|
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: 1485.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAIVAALGDTPAKKGHGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVESLDDGQELMATDN 338
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 419 QNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 499 ILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPDKKRKY 578
Cdd:cd14927 401 ILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 579 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSVSDPKPGFKEKRKKAASFQTVSQL 658
Cdd:cd14927 481 EAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEDPKSGVKEKRKKAASFQTVSQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 659 HKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHAI 738
Cdd:cd14927 561 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAI 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 1529987947 739 PDDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 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: 1345.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAIVAALGdtpakKGHGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASS-----KKKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVESLDDGQELMATDN 338
Cdd:cd01377 156 TGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd01377 236 AFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 419 QNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd01377 316 QNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 499 ILEQEEYKREGIEWTFIDFGLDLQACIDLIEKP-MGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPrpdKKRK 577
Cdd:cd01377 396 VLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKP---KPKK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 578 YEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSvsdpkpGFKEKRKKAASFQTVSQ 657
Cdd:cd01377 473 SEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGG------GGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 658 LHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHA 737
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*..
gi 1529987947 738 IPDDkFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 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: 1170.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAIVAALGDTPAKKGhgpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLG---------ALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKpELLDMLLVSSNPYDYHFCSQGVTTVESLDDGQELMATDN 338
Cdd:cd14929 152 RGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd14929 231 AMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 419 QNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14929 311 QNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 499 ILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPDKKrKY 578
Cdd:cd14929 391 VLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKK-KF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 579 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSVSDpkpgFKEK-RKKAASFQTVSQ 657
Cdd:cd14929 470 EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQ----FGEKkRKKGASFQTVAS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 658 LHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHA 737
Cdd:cd14929 546 LHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRT 625
|
650 660 670
....*....|....*....|....*....|....*..
gi 1529987947 738 IPDDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14929 626 FPKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 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: 1153.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 180 SGAGKTVNTKRVIQYFAIVAALGDTPAKKghgpATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKKK----DSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVESLDDGQELMATDNA 339
Cdd:cd14913 158 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 420 NVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14913 318 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 500 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPDKKRKyE 579
Cdd:cd14913 398 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRA-E 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSVSDPKpgfKEKRKKAASFQTVSQLH 659
Cdd:cd14913 477 AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKK---KVAKKKGSSFQTVSALF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 660 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHAIP 739
Cdd:cd14913 554 RENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIP 633
|
650 660 670
....*....|....*....|....*....|....*
gi 1529987947 740 DDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 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: 1111.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 180 SGAGKTVNTKRVIQYFAIVAALGDTpAKKGHGPATktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDR-SKKDQTPGK---GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVESLDDGQELMATDNA 339
Cdd:cd14917 158 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14917 238 FDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 420 NVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14917 318 NVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 500 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRpDKKRKYE 579
Cdd:cd14917 398 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPR-NIKGKPE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSvsdPKPGFKEKRKKAASFQTVSQLH 659
Cdd:cd14917 477 AHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADA---PIEKGKGKAKKGSSFQTVSALH 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 660 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHAIP 739
Cdd:cd14917 554 RENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 633
|
650 660 670
....*....|....*....|....*....|....*
gi 1529987947 740 DDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 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: 1075.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 180 SGAGKTVNTKRVIQYFAIVAALGDTPAKKGhgpATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKKEN---PNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVESLDDGQELMATDNA 339
Cdd:cd14916 159 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 420 NVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 500 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRpDKKRKYE 579
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPR-NVKGKQE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSVSDPKPgfKEKRKKAASFQTVSQLH 659
Cdd:cd14916 478 AHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKG--KGGKKKGSSFQTVSALH 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 660 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHAIP 739
Cdd:cd14916 556 RENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 635
|
650 660 670
....*....|....*....|....*....|....*
gi 1529987947 740 DDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 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: 1049.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 180 SGAGKTVNTKRVIQYFAIVAALGDtpaKKGHGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGD---KKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVESLDDGQELMATDNA 339
Cdd:cd14923 159 GKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14923 239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 420 NVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 500 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPdKKRKYE 579
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKP-AKGKAE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSvSDPKPGFKEKRKKAASFQTVSQLH 659
Cdd:cd14923 478 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEA-GDSGGSKKGGKKKGSSFQTVSAVF 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 660 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHAIP 739
Cdd:cd14923 557 RENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIP 636
|
650 660 670
....*....|....*....|....*....|....*
gi 1529987947 740 DDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 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 1529987947 87 IEDMAMLTHLNEASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 167 RNRENQSMLITGESGAGKTVNTKRVIQYFAIVAalgdtpakkGHGPATKtGGTLEDQIIEANPAMEAFGNAKTLRNDNSS 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVS---------GSGSAGN-VGRLEEQILQSNPILEAFGNAKTVRNNNSS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 247 RFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVsSNPYDYHFCSQ-GVTTVE 325
Cdd:pfam00063 151 RFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TNPKDYHYLSQsGCYTID 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 326 SLDDGQELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLH 405
Cdd:pfam00063 230 GIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 406 PRVKVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINF 484
Cdd:pfam00063 310 RRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLdVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 485 TNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPMGIMSILEEECMFPKATDNSFKAKMYDNHiGK 563
Cdd:pfam00063 390 VNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 564 SPNFQKPRPdkkrKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSVSDPKPGFK 643
Cdd:pfam00063 468 HPHFQKPRL----QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKS 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 644 -EKRKKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRIL 722
Cdd:pfam00063 544 tPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRIT 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1529987947 723 YAEFKQRYRILNPHAIPDDkFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:pfam00063 624 FQEFVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| 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: 1032.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 101 VLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 181 GAGKTVNTKRVIQYFAIVAALGDtpakKGHGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTG 260
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGE----KKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 261 KLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVESLDDGQELMATDNAM 340
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 341 DILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQN 420
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 421 VEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFIL 500
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 501 EQEEYKREGIEWTFIDFGLDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPdKKRKYEA 580
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKV-VKGKAEA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 581 HFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSVSDPKPGFKekrKKAASFQTVSQLHK 660
Cdd:cd14918 478 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAK---KKGSSFQTVSALFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 661 ENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHAIPD 740
Cdd:cd14918 555 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE 634
|
650 660 670
....*....|....*....|....*....|....
gi 1529987947 741 DKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14918 635 GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| 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: 1028.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 180 SGAGKTVNTKRVIQYFAIVAALGDTpaKKGHGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVESLDDGQELMATDNA 339
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14910 240 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 420 NVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14910 320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 500 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPdKKRKYE 579
Cdd:cd14910 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKVE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDsvSDPKPGFKEKRKKAASFQTVSQLH 659
Cdd:cd14910 479 AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAE--AEEGGGKKGGKKKGSSFQTVSALF 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 660 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHAIP 739
Cdd:cd14910 557 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 636
|
650 660 670
....*....|....*....|....*....|....*
gi 1529987947 740 DDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14910 637 EGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| 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: 1026.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 180 SGAGKTVNTKRVIQYFAIVAALGDTpaKKGHGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVESLDDGQELMATDNA 339
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14915 240 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 420 NVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 500 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPdKKRKYE 579
Cdd:cd14915 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENyvGSDSVSDPKPGFKEKRKKAASFQTVSQLH 659
Cdd:cd14915 479 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG--GQTAEAEGGGGKKGGKKKGSSFQTVSALF 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 660 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHAIP 739
Cdd:cd14915 557 RENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 636
|
650 660 670
....*....|....*....|....*....|....*
gi 1529987947 740 DDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14915 637 EGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| 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: 1020.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 180 SGAGKTVNTKRVIQYFAIVAALGDTpaKKGHGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVESLDDGQELMATDNA 339
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14912 240 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 420 NVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 500 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPdKKRKYE 579
Cdd:cd14912 400 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKV-VKGKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSVSDPKPGFKEKRKKAASFQTVSQLH 659
Cdd:cd14912 479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAKKGGKKKGSSFQTVSALF 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 660 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHAIP 739
Cdd:cd14912 559 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 638
|
650 660 670
....*....|....*....|....*....|....*
gi 1529987947 740 DDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 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: 1012.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAIVAALGDTpakkghgpATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQ--------SSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVESLDDGQELMATDN 338
Cdd:cd14934 153 TGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd14934 233 AFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 419 QNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14934 313 QNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 499 ILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPDKKRKY 578
Cdd:cd14934 393 VLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKGP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 579 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYEnyvgsdsvSDPKPGFKEKRKKAASFQTVSQL 658
Cdd:cd14934 473 EAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFK--------EEEAPAGSKKQKRGSSFMTVSNF 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 659 HKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHAI 738
Cdd:cd14934 545 YREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVI 624
|
650 660 670
....*....|....*....|....*....|....*.
gi 1529987947 739 PDDkFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14934 625 PQG-FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| 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: 1003.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAIVAALGDTPakkghgPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTD------EAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVESLDDGQELMATDN 338
Cdd:cd14909 155 TGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd14909 235 AFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 419 QNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14909 315 RNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 499 ILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPDKKRKY 578
Cdd:cd14909 395 VLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 579 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDsvSDPKPGFKEKRKKAASFQTVSQL 658
Cdd:cd14909 475 AAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQS--GGGEQAKGGRGKKGGGFATVSSA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 659 HKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHAI 738
Cdd:cd14909 553 YKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGI 632
|
650 660 670
....*....|....*....|....*....|....*.
gi 1529987947 739 PDDKfvDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14909 633 QGEE--DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| 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: 1000.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 80 NPPKYDLIEDMAMLTHLNEASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIAD 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 160 NAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAIVAAlgdtpakkghgpATKTGGTLEDQIIEANPAMEAFGNAKT 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG------------SNTEVGSVEDQILESNPILEAFGNAKT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 240 LRNDNSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQ 319
Cdd:smart00242 149 LRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 320 GVT-TVESLDDGQELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEA-DGTESADKASYLMGVSSA 397
Cdd:smart00242 228 GGClTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTvKDKEELSNAAELLGVDPE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 398 DLIKGLLHPRVKVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSF 477
Cdd:smart00242 308 ELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 478 EQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPMGIMSILEEECMFPKATDNSFKAKM 556
Cdd:smart00242 388 EQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 557 YDNHiGKSPNFQKPRpdkkRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSdsvs 636
Cdd:smart00242 467 NQHH-KKHPHFSKPK----KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSN---- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 637 dpkpgfKEKRKKaasFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKG 716
Cdd:smart00242 538 ------AGSKKR---FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAG 608
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 717 FPNRILYAEFKQRYRILNPHAIPDDKFvDSRKAAEKLLASLDIDHNQYRFGHTKVFFKAGLLGHLEELRD 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: 871.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 36 RAWIPDEKEAYIEIEIKELSGDKVIV----ETKDGRTLTVKVDDIQQ--MNPPKYDLIEDMAMLTHLNEASVLYNLRRRY 109
Cdd:COG5022 11 GCWIPDEEKGWIWAEIIKEAFNKGKVteegKKEDGESVSVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPAVLHNLEKRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 110 SAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITGESGAGKTVNTK 189
Cdd:COG5022 91 NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 190 RVIQYFAIVAAlGDTPAKkghgpatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDI 269
Cdd:COG5022 171 RIMQYLASVTS-SSTVEI----------SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 270 YLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQG-VTTVESLDDGQELMATDNAMDILGFLPD 348
Cdd:COG5022 240 YLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQ-NPKDYIYLSQGgCDKIDGIDDAKEFKITLDALKTIGIDEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 349 EKYGCYKIVGAIMHFGNMKFKqKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVIYAV 428
Cdd:COG5022 319 EQDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 429 GALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKRE 508
Cdd:COG5022 398 DSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 509 GIEWTFIDFgLDLQACIDLIEK--PMGIMSILEEECMFPKATDNSFKAKMYDN-HIGKSPNFQKPR-PDKKrkyeahFEL 584
Cdd:COG5022 478 GIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRfRDNK------FVV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 585 VHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSvsdpkpgfkeKRKkaasFQTVSQLHKENLN 664
Cdd:COG5022 551 KHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIES----------KGR----FPTLGSRFKESLN 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 665 KLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHAIPDDKFV 744
Cdd:COG5022 617 SLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYT 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 745 ---DSRKAAEKLLASLDIDHNQYRFGHTKVFFKAGLLGHLEELRDERLAKVLTLLQAVARGKIMRLELQRMMERREALMI 821
Cdd:COG5022 697 wkeDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQV 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 822 IQWNIRAFNAVKHWPWMKLFFKIKPLLRSAATEKELAALKVELAKLKEALEKsEIKRKELEERQVSLIQEKNDLSLQLQA 901
Cdd:COG5022 777 IQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKR-EKKLRETEEVEFSLKAEVLIQKFGRSL 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 902 EQDNLADAEDRCDLLIKTKIQLEAKVKELMErLEDEEEMSSNVLAKKRKLEDECAELKKDID-----DLEITLAKIEKEK 976
Cdd:COG5022 856 KAKKRFSLLKKETIYLQSAQRVELAERQLQE-LKIDVKSISSLKLVNLELESEIIELKKSLSsdlieNLEFKTELIARLK 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 977 HAIEN-KVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMD 1055
Cdd:COG5022 935 KLLNNiDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQES 1014
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1529987947 1056 LERVKRKLEGDlkLSLESVMdlendkqqleeklkKKDFEMNELSTRIEDEQALVNQLQKKIKELQART 1123
Cdd:COG5022 1015 TKQLKELPVEV--AELQSAS--------------KIISSESTELSILKPLQKLKGLLLLENNQLQARY 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: 828.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSES-PPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSADlPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 178 GESGAGKTVNTKRVIQYFAIVAALGDTPAKKghgpatkTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSS-------SASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHF----CSQGVTTVESLDDGQEL 333
Cdd:cd00124 154 PTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDDAEEF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 334 MATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREE--QAEADGTESADKASYLMGVSSADLIKGLLHPRVKVG 411
Cdd:cd00124 234 QELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 412 NEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQ--YFIGVLDIAGFEIFELNSFEQLCINFTNEKL 489
Cdd:cd00124 314 GETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 490 QQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPMGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQ 568
Cdd:cd00124 394 QQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 569 KPRPDKKrkyeaHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSAnkllaslyenyvgsdsvsdpkpgfkekrkk 648
Cdd:cd00124 473 KKRKAKL-----EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS------------------------------ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 649 aasfqtvsqLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQ 728
Cdd:cd00124 518 ---------QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLK 588
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1529987947 729 RYRILNPHAiPDDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 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: 795.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAIVAAL----GDTPAKKGHGPATKTGGtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 254
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgSGAVPHPAVNPAVLIGE-LEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 255 HFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS-----QKKPELLDmllvssNPYDYHFCSQGVTTVESLDD 329
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAgatpeQREKFILD------DVKSYAFLSNGSLPVPGVDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 330 GQELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVK 409
Cdd:cd14911 234 YAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 410 VGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEK 488
Cdd:cd14911 314 VGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLdRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 489 LQQFFNHHMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQ 568
Cdd:cd14911 394 LQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFM 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 569 KprpdKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENY----VGSDSVSDPKPGfke 644
Cdd:cd14911 473 K----TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAeivgMAQQALTDTQFG--- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 645 KRKKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYA 724
Cdd:cd14911 546 ARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1529987947 725 EFKQRYRILNPHAIPdDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14911 626 EFRQRYELLTPNVIP-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: 778.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAIVAAlgdtpAKKGhGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVAS-----SHKG-RKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPEL-LDMLLVSSNpyDYHFCSQGVTTVESLDDGQELMATD 337
Cdd:cd14920 155 TGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 338 NAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVK 417
Cdd:cd14920 233 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 418 GQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLyTSLPRQ--YFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNH 495
Cdd:cd14920 313 AQTKEQADFAVEALAKATYERLFRWLVHRINKAL-DRTKRQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 496 HMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPM---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKPRp 572
Cdd:cd14920 392 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPR- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 573 dkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYEN---YVGSDSVSD-PKPGFKEKRK- 647
Cdd:cd14920 470 --QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrIVGLDQVTGmTETAFGSAYKt 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 648 KAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFK 727
Cdd:cd14920 548 KKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1529987947 728 QRYRILNPHAIPdDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14920 628 QRYEILTPNAIP-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: 729.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAIVAAlgDTPAKKGHGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVAS--SFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPyDYHFCSQGVTTVESLDDGQELMATDN 338
Cdd:cd14932 159 NGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYS-KYRFLSNGNVTIPGQQDKELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 419 QNVEQVIYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHM 497
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALdKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 498 FILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPM---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKPrpdK 574
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQ-GNNPKFQKP---K 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 575 KRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENY---VGSDSV---SDPKPGFKEKRKk 648
Cdd:cd14932 474 KLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdriVGLDKVagmGESLHGAFKTRK- 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 649 aASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQ 728
Cdd:cd14932 553 -GMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1529987947 729 RYRILNPHAIPDDkFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14932 632 RYEILTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| 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: 699.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAIVAAlgdtpAKKGHGPATKTgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVAS-----SHKGKKDTSIT-GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELL-DMLLVSSNpyDYHFCSQGVTTVESLDDGQELMATD 337
Cdd:cd14921 155 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 338 NAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVK 417
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 418 GQNVEQVIYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHH 496
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKALdKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 497 MFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPM---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKPrpd 573
Cdd:cd14921 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKP--- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 574 KKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENY---VGSDSVSDPKPGF--KEKRKK 648
Cdd:cd14921 469 KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdriVGLDQMAKMTESSlpSASKTK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 649 AASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQ 728
Cdd:cd14921 549 KGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1529987947 729 RYRILNPHAIPDDkFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14921 629 RYEILAANAIPKG-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: 690.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAIVAALGDTpaKKGHGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKT--KKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQGVTTVESLDDGQELMATDN 338
Cdd:cd15896 159 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLE-NYNNYRFLSNGNVTIPGQQDKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 419 QNVEQVIYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHM 497
Cdd:cd15896 318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALdKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 498 FILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPM---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKPrpdK 574
Cdd:cd15896 398 FILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKP---K 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 575 KRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENY---VGSDSVS--DPKPGFKEKRKka 649
Cdd:cd15896 474 KLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVdriVGLDKVSgmSEMPGAFKTRK-- 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 650 ASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQR 729
Cdd:cd15896 552 GMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1529987947 730 YRILNPHAIPDDkFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd15896 632 YEILTPNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| 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: 689.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAIVAALGDTPAKKGhgpatkTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPG------VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYdYHFCSQGVTTveslDDGQE---LMA 335
Cdd:cd14930 155 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSS----SPGQErelFQE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 336 TDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 415
Cdd:cd14930 230 TLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 416 VKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSlPRQ--YFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFF 493
Cdd:cd14930 310 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRS-PRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 494 NHHMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPM---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKP 570
Cdd:cd14930 389 NHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 571 RpdkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLY---ENYVGSDSVSDPKPGFKEKRK 647
Cdd:cd14930 468 R---HLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRP 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 648 KAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFK 727
Cdd:cd14930 545 RRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFR 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1529987947 728 QRYRILNPHAIPDDkFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14930 625 QRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| 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: 685.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAIVAAlgdtpakkgHGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVAS---------SHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsnPYD-YHFCSQGVTTVESLDDGQELMATD 337
Cdd:cd14919 152 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE--PYNkYRFLSNGHVTIPGQQDKDMFQETM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 338 NAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVK 417
Cdd:cd14919 230 EAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 418 GQNVEQVIYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHH 496
Cdd:cd14919 310 AQTKEQADFAIEALAKATYERMFRWLVLRINKALdKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 497 MFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPM---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKPrpd 573
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKP--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 574 KKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENY---VGSDSVSDPK----PGFKEKR 646
Cdd:cd14919 466 KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriIGLDQVAGMSetalPGAFKTR 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 647 KkaASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEF 726
Cdd:cd14919 546 K--GMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEF 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1529987947 727 KQRYRILNPHAIPDDkFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14919 624 RQRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| 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: 681.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 100 SVLYNLRRRYS-AWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAIVAalgdtpakkghGPATKTGGTlEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVG-----------GSSSGETQV-EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQK-KPELLDMLLVSSNpyDYHFCSQG-VTTVESLDDGQELMAT 336
Cdd:cd01380 150 NYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKELHLGSAE--DFFYTNQGgSPVIDGVDDAAEFEET 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 337 DNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVV 416
Cdd:cd01380 228 RKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 417 KGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLP--RQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFN 494
Cdd:cd01380 308 KPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 495 HHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHIGK-SPNFQKPRPD 573
Cdd:cd01380 388 QHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 574 KKRkyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANkllaslyenyvgsdsvsdpkpgfkekRKKaasfq 653
Cdd:cd01380 467 NTA-----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN--------------------------RKK----- 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 654 TVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRIL 733
Cdd:cd01380 511 TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVL 590
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1529987947 734 NP--HAIPDDKfvdsRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd01380 591 LPskEWLRDDK----KKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| 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: 655.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 180 SGAGKTVNTKRVIQYFAIVAalgdtpakkghGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVS-----------GGSESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVESLDDGQELMATDNA 339
Cdd:cd01378 151 GEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADgTESADKASYLMGVSSADLIKGLLHPRVKVGNEY---VV 416
Cdd:cd01378 231 MKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 417 KGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQ-YFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFfnh 495
Cdd:cd01378 310 VPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQI--- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 496 hmFIL-----EQEEYKREGIEWTFIDFgLDLQACIDLIE-KPMGIMSILEEECMFP-KATDNSFKAKMydNHIGKSPNFQ 568
Cdd:cd01378 387 --FIEltlkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL--NQLFSNHPHF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 569 KPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSvsdpkpgfkEKRKK 648
Cdd:cd01378 462 ECPSGHFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDS---------KKRPP 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 649 AASFQTvsqlhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQ 728
Cdd:cd01378 533 TAGTKF-----KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLE 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1529987947 729 RYRILNPHAIPDDKFvDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd01378 608 RYKLLSPKTWPAWDG-TWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| 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: 649.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAIVAALGDtpakkghgpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS---------------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVsSNPYDYHFCSQG-VTTVESLDDGQELMATD 337
Cdd:cd01381 146 NGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLEL-GDASDYYYLTQGnCLTCEGRDDAAEFADIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 338 NAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQRE--EQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 415
Cdd:cd01381 225 SAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 416 VKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYF---IGVLDIAGFEIFELNSFEQLCINFTNEKLQQF 492
Cdd:cd01381 305 VSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 493 FNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLI-EKPMGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKPr 571
Cdd:cd01381 385 FVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 572 pdkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSvsdpkpgfkEKRKKAas 651
Cdd:cd01381 462 ---KSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGS---------ETRKKS-- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 652 fQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYR 731
Cdd:cd01381 528 -PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYR 606
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1529987947 732 ILNPhAIPDDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd01381 607 VLVP-GIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| 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: 621.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 180 SGAGKTVNTKRVIQYFAIVaalgdtpakkghgpaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAV---------------TNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDAS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS--QKKPELLDMLLVSSnPYDYHFCSQ-GVTTVESLDDGQELMAT 336
Cdd:cd14883 147 GHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAgaKHSKELKEKLKLGE-PEDYHYLNQsGCIRIDNINDKKDFDHL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 337 DNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAE-ADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 415
Cdd:cd14883 226 RLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 416 VKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNH 495
Cdd:cd14883 306 EIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 496 HMFILEQEEYKREGIEWTFIDFGlDLQACIDLIEK-PMGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKPrpdK 574
Cdd:cd14883 386 YVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKP---D 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 575 KRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASL--YENYVGSDSVSDPKPGFKEKRKKAASF 652
Cdd:cd14883 461 RRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELftYPDLLALTGLSISLGGDTTSRGTSKGK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 653 QTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRI 732
Cdd:cd14883 541 PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLC 620
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1529987947 733 LNPHAI-PDDKfvDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 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: 617.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKgkRRSESPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 180 SGAGKTVNTKRVIQYfaiVAALGdtpakkGHGPAtktggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd01383 80 SGAGKTETAKIAMQY---LAALG------GGSSG------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQ-GVTTVESLDDGQELMATDN 338
Cdd:cd01383 145 GKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQsNCLTIDGVDDAKKFHELKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd01383 224 ALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 419 QNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTS-LPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHM 497
Cdd:cd01383 304 LTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGkRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 498 FILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPMGIMSILEEECMFPKATDNSFKAKMyDNHIGKSPNFQKPRpdkkr 576
Cdd:cd01383 384 FKLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER----- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 577 kyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSvsdpKPGFKEKRKKAASF-QTV 655
Cdd:cd01383 457 --GGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASR----KALPLTKASGSDSQkQSV 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 656 SQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNP 735
Cdd:cd01383 531 ATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLP 610
|
650 660 670
....*....|....*....|....*....|....*....
