltrgkTSFTQMIEELKRQLEEETKSKNALAHALQASRHDcdlLREQYEEEVea 1361
Cdd:COG4913 753 ----ERFAAALGD-------------------AVERELRENLEERIDALRARLNRAEEELERAMRA---FNREWPAET-- 804
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1394781870 1362 kSELQRSLSkANAEVAQWRTKYETDAI-QRTEELEEAKKKLAIR 1404
Cdd:COG4913 805 -ADLDADLE-SLPEYLALLDRLEEDGLpEYEERFKELLNENSIE 846
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
956-1188 |
2.01e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 956 AELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKL 1035
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1036 EQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKKDFEMNQLnsRIEDQQVLEAQLQKK 1115
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL--EQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394781870 1116 IKELQARIEELEEELEAERAARAKVEKQRAEVARELEELSERLEEAGGATAIQLEMNKKREAEFLKLRRDLEE 1188
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1244-1786 |
2.10e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.28 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1244 EYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQ--RARLQTESGELSRLLEEKESFINQLTRGKTSFTQMIE 1321
Cdd:NF041483 524 ETLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERaiAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAE 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1322 ELKRQLEEETKSKNALAhalqASRhdCDLLREQYEEEVEA-KSELQRSLSKANAEVAQWRTKYETDAIQRTEELEEAKKK 1400
Cdd:NF041483 604 RIRREAAEETERLRTEA----AER--IRTLQAQAEQEAERlRTEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQE 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1401 LAIRLQEAEEAV-----EAAHAKCSSLEKTKHRLQTEIEDLsidLERANSAAAALDKKQR-NFDRIIAEWKQKYEETQAE 1474
Cdd:NF041483 678 SADRVRAEAAAAaervgTEAAEALAAAQEEAARRRREAEET---LGSARAEADQERERAReQSEELLASARKRVEEAQAE 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1475 LEASQKESRSLSTELfkLKNAYEESLDNLETLKRENKNLQEEIADLTDQISmsgktiHELEKLKKTLECEKSEIQA-ALE 1553
Cdd:NF041483 755 AQRLVEEADRRATEL--VSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAE------HAAERTRTEAQEEADRVRSdAYA 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1554 EAEGALEHEESKTLRIQLELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATL-DAEAKARNEAIRLRKKMEGDLNE 1632
Cdd:NF041483 827 ERERASEDANRLRREAQEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEAsDTLASAEQDAARTRADAREDANR 906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1633 MEIQL-SHANRQAAEAQKMVRQLQSQIKDLQIELDDTMRHNDDLK--EQAAALERRNNLLLAEVEELRA--------ALE 1701
Cdd:NF041483 907 IRSDAaAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVraDAAAQAEQLIAEATGEAERLRAeaaetvgsAQQ 986
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1702 QAERGRKLAEQELLEATERVNLLHSQntglinqkKKMEADiAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQ 1781
Cdd:NF041483 987 HAERIRTEAERVKAEAAAEAERLRTE--------AREEAD-RTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKA 1057
|
....*
gi 1394781870 1782 DTSAH 1786
Cdd:NF041483 1058 QEEAL 1062
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1204-1487 |
2.16e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1204 HADS-VAELSEQIDNLQRVKQKLEKEKSEMKMEVDDLSSNIEYLTKNKANAEKLCRTYEDQLNEAKSKVDELQRQLADvs 1282
Cdd:COG3883 13 FADPqIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1283 tqRARLQTESGELSrlleekeSFINQLTrGKTSFTQMIEELkrqleeetkskNALAhalQASRHDCDLLREQYEEEVEAK 1362
Cdd:COG3883 91 --RARALYRSGGSV-------SYLDVLL-GSESFSDFLDRL-----------SALS---KIADADADLLEELKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1363 SElqrslsKANAEVAQwrtkyetdaiqrtEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKHRLQTEIEDLSIDLER 1442
Cdd:COG3883 147 AK------KAELEAKL-------------AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1394781870 1443 ANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEASQKESRSLST 1487
Cdd:COG3883 208 AEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1540-1934 |
2.20e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 43.13 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1540 TLECEKSEIQAALEEAEGALEHEESKTlrIQLELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEA 1619
Cdd:pfam13166 86 TLGEESIEIQEKIAKLKKEIKDHEEKL--DAAEANLQKLDKEKEKLEADFLDECWKKIKRKKNSALSEALNGFKYEANFK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1620 IRLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQ--SQIKDLQIELDDTmrhnddlkEQAAALERRNNLLLAEVEELR 1697
Cdd:pfam13166 164 SRLLREIEKDNFNAGVLLSDEDRKAALATVFSDNKPeiAPLTFNVIDFDAL--------EKAEILIQKVIGKSSAIEELI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1698 A---ALEQAERGRKLAEQelleatervnllHSQNTGLINQ------KKKMEAdiaQLTTEVEEAVQECRNAEEKAKKAIT 1768
Cdd:pfam13166 236 KnpdLADWVEQGLELHKA------------HLDTCPFCGQplpaerKAALEA---HFDDEFTEFQNRLQKLIEKVESAIS 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1769 DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQiALKGGKKQIqkleARVRELE---GELDTEQKKTAEAQ 1845
Cdd:pfam13166 301 SLLAQLPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRR-ALEAKRKDP----FKSIELDsvdAKIESINDLVASIN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1846 KGIRKYERRIKELTYQTEEDRKNLARmqDLIDKLQTKVKSYKRQYEEAEQQANsnlvkyrkvqheldDAEERADIAETQV 1925
Cdd:pfam13166 376 ELIAKHNEITDNFEEEKNKAKKKLRL--HLVEEFKSEIDEYKDKYAGLEKAIN--------------SLEKEIKNLEAEI 439
|
....*....