gi 1529987947 736 HAIPDDKFVDSRKAAekLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd01383 611 EDVSASQDPLSTSVA--ILQQFNILPEMYQVGYTKLFFR 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: 582.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 178 GESGAGKTVNTKRVIQYFAIVAalgdtpakkghGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG-----------GRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQGVT-TVESLDDGQELMAT 336
Cdd:cd01384 150 DAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLK-DPKQFHYLNQSKCfELDGVDDAEEYRAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 337 DNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKqkqreEQAEADGTESADKASY--------LMGVSSADLIKGLLHPRV 408
Cdd:cd01384 229 RRAMDVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEKSEfhlkaaaeLLMCDEKALEDALCKRVI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 409 KVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEK 488
Cdd:cd01384 304 VTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 489 LQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPMGIMSILEEECMFPKATDNSFKAKMYDNhIGKSPNF 567
Cdd:cd01384 384 LQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 568 QKPrpdkKRKYEAhFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYEnyvgsdsvsdpkPGFKEKRK 647
Cdd:cd01384 462 SKP----KLSRTD-FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFP------------PLPREGTS 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 648 KAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFK 727
Cdd:cd01384 525 SSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1529987947 728 QRYRILNPHAipDDKFVDSRKAAEKLLASLDIdhNQYRFGHTKVFFK 774
Cdd:cd01384 605 DRFGLLAPEV--LKGSDDEKAACKKILEKAGL--KGYQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-774 |
2.03e-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: 545.31 E-value: 2.03e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 178 GESGAGKTVNTKRVIQYFAIVaalgdtpakkgHGpatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTES-----------WG---SGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNpydyhfcsqgvttvesLDDGQELMATD 337
Cdd:cd01382 147 EKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPL----------------LDDVGDFIRMD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 338 NAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREE----QAEADGTESADKASYLMGVSSADLIKGLLHpRVKVGNE 413
Cdd:cd01382 211 KAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSgggcNVKPKSEQSLEYAAELLGLDQDELRVSLTT-RVMQTTR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 414 YVVKGQ------NVEQVIYAVGALAKATYDRMFKWLVGRINRtlytSLPRQ---YFIGVLDIAGFEIFELNSFEQLCINF 484
Cdd:cd01382 290 GGAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQ----CIPFEtssYFIGVLDIAGFEYFEVNSFEQFCINY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 485 TNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPMGIMSILEEECMFPKATDNSFKAKMYDNHiGK 563
Cdd:cd01382 366 CNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKH-KN 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 564 SPNFQKPRPDKKRKY------EAhFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSVSD 637
Cdd:cd01382 444 HFRLSIPRKSKLKIHrnlrddEG-FLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDSK 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 638 PKPGfkekrkkAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGF 717
Cdd:cd01382 523 QKAG-------KLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGF 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1529987947 718 PNRILYAEFKQRYRILNPHAIPDdkfVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd01382 596 PSRTSFHDLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-774 |
9.93e-173 |
|
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: 540.52 E-value: 9.93e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAIVAalGDTpakkghgpatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVA--GST-------------NGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnpyDYHFCSQ-GVTTVESLDDGQELMATD 337
Cdd:cd14872 146 RGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA---AYGYLSLsGCIEVEGVDDVADFEEVV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 338 NAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASY---LMGVSSADLIKGLLHPRVKvgney 414
Cdd:cd14872 223 LAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLME----- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 415 vVKGQNV-------EQVIYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTN 486
Cdd:cd14872 298 -IKGCDPtripltpAQATDACDALAKAAYSRLFDWLVKKINESMrPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 487 EKLQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIEK-PMGIMSILEEECMFPKATDNSFKAKMYDNHIGKSp 565
Cdd:cd14872 377 EKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 566 NFQkprPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSVSDPKPGfkek 645
Cdd:cd14872 455 TFV---YAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGDQKTSKVTLG---- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 646 rkkaasfqtvSQLHKEnLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAE 725
Cdd:cd14872 528 ----------GQFRKQ-LSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHER 596
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1529987947 726 FKQRYRILnPHAIPDDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 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 |
2.57e-166 |
|
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: 538.22 E-value: 2.57e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 854 EKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELMER 933
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 934 LEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALQEAHQQ 1013
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1014 TLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDLENDKQQLEEKLKKKDF 1093
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1094 EMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSERLEEAGGATSAQIEMNK 1173
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1174 KREAEFLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEADDLASTVEQLSKGKATS 1253
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1254 EKMCRLYEDQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKQLEEENKA 1333
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1334 KNALAHSLQSSRHDCDLLREQYEEEQEAKGELQRALSKANAEVAQWRTKYETDAiQRTEELEEAKKKLVTRLQESEEIME 1413
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1414 ASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLK 1493
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1494 NSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLEL 1573
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1574 NQMKSDVDRKLAEKDEELDNLRRKHQRSLESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQLNHANRLASESQKLLRN 1653
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1654 LQIQIKDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQNDRARKLAEHELLEASERVNLLHSQNTGLIN 1733
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1734 QKKKLENDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIAL 1813
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1814 KGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEA 1893
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 1529987947 1894 EEQANTNLSKYRKLQHELDDAEERADTAETQVNKLRVR 1931
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-774 |
4.72e-164 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 517.79 E-value: 4.72e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLR----NRENQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 174 MLITGESGAGKTVNTKRVIQYFAIVAAlGDTPAKKGHGPAT-----KTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITS-GFAQGASGEGEAAseaieQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 249 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQGVTTVESLD 328
Cdd:cd14890 160 GKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQ-TPVEYFYLRGECSSIPSCD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 329 DGQELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGT-ESADKASYLMGVSSADLIKGLLHPR 407
Cdd:cd14890 239 DAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 408 VKVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNE 487
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 488 KLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPMGIMSIL------------EEECMFPKATDNSFKA 554
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFitlddcwrfkgeEANKKFVSQLHASFGR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 555 KMYDNHIGKS----PNFQKPRPDKKRkyeaHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLlaslyenyv 630
Cdd:cd14890 478 KSGSGGTRRGssqhPHFVHPKFDADK----QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI--------- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 631 gsdsvsdpkpgfkekRKKAASFQTVSQLHkenlnKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGI 710
Cdd:cd14890 545 ---------------REVSVGAQFRTQLQ-----ELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAI 604
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1529987947 711 RICRKGFPNRILYAEFKQRYRILNPHAIPDDKFVdsrkaaEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14890 605 QIRQQGFALREEHDSFFYDFQVLLPTAENIEQLV------AVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-774 |
5.08e-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: 517.41 E-value: 5.08e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 178 GESGAGKTVNTKRVIQYFAIVAA-LGDTPAKKghgpatktggtledqIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 256
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGgLNDSTIKK---------------IIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 257 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDmLLVSSNPYDYHFcSQGVTTVESLDDGQELMAT 336
Cdd:cd14903 146 DKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERL-FLDSANECAYTG-ANKTIKIEGMSDRKHFART 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 337 DNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAE--ADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEY 414
Cdd:cd14903 224 KEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 415 VVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFN 494
Cdd:cd14903 304 YTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 495 HHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPDK 574
Cdd:cd14903 384 QDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 575 krkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSVSDPKPGFKEKRK--KAASF 652
Cdd:cd14903 463 -----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRrgGALTT 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 653 QTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRI 732
Cdd:cd14903 538 TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1529987947 733 LNPHAipDDKFVDSRKAAEKLLASLDIDH-NQYRFGHTKVFFK 774
Cdd:cd14903 618 FLPEG--RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-774 |
1.17e-163 |
|
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: 515.29 E-value: 1.17e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 180 SGAGKTVNTKRVIQYfaiVAALGDTPAKkghgpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd01379 82 SGAGKTESANLLVQQ---LTVLGKANNR-----------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIM----SQKKpeLLDMLLVSSNPYDY-HFCSQGVTTVESLDDGQE-L 333
Cdd:cd01379 148 GAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYaglaEDKK--LAKYKLPENKPPRYlQNDGLTVQDIVNNSGNREkF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 334 MATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQ----AEADGTESADKASYLMGVSSADLIKGLLHPRVK 409
Cdd:cd01379 226 EEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 410 VGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLY---TSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTN 486
Cdd:cd01379 306 TRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKpdrSASDEPLSIGILDIFGFENFQKNSFEQLCINIAN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 487 EKLQQFFNHHMFILEQEEYKREGIEWTFIDFG-----LDLqacidLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHi 561
Cdd:cd01379 386 EQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 562 gKSPNFQKPRPDkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLAslyenyvgsdsvsdpkpg 641
Cdd:cd01379 460 -KSKYYWRPKSN-----ALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 642 fkekrkkaasfQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRI 721
Cdd:cd01379 516 -----------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRI 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1529987947 722 LYAEFKQRYRILNPHAipDDKFVDSRKAAEKLLASLDIDHnqYRFGHTKVFFK 774
Cdd:cd01379 585 LFADFLKRYYFLAFKW--NEEVVANRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-774 |
1.90e-162 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 513.47 E-value: 1.90e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSESPpHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSISKSP-HVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 178 GESGAGKTVNTKRVIQYFAIVAAlgdtpakkghgPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF- 256
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGS-----------EDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFs 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 257 --------GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS-----------------------QKKPELLDML 305
Cdd:cd14888 149 klkskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 306 LVSS-NPYDYHFCSqGVTTVESLDDGQELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQA---EADG 381
Cdd:cd14888 229 SFEPhLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASC 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 382 TESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYF 460
Cdd:cd14888 308 TDDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIgYSKDNSLLF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 461 IGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLI-EKPMGIMSILE 539
Cdd:cd14888 388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 540 EECMFPKATDNSFKAKMYDNHIGKSpnfqkpRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSAN 619
Cdd:cd14888 467 EECFVPGGKDQGLCNKLCQKHKGHK------RFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKN 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 620 KLLASLYENYVGSDSVSDPkpgfkEKRKkaasFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLH 699
Cdd:cd14888 541 PFISNLFSAYLRRGTDGNT-----KKKK----FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNE 611
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 700 QLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPhaipddkfvdsrkaaekllASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14888 612 QLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN-------------------GEGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-772 |
3.41e-161 |
|
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: 509.72 E-value: 3.41e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAY------KGKRRSESPPHIYSIADNAYNDMLRNRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 171 --NQSMLITGESGAGKTVNTKRVIQYFAIVAAlgdtpaKKGHGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS------ATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 249 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKP-ELLDMLLVSSNPYDYHFCSQGVTTVESL 327
Cdd:cd14901 155 GKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSdELHALGLTHVEEYKYLNSSQCYDRRDGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 328 DDGQELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTES-ADKASYLMGVSSADLIKGLLHP 406
Cdd:cd14901 235 DDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLAnVRAACDLLGLDMDVLEKTLCTR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 407 RVKVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQY-FIGVLDIAGFEIFELNSFEQLCINF 484
Cdd:cd14901 315 EIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaYSESTGASrFIGIVDIFGFEIFATNSLEQLCINF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 485 TNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPMGIMSILEEECMFPKATDNSFKAKMYDNhIGK 563
Cdd:cd14901 395 ANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 564 SPNFQKprpDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASlyenyvgsdsvsdpkpgfk 643
Cdd:cd14901 473 HASFSV---SKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 644 ekrkkaasfqTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILY 723
Cdd:cd14901 531 ----------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPH 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1529987947 724 AEFKQRYRILNPHAIPDDKFVDSRKAAEKLLASLDI----DHNQYRFGHTKVF 772
Cdd:cd14901 601 DAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSElnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-774 |
2.27e-160 |
|
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: 507.37 E-value: 2.27e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAIVAalgdtpaKKGHGPATktggtleDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN-------QRRNNLVT-------EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-E 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS------QKKPELLDmllvssnPYDYHFCSQGVTT-VESLDDGQ 331
Cdd:cd01387 146 GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAglpaqlRQKYGLQE-------AEKYFYLNQGGNCeIAGKSDAD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 332 ELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQRE---EQAEADGTESADKASYLMGVSSADLIKGLLHPRV 408
Cdd:cd01387 219 DFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 409 KVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEK 488
Cdd:cd01387 299 ETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANEN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 489 LQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLI-EKPMGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNF 567
Cdd:cd01387 379 LQYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELY 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 568 QKPRPDkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSVSDPKPG---FKE 644
Cdd:cd01387 457 SKPRMP-----LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGkgrFVT 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 645 KRKKAasfQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYA 724
Cdd:cd01387 532 MKPRT---PTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQ 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1529987947 725 EFKQRYRILNPHAIPDDKFVDSRKAAEKLLASLDIDhNQYRFGHTKVFFK 774
Cdd:cd01387 609 VFIDRYRCLVALKLPRPAPGDMCVSLLSRLCTVTPK-DMYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-774 |
2.38e-160 |
|
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: 508.45 E-value: 2.38e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYfaiVAALgdtpAKKGHGPATktggtlEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01385 81 ESGSGKTESTNFLLHH---LTAL----SQKGYGSGV------EQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSqKKPELLDMLLVSSNPYDYHFCSQGVT-TVESLDDGQELMATD 337
Cdd:cd01385 148 NGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLA-GASEEERKELHLKQPEDYHYLNQSDCyTLEGEDEKYEFERLK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 338 NAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQK--QREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 415
Cdd:cd01385 227 QAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 416 VKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTL----YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQ 491
Cdd:cd01385 307 ILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 492 FFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPMGIMSILEEECMFPKATDNSFKAKmYDNHIGKSPNFQKP 570
Cdd:cd01385 387 YFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 571 rpdkkRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLyenyVGSDSVS-------------- 636
Cdd:cd01385 465 -----QVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL----IGIDPVAvfrwavlraffram 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 637 --------------------DPKPGFKE--KRKKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDP 694
Cdd:cd01385 536 aafreagrrraqrtaghsltLHDRTTKSllHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDD 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 695 FLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHAIpdDKFVDSRKaaeKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd01385 616 ELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGL--ISSKEDIK---DFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-774 |
7.72e-156 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 494.70 E-value: 7.72e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 178 GESGAGKTVNTKRVIQYfaiVAALGDTPAKKGHGPATKTggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14873 81 GESGAGKTESTKLILKF---LSVISQQSLELSLKEKTSC---VEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNIC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQ-GVTTVESLDDGQELMAT 336
Cdd:cd14873 155 QKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST-PENYHYLNQsGCVEDKTISDQESFREV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 337 DNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFkqkqreeqAEADGTESADK-----ASYLMGVSSADLIKGLLHPRVKVG 411
Cdd:cd14873 234 ITAMEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 412 NEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSlPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQ 491
Cdd:cd14873 306 GEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGK-EDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 492 FFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKPR 571
Cdd:cd14873 385 YFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 572 PDkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSVSDPKPGFKEKRKkaas 651
Cdd:cd14873 463 VA-----VNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRP---- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 652 fqTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYR 731
Cdd:cd14873 534 --TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYK 611
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1529987947 732 ILNPHAIPDDkfvDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14873 612 VLMRNLALPE---DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-774 |
5.12e-153 |
|
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: 487.34 E-value: 5.12e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKG--KRRSESPPHIYSIADNAYNDMLRNR----EN 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 172 QSMLITGESGAGKTVNTKRVIQYFAIVAALGDTPAKKGhgPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKF 251
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSK--GAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 252 IRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKpELLDMLLVSSNPYDYHFCSQG-VTTVESLDDG 330
Cdd:cd14892 159 IQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGnCVEVDGVDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 331 QELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQ--KQREEQAEADGTESADKASYLMGVSSADLIKGLLhPRV 408
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLV-TQT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 409 KVGNeyvvKGQNVE------QVIYAVGALAKATYDRMFKWLVGRINR----------TLYTSLPRQYFIGVLDIAGFEIF 472
Cdd:cd14892 317 TSTA----RGSVLEikltarEAKNALDALCKYLYGELFDWLISRINAchkqqtsgvtGGAASPTFSPFIGILDIFGFEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 473 ELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIEK-PMGIMSILEEECMFP-KATDN 550
Cdd:cd14892 393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 551 SFKAKMYDNHIGKSPNFQKPRPDKKrkyeaHFELVHYAGVVPYNIIGWLDKNKDPLnetvvacfqksANKLLASLyenyv 630
Cdd:cd14892 472 QLLTIYHQTHLDKHPHYAKPRFECD-----EFVLRHYAGDVTYDVHGFLAKNNDNL-----------HDDLRDLL----- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 631 gsdsvsdpkpgfkEKRKKaasFQTvsqlhkeNLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGI 710
Cdd:cd14892 531 -------------RSSSK---FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVV 587
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1529987947 711 RICRKGFPNRILYAEFKQRYRIL-----NPHAIPDDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14892 588 RIRREGFPIRRQFEEFYEKFWPLarnkaGVAASPDACDATTARKKCEEIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-774 |
8.22e-145 |
|
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: 463.78 E-value: 8.22e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKR-RSESPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 178 GESGAGKTVNTKRVIQYFAIVAALGDTpakkghgpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDS--------------DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVsSNPYDYHFCSQGVTTVESLDDGQEL---- 333
Cdd:cd14897 147 ENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELeyyr 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 334 -MATD--NAMDILGFLPDEKYGCYKIVGAIMHFGNMKFkqkqrEEQAEADGTESADK-----ASYLMGVSSADLIKGLLH 405
Cdd:cd14897 226 qMFHDltNIMKLIGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALIS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 406 PRVKVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYF-----IGVLDIAGFEIFELNSFEQL 480
Cdd:cd14897 301 NVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 481 CINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLI-EKPMGIMSILEEECMFPKATDNSFKAKMyDN 559
Cdd:cd14897 381 CINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 560 HIGKSPNFQKPRPDKkrkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVgsdsvsdpk 639
Cdd:cd14897 459 YCGESPRYVASPGNR-----VAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSYF--------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 640 pgfkekrkkaasfqtvsqlhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPN 719
Cdd:cd14897 525 --------------------KRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPI 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 720 RILYAEFKQRYRILNPHaiPDDKFVDSRKAAEKLLASLDIDhnQYRFGHTKVFFK 774
Cdd:cd14897 585 RIKYEDFVKRYKEICDF--SNKVRSDDLGKCQKILKTAGIK--GYQFGKTKVFLK 635
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-774 |
1.34e-140 |
|
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: 453.33 E-value: 1.34e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGK--------RRSESPPHIYSIADNAYNDMLRNR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 170 ENQSMLITGESGAGKTVNTKRVIQYFAIVAALGDTPAKKGHGP-----ATKTGGTLEDQIIEANPAMEAFGNAKTLRNDN 244
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 245 SSRFGKFIRIHFG-PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYD-YHFCSQGV 321
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDrYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 322 T-TVESLDDGQELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQ--REEQAEADGTESADKASYLMGVSSAD 398
Cdd:cd14907 241 CyEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 399 LIKGLLHPRVKVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTL--YTSLPRQYF------IGVLDIAGFE 470
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpKDEKDQQLFqnkylsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 471 IFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTF--IDFgLDLQACIDLIEK-PMGIMSILEEECMFPKA 547
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 548 TDNSFKAKMYDNHiGKSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYE 627
Cdd:cd14907 480 TDEKLLNKIKKQH-KNNSKLIFPNKINKDT----FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFS 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 628 NYVGSDSVSDPKPGFKEKRKKaasfqTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVL 707
Cdd:cd14907 555 GEDGSQQQNQSKQKKSQKKDK-----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVL 629
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1529987947 708 EGIRICRKGFPNRILYAEFKQRYRILNphaipddkfvdsrkaaekllasldidhNQYRFGHTKVFFK 774
Cdd:cd14907 630 ESIRVRKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-737 |
3.08e-140 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 450.91 E-value: 3.08e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP------------VYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLR 167
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPglyssdtmakylLSFEARSSSTRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 168 NR----ENQSMLITGESGAGKTVNTKRVIQYFAIVaalGDTPAKKGHGpATKTGGTLEDQIIEANPAMEAFGNAKTLRND 243
Cdd:cd14900 82 GLngvmSDQSILVSGESGSGKTESTKFLMEYLAQA---GDNNLAASVS-MGKSTSGIAAKVLQTNILLESFGNARTLRND 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 244 NSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLdmllvssnpydyhfcsqgvtt 323
Cdd:cd14900 158 NSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAAR--------------------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 324 veSLDDGQELMAtdnAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTE-------SADKASYLMGVSS 396
Cdd:cd14900 217 --KRDMYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDlapssiwSRDAAATLLSVDA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 397 ADLIKGLLHPRVKVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTL-----YTSLPRQYFIGVLDIAGFEI 471
Cdd:cd14900 292 TKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 472 FELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLI-EKPMGIMSILEEECMFPKATDN 550
Cdd:cd14900 372 FPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECVMPKGSDT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 551 SFKAKMYdNHIGKSPNFQKPRPDKKRkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANkllaslyenyv 630
Cdd:cd14900 451 TLASKLY-RACGSHPRFSASRIQRAR---GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYGLQ----------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 631 gsdsvsdpkpgfkekrkkaasfqtvsqlHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGI 710
Cdd:cd14900 516 ----------------------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAV 567
|
650 660 670
....*....|....*....|....*....|.