gi 1394781870 1926 NKLRARSRE 1934
Cdd:pfam13166 440 KKLREEIKE 448
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1546-1705 |
2.26e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.34 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1546 SEIQAALEEAEGALEHEESK--TLRIQLELNQVKADVDRKLAEKDEEFENLRRNHQRamdsMQATLDAEAKARNeairlr 1623
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQlaRLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELER----YQALYKKGAVSQQ------ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1624 kkmegdlnemeiQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDtmrhnddlKEQAAALErrnnlllAEVEELRAALEQA 1703
Cdd:COG1566 149 ------------ELDEARAALDAAQAQLEAAQAQLAQAQAGLRE--------EEELAAAQ-------AQVAQAEAALAQA 201
|
..
gi 1394781870 1704 ER 1705
Cdd:COG1566 202 EL 203
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1774-1930 |
2.49e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1774 AEELKKEQDTSAHLERMKKNMEQTIKDLQmrldeaeqialkggkKQIQKLEARVRELEGELDtEQKKTaeaqkgIRKYER 1853
Cdd:COG2433 391 PEEEPEAEREKEHEERELTEEEEEIRRLE---------------EQVERLEAEVEELEAELE-EKDER------IERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394781870 1854 RIKELtyQTEEDRKNLARmqdlidklqTKVKSYKRQYEEaeqqansnlvkyrkVQHELDDAEERADIAETQVNKLRA 1930
Cdd:COG2433 449 ELSEA--RSEERREIRKD---------REISRLDREIER--------------LERELEEERERIEELKRKLERLKE 500
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
787-1105 |
2.51e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 787 ERLAKILTMLQARIRGrlMRIEYQKIISRRDALYTIQwniRAFNVVKNWSWMKLffKIKPLLRS-AQTEKEMATMKE--- 862
Cdd:COG4913 613 AALEAELAELEEELAE--AEERLEALEAELDALQERR---EALQRLAEYSWDEI--DVASAEREiAELEAELERLDAssd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 863 EFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERcdLLIKAKIQLEAKVKELTERVEDEEEINS 942
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR--LEAAEDLARLELRALLEERFAAALGDAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 943 dLTSKKRKLEDECAELKKDIDDLEITLAKVEKE-KHATENKVKNLIEEMAALDEVIAKLT------------KEKKALQE 1009
Cdd:COG4913 764 -ERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALLDrleedglpeyeeRFKELLNE 842
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1010 AHQQALDDLQAEedkvntLTKAKVKLEQQVDDLESSLEQ-----EKKIRMDLERAKRKlegDLKLTQESVMDLENDKQQL 1084
Cdd:COG4913 843 NSIEFVADLLSK------LRRAIREIKERIDPLNDSLKRipfgpGRYLRLEARPRPDP---EVREFRQELRAVTSGASLF 913
|
330 340
....*....|....*....|..
gi 1394781870 1085 EEKLKKKDFE-MNQLNSRIEDQ 1105
Cdd:COG4913 914 DEELSEARFAaLKRLIERLRSE 935
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1348-1563 |
2.57e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1348 CDLLREQYEEEVEAKSELQRSLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLAIRLQEAEEAVEAAHAKCSSLEKTKH 1427
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1428 RLQTEIE------DLSIDLERANS----AAAALDKKQRNFDRIIAEWKQKYEETQAELE--------ASQKESRSLSTEL 1489
Cdd:PRK05771 118 ELEQEIErlepwgNFDLDLSLLLGfkyvSVFVGTVPEDKLEELKLESDVENVEYISTDKgyvyvvvvVLKELSDEVEEEL 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394781870 1490 fkLKNAYEE-SLDNLETLKRENKNLQEEIADLTDQISmsgKTIHELEKLKKTLEcekSEIQAALEEAEGALEHEE 1563
Cdd:PRK05771 198 --KKLGFERlELEEEGTPSELIREIKEELEEIEKERE---SLLEELKELAKKYL---EELLALYEYLEIELERAE 264
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
849-1145 |
2.58e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 42.79 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 849 RSAQTEKEMATMKEEFQKLKEALEKSEAKRKEL---------------EEKQVTMIQEKNDLAlQLQAEQDNL-----AD 908
Cdd:pfam03528 9 RVAELEKENAEFYRLKQQLEAEFNQKRAKFKELylakeedlkrqnavlQEAQVELDALQNQLA-LARAEMENIkavatVS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 909 AEERCDLLIKAKIQLEAKVKELTERVED-----EEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHaTENKV 983
Cdd:pfam03528 88 ENTKQEAIDEVKSQWQEEVASLQAIMKEtvreyEVQFHRRLEQERAQWNQYRESAEREIADLRRRLSEGQEEEN-LEDEM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 984 KNLIEEMAALDEVIAKLTKEKKALQeahqqalDDLQAEEDKVNTLTKAKVKleqqvdDLESSLEQEKKIRMDLERAKRKL 1063
Cdd:pfam03528 167 KKAQEDAEKLRSVVMPMEKEIAALK-------AKLTEAEDKIKELEASKMK------ELNHYLEAEKSCRTDLEMYVAVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1064 EGDLKLTQESVMDLENDKQQLEEKLKKKDFEMNQLNSRIE--DQQVLEAQ--LQKKIKELQARIEELEEELEAERAARAK 1139
Cdd:pfam03528 234 NTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQkaNDQFLESQrlLMRDMQRMESVLTSEQLRQVEEIKKKDQ 313
|
....*.