gi 1529987947 711 RICRKGFPNRILYAEFKQRYRIL----NPHA 737
Cdd:cd14900 568 RVARAGFPIRLLHDEFVARYFSLarakNRLL 598
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-774 |
1.27e-138 |
|
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: 447.18 E-value: 1.27e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNL--RRRYSAWMIYTYSGLFCVTVNPYKWLPvytAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRE---NQS 173
Cdd:cd14891 1 AGILHNLeeRSKLDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 174 MLITGESGAGKTVNTKRVIQYFAIVAALGDTPAKKGHGPATKT----GGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFG 249
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKrklsVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 250 KFIRIHFGPTG-KLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQ-GVTTVESL 327
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLS-PEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 328 DDGQELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKA----SYLMGVSSADLIKGL 403
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEAlataAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 404 LHPRVKVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTL---YTSLPrqyFIGVLDIAGFEIFEL-NSFEQ 479
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLghdPDPLP---YIGVLDIFGFESFETkNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 480 LCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLI-EKPMGIMSILEEECMFPKATDNSFKAKMYD 558
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 559 NHiGKSPNFqkPRPDKKRKYEAhFELVHYAGVVPYNIIGWLDKNKDPLNETvVACFQKSANKLLASLYEnyvgsdsvsdp 638
Cdd:cd14891 473 TH-KRHPCF--PRPHPKDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPED-FEDLLASSAKFSDQMQE----------- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 639 kpgfkekrkkaasfqtvsqlhkenlnkLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFP 718
Cdd:cd14891 537 ---------------------------LVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLP 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1529987947 719 NRILYAEFKQRYRILNPHAI------PDDKFVdsrkaaEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14891 590 TRVTYAELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-774 |
1.41e-138 |
|
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: 447.43 E-value: 1.41e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 101 VLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDML----RNRENQSMLI 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 177 TGESGAGKTVNTKRVIQYFAIVAalgdtpakkghgpatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC---------------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 257 gPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI---MSQKKPELLDMLlvssNPYDYHFCSQGVTTVESLDD-GQE 332
Cdd:cd14889 148 -RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLL----DPGKYRYLNNGAGCKREVQYwKKK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 333 LMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREE-QAEADGTESADKASYLMGVSSADLIKGLLHPRVKVG 411
Cdd:cd14889 223 YDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 412 NEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLytsLPRQYF------IGVLDIAGFEIFELNSFEQLCINFT 485
Cdd:cd14889 303 GEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQACINLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 486 NEKLQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDL-IEKPMGIMSILEEECMFPKATDNSFKAKMyDNHIGKS 564
Cdd:cd14889 380 NEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 565 PNFQKPRpDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSVSDPKPG--- 641
Cdd:cd14889 458 SYYGKSR-SKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKlpq 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 642 -----FKEKRKkaasfQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKG 716
Cdd:cd14889 533 agsdnFNSTRK-----QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREG 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 717 FPNRILYAEFKQRYRIL--NPhAIPDDKfvdsrKAAEKLLASLDIdhNQYRFGHTKVFFK 774
Cdd:cd14889 608 FSWRPSFAEFAERYKILlcEP-ALPGTK-----QSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-752 |
1.07e-132 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 433.16 E-value: 1.07e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYK--------GKRRSESPPHIYSIADNAYNDMLRN- 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 169 RENQSMLITGESGAGKTVNTKRVIQYFAIVAAlgDTPAKKGHGPATKTGGTledQIIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGR--DQSSTEQEGSDAVEIGK---RILQTNPILESFGNAQTIRNDNSSRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 249 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYDYH---FCSQGVTTV 324
Cdd:cd14902 156 GKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLgLQKGGKYELLnsyGPSFARKRA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 325 ESLDDGQELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESA---DKASYLMGVSSADLIK 401
Cdd:cd14902 236 VADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLET 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 402 GLLHPRVKVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTL-------YTSLPRQYF--IGVLDIAGFEIF 472
Cdd:cd14902 316 LLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEInyfdsavSISDEDEELatIGILDIFGFESL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 473 ELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPMGIMSILEEECMFPKATDNS 551
Cdd:cd14902 396 NRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGSNQA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 552 FKAKMYDNHIGkspnfqkprpdkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLyenyVG 631
Cdd:cd14902 475 LSTKFYRYHGG----------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAI----GA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 632 SDSVSDP-KPGFKEKRKKAASFQT--VSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLE 708
Cdd:cd14902 535 DENRDSPgADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLE 614
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1529987947 709 GIRICRKGFPNRILYAEFKQRYRILNPhaipddkFVDSRKAAEK 752
Cdd:cd14902 615 AVRIARHGYSVRLAHASFIELFSGFKC-------FLSTRDRAAK 651
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-774 |
7.95e-132 |
|
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: 428.21 E-value: 7.95e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 178 GESGAGKTVNTKRVIQYFAIVAAlgdtpakkghGPATKTggtlEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG----------GRKDKT----IAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNpYDYHFCSQGV--TTVESLDDGQELMA 335
Cdd:cd14904 147 GRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPN-CQYQYLGDSLaqMQIPGLDDAKLFAS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 336 TDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGtESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 415
Cdd:cd14904 226 TQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNG-SQLSQVAKMLGLPTTRIEEALCNRSVVTRNESV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 416 VKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQY-FIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFN 494
Cdd:cd14904 305 TVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 495 HHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKMYDNH--IGKSPNFQKPRP 572
Cdd:cd14904 385 TDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 573 DKkrkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENyvgSDSVSDPKPGFKEKRKKAAsf 652
Cdd:cd14904 464 KR-----TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGS---SEAPSETKEGKSGKGTKAP-- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 653 QTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRI 732
Cdd:cd14904 534 KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAI 613
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1529987947 733 LNPHAIPDDkfvDSRKAAEKLLASLDIDHN-QYRFGHTKVFFK 774
Cdd:cd14904 614 MFPPSMHSK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
61-827 |
1.13e-131 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 433.69 E-value: 1.13e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 61 VETKDGRTLTVKVDDI----QQMNPPKYDlieDMAMLTHLNEASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTA 136
Cdd:PTZ00014 71 IDPPTNSTFEVKPEHAfnanSQIDPMTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 137 PVVAAYKGKRRSES-PPHIYSIADNAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAivaalgdtPAKKGhgpatK 215
Cdd:PTZ00014 148 DWIRRYRDAKDSDKlPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA--------SSKSG-----N 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 216 TGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS 295
Cdd:PTZ00014 215 MDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 296 QKKPELLDML-LVSSNpyDYHFCSQGVTTVESLDDGQELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQRE 374
Cdd:PTZ00014 295 GANDEMKEKYkLKSLE--EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEG 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 375 EQAEA-----DGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINR 449
Cdd:PTZ00014 373 GLTDAaaisdESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 450 TLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGI-----EWTfidfglDLQAC 524
Cdd:PTZ00014 453 TIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGIsteelEYT------SNESV 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 525 IDLI-EKPMGIMSILEEECMFPKATDNSFKAKMYdNHIGKSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNK 603
Cdd:PTZ00014 527 IDLLcGKGKSVLSILEDQCLAPGGTDEKFVSSCN-TNLKNNPKYKPAKVDSNKN----FVIKHTIGDIQYCASGFLFKNK 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 604 DPLNETVVACFQKSANKLLASLYENYVGSDSvsdpkpgfkekrkKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIP 683
Cdd:PTZ00014 602 DVLRPELVEVVKASPNPLVRDLFEGVEVEKG-------------KLAKGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKP 668
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 684 NETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNpHAIPDDKFVDSRKAAEKLLASLDIDHNQ 763
Cdd:PTZ00014 669 NENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD-LAVSNDSSLDPKEKAEKLLERSGLPKDS 747
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 764 YRFGHTKVFFKAGLLGHLEELRDERLAKVLTLLQaVARGKIMRLELQRMMERR-EALMIIQWNIR 827
Cdd:PTZ00014 748 YAIGKTMVFLKKDAAKELTQIQREKLAAWEPLVS-VLEALILKIKKKRKVRKNiKSLVRIQAHLR 811
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-774 |
2.21e-124 |
|
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: 408.53 E-value: 2.21e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYK--GKRRS---ESP----PHIYSIADNAYNDMLRN- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 169 RENQSMLITGESGAGKTVNTKRVIQYFAIVAAlGDTPAKKGHGPATKtgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGN-GEEGAPNEGEELGK--LSIMDRVLQSNPILEAFGNARTLRNDNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 249 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIM------SQKKPELLDMLLVSSN-PYDYHFCSQG- 320
Cdd:cd14908 158 GKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggdeeEHEKYEFHDGITGGLQlPNEFHYTGQGg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 321 VTTVESLDDGQELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASY---LMGVSSA 397
Cdd:cd14908 238 APDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 398 DLIKGLLHPRVKVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQY--FIGVLDIAGFEIFELN 475
Cdd:cd14908 318 KLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrsSVGVLDIFGFECFAHN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 476 SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPMGIMSILEEECMFP-KATDNSFK 553
Cdd:cd14908 398 SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 554 AKMYDNHIgksPNFQKPRPDKKR-------KYEAHFELVHYAGVVPYNI-IGWLDKNKDPLnetvvacfQKSANKLLASl 625
Cdd:cd14908 477 SRLYETYL---PEKNQTHSENTRfeatsiqKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEI--------PLTADSLFES- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 626 yenyvgsdsvsdpkpgfkekrkkaasfqtvSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNG 705
Cdd:cd14908 545 ------------------------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGG 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 706 VLEGIRICRKGFPNRILYAEFKQRYRILNPhAIPDD----------------KFVDSRKAAEKLLASLDIDHN----QYR 765
Cdd:cd14908 595 VLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVvlswsmerldpqklcvKKMCKDLVKGVLSPAMVSMKNipedTMQ 673
|
....*....
gi 1529987947 766 FGHTKVFFK 774
Cdd:cd14908 674 LGKSKVFMR 682
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-774 |
1.88e-121 |
|
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: 398.77 E-value: 1.88e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYfaiVAALGDTPAKKGhgpatktggtlEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQF---LSSLYQDQTEDR-----------LRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-Q 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQG-VTTVESLDDGQELMATD 337
Cdd:cd14896 146 HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQG-PETYYYLNQGgACRLQGKEDAQDFEGLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 338 NAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESAD--KASYLMGVsSADLIKGLLHPRVKVGN-EY 414
Cdd:cd14896 225 KALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQV-PPERLEGAVTHRVTETPyGR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 415 VVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLytSLPRQY----FIGVLDIAGFEIFELNSFEQLCINFTNEKLQ 490
Cdd:cd14896 304 VSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWL--APPGEAesdaTIGVVDAYGFEALRVNGLEQLCINLASERLQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 491 QFFNHHMFILEQEEYKREGIEWTFIDfGLDLQACIDLI-EKPMGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQK 569
Cdd:cd14896 382 LFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 570 PR---PDkkrkyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENyvgsdsvSDPKPGFKEKR 646
Cdd:cd14896 460 PQlplPV--------FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE-------AEPQYGLGQGK 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 647 KKAAS-FQtvsqlhkENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAE 725
Cdd:cd14896 525 PTLASrFQ-------QSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQA 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1529987947 726 FKQRYRILNPHAIPDdkFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14896 598 FLARFGALGSERQEA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
105-774 |
2.32e-120 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 397.79 E-value: 2.32e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 105 LRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTapvVAAYKGKRRSES--PPHIYSIADNAYNDMLR-------NRENQSM 174
Cdd:cd14895 7 LAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEMPGWTalPPHVFSIAEGAYRSLRRrlhepgaSKKNQTI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 175 LITGESGAGKTVNTKRVIQYFAIVA--ALGDTPAKKGHGpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFI 252
Cdd:cd14895 84 LVSGESGAGKTETTKFIMNYLAESSkhTTATSSSKRRRA-------ISGSELLSANPILESFGNARTLRNDNSSRFGKFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 253 RIHFGP-----TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYDYHFCSQGVTTV-- 324
Cdd:cd14895 157 RMFFEGheldtSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELqLELLSAQEFQYISGGQCYQrn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 325 ESLDDGQELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESA------------------D 386
Cdd:cd14895 237 DGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqhlD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 387 KASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRIN----RTLYTSLPRQY--- 459
Cdd:cd14895 317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNsaspQRQFALNPNKAank 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 460 ----FIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGLDlQACIDLIE-KPMGI 534
Cdd:cd14895 397 dttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEqRPSGI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 535 MSILEEECMFPKATDNSFKAKMYDNHIGKSpNFQKPRPDKKrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACF 614
Cdd:cd14895 476 FSLLDEECVVPKGSDAGFARKLYQRLQEHS-NFSASRTDQA---DVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 615 QKSANKLLASLYENYVGSDSVSDPKPGFKEKRKKA--ASFQTVSQLhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIM 692
Cdd:cd14895 552 GKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSvlSSVGIGSQF-KQQLASLLDVVQQTQTHYIRCIKPNDESASDQF 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 693 DPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHAIPDDkfvdsrKAAEKLLASLDIDHNQyrFGHTKVF 772
Cdd:cd14895 631 DMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASD------ATASALIETLKVDHAE--LGKTRVF 702
|
..
gi 1529987947 773 FK 774
Cdd:cd14895 703 LR 704
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-743 |
4.87e-116 |
|
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: 385.99 E-value: 4.87e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSE----------SPPHIYSIADNAYNDMLR 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAYDHNSQfgdrvtstdpREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 168 NRENQSMLITGESGAGKTVNTKRVIQYFAIVAALGDTPAKKGHG---PATKTGGTLEDQIIEANPAMEAFGNAKTLRNDN 244
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESispPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 245 SSRFGKFIRIHF-GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQK----KPELLDMLLVSSNPYDYHFCSQ 319
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 320 GVTTV--ESLDDGQELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQ--KQREEQAEADGTESA---------- 385
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 386 DKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQY------ 459
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 460 ---------FIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE- 529
Cdd:cd14899 401 vddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEh 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 530 KPMGIMSILEEECMFPKATDNSFKAKMYDNHIGKS--PNFqkpRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLN 607
Cdd:cd14899 480 RPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNshPHF---RSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFC 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 608 ETVVACFQKSANKLLASL----YENYVGSDSVSDPKPGFKEKRKKAASFQ-TVSQLHKENLNKLMTNLRSTQPHFVRCII 682
Cdd:cd14899 557 ESAAQLLAGSSNPLIQALaagsNDEDANGDSELDGFGGRTRRRAKSAIAAvSVGTQFKIQLNELLSTVRATTPRYVRCIK 636
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1529987947 683 PNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYR--ILNPHAIPDDKF 743
Cdd:cd14899 637 PNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRrvLLSLYKWGDNDF 699
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-774 |
1.48e-115 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 382.03 E-value: 1.48e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKG-KRRSESPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 178 GESGAGKTVNTKRVIQYFAivaalgdtPAKKGhgpatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA--------SAKSG-----NMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS------QKKPELLDMllvssnpYDYHFCSQGVTTVESLDDGQ 331
Cdd:cd14876 148 SEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKgadsemKSKYHLLGL-------KEYKFLNPKCLDVPGIDDVA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 332 ELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADK-----ASYLMGVSSADLIKGLLHP 406
Cdd:cd14876 221 DFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVDDAAAISNESLevfkeACSLLFLDPEALKRELTVK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 407 RVKVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTN 486
Cdd:cd14876 301 VTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 487 EKLQQFFNHHMFILEQEEYKREGI-----EWTfidfglDLQACID-LIEKPMGIMSILEEECMFPKATDNSFKAKMYDNh 560
Cdd:cd14876 381 EMLQKNFIDIVFERESKLYKDEGIptaelEYT------SNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 561 IGKSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVgsdsvsdpkp 640
Cdd:cd14876 454 LKSNGKFKPAKVDSNIN----FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVV---------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 641 gfKEKRKKAASFQTVSQLHKeNLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNR 720
Cdd:cd14876 520 --VEKGKIAKGSLIGSQFLK-QLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYR 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1529987947 721 ILYAEFKQRYRILNPhAIPDDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14876 597 RPFEEFLYQFKFLDL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-772 |
1.29e-108 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 362.25 E-value: 1.29e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSES-PPHIYSIADNAYNDMLRNRE--NQSM 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 175 LITGESGAGKTVNTKRVIQYFAIVAALGDTPakKGHgpatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSW--ESH----KIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 255 HFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS-QKKPELLDMLLVSSNPYDYhfcsqgVTTVESLDDGQEL 333
Cdd:cd14880 155 QLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKgASADERLQWHLPEGAAFSW------LPNPERNLEEDCF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 334 MATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQA---EADGTESADKASYLMGVSSADLIKGLLHPRVKV 410
Cdd:cd14880 229 EVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 411 GNEYVV--KGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPR-QYFIGVLDIAGFEIFELNSFEQLCINFTNE 487
Cdd:cd14880 309 GKQQQVfkKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 488 KLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPMGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPN 566
Cdd:cd14880 389 KLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPC 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 567 FQKPRPDKkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSVSDPKpgfkeKR 646
Cdd:cd14880 468 LGHNKLSR----EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPS-----GQ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 647 KKAASFQTVSQLhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEF 726
Cdd:cd14880 539 SRAPVLTVVSKF-KASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNF 617
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1529987947 727 KQRYRILNPHAIPDDKFVDSRKAAEKLLASLDIdhnqyrfGHTKVF 772
Cdd:cd14880 618 VERYKLLRRLRPHTSSGPHSPYPAKGLSEPVHC-------GRTKVF 656
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-774 |
1.37e-106 |
|
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: 356.12 E-value: 1.37e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRS-----ESPPHIYSIADNAYNDMLRNRENQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 173 SMLITGESGAGKTVNTKRVIQYFAivaalgdtpakkgHGPATKTGgTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFI 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFA-------------YGHSTSST-DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 253 RIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYdYHFCSQG-VTTVESLDDGQ 331
Cdd:cd14886 147 KLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASkCYDAPGIDDQK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 332 ELMATDNAMDILgFLPDEKYGCYKIVGAIMHFGNMKFKQKQR---EEQAEADGTESADKASYLMGVSSADLIKGLLHPRV 408
Cdd:cd14886 226 EFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 409 KVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEK 488
Cdd:cd14886 305 VINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANER 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 489 LQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIEKP-MGIMSILEEECMFPKATDNSFKAKMyDNHIgKSPNF 567
Cdd:cd14886 385 LQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 568 QkprPDKKRkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENyvgsdsVSDPKPGFKEKrk 647
Cdd:cd14886 462 I---PGKGS--QCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSD------IPNEDGNMKGK-- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 648 kaasfqTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFK 727
Cdd:cd14886 529 ------FLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFF 602
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1529987947 728 QRYRILNPHA-IPDDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14886 603 HRNKILISHNsSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-774 |
6.03e-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: 354.89 E-value: 6.03e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMI-YTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSES-PPHIYSIADNAYNDM-LRNRENQSML 175
Cdd:cd14875 1 ATLLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 176 ITGESGAGKTVNTKRVIQYfaivaaLGDTPAKKGHGPATKTggtLEDQIIE----ANPAMEAFGNAKTLRNDNSSRFGKF 251
Cdd:cd14875 81 ISGESGSGKTENAKMLIAY------LGQLSYMHSSNTSQRS---IADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 252 IRIHFGPT-GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTV------ 324
Cdd:cd14875 152 IKLYFDPTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 325 ESLDDGQELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESAdKASYLMGVSSADLIKGLL 404
Cdd:cd14875 232 KTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLRECFL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 405 hprVKVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLY--TSLPRQYFIGVLDIAGFEIFELNSFEQLCI 482
Cdd:cd14875 311 ---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpqGDCSGCKYIGLLDIFGFENFTRNSFEQLCI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 483 NFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPMGIMSILEEECMFPKATDNSFKAKMYDNHI 561
Cdd:cd14875 388 NYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 562 GKSPNFQKPrpdkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDsvsdpkpg 641
Cdd:cd14875 467 NKSPYFVLP----KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLA-------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 642 fkeKRKkaasfQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRI 721
Cdd:cd14875 535 ---RRK-----QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRR 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1529987947 722 LYAEF-KQRYRILNPHAIPDDKFVDSRKAAEKLLASLDIDHN----QYRFGHTKVFFK 774
Cdd:cd14875 607 PIEQFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYYQRLYGwakpNYAVGKTKVFLR 664
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-734 |
1.38e-105 |
|
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: 355.44 E-value: 1.38e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRR-SESPPHIYSIADNAYNDMLRNRENQSMLI 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 177 TGESGAGKTVNTKRVIQYfaIVAALGDTPAKKGHGpaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 256
Cdd:cd14906 81 SGESGSGKTEASKTILQY--LINTSSSNQQQNNNN--NNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 257 GPT-GKLASADIDIYLLEKSRvIFQQPGER--SYHIYYQIMSQKKPELLDMLLVSSNPYDYHFC---------------- 317
Cdd:cd14906 157 RSSdGKIDGASIETYLLEKSR-ISHRPDNInlSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLdarddvissfksqssn 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 318 --SQGVTTVESLDDGQELMATDNAMDIlgflpdEKYGC---YKIVGAIMHFGNMKFKQKQ---REEQAEADGTESADKAS 389
Cdd:cd14906 236 knSNHNNKTESIESFQLLKQSMESMSI------NKEQCdaiFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 390 YLMGVSSADLIKGLLHPRVKVGNEYVV--KGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTL-----------YTSLP 456
Cdd:cd14906 310 KLLGYIESVFKQALLNRNLKAGGRGSVycRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFnqntqsndlagGSNKK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 457 RQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPMGIM 535
Cdd:cd14906 390 NNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGIL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 536 SILEEECMFPKATDNSFKAK---MYDNhigkspnfqKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVA 612
Cdd:cd14906 469 SLLDDECIMPKGSEQSLLEKynkQYHN---------TNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVED 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 613 CFQKSANKLLASLYENYVGSDSVSDpkpgfkekrKKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIM 692
Cdd:cd14906 540 LLLASSNFLKKSLFQQQITSTTNTT---------KKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNF 610
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1529987947 693 DPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILN 734
Cdd:cd14906 611 NNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIV 652
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-774 |
2.07e-105 |
|
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: 354.31 E-value: 2.07e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAIVAALGDTPAKKghgpatktggtleDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSV-------------EKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML----LVSSNpydyhfcSQGVTTVESLDDGQ--- 331
Cdd:cd01386 148 AGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELhlnqLAESN-------SFGIVPLQKPEDKQkaa 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 332 -ELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGN---MKFKQKQREEQAEadgTESADKASYLMGVSSADLIKGLLHPR 407
Cdd:cd01386 221 aAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFAR---PEWAQRAAYLLGCTLEELSSAIFKHH 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 408 VKVGNEYVVKGQNVEQV------------IYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELN 475
Cdd:cd01386 298 LSGGPQQSTTSSGQESParsssggpkltgVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 476 ------SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEK---------------PMGI 534
Cdd:cd01386 378 gsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 535 MSILEEECMFPKATDNSFKAKMYdNHIGKSPNFQKPRPDKKRKYEAHFELVHYAGV--VPYNIIGWLDKNK-DPLNETVV 611
Cdd:cd01386 458 LWLLDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNAT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 612 ACFQKSANKLLASlyenyvgsdsvsdpkpgfkekRKKAASFQTvsqlhKENLNKLMTNLRSTQPHFVRCIIP--NETKTP 689
Cdd:cd01386 537 QLLQESQKETAAV---------------------KRKSPCLQI-----KFQVDALIDTLRRTGLHFVHCLLPqhNAGKDE 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 690 GIMDPF----------LVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPH----AIPDDKFVDSRKAAEKLLA 755
Cdd:cd01386 591 RSTSSPaagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPltkkLGLNSEVADERKAVEELLE 670
|
730
....*....|....*....
gi 1529987947 756 SLDIDHNQYRFGHTKVFFK 774
Cdd:cd01386 671 ELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-774 |
2.96e-93 |
|
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: 317.34 E-value: 2.96e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYtapvVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFAivaalgdtpakkghgPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL---------------SGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPyDYHFCSQGVTTVESLDDGQE---LMA 335
Cdd:cd14937 142 YQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDfgnLMI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 336 TDNAMDilgfLPDEKYGCYKIVGAIMHFGNMKFKQ-----KQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKV 410
Cdd:cd14937 221 SFDKMN----MHDMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 411 GNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQ 490
Cdd:cd14937 297 ANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIH 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 491 QFFNHHMFILEQEEYKREGIEWTFIDFGLDlQACIDLIEKPMGIMSILEEECMFPKATDNSFkAKMYDNHIGKSPNFQKp 570
Cdd:cd14937 377 SIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYAS- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 571 rpdKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSVSdpkpgfkekRKKAA 650
Cdd:cd14937 454 ---TKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLG---------RKNLI 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 651 SFQtvsqlHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRIcRKGFPNRILYAEFKQRY 730
Cdd:cd14937 522 TFK-----YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1529987947 731 RILNPHAIPDDKFVDSRKAAEKLLASLDIDhnQYRFGHTKVFFK 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 |
4.85e-93 |
|
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: 314.53 E-value: 4.85e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKwlPVYTAPVVAAYKgKRRSESPPHIYSIADNAYNDMLRNrENQSMLITGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 180 SGAGKTVNTKRVIQYFAivaalgdtpakkghgPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgpT 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLV---------------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKpelldmLLVSSNPYDYHFCSQGVTTVESLDdgQELMATDNA 339
Cdd:cd14898 141 GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESIVQLS--EKYKMTCSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 340 MDILGFLPDEKYGcyKIVGAIMHFGNMKFKQkqrEEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14898 213 MKSLGIANFKSIE--DCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 420 NVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQyfIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14898 288 TLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 500 LEQEEYKREGIEWTFIDFgLDLQACIDLIEKPMGIMSILEEECMFPKATDNSFKAKM--YDNHigkspnFQKPRPDKKRK 577
Cdd:cd14898 366 AKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNG------FINTKARDKIK 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 578 yeahfeLVHYAGVVPYNIIGWLDKNKDPLNETVVAcfqksankllaslyenyvgsdsvsdpKPGFKEKRKKaasfQTVSQ 657
Cdd:cd14898 439 ------VSHYAGDVEYDLRDFLDKNREKGQLLIFK--------------------------NLLINDEGSK----EDLVK 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 658 LHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHA 737
Cdd:cd14898 483 YFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-774 |
2.61e-91 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 312.13 E-value: 2.61e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAY---KGKRRSESPPHIYSIADNAYNDMLRNRENQSML 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 176 ITGESGAGKTVNTKRVIQYFAivaalgdtpakkghGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 255
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLT--------------CRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 256 FGPTGK-LASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQG----VTTVESLDDG 330
Cdd:cd14878 147 FCERKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQTmredVSTAERSLNR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 331 QELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKV 410
Cdd:cd14878 226 EKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 411 GNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTL-----YTSLPrQYFIGVLDIAGFEIFELNSFEQLCINFT 485
Cdd:cd14878 306 KGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdeQKSMQ-TLDIGILDIFGFEEFQKNEFEQLCVNMT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 486 NEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGLDLQACIDLI-EKPMGIMSILEEECMFPKATDNSFKAKMY------D 558
Cdd:cd14878 385 NEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDFFfQKPSGFLSLLDEESQMIWSVEPNLPKKLQsllessN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 559 NHIGKSPNFQKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLyenyvgsdsvsdp 638
Cdd:cd14878 465 TNAVYSPMKDGNGNVALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 639 kpgFKEKRKKAASfqtvsQLHKeNLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFP 718
Cdd:cd14878 532 ---FQSKLVTIAS-----QLRK-SLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYP 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1529987947 719 NRILYAEFKQRYRILNPHAIPDDKfvdSRKAAEKL-LASLDIDHNQYRFGHTKVFFK 774
Cdd:cd14878 603 VRLSFSDFLSRYKPLADTLLGEKK---KQSAEERCrLVLQQCKLQGWQMGVRKVFLK 656
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-774 |
1.75e-88 |
|
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: 305.80 E-value: 1.75e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSA--------WMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 171 NQSMLITGESGAGKTVNTKRVIQYFAIVAalgdtpaKKGHGPATKTggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGK 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVS-------DRRHGADSQG---LEARLLQSGPVLEAFGNAHTVLNANSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 251 FIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI-MSQKKPELLDMLLVSSNPYDYhfcsqgvttvesldd 329
Cdd:cd14887 151 MLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALcNAAVAAATQKSSAGEGDPEST--------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 330 gqELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGT--------ESADKASYLMGVSS----- 396
Cdd:cd14887 216 --DLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvgceETAADRSHSSEVKClssgl 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 397 ---ADLIKGLLHPRVKVGNEYVVKGQN-------------------VEQVIYAVGALAKATYDRMFKWLVGRINRTLYTS 454
Cdd:cd14887 294 kvtEASRKHLKTVARLLGLPPGVEGEEmlrlalvsrsvretrsffdLDGAAAARDAACKNLYSRAFDAVVARINAGLQRS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 455 LPRQY--------------FIGVLDIAGFEIFE---LNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREG--IEWTFI 515
Cdd:cd14887 374 AKPSEsdsdedtpsttgtqTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQDCS 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 516 DFGLDLQACIDLIEKP------------------------MGIMSILEEE-CMFPKATDNSFKA----KMYDNHIGKSPN 566
Cdd:cd14887 454 AFPFSFPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSdlfyEKLNKNIINSAK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 567 FQKPRPDKKRKyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFqksankLLASLYENYVGSDSVSDPKpGFKEKR 646
Cdd:cd14887 534 YKNITPALSRE-NLEFTVSHFACDVTYDARDFCRANREATSDELERLF------LACSTYTRLVGSKKNSGVR-AISSRR 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 647 KkaasfqTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEF 726
Cdd:cd14887 606 S------TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVEL 679
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1529987947 727 KQRYRILNPHAIpdDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFFK 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 |
2.03e-74 |
|
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: 262.10 E-value: 2.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 96 LNEASVLYNLRRRYSAWMIYTY---SGLfcVTVNPYKWLPVYTAPVVAAYKGKRRSES-------PPHIYSIADNAYNDM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGSEYYDTTsgskeplPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 166 LRNRENQSMLITGESGAGKTVNTKRVIQyfaivaALGD--TPAKKGhgpaTKtggtLEDQIIEANPAMEAFGNAKTLRND 243
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLR------QLLRlsSHSKKG----TK----LSSQISAAEFVLDSFGNAKTLTNP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 244 NSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYDY---HFCSQ 319
Cdd:cd14879 145 NASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLgLDDPSDYALlasYGCHP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 320 GVTTVESlDDG---QELMAtdnAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQ--REEQAEADGTESADKASYLMGV 394
Cdd:cd14879 225 LPLGPGS-DDAegfQELKT---ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 395 SSADLiKGLLHPRVK-VGNEYVvkgqnveqVIY--AVGA------LAKATYDRMFKWLVGRINRTLytSLPRQY---FIG 462
Cdd:cd14879 301 SPEDL-ETSLTYKTKlVRKELC--------TVFldPEGAaaqrdeLARTLYSLLFAWVVETINQKL--CAPEDDfatFIS 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 463 VLDIAGFEIF---ELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLI-EKPMGIMSIL 538
Cdd:cd14879 370 LLDFPGFQNRsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGIL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 539 EEEC-MFPKATDNSFKAKMYDNHIGKSPnFQKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNetvvacfqks 617
Cdd:cd14879 449 DDQTrRMPKKTDEQMLEALRKRFGNHSS-FIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLS---------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 618 ankllaslyenyvgSDSVSdpkpgfkekrkkaaSFQTVSQLhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLV 697
Cdd:cd14879 518 --------------PDFVN--------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRV 568
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1529987947 698 LHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYrilnphaIPDDKFVDSRKAAEKLLASLDIDHNQYRFGHTKVFF 773
Cdd:cd14879 569 KAQIRSLGLPELAARLRVEYVVSLEHAEFCERY-------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-773 |
1.11e-70 |
|
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: 250.80 E-value: 1.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAaykgkRRSESPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVGNPLTLTST-----RSSPLAPQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 180 SGAGKTVNTKRVI-QYFAIVAALGDTPAKKgHGPATKTggtledqiieanpAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 258
Cdd:cd14881 77 SGSGKTYASMLLLrQLFDVAGGGPETDAFK-HLAAAFT-------------VLRSLGSAKTATNSESSRIGHFIEVQV-T 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYDYHFCSQGVTTVESLDDGQELMATD 337
Cdd:cd14881 142 DGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLhLDGYSPANLRYLSHGDTRQNEAEDAARFQAWK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 338 NAMDILG--FLpdekyGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASyLMGVSSADLIKGLlHPRVKVGNEYV 415
Cdd:cd14881 222 ACLGILGipFL-----DVVRVLAAVLLLGNVQFIDGGGLEVDVKGETELKSVAA-LLGVSGAALFRGL-TTRTHNARGQL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 416 VKGQNVEQVIYAV-GALAKATYDRMFKWLVGRINrtlytSLPRQY----------FIGVLDIAGFEIFELNSFEQLCINF 484
Cdd:cd14881 295 VKSVCDANMSNMTrDALAKALYCRTVATIVRRAN-----SLKRLGstlgthatdgFIGILDMFGFEDPKPSQLEHLCINL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 485 TNEKLQQFFNHHMFILEQEEYKREGIEwTFIDFG-LDLQACIDLIEK-PMGIMSILEEECMfPKATDNSFKAKMYDNHIG 562
Cdd:cd14881 370 CAETMQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQ 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 563 kSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLlaslyenyvgsdsvsdpkpgf 642
Cdd:cd14881 448 -NPRLFEAKPQDDRM----FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF--------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 643 kekrkkaaSFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRIL 722
Cdd:cd14881 502 --------GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMR 573
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1529987947 723 YAEFKQRYRILNPHAIP---DDKFVDSRKAAEKLLASLDIDHN-----QYRFGHTKVFF 773
Cdd:cd14881 574 FKAFNARYRLLAPFRLLrrvEEKALEDCALILQFLEAQPPSKLssvstSWALGKRHIFL 632
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-725 |
3.15e-69 |
|
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: 247.90 E-value: 3.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSES-------PPHIYSIADNAYNDMLRNRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 171 NQSMLITGESGAGKTVNTKRVIQYFAIVaalgdtpakkgHGPATKTggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGK 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI-----------QTDSQMT--ERIDKLIYINNILESMSNATTIKNNNSSRCGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 251 FIRIHF---------GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGV 321
Cdd:cd14884 148 INLLIFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 322 ------------TTVESLDDGQELMATD--NAMDILGFLPDEKYGCYKI------VGAIMHFGNMKFKQkqreeqaeadg 381
Cdd:cd14884 228 shqkrsvkgtlrLGSDSLDPSEEEKAKDekNFVALLHGLHYIKYDERQIneffdiIAGILHLGNRAYKA----------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 382 tesadkASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQ--- 458
Cdd:cd14884 297 ------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDesd 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 459 ---------YFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTfidfGLDLQACIDLIE 529
Cdd:cd14884 371 nediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICC----SDVAPSYSDTLI 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 530 KPMGIMSILEE-----ECMFPKATDNSFK-----AKMY----DNHIGKSPNFQKPRPDKKRKYEAH-FELVHYAGVVPYN 594
Cdd:cd14884 447 FIAKIFRRLDDitklkNQGQKKTDDHFFRyllnnERQQqlegKVSYGFVLNHDADGTAKKQNIKKNiFFIRHYAGLVTYR 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 595 IIGWLDKNKDPLNETVVACFQKSANKLLAslyENYVGsdsvsdpkpgfkekrKKAASFQTVSQLHKENLNKLMTNLRSTQ 674
Cdd:cd14884 527 INNWIDKNSDKIETSIETLISCSSNRFLR---EANNG---------------GNKGNFLSVSKKYIKELDNLFTQLQSTD 588
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1529987947 675 PHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAE 725
Cdd:cd14884 589 MYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-735 |
7.69e-67 |
|
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: 239.39 E-value: 7.69e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYkgkrrsesppHIYSIADNAYNDMLRNRENQSMLI-T 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNAESIVfG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 178 GESGAGKTVNTKRVIQYfaivaaLGDTPAKKghgPATKTGGTLEDQIieanpamEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKY------LTSQPKSK---VTTKHSSAIESVF-------KSFGCAKTLKNDEATRFGCSIDLLYK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNpYDYHFCSQGVTTVESLDDGQELMATD 337
Cdd:cd14874 135 RNVLTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL-QKFFYINQGNSTENIQSDVNHFKHLE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 338 NAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQR---EEQAEADGTESADK-ASYLMGVSSADLIKGLLhPRVKVGNE 413
Cdd:cd14874 214 DALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnvEQDVVEIGNMSEVKwVAFLLEVDFDQLVNFLL-PKSEDGTT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 414 YvvkgqNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLpRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFF 493
Cdd:cd14874 293 I-----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPL-HTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 494 NHHMFILEQEEYKREGIEwtfIDFglDLQACID-------LIEKPMGIMSILEEECMFPKATDNSFKAKMYDNHIGKSpN 566
Cdd:cd14874 367 VKHSFHDQLVDYAKDGIS---VDY--KVPNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRS-S 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 567 FQKPRpdKKRKYEahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYvgSDSVSDpkpgfkekr 646
Cdd:cd14874 441 YGKAR--NKERLE--FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY--SSNTSD--------- 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 647 kkaaSFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEF 726
Cdd:cd14874 506 ----MIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTF 581
|
....*....
gi 1529987947 727 KQRYRILNP 735
Cdd:cd14874 582 ARQYRCLLP 590
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-774 |
1.30e-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: 227.32 E-value: 1.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 180 SGAGKTVNTKRVIQYFAIvaaLGdtpaKKGHGPATKtggtledqIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCY---LG----DGNRGATGR--------VESSIKAILALVNAGTPLNADSTRCILQYQLTFGST 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS--QKKPELLDMLLVSSNPYDYHFCSQGVTTVESL---DDGQELM 334
Cdd:cd14882 147 GKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEVPPSKLKyrrDDPEGNV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 335 AT----DNAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREeqAEADGTESADKASYLMGVSSADLIKGLLHPRVKV 410
Cdd:cd14882 227 ERykefEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLIK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 411 GNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLytSLPR-----QYFIGVLDIAGFEIFELNSFEQLCINFT 485
Cdd:cd14882 305 GGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKM--SFPRavfgdKYSISIHDMFGFECFHRNRLEQLMVNTL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 486 NEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPMGIMSILeeecmfpkatDNSFKAKMYDNHIGKSP 565
Cdd:cd14882 383 NEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYII----------DDASRSCQDQNYIMDRI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 566 NfQKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENyvgsdsvsdpkPGFKEK 645
Cdd:cd14882 453 K-EKHSQFVKKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-----------SQVRNM 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 646 RKKAASFQTVSQlhkENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAE 725
Cdd:cd14882 521 RTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQE 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1529987947 726 FKQRYRILnphAIPDDKFVDSRKAAEKLLAsLDIDHNQYRFGHTKVFFK 774
Cdd:cd14882 598 FLRRYQFL---AFDFDETVEMTKDNCRLLL-IRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-773 |
4.03e-61 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 225.24 E-value: 4.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 102 LYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRR----------SESPPHIYSIADNAYNDMLRNREN 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 172 QSMLITGESGAGKTVNTKRVIQYFAIVAAlGDTPAKKGHGpATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKF 251
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGD-ETEPRPDSEG-ASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 252 IRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS--QKKPELLDMLLVSSNPYDYHFCSQG--VTTVESL 327
Cdd:cd14893 162 ISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAgvQHDPTLRDSLEMNKCVNEFVMLKQAdpLATNFAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 328 D--DGQELMATDNAMDIlgfLPDEKYGCYKIVGAIMHFGNMKF--KQKQREEQAEADGTESADKAS-YLMGVSSADLIKG 402
Cdd:cd14893 242 DarDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFvpDPEGGKSVGGANSTTVSDAQScALKDPAQILLAAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 403 LL--HPRV------------KVGNEYV--VKGQNVEQVIYAVGALAKATYDRMFKWLVGRINRTLYTSLPR--------- 457
Cdd:cd14893 319 LLevEPVVldnyfrtrqffsKDGNKTVssLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksnivin 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 458 QYFIGVLDIAGFEIFE--LNSFEQLCINFTNEKLQQFFNHHMF-----ILEQEEYKREG--IEWTFIDFGLDLQACIDLI 528
Cdd:cd14893 399 SQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLainfsFLEDESQQVENrlTVNSNVDITSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 529 E-KPMGIMSILEEECMFPKATDNSFKAKMY--DNHIG--KSPN----FQKPRPDKKRKYEAHFELVHYAGVVPYNIIGWL 599
Cdd:cd14893 479 EdKPFGIFDLLTENCKVRLPNDEDFVNKLFsgNEAVGglSRPNmgadTTNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 600 DKNKDPLNETVVACFQKSANKLLASLYENYVGSDSVSDPKPGFKEKRKKAASFQTVSQLHKENLN--------------K 665
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 666 LMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPHaipddkfvd 745
Cdd:cd14893 639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVCGH--------- 709
|
730 740 750
....*....|....*....|....*....|..
gi 1529987947 746 sRKAAEKLLASLD----IDHNQYRFGHTKVFF 773
Cdd:cd14893 710 -RGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
105-726 |
1.24e-60 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 222.28 E-value: 1.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 105 LRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRrsESPPHIYSIADNAYNDMLRNRENQSMLITGESGAG 183
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 184 KTVNTKRVIQYFAIVaalgDTPAKKghgpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLA 263
Cdd:cd14905 85 KSENTKIIIQYLLTT----DLSRSK----------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 264 SADIDIYLLEKSRVIFQQPGERSYHIYYQIM---SQKKPELLDMLLVSSnpydYHFCSQGVT-TVESLDDGQELMATDNA 339
Cdd:cd14905 151 GAKLYSYFLDENRVTYQNKGERNFHIFYQFLkgiTDEEKAAYQLGDINS----YHYLNQGGSiSVESIDDNRVFDRLKMS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 340 MDILGFlPDEKYG-CYKIVGAIMHFGNMKFKQKQreEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVvkg 418
Cdd:cd14905 227 FVFFDF-PSEKIDlIFKTLSFIIILGNVTFFQKN--GKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAV--- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 419 QNVEqviyavgALAKATYDRMFKWLVGRINRTLYtslPRQY--FIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHH 496
Cdd:cd14905 301 ENRD-------SLARSLYSALFHWIIDFLNSKLK---PTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 497 MFILEQEEYKREGIEW-TFIDFGlDLQACIDLIEKpmgIMSILEEECMFPKATDNSFKAKMyDNHIGKSPNFQKpRPDKk 575
Cdd:cd14905 371 VLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL-QNFLSRHHLFGK-KPNK- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 576 rkyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVGSDSVSDPKPGFKEKRKKAASFQTV 655
Cdd:cd14905 444 ------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSRDGVFNINATVAELNQMFDAKNTAKKSPLSI 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 656 SQL-------HKENLNK-----------------------LMTNLRSTQP---------HFVRCIIPNETKTPGIMDPFL 696
Cdd:cd14905 518 VKVllscgsnNPNNVNNpnnnsgggggggnsgggsgsggsTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVKS 597
|
650 660 670
....*....|....*....|....*....|....
gi 1529987947 697 VLHQLRCNGVLEGIRICRKGFP----NRILYAEF 726
Cdd:cd14905 598 VNEQIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-254 |
2.07e-55 |
|
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: 190.63 E-value: 2.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 121 FCVTVNPYKWLPVYTAPVV-AAYKGKRRSESPPHIYSIADNAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAIVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1529987947 200 ALGDTPAK-KGHGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 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 |
2.01e-40 |
|
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: 161.54 E-value: 2.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSESPP-HIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEDLSlNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 179 ESGAGKTVNTKRVIQYFA---------IVAALGDTPAKKGHGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFG 249
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAyqvkgsrrlPTNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 250 KFIRIHFgPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVESlDD 329
Cdd:cd14938 162 KFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFS-DY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 330 GQELMATDNAMDILGFLPDEKYGCYKIVGAIMHFGN-------------MKFKQKQRE----------EQAEADGTESAD 386
Cdd:cd14938 240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDENV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 387 K----ASYLMGVSSADLIKGLLHPRVkVGNEYVVKGQNVEQVIYAVGALAKATYDRMFKWLVGRINrTLYTSLPR----Q 458
Cdd:cd14938 320 KnlllACKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKIN-EKCTQLQNininT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 459 YFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPM--GIMS 536
Cdd:cd14938 398 NYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 537 ILEEECMfPKATDNSFKAKMYDNHIGKSPNFQKPRPDKKRKyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQK 616
Cdd:cd14938 478 LLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNK--KTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 617 SANKLLASL--YENYVGSDSVSDPKPGFKE-------KRKKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETK 687
Cdd:cd14938 555 SENEYMRQFcmFYNYDNSGNIVEEKRRYSIqsalklfKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 688 TP-GIMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPhaipddkfvDSRKAAEKLLASLDIDHNQYRF 766
Cdd:cd14938 635 RElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMI 705
|
....*.