gi 1394781870 1140 VEKQRA 1145
Cdd:pfam03528 314 EEHKRA 319
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1605-1812 |
2.61e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1605 MQATLDAEAKARNEAIRLRKKMEGDLnEMEIQLSHANRQAAEAQkmVRQLQSQIKDLQIELDDTMRHNDDLKEQ------ 1678
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQR-EKEKERYKRDREQWERQ--RRELESRVAELKEELRQSREKHEELEEKykelsa 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1679 -AAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVEEAVQECR 1757
Cdd:pfam07888 109 sSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394781870 1758 NAEEKAKKA-------ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDL---QMRLDEAEQIA 1812
Cdd:pfam07888 189 SLSKEFQELrnslaqrDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELrslQERLNASERKV 253
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1437-1771 |
2.78e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1437 SIDLERANSAAAALDKKQRNFdriiaewKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEE 1516
Cdd:PLN02939 99 RASMQRDEAIAAIDNEQQTNS-------KDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1517 IADLTDQISMSGKTIHELEKLKKTLECEKSEIQAALEEAEGALEHEESKTLRIQLELNQVKadvdrklaekdEEFENLRR 1596
Cdd:PLN02939 172 INILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLK-----------EENMLLKD 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1597 NhqraMDSMQATLDAEAKARNEAIRLRKK---MEGDLNEMEIQLSHANRQAAEAQKM-VRQLQSQIKDLQIELDDTMRHn 1672
Cdd:PLN02939 241 D----IQFLKAELIEVAETEERVFKLEKErslLDASLRELESKFIVAQEDVSKLSPLqYDCWWEKVENLQDLLDRATNQ- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1673 ddlKEQAAALERRNNLLLAEVEELRAALEQAERGRklaeqellEATERVNLLHSQNTGLINQKKKMEADIAQLTTEVEEA 1752
Cdd:PLN02939 316 ---VEKAALVLDQNQDLRDKVDKLEASLKEANVSK--------FSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQES 384
|
330 340
....*....|....*....|....
gi 1394781870 1753 VQECRNA-----EEKAKKAITDAA 1771
Cdd:PLN02939 385 IKEFQDTlsklkEESKKRSLEHPA 408
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1421-1568 |
2.79e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.05 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1421 SLEKTKHRLQTEIEDLSidlERANSAAAALDKKQRNFDRIIAEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESL 1500
Cdd:pfam09787 65 KLRGQIQQLRTELQELE---AQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1501 DNLETlkrenknlqeEIADLTDQI---SMSGKTIHELEKLKKTL--------------ECEKSEIQAALEEAEGALEHEE 1563
Cdd:pfam09787 142 KDREA----------EIEKLRNQLtskSQSSSSQSELENRLHQLtetliqkqtmlealSTEKNSLVLQLERMEQQIKELQ 211
|
....*
gi 1394781870 1564 SKTLR 1568
Cdd:pfam09787 212 GEGSN 216
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1572-1785 |
3.06e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1572 ELNQVKADVDRKLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKMV 1651
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1652 RQLQS--------QIKDLQIELDDTMRHNDDLKEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNl 1723
Cdd:COG3883 107 VLLGSesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA- 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394781870 1724 lhsqntGLINQKKKMEADIAQLTTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSA 1785
Cdd:COG3883 186 ------QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
901-1123 |
3.13e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 901 AEQDNLADAEERCDLLIKAKIQLEAKVKELTERVEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATE 980
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 981 NKVKNLIEEMAALDEVIAKLTKEKKALQEAhQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLESSLEQEKKIRmDLERAK 1060
Cdd:COG1340 85 EKLNELREELDELRKELAELNKAGGSIDKL-RKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKAL-EKNEKL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394781870 1061 RKLEGDLKLTQESVMDLENDKQQLEEKLKKKDFEMNQLNSRIEDQQVLEAQLQKKIKELQARI 1123
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKA 225
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1651-1753 |
3.14e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1651 VRQLQSQIKDLQIELDDTMRHNDDL-KEQAAALERRnnllLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNT 1729
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEAsFERLAELRDE----LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIP 488
|
90 100
....*....|....*....|....
gi 1394781870 1730 GLINQKKKMEADIAQLTTEVEEAV 1753
Cdd:COG0542 489 ELEKELAELEEELAELAPLLREEV 512
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
1459-1542 |
3.28e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 41.64 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1459 RIIAEWKQKYEETQAELEASQKESRSLSTELFKLKNAYEESLDNLETLKRENKNLQEEIADLTDQISMSGKTIHELEKlK 1538
Cdd:COG4026 128 PEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLK-K 206
|
....
gi 1394781870 1539 KTLE 1542
Cdd:COG4026 207 RLLE 210
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1583-1898 |
3.48e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.32 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1583 KLAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQikDLQ 1662
Cdd:pfam05667 230 GLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTE--KLQ 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1663 IELDDTMRHNDDLKEQaaalerrnnlllaeveelraalEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADI 1742
Cdd:pfam05667 308 FTNEAPAATSSPPTKV----------------------ETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSI 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1743 AQLTTEVEEavQECRNAEEKAKKAItdAAMMAEELKkeqDTSAHLERMKKNMEQTIKDLQmrldeaeQIALKGGKKQIQK 1822
Cdd:pfam05667 366 KQVEEELEE--LKEQNEELEKQYKV--KKKTLDLLP---DAEENIAKLQALVDASAQRLV-------ELAGQWEKHRVPL 431
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394781870 1823 LEArVRELEGELDteqKKTAEAQKGIRKyerrIKELTyqteedrknlARMQDLIDKLQTKVKSYKR---QYEEAEQQAN 1898
Cdd:pfam05667 432 IEE-YRALKEAKS---NKEDESQRKLEE----IKELR----------EKIKEVAEEAKQKEELYKQlvaEYERLPKDVS 492
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
937-1079 |
3.72e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 937 EEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKE----KHATENKVKNLIEEMAALDeviAKLTKEKKALQeahQ 1012
Cdd:cd22656 105 DATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKltdfENQTEKDQTALETLEKALK---DLLTDEGGAIA---R 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394781870 1013 QALDDLQAEEDKVNTLTKAKVK-----LEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLEN 1079
Cdd:cd22656 179 KEIKDLQKELEKLNEEYAAKLKakideLKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEK 250
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1676-1929 |
4.13e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.27 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1676 KEQAAALERRNNLLLAEVEELRAALEQAERGRKLAEQELLEATERVNLLHSQNTGLINQKKKMEADIA--QLTTEVEEAV 1753
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRdeQEEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1754 QECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQIQKLEARVR----E 1829
Cdd:pfam02463 260 IEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKeeieE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1830 LEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDLIDKLQTKVKSYKRQYEEAEQQANSNLVKYRKvqh 1909
Cdd:pfam02463 340 LEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQ--- 416
|
250 260
....*....|....*....|
gi 1394781870 1910 ELDDAEERADIAETQVNKLR 1929
Cdd:pfam02463 417 LEDLLKEEKKEELEILEEEE 436
|
|
| PRK05901 |
PRK05901 |
RNA polymerase sigma factor; Provisional |
850-1078 |
4.30e-03 |
|
RNA polymerase sigma factor; Provisional
Pssm-ID: 235640 [Multi-domain] Cd Length: 509 Bit Score: 41.90 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 850 SAQTEKEMATMKEEFQKLKEALEKS--------EAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLI---- 917
Cdd:PRK05901 3 TASTKAELAAEEEAKKKLKKLAAKSkskgfitkEEIKEALESKKKTPEQIDQVLIFLSGMVKDTDDATESDIPKKKtkta 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 918 ------------KAKIQLEAKVKELTERVEDEEEINSDLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKN 985
Cdd:PRK05901 83 akaaaakapakkKLKDELDSSKKAEKKNALDKDDDLNYVKDIDVLNQADDDDDDDDDDDLDDDDIDDDDDDEDDDEDDDD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 986 LIEEMAALDEV-IAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKA------------KVKLeqqvddLESslEQEKKI 1052
Cdd:PRK05901 163 DDVDDEDEEKKeAKELEKLSDDDDFVWDEDDSEALRQARKDAKLTATadpvkaylkqigKVKL------LNA--EEEVEL 234
|
250 260
....*....|....*....|....*....