gi 1529987947 767 GHTKVF 772
Cdd:cd14938 706 GNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1156-1916 |
2.91e-26 |
|
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: 118.24 E-value: 2.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1156 ERLEEAGGATSAQIEmNKKREAEFLKMRRDLEEAMLHHEATTAALRKKhadsvaELSEQIDSLQRVKQKLEKERSEAKME 1235
Cdd:TIGR02168 189 DRLEDILNELERQLK-SLERQAEKAERYKELKAELRELELALLVLRLE------ELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1236 ADDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAKNS 1315
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1316 FSQNVEELKKQLEEENKAKNALAHSLQSSRHDCDLLREQYEEEQEAKGELQRALSKANAEVAQWRTKYEtDAIQRTEELE 1395
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE-RLEDRRERLQ 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1396 EAKKKLVTRLQESEeiMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSEL 1475
Cdd:TIGR02168 421 QEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1476 EISQKESRGLST----------------ELFKLKNSYEETLD-----HLETIKRENKNLQEEITDLTDQISQGAKTIHEL 1534
Cdd:TIGR02168 499 ENLEGFSEGVKAllknqsglsgilgvlsELISVDEGYEAAIEaalggRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPL 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1535 EKMK-KGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDVdrKLAEKDEELDNLRRKHQRslESMQATLDAE- 1612
Cdd:TIGR02168 579 DSIKgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV--LVVDDLDNALELAKKLRP--GYRIVTLDGDl 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1613 ---------AKSRNEAVRLK-----KKMEGDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQ 1678
Cdd:TIGR02168 655 vrpggvitgGSAKTNSSILErrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1679 VAVTER-------RNNLLAAEVEELRALLEQNDRARKLAEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDD 1751
Cdd:TIGR02168 735 LARLEAeveqleeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1752 ---AVQECRNAEEKAKKAITDAAMMAEELKKE-QDTSAHLERMKKNMEqtikDLQMRLDEAEqIALKGGKKQVQKLEARV 1827
Cdd:TIGR02168 815 lneEAANLRERLESLERRIAATERRLEDLEEQiEELSEDIESLAAEIE----ELEELIEELE-SELEALLNERASLEEAL 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1828 KELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKS-YKRQTEEAEEQANTNLSKYRK 1906
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeYSLTLEEAEALENKIEDDEEE 969
|
810
....*....|
gi 1529987947 1907 LQHELDDAEE 1916
Cdd:TIGR02168 970 ARRRLKRLEN 979
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1152-1929 |
6.85e-26 |
|
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: 117.08 E-value: 6.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1152 EDLSERLEEAGGATSaqiemnkkreaefLKMRRdlEEAMLHHEATTAALrKKHADSVAELSEQIDSLQRVKQKLEKERse 1231
Cdd:TIGR02168 155 EERRAIFEEAAGISK-------------YKERR--KETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERYK-- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1232 akmeadDLASTVEQLSKgkatsekmcRLYEDQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQR 1311
Cdd:TIGR02168 217 ------ELKAELRELEL---------ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1312 AKNSFSQNVEELKKQLEEENKAKNALAHSLQSSRHDCDLLREQYEEEQEAKGELQRALSKANAEVAQWRTKYEtDAIQRT 1391
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE-SLEAEL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1392 EELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLERanaaaaaLDKKQRNFDKVLAEWKQKYEEc 1471
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER-------LEDRRERLQQEIEELLKKLEE- 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1472 qSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMK----------KGL 1541
Cdd:TIGR02168 433 -AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQenlegfsegvKAL 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1542 EMEKTEI-----------------QAALEEA-EGTLEHEESKTLRIQLE----LNQMKSDVDRKLAEKDEELDNLRRKHQ 1599
Cdd:TIGR02168 512 LKNQSGLsgilgvlselisvdegyEAAIEAAlGGRLQAVVVENLNAAKKaiafLKQNELGRVTFLPLDSIKGTEIQGNDR 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1600 RSLESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEV--QLNHANRLASesqKLLRNLQIQIKDVQLELDETVHQNEELKE 1677
Cdd:TIGR02168 592 EILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVvdDLDNALELAK---KLRPGYRIVTLDGDLVRPGGVITGGSAKT 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1678 QVAVTERRNNL--LAAEVEELRALLEQNDRARKLAEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDAVQE 1755
Cdd:TIGR02168 669 NSSILERRREIeeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1756 CRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQmrldeaeqialkggkKQVQKLEARVKELETELD 1835
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK---------------EELKALREALDELRAELT 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1836 AEQKKSQEYQKVVRKYERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAE 1915
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
810
....*....|....
gi 1529987947 1916 ERADTAETQVNKLR 1929
Cdd:TIGR02168 894 SELEELSEELRELE 907
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
843-1739 |
9.37e-26 |
|
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: 116.69 E-value: 9.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 843 KIKPLLRSAATEKELAALKVELAKLKEALEKSEIkrKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDlliktkiQ 922
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELRELELALLVLRL--EELREELEELQEELKEAEEELEELTAELQELEEKLE-------E 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 923 LEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTK 1002
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1003 EKKALQEAHQQTLDDLQAEEDKVNALTKAkakLEQQVDDLEGSLEQEKKLRMDLERVKRKLEgDLKLSLESvmdLENDKQ 1082
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQ---LETLRSKVAQLELQIASLNNEIERLEARLE-RLEDRRER---LQQEIE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1083 QLEEKLKKKdfEMNELSTRIEDEQALVNQLQKKIKELQARTeeleeeleadracrAKVEKQRSDVARELEDLSERLEEAg 1162
Cdd:TIGR02168 425 ELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEAL--------------EELREELEEAEQALDAAERELAQL- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1163 gatSAQIEMNKKREAEFLKMRRDLEEAMLHheattaalRKKHADSVAELSEQIdslqRVKQKLEKERSEA---------- 1232
Cdd:TIGR02168 488 ---QARLDSLERLQENLEGFSEGVKALLKN--------QSGLSGILGVLSELI----SVDEGYEAAIEAAlggrlqavvv 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1233 --KMEADDLASTVEQLSKGKATsekMCRLyeDQMNEAKAKADELQRQLNEANTQRAraqaesgevsrkLEERESMVSQLQ 1310
Cdd:TIGR02168 553 enLNAAKKAIAFLKQNELGRVT---FLPL--DSIKGTEIQGNDREILKNIEGFLGV------------AKDLVKFDPKLR 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1311 RAKNSFSQNVEELKKQLEEENKAKNALAHSLQSSRhDCDLLReqyeeeqeAKGELQRALSKANAEVAQWRTKYEtDAIQR 1390
Cdd:TIGR02168 616 KALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTL-DGDLVR--------PGGVITGGSAKTNSSILERRREIE-ELEEK 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1391 TEELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEE 1470
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1471 CQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQA 1550
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1551 ALEEAEGTLEheesktlRIQLELNQMKSDVDrKLAEKDEELDNLRRKHQRSLESMQATLDAEAKSRNEAVRLKKKMEGDL 1630
Cdd:TIGR02168 846 QIEELSEDIE-------SLAAEIEELEELIE-ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1631 NEMEVQLNHAN-RLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERRnnllaaeVEELRALLEQNDRARKL 1709
Cdd:TIGR02168 918 EELREKLAQLElRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR-------LKRLENKIKELGPVNLA 990
|
890 900 910
....*....|....*....|....*....|
gi 1529987947 1710 AEHELLEASERVNLLHSQNTGLINQKKKLE 1739
Cdd:TIGR02168 991 AIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
848-1436 |
2.00e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.95 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 848 LRSAATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKV 927
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 928 KELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKAL 1007
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1008 QEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDLENDKQQLEEK 1087
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1088 LKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARteeleeeLEADRACRAKVEKQRSDVARELEDLSERLEEAGGATSA 1167
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAAR-------LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1168 QIEMNKKREAEflkmrrdleeamlhhEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEADDLAST-VEQL 1246
Cdd:COG1196 531 GVEAAYEAALE---------------AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAaLARG 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1247 SKGKATSEKMCRLYEDQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKQ 1326
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1327 LEEENKAKNALAHSLQSSRHDCDLLREQYEEEQEAKGELQRALSKANAEVAQwRTKYETDAIQRTEELEEAKKKLVTRLQ 1406
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE-EQLEAEREELLEELLEEEELLEEEALE 754
|
570 580 590
....*....|....*....|....*....|
gi 1529987947 1407 ESEEIMEAsnakcSSLEKTKHRLQTEIEDL 1436
Cdd:COG1196 755 ELPEPPDL-----EELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
847-1414 |
4.84e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.33 E-value: 4.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 847 LLRSAATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAK 926
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 927 VKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKA 1006
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1007 LQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDLENDKQQLEE 1086
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1087 KLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACR--AKVEKQRSDVARELEDLSERLEEAGGA 1164
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlaGAVAVLIGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1165 TSAQIEMNKKREAEFLKMR---RDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEADDLAS 1241
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAkagRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1242 TVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVE 1321
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1322 ELKKQLEEENKAKNALAHSLQSSRHDCDLLREQYEEEQEAKgELQRALSKANAEVAQWRTKYETDAIQR--------TEE 1393
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE-ALEELPEPPDLEELERELERLEREIEAlgpvnllaIEE 789
|
570 580
....*....|....*....|.
gi 1529987947 1394 LEEAKKKLVTRLQESEEIMEA 1414
Cdd:COG1196 790 YEELEERYDFLSEQREDLEEA 810
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
856-1536 |
1.70e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.91 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 856 ELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDlliktkiQLEAKVKELMERLE 935
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE-------SLEAELEELEAELE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 936 DEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALQ-EAHQQT 1014
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1015 LDDLQAEEDKVNA----LTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEG---DLKLSLESVMDLENDKQQLEEK 1087
Cdd:TIGR02168 449 LEELQEELERLEEaleeLREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfseGVKALLKNQSGLSGILGVLSEL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1088 LK-KKDFEmNELSTRI-EDEQALV---NQLQKKIKELQAR-----------TEELEEELEADRACRAKVEKQRSDVAREL 1151
Cdd:TIGR02168 529 ISvDEGYE-AAIEAALgGRLQAVVvenLNAAKKAIAFLKQnelgrvtflplDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1152 EDLSERLEEAGGATSAQ----------IEMNKKREAEFL----------------KMRRDLEEAMLHHEATTAALRKKHA 1205
Cdd:TIGR02168 608 VKFDPKLRKALSYLLGGvlvvddldnaLELAKKLRPGYRivtldgdlvrpggvitGGSAKTNSSILERRREIEELEEKIE 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1206 ---DSVAELSEQIDSLQRVKQKLEKERSEAKMEADDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNEAN 1282
Cdd:TIGR02168 688 eleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1283 TQRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKQLEEENKAKNALAHSLQSSRHDCDLLREQYEEEQEAK 1362
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1363 GELQRALSKANAEVAQWRTKYETDAIQRT------EELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDL 1436
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEallnerASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1437 IIDLERANAaaaaldKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEE----TLDHLETIKRENK- 1511
Cdd:TIGR02168 928 ELRLEGLEV------RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvNLAAIEEYEELKEr 1001
|
730 740
....*....|....*....|....*..
gi 1529987947 1512 --NLQEEITDLTDQISQGAKTIHELEK 1536
Cdd:TIGR02168 1002 ydFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
864-1708 |
2.14e-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: 105.54 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 864 LAKLKEALEKSEIKRKELEERQVSLI-QEKNDLSLQLQAEQDNLADAEDRcdlLIKTKIQLEAKVKELMERLEDEEEMSS 942
Cdd:TIGR02169 203 LRREREKAERYQALLKEKREYEGYELlKEKEALERQKEAIERQLASLEEE---LEKLTEEISELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 943 NVlakKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAEE 1022
Cdd:TIGR02169 280 KI---KDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1023 DKVNALTKAKAKLEQQVDDLEGSL----EQEKKLRMDLERVKRK---LEGDLKLSLESVMDLENDKQQLEEKLKKKDFEM 1095
Cdd:TIGR02169 357 EEYAELKEELEDLRAELEEVDKEFaetrDELKDYREKLEKLKREineLKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1096 NELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSER---LEEAGGATSAQIEMN 1172
Cdd:TIGR02169 437 NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQaraSEERVRGGRAVEEVL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1173 KKREAEFLKMRRDLEEAmlhHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMeaddlasTVEQLSKGKAT 1252
Cdd:TIGR02169 517 KASIQGVHGTVAQLGSV---GERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRA-------TFLPLNKMRDE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1253 SEKMCRLYEDQMNEAKAKADELQRQLNEANTQ--RARAQAESGEVSRKLEERESMVSqLQRAKNSFSQNVEELKKQLEEE 1330
Cdd:TIGR02169 587 RRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYvfGDTLVVEDIEAARRLMGKYRMVT-LEGELFEKSGAMTGGSRAPRGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1331 NKAKNALAHSLQSSRHDCDLLREQYEEEQEAKGELQRALSKANAEVaqwrtkyeTDAIQRTEELEEAKKKLVTRLQESEE 1410
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL--------SDASRKIGEIEKEIEQLEQEEEKLKE 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1411 IMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEwkQKYEECQSELEISQKESRGLSTELF 1490
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLR 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1491 KLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQ 1570
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1571 LELNQMKsdvdRKLAEKDEELDNLRRKHQRSLESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQLNhANRLASESQKL 1650
Cdd:TIGR02169 896 AQLRELE----RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAE-LQRVEEEIRAL 970
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1651 --LRNLQIQikdvqlELDETVHQNEELKEQVAVterrnnlLAAEVEELRALLEQNDRARK 1708
Cdd:TIGR02169 971 epVNMLAIQ------EYEEVLKRLDELKEKRAK-------LEEERKAILERIEEYEKKKR 1017
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
986-1825 |
1.12e-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: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 986 LIEEMAALDETILKLTKEKKALQEAHQQtLDDLQAEEDKVNaltkakakleQQVDDLEGslEQEKKLR-MDLERVKRKLE 1064
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEEN-IERLDLIIDEKR----------QQLERLRR--EREKAERyQALLKEKREYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1065 GDLKLS-----LESVMDLENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKEL----QARTEELEEELEADRA 1135
Cdd:TIGR02169 225 GYELLKekealERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeQLRVKEKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1136 C------------------RAKVEKQRSDVARELEDLSERLEEAGGATSAQIEMNKKREAEFLKMRRDLEEAmlhhEATT 1197
Cdd:TIGR02169 305 SlersiaekereledaeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV----DKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1198 AALRKKHADSVAELSE----------QIDSLQRVKQKLEKERSEAKMEADDLASTVEQLSKGKATSEKMCRLYEDQMNEA 1267
Cdd:TIGR02169 381 AETRDELKDYREKLEKlkreinelkrELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1268 KAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKQLE---------EENKAKNALA 1338
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlGSVGERYATA 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1339 ------HSLQSSRHDCDLLREQYEE----------------EQEAKGELQRALSKANA-----EVAQWRTKYETD---AI 1388
Cdd:TIGR02169 541 ievaagNRLNNVVVEDDAVAKEAIEllkrrkagratflplnKMRDERRDLSILSEDGVigfavDLVEFDPKYEPAfkyVF 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1389 QRT---EELEEAKK-----KLVT---RLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNF 1457
Cdd:TIGR02169 621 GDTlvvEDIEAARRlmgkyRMVTlegELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRI 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1458 DKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIH----E 1533
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHkleeA 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1534 LEKMKKGLEMEK-TEIQAALEEAEGTLEHEESKTLRIQLELNqmKSDVDRKLAEKD-EELDNLRRKHQRSLESMQATLDA 1611
Cdd:TIGR02169 781 LNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLN--RLTLEKEYLEKEiQELQEQRIDLKEQIKSIEKEIEN 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1612 EAKSRNEAVRLKKKMEGDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERRNNLLAA 1691
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1692 EVEELRALLEQNDRARKLAEhELLEASERVNLLHSQNTGLINQKKKLENDLSMLsnevddavQECRNAEEKAKKAITDAA 1771
Cdd:TIGR02169 939 PKGEDEEIPEEELSLEDVQA-ELQRVEEEIRALEPVNMLAIQEYEEVLKRLDEL--------KEKRAKLEEERKAILERI 1009
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1529987947 1772 MMAEELKKEQDTSAhLERMKKNMEQTIKDL-----QMRLDEAE-------QIALKGGKKQVQKLEA 1825
Cdd:TIGR02169 1010 EEYEKKKREVFMEA-FEAINENFNEIFAELsggtgELILENPDdpfagglELSAKPKGKPVQRLEA 1074
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1268-1929 |
6.37e-21 |
|
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: 100.52 E-value: 6.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1268 KAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAKNsfsqnveelkKQLEEENKAKNALAHSLQSSRHD 1347
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE----------LKAELRELELALLVLRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1348 CDLLREQYEEEQEAKGELQRALSKANAEVaqwrtkyetdaiqrtEELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKH 1427
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKL---------------EELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1428 RLQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIK 1507
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1508 RENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLE--------LNQMKSD 1579
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelqeelerLEEALEE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1580 VDRKLAEKDEELDNLRRKHQR------SLESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQLNHANR--------LAS 1645
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQlqarldSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyeaaieaaLGG 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1646 ESQKLL-RNLQIQIKDVQ------------LELDETVHQ----------------------------------------- 1671
Cdd:TIGR02168 546 RLQAVVvENLNAAKKAIAflkqnelgrvtfLPLDSIKGTeiqgndreilkniegflgvakdlvkfdpklrkalsyllggv 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1672 -------------NEELKEQVAVT------------------------ERRNNL--LAAEVEELRALLEQNDRARKLAEH 1712
Cdd:TIGR02168 626 lvvddldnalelaKKLRPGYRIVTldgdlvrpggvitggsaktnssilERRREIeeLEEKIEELEEKIAELEKALAELRK 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1713 ELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKK 1792
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1793 NMEQTIKDLQMRLDEAEQiALKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEEDKKNLVRL 1872
Cdd:TIGR02168 786 ELEAQIEQLKEELKALRE-ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1529987947 1873 QDLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADTAETQVNKLR 1929
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1349-1929 |
1.13e-19 |
|
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: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1349 DLLREQYEEEQEAKGELQRALSKANAEVAQWRTKYEtdaiQRTEELEEAKKKLvTRLQESEEIMEASNAKcssLEKTKHR 1428
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELEELELEL-EEAQAEEYELLAELAR---LEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1429 LQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKR 1508
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1509 ENKNLQEEITDLTDQISQgaktiheLEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDVDRKLAEKD 1588
Cdd:COG1196 387 ELLEALRAAAELAAQLEE-------LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1589 EELDNLRRKHQRSLESMQATLDAEAKSRNEAVRLKkkmegDLNEMEVQLNHANRlASESQKLLRNLQIQIKDVQLELDEt 1668
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLL-----LLLEAEADYEGFLE-GVKAALLLAGLRGLAGAVAVLIGV- 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1669 vhqnEELKEQVAVTerrnnllAAEVEELRALLEQNDRARKLAEHELLEASERVNLLHSQntgLINQKKKLENDLSMLSNE 1748
Cdd:COG1196 533 ----EAAYEAALEA-------ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD---KIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1749 VDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQKLEARVK 1828
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1829 ELETELDAEQkksQEYQKVVRKYERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSkyrKLQ 1908
Cdd:COG1196 679 AELEELAERL---AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE---EEA 752
|
570 580
....*....|....*....|.
gi 1529987947 1909 HELDDAEERADTAETQVNKLR 1929
Cdd:COG1196 753 LEELPEPPDLEELERELERLE 773
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1114-1917 |
1.88e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.91 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1114 KKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSERLEEaggatsAQIEMNKKReaEFLKMRRDLEEAmlhh 1193
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLER------LRREREKAE--RYQALLKEKREY---- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1194 EATTAALRKKHAD-SVAELSEQIDSLQRVKQKLEKERSEAKMEADDLASTVEQLSK--GKATSEKMCRLYED------QM 1264
Cdd:TIGR02169 224 EGYELLKEKEALErQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkiKDLGEEEQLRVKEKigeleaEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1265 NEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKQLEEENKAKNALAHSLQSS 1344
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1345 RHDCDLLREQYEEEQEAKGELQRALSKANAEVAQWRTKYE------TDAIQRTEELEEAKKKLVTRLQESEEIMEASNAK 1418
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAdlnaaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1419 CSSLEKTKHRLQTEIEDLiidleranaaAAALDKKQRNFDKVLAEWKQKYEE------CQSELEISQKESRGLSTELFKL 1492
Cdd:TIGR02169 464 LSKYEQELYDLKEEYDRV----------EKELSKLQRELAEAEAQARASEERvrggraVEEVLKASIQGVHGTVAQLGSV 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1493 KNSYEETLD-----HLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMK-KGLEMEKTEIQAALEEAEGTLEHEE--- 1563
Cdd:TIGR02169 534 GERYATAIEvaagnRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRdERRDLSILSEDGVIGFAVDLVEFDPkye 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1564 ---SKTLRIQLELNQMKS-----------DVDRKLAEKDEELDNLRRKhQRSLESMQATLDAEAKSRNEAvrlKKKMEGD 1629
Cdd:TIGR02169 614 pafKYVFGDTLVVEDIEAarrlmgkyrmvTLEGELFEKSGAMTGGSRA-PRGGILFSRSEPAELQRLRER---LEGLKRE 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1630 LNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQN-----D 1704
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELearieE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1705 RARKLAEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDavqecrnAEEKAKKAITDAAMMAEELKKEQDTS 1784
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE-------IEQKLNRLTLEKEYLEKEIQELQEQR 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1785 AHLERMKKNMEQTIKDLQMRLDEAEQialkggkkQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEE 1864
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKEELEE--------ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1529987947 1865 DKKNLVRLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSkYRKLQHELDDAEER 1917
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEE 966
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
923-1859 |
2.47e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.52 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 923 LEAKVKELMERLEDEEEMSSNVLAKKRKLED-ECAELKKDIDDLEITLAKIEKEkhaienkvknlieeMAALDETILKLT 1001
Cdd:TIGR02169 192 IIDEKRQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQ--------------LASLEEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1002 KEKKALQEAHQQTLDDLQAEEDKVNALTKAKA-KLEQQVDDLEGSLEQekklrmdlervkrkLEGDLKLSLESVMDLEND 1080
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAEIAS--------------LERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1081 KQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSERLEE 1160
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1161 AGGATSAQIEMNKKREAEFLKMRRDLEEAMLHHEATTAALRKKhADSVAELSEQIDSLQRVKQKLEKERSEAKMEADDLA 1240
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK-ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1241 STVEQLSKGKATSEKMCRLYEDQMNEAKAKADELqrqlneantqRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNV 1320
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARASEERVRGGRAVEEVL----------KASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1321 EELKKQLEEEN----KAKNALAHS------LQSSRHDCDLLREqyeeeqeaKGELQRALskanaEVAQWRTKYETD---A 1387
Cdd:TIGR02169 553 VVEDDAVAKEAiellKRRKAGRATflplnkMRDERRDLSILSE--------DGVIGFAV-----DLVEFDPKYEPAfkyV 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1388 IQRT---EELEEAKK-----KLVT---RLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRN 1456
Cdd:TIGR02169 620 FGDTlvvEDIEAARRlmgkyRMVTlegELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRR 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1457 FDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQgaktihelek 1536
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE---------- 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1537 mkkgLEMEKTEIQAALEEAEGTLEHEesktlriqlelnqmksdvdrKLAEKDEELDNLRRKHQRslesmqatldaeaksr 1616
Cdd:TIGR02169 770 ----LEEDLHKLEEALNDLEARLSHS--------------------RIPEIQAELSKLEEEVSR---------------- 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1617 neavrlkkkMEGDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVEEL 1696
Cdd:TIGR02169 810 ---------IEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1697 RALLEQNDRARKLAEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEE 1776
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAEL 960
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1777 LKKEQDTSAhLERMKKNMEQTIKDLQMRLDEAEqialkgGKKQVQKLEARVKELETELDAEQKKS---QEYQKVVRKYER 1853
Cdd:TIGR02169 961 QRVEEEIRA-LEPVNMLAIQEYEEVLKRLDELK------EKRAKLEEERKAILERIEEYEKKKREvfmEAFEAINENFNE 1033
|
....*.