gi 1394781870 1053 RMDLE---RAKRKLEGDLKLTQESVMDLE 1078
Cdd:PRK05901 235 AKRIEaglYAEELLAEGEKLDPELRRDLQ 263
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1032-1549 |
4.41e-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: 42.04 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1032 KVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLK------KKDFEMNQLNSRIEDq 1105
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAeaeealREQAELNRLKKKYLE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1106 QVLEAQLQKKIKELQARiEELEEELEAERAARAKVEKQRAEVARELEELSERLEeaggataiQLEMNKKREAEFLKLRRD 1185
Cdd:pfam05557 87 ALNKKLNEKESQLADAR-EVISCLKNELSELRRQIQRAELELQSTNSELEELQE--------RLDLLKAKASEAEQLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1186 LEEAtlQHESTAAALRKKhaDSVAELSEQIDNLQRVKQKLEKEKS--EMKMEVDDLSSNIEYLTKNKANAEKLcrtyEDQ 1263
Cdd:pfam05557 158 LEKQ--QSSLAEAEQRIK--ELEFEIQSQEQDSEIVKNSKSELARipELEKELERLREHNKHLNENIENKLLL----KEE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1264 LNEAKSKVD---ELQRQLADVSTQRARLQTESGELSRLL----------EEKESFINQLTRGKTSFTQMIEELKRQLEEE 1330
Cdd:pfam05557 230 VEDLKRKLEreeKYREEAATLELEKEKLEQELQSWVKLAqdtglnlrspEDLSRRIEQLQQREIVLKEENSSLTSSARQL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1331 TKSKNALAHALQASRHDCDLLREQYEEEVEAKSELQRSLSKANAEVAQWR------------TKYETDAIQRTEELEEAK 1398
Cdd:pfam05557 310 EKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRailesydkeltmSNYSPQLLERIEEAEDMT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1399 KKLAIRLQEAEEAVEAAHAkcsslEKTKHRLQTEIEDLSIDLERANSAAAALDKKQRNFDriiaEWKQKYEETQAELEAS 1478
Cdd:pfam05557 390 QKMQAHNEEMEAQLSVAEE-----ELGGYKQQAQTLERELQALRQQESLADPSYSKEEVD----SLRRKLETLELERQRL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1479 QKESRSLSTELFKLK---------------------NAYEESLDNLETLKRENKNLQEEIADLTD--------QISMSGK 1529
Cdd:pfam05557 461 REQKNELEMELERRClqgdydpkktkvlhlsmnpaaEAYQQRKNQLEKLQAEIERLKRLLKKLEDdleqvlrlPETTSTM 540
|
570 580
....*....|....*....|
gi 1394781870 1530 TIHELEKLKKTLECEKSEIQ 1549
Cdd:pfam05557 541 NFKEVLDLRKELESAELKNQ 560
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1796-1936 |
4.51e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1796 QTIKDLQMRLDEAEQIalkggKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTEEDRKNLARMQDL 1875
Cdd:COG1579 7 RALLDLQELDSELDRL-----EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1876 IDK---------LQTKVKSYKRQYEEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKLRARSREVV 1936
Cdd:COG1579 82 LGNvrnnkeyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1748-1897 |
5.53e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.48 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1748 EVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKnmeQTIKDLQMRLDEAE-------QIALKGGKKQI 1820
Cdd:pfam15709 349 EVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQEEEErkqrlqlQAAQERARQQQ 425
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394781870 1821 QKLEARVRELEGELDTEQKKTAEAQKgirkyeRRIKELTYQTEEDRKNLARMQdlidklQTKVKSYKRQYEEAEQQA 1897
Cdd:pfam15709 426 EEFRRKLQELQRKKQQEEAERAEAEK------QRQKELEMQLAEEQKRLMEMA------EEERLEYQRQKQEAEEKA 490
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
849-1022 |
5.80e-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: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 849 RSAQTEKEMATMKEEFQKLKEALekseakrkeleEKQVTMIQEKNDLALQLQA--EQDNLADAEERCDLLikaKIQLEAK 926
Cdd:COG3883 66 EIDKLQAEIAEAEAEIEERREEL-----------GERARALYRSGGSVSYLDVllGSESFSDFLDRLSAL---SKIADAD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 927 VKELTERVEDEEEinsdLTSKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVIAKLTKEKKA 1006
Cdd:COG3883 132 ADLLEELKADKAE----LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
170
....*....|....*.
gi 1394781870 1007 LQEAHQQALDDLQAEE 1022
Cdd:COG3883 208 AEAAAAAAAAAAAAAA 223
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1598-1765 |
5.93e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1598 HQRamDSMQATLDA----------------------EAKAR-------NEAIR-LRKKMEGDLNE-MEIQLSHANRQAAE 1646
Cdd:COG2433 333 HER--DALAAALKAydayknkfervekkvppdvdrdEVKARvirglsiEEALEeLIEKELPEEEPeAEREKEHEERELTE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1647 AQKMVRQLQSQIKDLQielddtmRHNDDLKEQAAALERRNNLLLAEVEELRaaleQAERGRKLAEQELleatervnllhs 1726
Cdd:COG2433 411 EEEEIRRLEEQVERLE-------AEVEELEAELEEKDERIERLERELSEAR----SEERREIRKDREI------------ 467
|
170 180 190
....*....|....*....|....*....|....*....