gi 1529987947 1854 RIKELS 1859
Cdd:TIGR02169 1034 IFAELS 1039
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1211-1941 |
2.70e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 95.59 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1211 LSEQIDSLQRVKQKLEKERSEAKMEADDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNEA----NTQRA 1286
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEArkaeDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1287 RAQAESGEVSRKLEERESM-VSQLQRAKNSfsQNVEELKKQLEEENKAKNALAHSLQSSRHDCDLLREQyeEEQEAKGEL 1365
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEdARKAEAARKA--EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKA--EEERNNEEI 1254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1366 QRALSKANAEVAQWRTKYETDAIQRTEELEEAK-KKLVTRLQESEEIMEASNAKCSSLEKTKhrlqteiedliidleran 1444
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEeKKKADEAKKAEEKKKADEAKKKAEEAKK------------------ 1316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1445 aaAAALDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSyeetldhletiKRENKNLQEEITDLTDQI 1524
Cdd:PTZ00121 1317 --ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-----------AEAAEKKKEEAKKKADAA 1383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1525 SQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLElnqmKSDVDRKLAEKDEELDNLRRKHQRSLES 1604
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK----KADEAKKKAEEAKKADEAKKKAEEAKKA 1459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1605 MQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQLNHANRLASESQKllrNLQIQIKDVQLELDETVHQNEELKEqvaVTER 1684
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK---AAEAKKKADEAKKAEEAKKADEAKK---AEEA 1533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1685 RNNLLAAEVEELRalleqndRARKLAEHELLEASERVNLlhsqntglINQKKKLENDLSMLSNEVDDAVQ-ECRNAEEKA 1763
Cdd:PTZ00121 1534 KKADEAKKAEEKK-------KADELKKAEELKKAEEKKK--------AEEAKKAEEDKNMALRKAEEAKKaEEARIEEVM 1598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1764 KKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQI-ALKGGKKQVQKLEARVKELETELDAEQKKSQ 1842
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkKAEELKKAEEENKIKAAEEAKKAEEDKKKAE 1678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1843 EYQKVVRKYERRIKELSYQAEEDKKnlvrlqdlIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADTA- 1921
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKK--------AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAk 1750
|
730 740
....*....|....*....|..
gi 1529987947 1922 --ETQVNKLRVRTRDQVSKLAE 1941
Cdd:PTZ00121 1751 kdEEEKKKIAHLKKEEEKKAEE 1772
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1141-1869 |
5.57e-19 |
|
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: 94.41 E-value: 5.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1141 EKQRSDVARELEDLSERLEEAGGATSAQIEMNKKREAEFLKMRRDLEEAMlhHEATTAALRKKhaDSVAELSEQIDSLQR 1220
Cdd:pfam15921 102 EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV--HELEAAKCLKE--DMLEDSNTQIEQLRK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1221 VKQKLE-------------KERSEAKMEADDLASTVEQLSKGKATSeKMCRLYEDQMNEAKAKADELQRQLNEANTQRAR 1287
Cdd:pfam15921 178 MMLSHEgvlqeirsilvdfEEASGKKIYEHDSMSTMHFRSLGSAIS-KILRELDTEISYLKGRIFPVEDQLEALKSESQN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1288 A-----QAESGEVSRKLEERESMVSQL-QRAKNSFSQNVEELKKQLEEENKAKNA----------LAHSLQSSRHDCDLL 1351
Cdd:pfam15921 257 KielllQQHQDRIEQLISEHEVEITGLtEKASSARSQANSIQSQLEIIQEQARNQnsmymrqlsdLESTVSQLRSELREA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1352 REQYEEEQEakgELQRALSKANAEVAQWRTKYETDAiQRTEELEEAKKKLVTRLQESEEIMeasnakcsSLEKTKHRLQT 1431
Cdd:pfam15921 337 KRMYEDKIE---ELEKQLVLANSELTEARTERDQFS-QESGNLDDQLQKLLADLHKREKEL--------SLEKEQNKRLW 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1432 EIE---DLIIDLERANaaaaaLDKKQRNFDKVLAEWKQKYEECQSELEISQKESRG----------LSTELFKLKNSYEE 1498
Cdd:pfam15921 405 DRDtgnSITIDHLRRE-----LDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGkneslekvssLTAQLESTKEMLRK 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1499 TLDHLETIKRENKNLQEEITDLTDQISQGAKTIH----ELEKMKKGLEMEKTEIQAaleeaegtLEHEESKTLRIQLELN 1574
Cdd:pfam15921 480 VVEELTAKKMTLESSERTVSDLTASLQEKERAIEatnaEITKLRSRVDLKLQELQH--------LKNEGDHLRNVQTECE 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1575 QMKsdvdRKLAEKDEELDNLRRKhqrsLESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQLNHANRLASESQKLLRNL 1654
Cdd:pfam15921 552 ALK----LQMAEKDKVIEILRQQ----IENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1655 QIQIKDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVE----ELRALLEQNDRARKLAEHELLEASERVNLLHSQNTG 1730
Cdd:pfam15921 624 EARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKtsrnELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKS 703
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1731 LINQKKKLENDLSMLSNEVDDAVQECRNAEEK--AKKAITDAAMMAEELKKEQDTSAHLER--MKKNMEQTIKDLQMRLD 1806
Cdd:pfam15921 704 AQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQitAKRGQIDALQSKIQFLEEAMTNANKEKhfLKEEKNKLSQELSTVAT 783
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 1807 EAEQIA--LKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEEDKKNL 1869
Cdd:pfam15921 784 EKNKMAgeLEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKEL 848
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1353-1941 |
6.30e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 94.35 E-value: 6.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1353 EQYEEEQEAKGELQRALSKANAEVAqwRTKYETdAIQRTEELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTE 1432
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRLEEL--REELEE-LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1433 IEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKN 1512
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1513 LQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLE--HEESKTLRIQLELNQMKsDVDRKLAEKDEE 1590
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErlQQEIEELLKKLEEAELK-ELQAELEELEEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1591 LDNLrrkhQRSLESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQLNHANRLASESQKLLRNLqIQIKDVQLELDETVH 1670
Cdd:TIGR02168 449 LEEL----QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV-KALLKNQSGLSGILG 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1671 QneeLKEQVAVTER-RNNLLAAEVEELRALL-EQNDRARKLAEHELLEASERVNLLHsqnTGLINQKKKLENDLSMLSNE 1748
Cdd:TIGR02168 524 V---LSELISVDEGyEAAIEAALGGRLQAVVvENLNAAKKAIAFLKQNELGRVTFLP---LDSIKGTEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1749 --VDDAVQECRNAEEKAKKAI-------------TDAAMMAEELKKE-------------------QDTSAHLERMKKNM 1794
Cdd:TIGR02168 598 egFLGVAKDLVKFDPKLRKALsyllggvlvvddlDNALELAKKLRPGyrivtldgdlvrpggvitgGSAKTNSSILERRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1795 EqtIKDLQmrldeaeqialkggkKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEEDKKNLVRLQD 1874
Cdd:TIGR02168 678 E--IEELE---------------EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1529987947 1875 LIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADTAETQVNKLRVRTRDQVSKLAE 1941
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE 807
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
849-1604 |
9.54e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.05 E-value: 9.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 849 RSAATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLslQLQAEQDNLADAEDRCDLLIKTKIQLEAKVK 928
Cdd:PTZ00121 1189 KAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEA--KKDAEEAKKAEEERNNEEIRKFEEARMAHFA 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 929 ELMERLEDEEEMSSNVLAKkrkledecAELKKDIDDLEitlaKIEKEKHAIENKVKnlIEEMAALDETILKLTKEKKALQ 1008
Cdd:PTZ00121 1267 RRQAAIKAEEARKADELKK--------AEEKKKADEAK----KAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKKAD 1332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1009 EAHQQTlddlqaeEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEgDLKLSLESVMDLENDKQQLEEKL 1088
Cdd:PTZ00121 1333 AAKKKA-------EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD-AAKKKAEEKKKADEAKKKAEEDK 1404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1089 KKKD-FEMNELSTRIEDEQALVNQLQKKIKELQARteeleeeleADRACRAKVEKQRSDVARELEDLSERLEEAGGATSA 1167
Cdd:PTZ00121 1405 KKADeLKKAAAAKKKADEAKKKAEEKKKADEAKKK---------AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1168 QIEMNKKREAEFLKMRRDlEEAMLHHEATTAALRKKHADSVAELSEQidslqrvKQKLEKERSEAKMEADDLASTVEqls 1247
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKKAEEA-------KKADEAKKAEEAKKADEAKKAEE--- 1544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1248 kgKATSEKMCRLYEDQMNEAKAKADELQRQLNEANTQRARAqaesgEVSRKLEER--ESMVSQLQRAKNSFSQNVEELKK 1325
Cdd:PTZ00121 1545 --KKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA-----EEAKKAEEAriEEVMKLYEEEKKMKAEEAKKAEE 1617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1326 QLEEENKAKNAlahslQSSRHDCDLLREQYEEEQEAKGELQRALSKANAEVAQWRTKYETDAiQRTEEL----EEAKKKL 1401
Cdd:PTZ00121 1618 AKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkkaeEDEKKAA 1691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1402 VTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEdliidlERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELEISQKE 1481
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAEEKKKAEELKKA------EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKE 1765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1482 SRGLSTELFKLKNSYEEtldhlETIKRENKNLQEEITDLTDQISQGAKTIHELEK-----MKKGLEMEKTEIQAALEEAE 1556
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIE-----EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKegnlvINDSKEMEDSAIKEVADSKN 1840
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1529987947 1557 GTLEhEESKTLRIQLELNQMKSDVDRKLAEKDEELDNLRRKHQRSLES 1604
Cdd:PTZ00121 1841 MQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA 1887
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
851-1523 |
3.50e-18 |
|
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: 91.78 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 851 AATEKELAALKVELAKLKEALEKSEIKRKELE-------------ERQVSLIQEK-NDLSLQLQAEQDNLADAEDRCDLL 916
Cdd:pfam01576 380 QALESENAELQAELRTLQQAKQDSEHKRKKLEgqlqelqarlsesERQRAELAEKlSKLQSELESVSSLLNEAEGKNIKL 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 917 IKTKIQLEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDET 996
Cdd:pfam01576 460 SKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 997 ILKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMD 1076
Cdd:pfam01576 540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISAR 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1077 LENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSE 1156
Cdd:pfam01576 620 YAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKT 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1157 RLE----EAGGATSAQIEMNKKREAEFLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQidslqrVKQKLEKERSEA 1232
Cdd:pfam01576 700 QLEeledELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDE------RKQRAQAVAAKK 773
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1233 KMEAD--DLASTVEQLSKGKATSEKmcrlyedQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQ 1310
Cdd:pfam01576 774 KLELDlkELEAQIDAANKGREEAVK-------QLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQ 846
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1311 -------RAKNSFSQNVEELKKQLEEENKAKNALAHSLQSSRHDCDLLREQYEEEQEAKGELQRALSKANAEVAQWRTKY 1383
Cdd:pfam01576 847 edlaaseRARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTEL 926
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1384 --ETDAIQRTE----ELEEAKKKLVTRLQESEeimeasNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNF 1457
Cdd:pfam01576 927 aaERSTSQKSEsarqQLERQNKELKAKLQEME------GTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRT 1000
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1529987947 1458 DKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQ 1523
Cdd:pfam01576 1001 EKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATES 1066
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1266-1836 |
7.46e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.38 E-value: 7.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1266 EAKAKADELQRQL-----NEANTQRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKQLEEENKAKNALAHS 1340
Cdd:COG1196 217 ELKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1341 LQSSRHDCDLLREQYEEEQEAKGELQRALSKANAEVAQwrtkyetdAIQRTEELEEAKKKLVTRLQESEEIMEASNAKCS 1420
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEE--------LEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1421 SLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETL 1500
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1501 DHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDV 1580
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1581 DRKLAEKDEELDNLRrkhqRSLESMQATLDAEAKSRNEAVRLKKKMEGDLNemEVQLNHANRLASESQKLLRNLQIQIKD 1660
Cdd:COG1196 529 LIGVEAAYEAALEAA----LAAALQNIVVEDDEVAAAAIEYLKAAKAGRAT--FLPLDKIRARAALAAALARGAIGAAVD 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1661 VQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQNDRARKLAEHELLEASERVNLLHSQNTGLINQKKKLEN 1740
Cdd:COG1196 603 LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1741 DLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQV 1820
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570
....*....|....*.
gi 1529987947 1821 QKLEARVKELETELDA 1836
Cdd:COG1196 763 EELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1208-1780 |
9.71e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.00 E-value: 9.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1208 VAELSEQIDSLQRVKQKLEKERsEAKMEADDLASTVEQLSKGKATSEKmcRLYEDQMNEAKAKADELQRQLNEANTQRAR 1287
Cdd:COG1196 195 LGELERQLEPLERQAEKAERYR-ELKEELKELEAELLLLKLRELEAEL--EELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1288 AQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKQLEEENKAKNALAHSLQSSRHDCDLLREQYEEEQEAKGELQR 1367
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1368 ALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQESEEIMEasnakcssLEKTKHRLQTEIEDLIIDLERANAAA 1447
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE--------LAAQLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1448 AALDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRE------NKNLQEEITDLT 1521
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEElaeaaaRLLLLLEAEADY 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1522 DQISQGAKTIHELEKMKKGLEMEKTEIQ------AALEEAEGTLEHE-----ESKTLRIQLELNQMKSDVDRKLAEKDEE 1590
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVAVLIGveaayeAALEAALAAALQNivvedDEVAAAAIEYLKAAKAGRATFLPLDKIR 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1591 LDNLRRKHQRSLESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQ--LNHANRLASESQKLLRNLQIQIKDVQLELDET 1668
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAarLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1669 VHQNEELKEQVAVTERRNNLLAAEVEELRALLEQNDRARKLAEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNE 1748
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
570 580 590
....*....|....*....|....*....|..
gi 1529987947 1749 VDDAVQECRNAEEKAKKAITDAAMMAEELKKE 1780
Cdd:COG1196 744 EEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1286-1941 |
1.27e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 89.74 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1286 ARAQAESGEVSRKLEERESMVS----QLQRAKNSFSQNVEELKKQLEEENKAKNALAHSLQSSRHDCDLLREQYEEEQEA 1361
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDekrqQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1362 KGELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLE 1441
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1442 RANAAAAALDKKQRNFDKVLAEW-------KQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQ 1514
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRDKLteeyaelKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1515 EEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEheesktlriqlELNQMKSDVDRKLAEKDEELDNL 1594
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE-----------QLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1595 RRKhQRSLESMQATLDAEAKSRNEAVR--------LKKKMEG------DLNEMEVQLNHA------NRL----------A 1644
Cdd:TIGR02169 482 EKE-LSKLQRELAEAEAQARASEERVRggraveevLKASIQGvhgtvaQLGSVGERYATAievaagNRLnnvvveddavA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1645 SESQKLLRNLQI---------QIKDVQLELDETVHQN-----------EELKEQVAVTERRNNLLAAEVEELRALLEQ-- 1702
Cdd:TIGR02169 561 KEAIELLKRRKAgratflplnKMRDERRDLSILSEDGvigfavdlvefDPKYEPAFKYVFGDTLVVEDIEAARRLMGKyr 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1703 ------------------NDRARKLA------EHELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDAVQECRN 1758
Cdd:TIGR02169 641 mvtlegelfeksgamtggSRAPRGGIlfsrsePAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1759 AEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAE-------------------------QIAL 1813
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEedlhkleealndlearlshsripeiQAEL 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1814 KGGKKQVQKLEARVKELETELDAE-------QKKSQEYQKVVRKYERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSY 1886
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNRLtlekeylEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 1887 KRQTEEAEEQANTNLSKYRKLQHELDDAEERADTAETQVNKLRVRTRDQVSKLAE 1941
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1138-1938 |
1.80e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 89.36 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1138 AKVEKQRsdvaRELEDLSERLEEAGGATSAQIEMNKKREAEFLKMRR--DLEEAMLHHEATTAALRKKHAD-SVAELSEQ 1214
Cdd:TIGR02169 170 RKKEKAL----EELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqALLKEKREYEGYELLKEKEALErQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1215 IDSLQRVKQKLEKERSEAKMEADDLASTVEQLSK--GKATSEKMCRLYED------QMNEAKAKADELQRQLNEANTQRA 1286
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKkiKDLGEEEQLRVKEKigeleaEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1287 RAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKQLEEENKAKNALAHSLQSSRHDCDLLREQYEEEQEAKGELQ 1366
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1367 RALSKANAEVAQWRTKYE------TDAIQRTEELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLiidl 1440
Cdd:TIGR02169 406 RELDRLQEELQRLSEELAdlnaaiAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV---- 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1441 eranaaAAALDKKQRNFDKVLAEWKQKYEE------CQSELEISQKESRGLSTELFKLKNSYEETLD-----HLETIKRE 1509
Cdd:TIGR02169 482 ------EKELSKLQRELAEAEAQARASEERvrggraVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaagnRLNNVVVE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1510 NKNLQEEITDLTDQISQGAKTIHELEKMK-KGLEMEKTEIQAALEEAEGTLEHEE------SKTLRIQLELNQMKS---- 1578
Cdd:TIGR02169 556 DDAVAKEAIELLKRRKAGRATFLPLNKMRdERRDLSILSEDGVIGFAVDLVEFDPkyepafKYVFGDTLVVEDIEAarrl 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1579 -------DVDRKLAEKDEELDNLRRKhQRSLESMQATLDAEAKSRNEAvrlKKKMEGDLNEMEVQLNHANRLASESQKLL 1651
Cdd:TIGR02169 636 mgkyrmvTLEGELFEKSGAMTGGSRA-PRGGILFSRSEPAELQRLRER---LEGLKRELSSLQSELRRIENRLDELSQEL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1652 RNLQIQIKDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQN-----DRARKLAEHELLEASERVNLLHS 1726
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELearieELEEDLHKLEEALNDLEARLSHS 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1727 QNTGLINQKKKLENDLSMLSNEVDDAvqecrnaEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLD 1806
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREI-------EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1807 EAEQialkggkkQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSY 1886
Cdd:TIGR02169 865 ELEE--------ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1887 KR-----------------------------------------QTEEAEEQANTNLSKYRKLQHELDDAEERADTAETQV 1925
Cdd:TIGR02169 937 EDpkgedeeipeeelsledvqaelqrveeeiralepvnmlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
890
....*....|...