gi 1394781870 1727 qntglinqkKKMEADIAQLTTEVEEAVQECRNAEEKAKK 1765
Cdd:COG2433 468 ---------SRLDREIERLERELEEERERIEELKRKLER 497
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
838-1047 |
6.00e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 838 MKLFFKIKPLLRSAQTEKEmATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNdlalQLQAEQDNLADAEERC---- 913
Cdd:PRK05771 56 SEALDKLRSYLPKLNPLRE-EKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEIS----ELENEIKELEQEIERLepwg 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 914 --DLLIKAKIQLE---AKVKELTERVEDEEEINSD----LTSKKRKLEDECA--ELKKDIDDLEITLAKVEKEkhatenk 982
Cdd:PRK05771 131 nfDLDLSLLLGFKyvsVFVGTVPEDKLEELKLESDvenvEYISTDKGYVYVVvvVLKELSDEVEEELKKLGFE------- 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394781870 983 vKNLIEEMAALDEVIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKA-KVKLEQQVDDLESSLE 1047
Cdd:PRK05771 204 -RLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLAlYEYLEIELERAEALSK 268
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
851-1710 |
6.36e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 851 AQTEKeMATMKEEFQKLKEALEKSEAKRKELEEkQVTMIQEKNDL-------------------------ALQLQAEQDN 905
Cdd:COG3096 344 RQQEK-IERYQEDLEELTERLEEQEEVVEEAAE-QLAEAEARLEAaeeevdslksqladyqqaldvqqtrAIQYQQAVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 906 LADAEERCDLlikAKIQLEAKVKELTERVEDEEEINSDLTSKKRKLedecaelkkdiddleiTLAKVEKEKHAtenKVKN 985
Cdd:COG3096 422 LEKARALCGL---PDLTPENAEDYLAAFRAKEQQATEEVLELEQKL----------------SVADAARRQFE---KAYE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 986 LIEEMAalDEVIAkltkekkalQEAHQQALDDLQAEEDKVNTLTKAkVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEG 1065
Cdd:COG3096 480 LVCKIA--GEVER---------SQAWQTARELLRRYRSQQALAQRL-QQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQ 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1066 DLkltqESVMDLENDKQQLEEKLKKKDfemNQLNSRIEDQQVLEAQLQkkikELQARIEELEEELEAERAARAKVEKQRA 1145
Cdd:COG3096 548 QL----DAAEELEELLAELEAQLEELE---EQAAEAVEQRSELRQQLE----QLRARIKELAARAPAWLAAQDALERLRE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1146 EVARELEELSERLEeaggatAIQLEMNKKREAEFLKlrrdlEEATLQHESTAAALRKKHADSVAELSEqidnLQRVKQKL 1225
Cdd:COG3096 617 QSGEALADSQEVTA------AMQQLLEREREATVER-----DELAARKQALESQIERLSQPGGAEDPR----LLALAERL 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1226 ekeksemkmevddlssnieyltknkaNAEKLCRTYED-----------------------QLNEAKSKVDELQRQLADV- 1281
Cdd:COG3096 682 --------------------------GGVLLSEIYDDvtledapyfsalygparhaivvpDLSAVKEQLAGLEDCPEDLy 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1282 -------STQRARLQTESGELSRL--LEEKE---SFINQLTR-GKTSFTQMIEELKRQLEE--ETKSKNA--------LA 1338
Cdd:COG3096 736 liegdpdSFDDSVFDAEELEDAVVvkLSDRQwrySRFPEVPLfGRAAREKRLEELRAERDElaEQYAKASfdvqklqrLH 815
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1339 HALQA--SRHDCDLLREQYEEEVEA----KSELQRSLSKANAEVAQWRTKYEtdaiQRTEELEEAKKKLAirlqeaeeav 1412
Cdd:COG3096 816 QAFSQfvGGHLAVAFAPDPEAELAAlrqrRSELERELAQHRAQEQQLRQQLD----QLKEQLQLLNKLLP---------- 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1413 eaahaKCSSLEKTKHrlQTEIEDLSIDLERANSAAAALDKKQRN---FDRIIAEWK---QKYEETQAELEASQKESRSLS 1486
Cdd:COG3096 882 -----QANLLADETL--ADRLEELREELDAAQEAQAFIQQHGKAlaqLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLK 954
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1487 TELFKLKN--------AYEESLDNLetlkrenknlqEEIADLTDQISmsgktihelEKLKKTlECEKSEIQAALEEAEGa 1558
Cdd:COG3096 955 QQIFALSEvvqrrphfSYEDAVGLL-----------GENSDLNEKLR---------ARLEQA-EEARREAREQLRQAQA- 1012
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1559 lEHEESKTLRIQLELN-QVKADVdrkLAEKDEEFENLrrnhqramdSMQATLDAEAKARNEAIRL----------RKKME 1627
Cdd:COG3096 1013 -QYSQYNQVLASLKSSrDAKQQT---LQELEQELEEL---------GVQADAEAEERARIRRDELheelsqnrsrRSQLE 1079
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1628 GDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDTMR---HNDDLKEqaaaLERRNNLLLaEVEELRAALEQAE 1704
Cdd:COG3096 1080 KQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRlarDNDVERR----LHRRELAYL-SADELRSMSDKAL 1154
|
....*.
gi 1394781870 1705 RGRKLA 1710
Cdd:COG3096 1155 GALRLA 1160
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
862-1041 |
7.35e-03 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 40.33 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 862 EEFQKLKEALEKSEAKRKELEEKQVTMiQEKNDLALQLQAEQDNLADAEERCDL------LIKAKIQLEAKVKELTERVE 935
Cdd:pfam15934 45 EQEQQLKEFTVQNQRLACQIDNLHETL-KDRDHQIKQLQSMITGYSDISENNRLkeeihdLKQKNCVQARVVRKMGLELK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 936 DEEEINSDLTSKKRKL----EDECAELK---KDIDDLEITLAKVEKEKHATENKVKNLIEEMAALdeviakltKEKKALQ 1008
Cdd:pfam15934 124 GQEEQRVELCDKYESLlgsfEEQCQELKranRRVQSLQTRLSQVEKLQEELRTERKILREEVIAL--------KEKDAKS 195
|
170 180 190
....*....|....*....|....*....|....*..
gi 1394781870 1009 EAHQQALDD----LQAEEDKVNTLTKaKVKLEQQVDD 1041
Cdd:pfam15934 196 NGRERALQDqlkcCQTEIEKSRTLIR-NMQSHLQLED 231
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
860-1105 |
7.50e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.74 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 860 MKEEFQKLKEALEKSEAKRKELEEKQVTMIQEKNDLALQLQAEQDNLADAEERCDLLIKAKIQLEAKvkeltervedEEE 939
Cdd:PTZ00440 726 YTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNK----------ENK 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 940 INSDLTSkkrkLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEVI--AKLTKEKKALQEAHQQALDD 1017
Cdd:PTZ00440 796 ISNDINI----LKENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQKFPTEDENLnlKELEKEFNENNQIVDNIIKD 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1018 LQAEEDKVNTLTK---AKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLTQESVMDLENDKQQLEEKLKKK--D 1092
Cdd:PTZ00440 872 IENMNKNINIIKTlniAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKLNLLNNLNKEKEKIEKQlsD 951
|
250
....*....|...
gi 1394781870 1093 FEMNQLNSRIEDQ 1105
Cdd:PTZ00440 952 TKINNLKMQIEKT 964
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
811-934 |
7.62e-03 |
|
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).
Pssm-ID: 409646 [Multi-domain] Cd Length: 149 Bit Score: 39.03 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 811 KIISRRDALYTIQWNIRAFNVVKnwswmKLFFKIKPLLRSAQTEKEMATMKEEFQKLKEALEKSEAKRKELEEKQVTMIQ 890
Cdd:cd21759 40 KILYRREALIKIQKTVRGYLARK-----KHRPRIKGLRKIRALEKQLKEMEEIASQLKKDKDKWTKQVKELKKEIDALIK 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1394781870 891 E-KNDlalqlqaEQDNLADAEERCDLLIKakiQLEAKVKELTERV 934
Cdd:cd21759 115 KiKTN-------DMITRKEIDKLYNALVK---KVDKQLAELQKKL 149
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1549-1704 |
7.92e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1549 QAALEEAEGALEHEESKTLRIQLELNQVKADVDRKlAEKDEEFENLRRNHQRAMDSMQATLDAEAKARNEAIRLRKKMEG 1628
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDRLQALESEL-AISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPI 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394781870 1629 DLNEMEiQLSHANRQAAEAQKMVRQLQSQIKdlQIELDDTMRHNDDLKEQAAALERRNnlllAEVEELRAALEQAE 1704
Cdd:pfam00529 136 GGISRE-SLVTAGALVAQAQANLLATVAQLD--QIYVQITQSAAENQAEVRSELSGAQ----LQIAEAEAELKLAK 204
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1742-1928 |
7.98e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.01 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1742 IAQLTTEVEEAVQECRNAEEK---AKKAITDAAMMAEELKKE-QDTSAHLERMKKNMEQTIKDLQM---RLDEAEQiALK 1814
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKleeAEKRAEKAEAEVAALNRRiQLLEEELERTEERLAEALEKLEEaekAADESER-GRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1815 GGKKQIQKLEARVRELEGELDTEQKKTAEAQKGIRKYERRIKELTYQTE--EDRKNLA--RMQDLIDKLQT---KVKSYK 1887
Cdd:pfam00261 82 VLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLEraEERAELAesKIVELEEELKVvgnNLKSLE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1394781870 1888 RQYEEAEQQANSNLVKYRKVQHELDDAEERADIAETQVNKL 1928
Cdd:pfam00261 162 ASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL 202
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1279-1649 |
8.53e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 40.86 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1279 ADVSTQRARLQTESGELSRLLEEKESFINQlTRGKtsftqmIEELKRQLEEETKSKNAlahALQASRHDCDLLREQYEEe 1358
Cdd:pfam03528 4 EDLQQRVAELEKENAEFYRLKQQLEAEFNQ-KRAK------FKELYLAKEEDLKRQNA---VLQEAQVELDALQNQLAL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1359 veAKSELQRSlsKANAEVAQWRTKYETDAIQRTEELEEAKKKLAIRlqeaeeaveaaHAKCSSLEKTKHRLQTEiedlsi 1438
Cdd:pfam03528 73 --ARAEMENI--KAVATVSENTKQEAIDEVKSQWQEEVASLQAIMK-----------ETVREYEVQFHRRLEQE------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1439 dleransaAAALDKKQRNFDRIIAEWKQKYEETQAELeasqkesrslstelfKLKNAYEESLDNLETLKRENKNLQEEIA 1518
Cdd:pfam03528 132 --------RAQWNQYRESAEREIADLRRRLSEGQEEE---------------NLEDEMKKAQEDAEKLRSVVMPMEKEIA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1519 DLTDQISMSGKTIHELE-----KLKKTLECEKS-----EIQAALEEAEGALEHEESKTLRIQLElnqvkaDVDRKLAEKD 1588
Cdd:pfam03528 189 ALKAKLTEAEDKIKELEaskmkELNHYLEAEKScrtdlEMYVAVLNTQKSVLQEDAEKLRKELH------EVCHLLEQER 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394781870 1589 EEFENLRRNHQRAMDSMQatldaeakarnEAIRLrkkMEGDLNEMEIQLSHAN-RQAAEAQK 1649
Cdd:pfam03528 263 QQHNQLKHTWQKANDQFL-----------ESQRL---LMRDMQRMESVLTSEQlRQVEEIKK 310
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1651-1896 |
8.74e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1651 VRQLQSQIKDLQIELDDTmrhNDDLKEQAAALERRNNLLLAEVEELRAALEQAergRKLAEQelleatervnllhsqntg 1730
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHI---QQQIKTYNKNIEEQRKKNGENIARKQNKYDEL---VEEAKT------------------ 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1731 linqkkkMEADIAQLTTEVEEAVQECRNAEEKAKK---AITDAAMMAEELKKE--------------QDTSAHLERMKKN 1793
Cdd:PHA02562 232 -------IKAEIEELTDELLNLVMDIEDPSAALNKlntAAAKIKSKIEQFQKVikmyekggvcptctQQISEGPDRITKI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1794 MEQtIKDLQMRLDEAeqialkggKKQIQKLEarvrELEGELDTEQKKTAEAQKGIRKYERRIKELtyqteedRKNLARMQ 1873
Cdd:PHA02562 305 KDK-LKELQHSLEKL--------DTAIDELE----EIMDEFNEQSKKLLELKNKISTNKQSLITL-------VDKAKKVK 364
|
250 260
....*....|....*....|...