gi 1529987947 1926 NKLRVRTRDQVSK 1938
Cdd:TIGR02169 1017 REVFMEAFEAINE 1029
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1009-1844 |
5.03e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 87.87 E-value: 5.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1009 EAHQQTLDDLQAEEDKVNAL-TKAKAKLEQQVDDLEGSLEQ---EKKLRMDLERVKRKLEGDLKLSLE-SVMDLENDKQQ 1083
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLRNQLQnTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1084 LEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEAD-----RACRAKVEKQRSDVARELEDLSERL 1158
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMstmhfRSLGSAISKILRELDTEISYLKGRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1159 EEAGGATSAQIEMNKKREAEFLKMRRD-LEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEAD 1237
Cdd:pfam15921 241 FPVEDQLEALKSESQNKIELLLQQHQDrIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1238 DLASTVEQLskgKATSEKMCRLYEDQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEEresMVSQLQRAKNSFS 1317
Cdd:pfam15921 321 DLESTVSQL---RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK---LLADLHKREKELS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1318 qnVEELKKQLEEENKAKNALAhslqssrhdCDLLREQYEEEQEakgELQR--ALSKANAEVAQWRTKYETDAIQRTEELE 1395
Cdd:pfam15921 395 --LEKEQNKRLWDRDTGNSIT---------IDHLRRELDDRNM---EVQRleALLKAMKSECQGQMERQMAAIQGKNESL 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1396 EAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLEranaaaaaldKKQRNFDKVLAEwkqkYEECQSEL 1475
Cdd:pfam15921 461 EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ----------EKERAIEATNAE----ITKLRSRV 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1476 EISQKESRGLSTELFKLKNSYEETldhlETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEa 1555
Cdd:pfam15921 527 DLKLQELQHLKNEGDHLRNVQTEC----EALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIND- 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1556 egtleheesKTLRIQlELNQMKSDVDRKLAEKDEELDNlrrkhqrsLESMQATLDAEAKSRNEAVR-LKKKMEGDLNEME 1634
Cdd:pfam15921 602 ---------RRLELQ-EFKILKDKKDAKIRELEARVSD--------LELEKVKLVNAGSERLRAVKdIKQERDQLLNEVK 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1635 VQLNHANRLASESQKLLRNLQiqikdvqleldetvHQNEELkeqvavtERRNNLLAAEVEELRALLEQNDRARKLAEHEL 1714
Cdd:pfam15921 664 TSRNELNSLSEDYEVLKRNFR--------------NKSEEM-------ETTTNKLKMQLKSAQSELEQTRNTLKSMEGSD 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1715 LEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNM 1794
Cdd:pfam15921 723 GHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRL 802
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1529987947 1795 EQTIKDLQMRLDEAE-QIALKGGKKQVQKLEARVKELETELDAEQKKSQEY 1844
Cdd:pfam15921 803 KEKVANMEVALDKASlQFAECQDIIQRQEQESVRLKLQHTLDVKELQGPGY 853
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
781-1312 |
5.34e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.68 E-value: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 781 LEELRDERLAKVLTLLQAVARGKIMRLELQRMMERREALmiiqwnirafnavkhwpwmklffkikpLLRSAATEKELAAL 860
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEA---------------------------QAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 861 KVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELMERLEDEEEM 940
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 941 SSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQA 1020
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1021 EEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDlklsLESVMDLENDKQQLEEKLKKKDFEMNELST 1100
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF----LEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1101 RIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSERLEEAGGATSAQIEMNKKREAEFL 1180
Cdd:COG1196 537 EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1181 KMRRDLEEAML--HHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEADDLASTVEQLskgkatsEKMCR 1258
Cdd:COG1196 617 VLGDTLLGRTLvaARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL-------AERLA 689
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1529987947 1259 LYEDQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRA 1312
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1229-1937 |
2.81e-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: 85.61 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1229 RSEAKMEA--DDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQ---LNEANTQRARAQAES-------GEVS 1296
Cdd:pfam01576 2 RQEEEMQAkeEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAEtelCAEAEEMRARLAARKqeleeilHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1297 RKLEERESMVSQLQRAKNSFSQNVEElkkqleeenkaknalahslqssrhdcdlLREQYEEEQEAKGELQRALSKANAEV 1376
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQD----------------------------LEEQLDEEEAARQKLQLEKVTTEAKI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1377 AQWRTKYETDAIQRTEeLEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRN 1456
Cdd:pfam01576 134 KKLEEDILLLEDQNSK-LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1457 FDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEK 1536
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1537 MKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDVDRKLAEKDEELDNLRRKHQRSLESMQATLDAEAKSR 1616
Cdd:pfam01576 293 QRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNK 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1617 NEAVRLKKKMEGDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVterrnnlLAAEVEEL 1696
Cdd:pfam01576 373 ANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK-------LQSELESV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1697 RALLEQNDrarklaehelleaservnllhsqntgliNQKKKLENDLSMLSNEVDDAvQECRNAEEKAKKAIT-------- 1768
Cdd:pfam01576 446 SSLLNEAE----------------------------GKNIKLSKDVSSLESQLQDT-QELLQEETRQKLNLStrlrqled 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1769 DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQI--ALKGGKKQVQKlearvkELETELDAEQKKSQEYQK 1846
Cdd:pfam01576 497 ERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTleALEEGKKRLQR------ELEALTQQLEEKAAAYDK 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1847 VVRKYERRIKELS------YQAEEDKKNLVRLQDLIDKLQVKVKS----YKRQTEEAEEQANTNLSKYRKLQHELDDAEE 1916
Cdd:pfam01576 571 LEKTKNRLQQELDdllvdlDHQRQLVSNLEKKQKKFDQMLAEEKAisarYAEERDRAEAEAREKETRALSLARALEEALE 650
|
730 740
....*....|....*....|.
gi 1529987947 1917 RADTAETQVNKLRVRTRDQVS 1937
Cdd:pfam01576 651 AKEELERTNKQLRAEMEDLVS 671
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1616-1931 |
3.66e-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: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1616 RNEAVRLKKKMEGDLN-------EMEVQLNhanRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERRNNL 1688
Cdd:COG1196 174 KEEAERKLEATEENLErledilgELERQLE---PLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1689 LAAEVEELRALLEQNDRARKLAEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDAVQECRNAEEKAKKAIT 1768
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1769 DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQKLEARVkELETELDAEQKKSQEYQKVV 1848
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL-EALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1849 RKYERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADTAETQVNKL 1928
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
...
gi 1529987947 1929 RVR 1931
Cdd:COG1196 490 AAR 492
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1380-1916 |
4.64e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 84.35 E-value: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1380 RTKYETDAIQRTEELE----EAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQT------EIEDLIIDLERANAAAAA 1449
Cdd:PRK03918 177 RIERLEKFIKRTENIEelikEKEKELEEVLREINEISSELPELREELEKLEKEVKEleelkeEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1450 LDKKQRNFDKVLAEWKQKYEECQSELEISqKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAK 1529
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1530 TIHELEKMKKglemEKTEIQAALEEAEGTLEHEEsKTLRIQLELNQMKSDVDRKLAEK-DEELDNLRRKHQ------RSL 1602
Cdd:PRK03918 336 KEERLEELKK----KLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEeieeeiSKI 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1603 ESMQATLDAEAKSRNEAVRLKKKMEGdlnemevQLNHANRLASESQK--LLRNLQIQIKDVQLELDETVHQNEELK---- 1676
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKAKG-------KCPVCGRELTEEHRkeLLEEYTAELKRIEKELKEIEEKERKLRkelr 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1677 --EQVAVTERRNNLLAAEVEELRALLEqndRARKLAEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLsnevddavq 1754
Cdd:PRK03918 484 elEKVLKKESELIKLKELAEQLKELEE---KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL--------- 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1755 ecrNAEEKAKKAITDAAMMAEELKKEQdtsahLERMKKNMEQTIKDLQMRLDEAEQ-----IALKGGKKQVQKLEARVKE 1829
Cdd:PRK03918 552 ---EELKKKLAELEKKLDELEEELAEL-----LKELEELGFESVEELEERLKELEPfyneyLELKDAEKELEREEKELKK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1830 LETELDAEQKKSQEYQKVVRKYERRIKELsyQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQH 1909
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEEL--EKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKE 701
|
....*..
gi 1529987947 1910 ELDDAEE 1916
Cdd:PRK03918 702 ELEEREK 708
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1427-1935 |
1.19e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.45 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1427 HRLQTEIEDLiiDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETI 1506
Cdd:COG1196 216 RELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1507 KRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDVDRKLAE 1586
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1587 KDEELDNLRRKHQRSLESMQATLDAEAKSRNEAVRLKKKmEGDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELD 1666
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1667 ETVHQNEELKEQVAVTERRNNLLAAEVEELRALLeqndrARKLAEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLS 1746
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEEL-----AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1747 NEVDDAVQECRNAEEKAKKAI--------TDAAMMAEELKKEQD---TSAHLERMKKNMEQTIKDLQMRLDEA-EQIALK 1814
Cdd:COG1196 528 VLIGVEAAYEAALEAALAAALqnivveddEVAAAAIEYLKAAKAgraTFLPLDKIRARAALAAALARGAIGAAvDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1815 GGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKEL------------SYQAEEDKKNLVRLQDLIDKLQVK 1882
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLegeggsaggsltGGSRRELLAALLEAEAELEELAER 687
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1529987947 1883 VKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADTAETQVNKLRVRTRDQ 1935
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
224-714 |
1.34e-15 |
|
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: 82.87 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 224 IIEANPAMEAFGNAKTLRNDNSSRFGKF--IRIHFGPTG---KLASADIDIYLLEKSRVIFQQ------PGERSYHIYYQ 292
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 293 IMSQ----------KKPELLDMLLVSSNPY----DYH---FCSQGVTTVESLDDGQELMatdNAMDILGFLPDEKYGCYK 355
Cdd:cd14894 329 MVAGvnafpfmrllAKELHLDGIDCSALTYlgrsDHKlagFVSKEDTWKKDVERWQQVI---DGLDELNVSPDEQKTIFK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 356 IVGAIMHFGNMKFKQKQREEQAEADGT---ESADKASYLMGVSSADLIKGLLHPR---VKVGNEYVVKGQNVEQVIYAVG 429
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 430 ALAKATYDRMFKWLVGRINRTLY----------------TSLPRQY-FIGVLDIAGFEIFELNSFEQLCINFTNEKLqqf 492
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATKmsalstdgnkhqmdsnASAPEAVsLLKIVDVFGFEDLTHNSLDQLCINYLSEKL--- 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 493 fnhhmfileqeeYKRE----GIEWTFIDFGLDLQACIDLI---EKPMGIMSILEEECMFPKATDNS----------FKAK 555
Cdd:cd14894 563 ------------YAREeqviAVAYSSRPHLTARDSEKDVLfiyEHPLGVFASLEELTILHQSENMNaqqeekrnklFVRN 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 556 MYDNHIGKSPNFQKPRPDKKRKYEA-----HFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKS-ANKLLASLYENY 629
Cdd:cd14894 631 IYDRNSSRLPEPPRVLSNAKRHTPVllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSnSSHFCRMLNESS 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 630 VGSDSVSDPKPGFKEKRKKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFLVLHQLRCNGVLEG 709
Cdd:cd14894 711 QLGWSPNTNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQ 790
|
....*
gi 1529987947 710 IRICR 714
Cdd:cd14894 791 MEICR 795
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
32-76 |
1.50e-15 |
|
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: 72.08 E-value: 1.50e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1529987947 32 DGKKRAWIPDEKEAYIEIEIKELSGDKVIVETKDGRTLTVKVDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1398-1935 |
2.09e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 82.80 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1398 KKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELEI 1477
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1478 SQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEG 1557
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1558 TLEHEESKTLRIQLELNQMKSDVDRKLAEKDEELDNL----RRKHQRSLESMQATLDAEAKSRNEAVRLKKKMEGDLNEM 1633
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeeaeLKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1634 EVQLNHANRLASESQKLLRNLQ-------------IQIKDVQLELDE---------TVHQNEELKEQVAVTERRNNLL-- 1689
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLErlqenlegfsegvKALLKNQSGLSGilgvlseliSVDEGYEAAIEAALGGRLQAVVve 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1690 -AAEVEELRALLEQNDRAR------KLAEHELLEASERVNLLHSQNT-----GLINQKKKLENDLSML------------ 1745
Cdd:TIGR02168 554 nLNAAKKAIAFLKQNELGRvtflplDSIKGTEIQGNDREILKNIEGFlgvakDLVKFDPKLRKALSYLlggvlvvddldn 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1746 -------------------------------SNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNM 1794
Cdd:TIGR02168 634 alelakklrpgyrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAE---LRKELEEL 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1795 EQTIKDLQMRLDEAEQiALKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEEDKKNLVRLQD 1874
Cdd:TIGR02168 711 EEELEQLRKELEELSR-QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1529987947 1875 LIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADTAETQVNKLRVRTRDQ 1935
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1017-1810 |
2.39e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.50 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1017 DLQAEEDKV--NALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDLEN-----DKQQLEEKLK 1089
Cdd:PTZ00121 1080 DFDAKEDNRadEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEarkaeDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1090 KKDFEMNELSTRIEDEQAlVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDlSERLEEAGGATSAQI 1169
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKK-AEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAED-AKKAEAVKKAEEAKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1170 EMNKKREAEFLKMR---RDLEEAMLHH----EATTAALRKKHADSV--AELSEQIDSLQRVKQKLE----KERSEAKMEA 1236
Cdd:PTZ00121 1238 DAEEAKKAEEERNNeeiRKFEEARMAHfarrQAAIKAEEARKADELkkAEEKKKADEAKKAEEKKKadeaKKKAEEAKKA 1317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1237 DDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRA---- 1312
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdeak 1397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1313 KNSFSQNVEELKKQLEEENKAKNALAHSLQSSRHDCDLLREQYEEEQEAKGELQRALSKANAEVAQWRT---KYETDAIQ 1389
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAeeaKKADEAKK 1477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1390 RTEE---LEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLiidleRANAAAAALDKKQRNFDKVLAEWKQ 1466
Cdd:PTZ00121 1478 KAEEakkADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEA-----KKAEEAKKADEAKKAEEKKKADELK 1552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1467 KYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKREN--KNLQEEITDLTDQISQGAKTIHELEKMKKGLEME 1544
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1545 KTEIQAALEEAEgtlEHEESKTLRIQLELNQMKSDVDRKLAEKDEELDNLRRKHQRSLESMQATLDAEAKSRNEAVRLKK 1624
Cdd:PTZ00121 1633 KKVEQLKKKEAE---EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1625 KMEGDLNEME----------VQLNHANRLASESQKLLRNLQI----QIKDVQLELDETVHQNEELKEQVAVTErrnnlla 1690
Cdd:PTZ00121 1710 KEAEEKKKAEelkkaeeenkIKAEEAKKEAEEDKKKAEEAKKdeeeKKKIAHLKKEEEKKAEEIRKEKEAVIE------- 1782
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1691 aevEELRALLEQNDRARKLAEHELLEASERVNLLHSQNTGLINQKKKLENdlSMLSNEVDDAVQECRNAEEKAKKAITDA 1770
Cdd:PTZ00121 1783 ---EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMED--SAIKEVADSKNMQLEEADAFEKHKFNKN 1857
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1529987947 1771 AMMAEELKKEQDTSAH---LERMKKNMEQTIKDLQMRLDEAEQ 1810
Cdd:PTZ00121 1858 NENGEDGNKEADFNKEkdlKEDDEEEIEEADEIEKIDKDDIER 1900
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
849-1123 |
5.40e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 81.26 E-value: 5.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 849 RSAATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVK 928
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 929 ELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALQ 1008
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1009 EAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSL-EQEKKLRMDLERVKRKLEGDLKLSLESVMDLENDKQQL--- 1084
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpv 987
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1529987947 1085 ----EEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQART 1123
Cdd:TIGR02168 988 nlaaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
920-1807 |
1.20e-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: 80.02 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 920 KIQLEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILK 999
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1000 LTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKlrmdleRVKRKLEGDLKLSLESVMDLEN 1079
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK------SELLKLERRKVDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1080 DKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARteeleeeLEADracrakvEKQRSDVARELEDLSERLE 1159
Cdd:pfam02463 322 EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL-------QEKL-------EQLEEELLAKKKLESERLS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1160 EAGGATSAQIEM--NKKREAEFLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEad 1237
Cdd:pfam02463 388 SAAKLKEEELELksEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL-- 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1238 dlastveqlskgkatsekmcrlyEDQMNEAKAKADELQRQLNEANTQRARA-QAESGEVSRKLEERESMVSQLQRAKNSF 1316
Cdd:pfam02463 466 -----------------------ELKKSEDLLKETQLVKLQEQLELLLSRQkLEERSQKESKARSGLKVLLALIKDGVGG 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1317 SQNVEELKKQLEEENKAKNALAHSLQssrhdCDLLREQYEEEQEAKGELQRALSKANAEVAQWRTKYETDAIQRTEELEE 1396
Cdd:pfam02463 523 RIISAHGRLGDLGVAVENYKVAISTA-----VIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1397 AKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLI-------------IDLERANAAAAALDKKQRNFDKVLAE 1463
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKesakakesglrkgVSLEEGLAEKSEVKASLSELTKELLE 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1464 WKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEM 1543
Cdd:pfam02463 678 IQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1544 EKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDVDRKLAEKDEELDNLRRKHQ--RSLESMQATLDAEAKSRNEAVR 1621
Cdd:pfam02463 758 KKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEaeLLEEEQLLIEQEEKIKEEELEE 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1622 LKKKMEGDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELDETVhQNEELKEQVAVTERRnnllaAEVEELRALLE 1701
Cdd:pfam02463 838 LALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK-DELESKEEKEKEEKK-----ELEEESQKLNL 911
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1702 QNDRARKLAEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQ 1781
Cdd:pfam02463 912 LEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYN 991
|
890 900
....*....|....*....|....*.
gi 1529987947 1782 DTSAHLERMKKNMEQTIKDLQMRLDE 1807
Cdd:pfam02463 992 KDELEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1390-1904 |
3.38e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1390 RTEELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLqTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYE 1469
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1470 ECQSEL-EISQKESRglsteLFKLKNSYEETLDHLETIKRENKnLQEEITDLTDQISQ-----GAKTIHELEKMKKGLEM 1543
Cdd:PRK03918 325 GIEERIkELEEKEER-----LEELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERlkkrlTGLTPEKLEKELEELEK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1544 EKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSD------VDRKLAEKDEEldNLRRKHQRSLESMQATLdaeaksrN 1617
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvCGRELTEEHRK--ELLEEYTAELKRIEKEL-------K 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1618 EAVRLKKKMEGDLNEMEVQLNHANRLASESQ--KLLRNLQIQIKDVQLE-LDETVHQNEELKEQVAVTERRNNLLAAEVE 1694
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1695 ELRALleqnDRARKLAEHELLEASERVNLLHsqntglinqkKKLENDLSMLSNEVDDAVQECRNAEEK---AKKAITDAA 1771
Cdd:PRK03918 550 KLEEL----KKKLAELEKKLDELEEELAELL----------KELEELGFESVEELEERLKELEPFYNEyleLKDAEKELE 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1772 MMAEELKKEQDTsahLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKY 1851
Cdd:PRK03918 616 REEKELKKLEEE---LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEI 692
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1529987947 1852 ERRIKELSYQAEEDKKNLVRLQDL---IDKLQVKVKSYKRQTEEAEEQANTNLSKY 1904
Cdd:PRK03918 693 KKTLEKLKEELEEREKAKKELEKLekaLERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
865-1236 |
3.98e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.57 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 865 AKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELMERLEDEEEMSSNV 944
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 945 LAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIE-----NKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQ 1019
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1020 AEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDLENDKQQLEEKLKKKDFEMNELS 1099
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1100 TRIEDEQALVNQLQKKIKELQARTEELEEELEADracrakveKQRSDVARELEDLSERLEEAGGATSAQIEMNKKREAEF 1179
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSEIEDPKGED--------EEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEY 981
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1529987947 1180 LKMRRDLEEamlhheattaaLRKKHadsvAELSEQIDSLQRVKQKLEKERSEAKMEA 1236
Cdd:TIGR02169 982 EEVLKRLDE-----------LKEKR----AKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
980-1376 |
7.22e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.40 E-value: 7.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 980 ENKVKNLIEEMAALDETILKLTKEKKALQEAHQQTlddlqaeEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERV 1059
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEEL-------EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1060 KRKLEGDLKLSLESVMDLENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAK 1139
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1140 VEKQRSDVARELEDLSERLEEAggatSAQIEMNKKReaeflkmRRDLEEAMlhheattaalrkkhadsvAELSEQIDSLQ 1219
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEEL----SEDIESLAAE-------IEELEELI------------------EELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1220 RVKQKLEKERSEAKMEADDLASTVEQLskgkatsekmcrlyEDQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKL 1299
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELREL--------------ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1300 EERESMVsqLQRAKNSFSQNVEELKKQLEEENKAKNALA------------HSLQSSRHdcDLLREQYEEEQEAKGELQR 1367
Cdd:TIGR02168 946 SEEYSLT--LEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaaieeYEELKERY--DFLTAQKEDLTEAKETLEE 1021
|
....*....
gi 1529987947 1368 ALSKANAEV 1376
Cdd:TIGR02168 1022 AIEEIDREA 1030
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
848-1429 |
7.57e-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: 77.47 E-value: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 848 LRSAATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNladAEDRCDLLIKTKIQLEAKV 927
Cdd:pfam15921 250 LKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTV 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 928 KELMERLEDeeemssnvlaKKRKLEDECAELKKD--IDDLEITLAKIEKEKHAIENkvKNLIEEMAALDETILKLTKEKK 1005
Cdd:pfam15921 327 SQLRSELRE----------AKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQLQKLLADLHKREKELS 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1006 ALQEAHQ-----------------QTLDDLQAEEDKVNALTKA-----KAKLEQQVDDLEG---SLEQEKKLRMDLERVK 1060
Cdd:pfam15921 395 LEKEQNKrlwdrdtgnsitidhlrRELDDRNMEVQRLEALLKAmksecQGQMERQMAAIQGkneSLEKVSSLTAQLESTK 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1061 ---RKLEGDL---KLSLES----VMDLENDKQQLEEKLKKKDFEMNELSTRIEdeqalvnqlqKKIKELQARTEELEEEL 1130
Cdd:pfam15921 475 emlRKVVEELtakKMTLESsertVSDLTASLQEKERAIEATNAEITKLRSRVD----------LKLQELQHLKNEGDHLR 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1131 EADRACRA-KVEKQRSD-----VARELEDLSERLEEAGGATSA--------QIEMNKKR-EAEFLKMRRDLEEAMLHH-E 1194
Cdd:pfam15921 545 NVQTECEAlKLQMAEKDkvieiLRQQIENMTQLVGQHGRTAGAmqvekaqlEKEINDRRlELQEFKILKDKKDAKIRElE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1195 ATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEADDLASTVEQLskgkatsEKMCRLYEDQMNEAKAKADEL 1274
Cdd:pfam15921 625 ARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDY-------EVLKRNFRNKSEEMETTTNKL 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1275 QRQLNEANT--QRARAQAESGE------------VSRKLEERESMVSQLQRAKNSFSQNVEELKKQLEEENKAKNALAHS 1340
Cdd:pfam15921 698 KMQLKSAQSelEQTRNTLKSMEgsdghamkvamgMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQE 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1341 LQSSRH-------DCDLLREQYEEEQEAKGELQRALSKANAEVAQWRtkyetDAIQRTEEleeakKKLVTRLQESEEIME 1413
Cdd:pfam15921 778 LSTVATeknkmagELEVLRSQERRLKEKVANMEVALDKASLQFAECQ-----DIIQRQEQ-----ESVRLKLQHTLDVKE 847
|
650
....*....|....*.