gi 1394781870 1874 DLIDKLQTKVKSYKRQYEEAEQQ 1896
Cdd:PHA02562 365 AAIEELQAEFVDNAEELAKLQDE 387
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1544-1785 |
8.94e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.09 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1544 EKSEIQAALEEAEGAlehEESKtlrIQLELNQvkADVDRKLAEKDEEfenlrrnHQRAMDSMQATLDAEAKARNEAIRlR 1623
Cdd:PRK05035 434 AKAEIRAIEQEKKKA---EEAK---ARFEARQ--ARLEREKAAREAR-------HKKAAEARAAKDKDAVAAALARVK-A 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1624 KKMEGDLNEMEIQLSHANRQAAEAQKMVRQLQSQIKDLQIELDDtmrHNDDLKEQ-AAALER----------RNNLLLAE 1692
Cdd:PRK05035 498 KKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAA---AADPKKAAvAAAIARakakkaaqqaANAEAEEE 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1693 VEELRAALEQAERGRKLAEQELLEATERVNllhSQNTGLINQKKKMEADIAQLTTEVEEAVQECRNAE-EKAKKAITDAA 1771
Cdd:PRK05035 575 VDPKKAAVAAAIARAKAKKAAQQAASAEPE---EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEpVDPRKAAVAAA 651
|
250
....*....|....
gi 1394781870 1772 MMAEELKKEQDTSA 1785
Cdd:PRK05035 652 IARAKARKAAQQQA 665
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
932-1148 |
9.28e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 932 ERVEDEEEInSDLTSKKRKLEDECAELKKDIDDLEITLAKVEkEKHATENKVKNLIEEM--AALDEVIAKLTKEKKALQE 1009
Cdd:PHA02562 154 KLVEDLLDI-SVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQ-QQIKTYNKNIEEQRKKngENIARKQNKYDELVEEAKT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1010 AHQQalddlqaeedkVNTLTKAKVKLEQQVDDLESSLeqeKKIRMDLERAKRKLEgdlKLTQESVMDLEND-----KQQL 1084
Cdd:PHA02562 232 IKAE-----------IEELTDELLNLVMDIEDPSAAL---NKLNTAAAKIKSKIE---QFQKVIKMYEKGGvcptcTQQI 294
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394781870 1085 EE------KLKKKDFEM----NQLNSRIEDQQVLE---AQLQKKIKELQARIEELEEELEAERAARAKVEK--QRAEVA 1148
Cdd:PHA02562 295 SEgpdritKIKDKLKELqhslEKLDTAIDELEEIMdefNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAaiEELQAE 373
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1356-1536 |
9.32e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1356 EEEVEAKSELQRSLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLAIRlqeaeeaVEAAHAKCSSLEKTKHRLQTEIED 1435
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK-------EENLDRKLELLEKREEELEKKEKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1436 lsidleransaaaaLDKKQRNFDRIIAEWKQKYEETQAELEasqkESRSLSTElfklkNAYEESLDNLEtlkrenKNLQE 1515
Cdd:PRK12704 119 --------------LEQKQQELEKKEEELEELIEEQLQELE----RISGLTAE-----EAKEILLEKVE------EEARH 169
|
170 180
....*....|....*....|.
gi 1394781870 1516 EIAdltdqismsgKTIHELEK 1536
Cdd:PRK12704 170 EAA----------VLIKEIEE 180
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1235-1386 |
9.60e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1235 EVDDLSSNIEYLT-------KNKANAEKLCRTYEDQLNEAKSKVDELQRQLADVSTQRARLQTESGELSRLLEEKESFIN 1307
Cdd:PRK09039 54 ALDRLNSQIAELAdllslerQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394781870 1308 QLTRGKTSFTQMIEELKRQLeeetkskNALAHALQASrhdcdllrEQYEEEVEAK-SELQRSLSKANAEVAQWRTKYETD 1386
Cdd:PRK09039 134 RALAQVELLNQQIAALRRQL-------AALEAALDAS--------EKRDRESQAKiADLGRRLNVALAQRVQELNRYRSE 198
|
|
| |