gi 1529987947 1414 ASNAKCSSLEKTKHRL 1429
Cdd:pfam15921 848 LQGPGYTSNSSMKPRL 863
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
842-1239 |
1.06e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 842 FKIKPLLRSAATEKELAALKVELAKLKEALEKSEIKRKELEE---------RQVSLIQEKNDLSLQLQAEQDNLADAEDR 912
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEElkkklkeleKRLEELEERHELYEEAKAKKEELERLKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 913 cdLLIKTKIQLEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKI--------EKEKHAIENK-- 982
Cdd:PRK03918 381 --LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEHRKELLEEyt 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 983 --VKNLIEEMAALDETILKLTKEKKALQEA---------HQQTLDDLQAEEDKVNALTkaKAKLEQQVDDLEGSLEQEKK 1051
Cdd:PRK03918 459 aeLKRIEKELKEIEEKERKLRKELRELEKVlkkeselikLKELAEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKLIK 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1052 LRMDLERVKRklegdlklSLESVMDLENDKQQLEEKLKKKDFEMNELSTRIEDEQ-ALVNQLQKKIKELQARTEELEEEL 1130
Cdd:PRK03918 537 LKGEIKSLKK--------ELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELK 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1131 EADRACRAKvEKQRSDVARELEDLSERLEEaggaTSAQIEMNKKREAEFLKMRRDLEEAMLHHEATTaaLRKKHADSVAE 1210
Cdd:PRK03918 609 DAEKELERE-EKELKKLEEELDKAFEELAE----TEKRLEELRKELEELEKKYSEEEYEELREEYLE--LSRELAGLRAE 681
|
410 420 430
....*....|....*....|....*....|....*
gi 1529987947 1211 LSEQIDSLQRVKQKLEK------ERSEAKMEADDL 1239
Cdd:PRK03918 682 LEELEKRREEIKKTLEKlkeeleEREKAKKELEKL 716
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
933-1542 |
1.63e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.26 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 933 RLEDEEEMSSNVLAKKRKLEDECAELKKDI---DDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALqE 1009
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIkrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-E 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1010 AHQQTLDDLQAEEDKVNaltKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEgDLKLSLESVMDLENDKQQLEEKLK 1089
Cdd:PRK03918 235 ELKEEIEELEKELESLE---GSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1090 KKDFEMNELSTRIEDEQALVNQLQKKIKELQarteeleeeleadracraKVEKQRSDVARELEDLSERLEEAGGATSAQI 1169
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLE------------------ELKKKLKELEKRLEELEERHELYEEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1170 EMNKkreaeflkmrrdleeamlhheattaaLRKKHAD-SVAELSEQIDSLQRVKQKLEKE-------RSEAKMEADDLAS 1241
Cdd:PRK03918 373 ELER--------------------------LKKRLTGlTPEKLEKELEELEKAKEEIEEEiskitarIGELKKEIKELKK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1242 TVEQLSKGKATSEKMCRLYEDQ-----MNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERE------SMVSQLQ 1310
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkELAEQLK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1311 RAKNSFSQ-NVEELKKQLEEENKAKNALAhslqSSRHDCDLLREQYEEEQEAKG---ELQRALSKANAEVAQWRTKYETD 1386
Cdd:PRK03918 507 ELEEKLKKyNLEELEKKAEEYEKLKEKLI----KLKGEIKSLKKELEKLEELKKklaELEKKLDELEEELAELLKELEEL 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1387 AIQRTEELEEakkklvtRLQESEEIMEASNaKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQ 1466
Cdd:PRK03918 583 GFESVEELEE-------RLKELEPFYNEYL-ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1529987947 1467 KYEEcqSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEItdltDQISQGAKTIHELEKMKKGLE 1542
Cdd:PRK03918 655 KYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL----EEREKAKKELEKLEKALERVE 724
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
838-1410 |
3.18e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.56 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 838 MKLFFKIKPLLRSAATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAedrcdllI 917
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA-------A 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 918 KTKIQlEAKVKELMERLEdeeemssnvlAKKRKLEDECAELKKDIDDLEitlaKIEKEKHAIENKVKnlIEEMAALDETI 997
Cdd:PTZ00121 1335 KKKAE-EAKKAAEAAKAE----------AEAAADEAEAAEEKAEAAEKK----KEEAKKKADAAKKK--AEEKKKADEAK 1397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 998 LKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAkleqqvDDLEGSLEQEKKlrmdLERVKRKLEGDLKlslesvmdL 1077
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKA------DEAKKKAEEAKK----ADEAKKKAEEAKK--------A 1459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1078 ENDKQQLEEKLKKKDFEMNELSTRIEDEqalvnqLQKKIKELQARteeleeeleADRACRAKVEKQRSDVARELE----- 1152
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADE------AKKKAEEAKKK---------ADEAKKAAEAKKKADEAKKAEeakka 1524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1153 DLSERLEEAGGATSAQIEMNKKREAEFLKMR--RDLEEAMLHHEATTAALRKKHADSVAELSEQIDSlQRVKQKLEKERS 1230
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE-ARIEEVMKLYEE 1603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1231 EAKMEADDLASTVEQLSKGkatsekmcrlyedqmnEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQ 1310
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKA----------------EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1311 RAKNSFSQNVEELKKQLEEENKAKNALAHSLQSSRhDCDLLREQYEEEQEAKGELQRALSKANAEVAQWRTKYETDAiQR 1390
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KK 1745
|
570 580
....*....|....*....|..
gi 1529987947 1391 TEEL--EEAKKKLVTRLQESEE 1410
Cdd:PTZ00121 1746 AEEAkkDEEEKKKIAHLKKEEE 1767
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
854-1695 |
4.00e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 75.01 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 854 EKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLslqlqaeqdnladaedrcDLLIKTKIQLEAKVKELMER 933
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKAL------------------EYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 934 LEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILK-LTKEKKALQEAHQ 1012
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEeLKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1013 QTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVK---RKLEGDLKLSLESVMDLENDKQQLEEKLK 1089
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEeelEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1090 KKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEeleadracrAKVEKQRSDVARELEDLSERLEEAGGATSAQI 1169
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL---------EILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1170 EMNKKREAEFLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEADDLASTVEQLSKG 1249
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1250 KATSEKMCRLYEDQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKQLEE 1329
Cdd:pfam02463 542 KVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKR 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1330 ENKAKNALAHSLQSSRHDCDLLREQYEEEQEAKGELQRALSKANAEVAQWRTK-YETDAIQRTEELEEAKKKLVTRLQES 1408
Cdd:pfam02463 622 AKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKElLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1409 EEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEEcQSELEISQKESRGLSTE 1488
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKE-EEKSELSLKEKELAEER 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1489 LFKLKNSYEETLDHLEtiKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEmEKTEIQAALEEAEGTLEHEESKTLR 1568
Cdd:pfam02463 781 EKTEKLKVEEEKEEKL--KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKE-EELEELALELKEEQKLEKLAEEELE 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1569 IQLELNQMKSDVDRKLAEKDEELDNLRRKHQRSLESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQLNHANRLASESQ 1648
Cdd:pfam02463 858 RLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEP 937
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 1529987947 1649 KLLRNLQIQIKDVQLELDETV-HQNEELKEQVAVTERRNNLLAAEVEE 1695
Cdd:pfam02463 938 EELLLEEADEKEKEENNKEEEeERNKRLLLAKEELGKVNLMAIEEFEE 985
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
851-1382 |
4.03e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.10 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 851 AATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLiqekNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEL 930
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEI----EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 931 MERLEDEEEMssnvlakkRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALQEa 1010
Cdd:PRK03918 279 EEKVKELKEL--------KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1011 hqqTLDDLQAEEDKVNALTKAKAKLEQqvddlegsLEQEKKLRMDL--ERVKRKLEgdlklslesvmDLENDKQQLEEKL 1088
Cdd:PRK03918 350 ---LEKRLEELEERHELYEEAKAKKEE--------LERLKKRLTGLtpEKLEKELE-----------ELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1089 KKKDFEMNELSTRIEDEQALVNQLQK--------------------------KIKELQARTEELEEELEADRACRAKVEK 1142
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelleeytaELKRIEKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1143 QRS---------DVARELEDLSERLEEAGgatsaqIEMNKKREAEFLKMRRDLEEamLHHEATTAalrKKHADSVAELSE 1213
Cdd:PRK03918 488 VLKkeseliklkELAEQLKELEEKLKKYN------LEELEKKAEEYEKLKEKLIK--LKGEIKSL---KKELEKLEELKK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1214 QIDSLQRVKQKLEKERSEAKMEADDLA-STVEQLSKGKATSEKMCRLYedqmNEAKAKADELQRQLNEANTQRARAQAES 1292
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEY----LELKDAEKELEREEKELKKLEEELDKAF 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1293 GEVSRKLEERESMVSQLQRAKNSFSQ----NVEELKKQLEEENKAKNALAHSLQSSRH----DCDLLREQYEEEQEAKGE 1364
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYSEeeyeELREEYLELSRELAGLRAELEELEKRREeikkTLEKLKEELEEREKAKKE 712
|
570
....*....|....*...
gi 1529987947 1365 LQRaLSKANAEVAQWRTK 1382
Cdd:PRK03918 713 LEK-LEKALERVEELREK 729
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
863-1685 |
4.07e-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: 75.08 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 863 ELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLAdaedRCDLLIKTkIQLEAKVKELMERLEDEEEMSS 942
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIR----ARDSLIQS-LATRLELDGFERGPFSERQIKN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 943 NVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIE----EMAALDETILKLTKEKKALQEAHQQTLDDL 1018
Cdd:TIGR00606 395 FHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRtielKKEILEKKQEELKFVIKELQQLEGSSDRIL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1019 QAEEDKVNALTK-AKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDL------KLSLESVMDLENDKQQLEEKLKKK 1091
Cdd:TIGR00606 475 ELDQELRKAERElSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMeqlnhhTTTRTQMEMLTKDKMDKDEQIRKI 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1092 DFE-MNELSTRIED------EQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSERLEEAGGA 1164
Cdd:TIGR00606 555 KSRhSDELTSLLGYfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1165 TSAQIEMNKKREaEFLKMRRDLeeamlhheATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEADDLastve 1244
Cdd:TIGR00606 635 QDEESDLERLKE-EIEKSSKQR--------AMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDL----- 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1245 qlskgkatsEKMCRLYEDQMNEAKAKADELQRQLNE----ANTQRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNV 1320
Cdd:TIGR00606 701 ---------QSKLRLAPDKLKSTESELKKKEKRRDEmlglAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1321 EELKKQLEEENKAKNALAhslqssrhDCDLLREQYEEEQEAKGELQRALSKANAeVAQWRTKYETDaiQRTEELEEAKKK 1400
Cdd:TIGR00606 772 TLLGTIMPEEESAKVCLT--------DVTIMERFQMELKDVERKIAQQAAKLQG-SDLDRTVQQVN--QEKQEKQHELDT 840
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1401 LVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEEcQSELEISQK 1480
Cdd:TIGR00606 841 VVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ-DSPLETFLE 919
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1481 ESRGLSTELFKLKN-SYEETLDHLETIKRENKNLQEEITDLTDQISQGAktihelEKMKKGLEMEKTEIQAALEEAEgtl 1559
Cdd:TIGR00606 920 KDQQEKEELISSKEtSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK------DDYLKQKETELNTVNAQLEECE--- 990
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1560 EHEEsktlRIQLELNQMKSDVDRKLAEKDEELDNL-RRKHQRSLESMQATLDAEAKSRNEAVRLKKKMEgdLNEMEVQLN 1638
Cdd:TIGR00606 991 KHQE----KINEDMRLMRQDIDTQKIQERWLQDNLtLRKRENELKEVEEELKQHLKEMGQMQVLQMKQE--HQKLEENID 1064
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 1529987947 1639 HANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERR 1685
Cdd:TIGR00606 1065 LIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMR 1111
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
855-1778 |
4.86e-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: 75.08 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 855 KELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKnDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELMERL 934
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 935 EDEEEMSSNVLAKKRKLEDECAELKKDIDdleitlakiekekHAIENKVKNLIEEMAALDETILKLTKEKKALQEAH--- 1011
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKtel 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1012 --QQTLDDLQAEEDKVNALTKAKAKLEQQ----VDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDLENDKQQLE 1085
Cdd:TIGR00606 346 lvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1086 EKLKKKDFEMNELSTRIEDEQAL----VNQLQKKIKELQARTEELEEELEADRACR------AKVEKQRSDVARELEDLS 1155
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEIlekkQEELKFVIKELQQLEGSSDRILELDQELRkaerelSKAEKNSLTETLKKEVKS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1156 ERLEEAGGATS----AQIEMNKKREAEFLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSE 1231
Cdd:TIGR00606 506 LQNEKADLDRKlrklDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1232 AKMEADDLAstveQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNEANTQRARaQAESGEVSRKLEERESMVSQLQR 1311
Cdd:TIGR00606 586 INQTRDRLA----KLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE-ESDLERLKEEIEKSSKQRAMLAG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1312 AKNSFSQNVEELKKQLE----------EENKAKNALAHSLQSSRHDCDLLREQYEEE---QEAKGELQRALSKANAEVAQ 1378
Cdd:TIGR00606 661 ATAVYSQFITQLTDENQsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESElkkKEKRRDEMLGLAPGRQSIID 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1379 WRTKYETDAIQRTEELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTK------HRLQTEIEDLIIDLERANAAAAALD- 1451
Cdd:TIGR00606 741 LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLtdvtimERFQMELKDVERKIAQQAAKLQGSDl 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1452 --------KKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKN---SYEETLDHLETIKRENKNLQEEITDL 1520
Cdd:TIGR00606 821 drtvqqvnQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEEQLVELSTEVQSL 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1521 TDQISQGAKTIHELEKMKKGLEMEKTEIQAAleeaegtlEHEESKtlRIQLELNQMKSDVDRKLAekdeeldnlrrkHQR 1600
Cdd:TIGR00606 901 IREIKDAKEQDSPLETFLEKDQQEKEELISS--------KETSNK--KAQDKVNDIKEKVKNIHG------------YMK 958
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1601 SLESmqatldaeaKSRNEAVRLKKKMEGDLNEMEVQLNhanrlasESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVA 1680
Cdd:TIGR00606 959 DIEN---------KIQDGKDDYLKQKETELNTVNAQLE-------ECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLT 1022
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1681 VTERRNNLLAAEvEELRALLEQNDRARKL---AEHELLEasERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDavQECR 1757
Cdd:TIGR00606 1023 LRKRENELKEVE-EELKQHLKEMGQMQVLqmkQEHQKLE--ENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE--PQFR 1097
|
970 980
....*....|....*....|.
gi 1529987947 1758 NAEEKAKKAITDAAMMAEELK 1778
Cdd:TIGR00606 1098 DAEEKYREMMIVMRTTELVNK 1118
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1260-1922 |
7.00e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 74.38 E-value: 7.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1260 YEDQMNEAKAKADELQRQLNEANTQRARaqaesgevsRKLEERESMVSqLQRAKNSFSQNVEELKKQLEEENKAKNALAH 1339
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEK---------QKFYLRQSVID-LQTKLQEMQMERDAMADIRRRESQSQEDLRN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1340 SLQSSRHdcdllreqyeEEQEAKGELQRALSKANAEVAQWRTKyetdAIQRTEELEEAKKKLVTRLQES-EEIMEASNAK 1418
Cdd:pfam15921 146 QLQNTVH----------ELEAAKCLKEDMLEDSNTQIEQLRKM----MLSHEGVLQEIRSILVDFEEASgKKIYEHDSMS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1419 C-------SSLEKTKHRLQTEIEDL---IIDLERANAAAAAldKKQRNFDKVLAEWKQKYEECQSELEIsqkESRGLSTE 1488
Cdd:pfam15921 212 TmhfrslgSAISKILRELDTEISYLkgrIFPVEDQLEALKS--ESQNKIELLLQQHQDRIEQLISEHEV---EITGLTEK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1489 LFKLKNSYEETLDHLETIKRENKN----LQEEITDLTDQISQGAKTIHELEKMKKGlEMEKTEIQAALEEAEGTleheES 1564
Cdd:pfam15921 287 ASSARSQANSIQSQLEIIQEQARNqnsmYMRQLSDLESTVSQLRSELREAKRMYED-KIEELEKQLVLANSELT----EA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1565 KTLRIQLelNQMKSDVDRKLAEKDEELDnlRRKHQRSLESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQLNHA--NR 1642
Cdd:pfam15921 362 RTERDQF--SQESGNLDDQLQKLLADLH--KREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEAllKA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1643 LASESQ-KLLRNLQ-IQIKDVQLE-LDETVHQNEELKEQV-----AVTERRNNLLAAE--VEELRALLEQNDRARKLAEH 1712
Cdd:pfam15921 438 MKSECQgQMERQMAaIQGKNESLEkVSSLTAQLESTKEMLrkvveELTAKKMTLESSErtVSDLTASLQEKERAIEATNA 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1713 ELLEASERVNLLHSQNTGLINQKKKLEN------DLSMLSNEVDDAVQECRNAEEKakkaitdaamMAEELKKEQDTSAH 1786
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEGDHLRNvqteceALKLQMAEKDKVIEILRQQIEN----------MTQLVGQHGRTAGA 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1787 LERMKKNMEQTIKDLQMRLDEAEQIALKGGKKqVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELsyqAEEDK 1866
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLELQEFKILKDKKDAK-IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL---LNEVK 663
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1529987947 1867 KNLVRLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADTAE 1922
Cdd:pfam15921 664 TSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
843-1522 |
7.28e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.33 E-value: 7.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 843 KIKPLL--RSAATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTK 920
Cdd:TIGR02169 280 KIKDLGeeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 921 IQLEAKVKELMERLEDEE-------EMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAAL 993
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDkefaetrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 994 DETILKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQ-EKKLRMDLERVK--RKLEGDLKLS 1070
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEaEAQARASEERVRggRAVEEVLKAS 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1071 LESVMDLENDKQQLEEKLKkkdfemnelstrIEDEQALVNQLQKKIKELQARTEELEEELEADRACRA------KVEKQR 1144
Cdd:TIGR02169 520 IQGVHGTVAQLGSVGERYA------------TAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRAtflplnKMRDER 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1145 SDVARELED----------------------------LSERLEEA------------------------GGATSAQ--IE 1170
Cdd:TIGR02169 588 RDLSILSEDgvigfavdlvefdpkyepafkyvfgdtlVVEDIEAArrlmgkyrmvtlegelfeksgamtGGSRAPRggIL 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1171 MNKKREAEFLKMRRDLEEamLHHEATTAALRKKHADS-VAELSEQIDSLQRVKQKLEKERSEAKMEADDLASTVEQL-SK 1248
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEG--LKRELSSLQSELRRIENrLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELeED 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1249 GKATSEKMCRlYEDQMNEAKAKADELQRQLNE-----ANTQRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEEL 1323
Cdd:TIGR02169 746 LSSLEQEIEN-VKSELKELEARIEELEEDLHKleealNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1324 KKQLEEENKAKNalahSLQSSRHDCDLLREQYEEEQEA----KGELQRALSKANAEVAQWRTKYETDAIQRtEELEEAKK 1399
Cdd:TIGR02169 825 TLEKEYLEKEIQ----ELQEQRIDLKEQIKSIEKEIENlngkKEELEEELEELEAALRDLESRLGDLKKER-DELEAQLR 899
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1400 KLVTRLQESEEIMEASNAKCSSLEKTKHRLQ---TEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWK----------Q 1466
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEeelSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRalepvnmlaiQ 979
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1529987947 1467 KYEECQSEL-EISQKESRglsteLFKLKNSYEETLDHLETIKRE---------NKNLQEEITDLTD 1522
Cdd:TIGR02169 980 EYEEVLKRLdELKEKRAK-----LEEERKAILERIEEYEKKKREvfmeafeaiNENFNEIFAELSG 1040
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
857-1229 |
1.33e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.41 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 857 LAALKVELAKLKEALEKSEIKRKELEERQvsliqekndlsLQLQAEQDNLADAEDRCDLLIKTKiQLEAKVKELMERLED 936
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAEL-----------DALQERREALQRLAEYSWDEIDVA-SAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 937 EEEmSSNVLakkRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALQEAHqqtLD 1016
Cdd:COG4913 680 LDA-SSDDL---AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LE 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1017 DLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQ-EKKLRMDLERVKRKLEGDLKLSLESVMDLEndkqqleeklkkkDFEm 1095
Cdd:COG4913 753 ERFAAALGDAVERELRENLEERIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLP-------------EYL- 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1096 nELSTRIEDEqALVnQLQKKIKELQARTEELEEELEAdracrAKVEKQRSDVARELEDLSERLEEA--GGATSAQIEMNK 1173
Cdd:COG4913 819 -ALLDRLEED-GLP-EYEERFKELLNENSIEFVADLL-----SKLRRAIREIKERIDPLNDSLKRIpfGPGRYLRLEARP 890
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1529987947 1174 KREAEFLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKER 1229
Cdd:COG4913 891 RPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRSEEEESDRRWRAR 946
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1253-1912 |
2.01e-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: 72.45 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1253 SEKMCRLYEDQMNEAkakaDELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKQLEEENK 1332
Cdd:pfam05483 73 SEGLSRLYSKLYKEA----EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1333 AKNAlahslqsSRHDCDLLRE--------------QYEEEQEAKGELQRALSKANAEVAQWRTKYETDAIQRTEELEEAK 1398
Cdd:pfam05483 149 ENNA-------TRHLCNLLKEtcarsaektkkyeyEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1399 KKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELEis 1478
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELE-- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1479 qkesrglstelfKLKNSYEETLDHLETIKRENKNLQEEITDLTDQisqGAKTIHELEKMKKGLEMEKTEIQAALEEAEGT 1558
Cdd:pfam05483 300 ------------DIKMSLQRSMSTQKALEEDLQIATKTICQLTEE---KEAQMEELNKAKAAHSFVVTEFEATTCSLEEL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1559 LEHEESKTLRIQLELNQMKSDVDRKLAEKdEELDNLRRKHQRSLESMQATLDAEAKSRNEavrlKKKMEGDLNEMEVQLN 1638
Cdd:pfam05483 365 LRTEQQRLEKNEDQLKIITMELQKKSSEL-EEMTKFKNNKEVELEELKKILAEDEKLLDE----KKQFEKIAEELKGKEQ 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1639 HANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELraLLEQndraRKLAEhellEAS 1718
Cdd:pfam05483 440 ELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL--LLEN----KELTQ----EAS 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1719 ERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTI 1798
Cdd:pfam05483 510 DMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1799 KDLQMRLDEAeqialkggKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEEDKKnlvRLQDLIDK 1878
Cdd:pfam05483 590 KILENKCNNL--------KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ---KFEEIIDN 658
|
650 660 670
....*....|....*....|....*....|....*..
gi 1529987947 1879 LQVKVKSYKRQTE---EAEEQANTNLSKYRKLQHELD 1912
Cdd:pfam05483 659 YQKEIEDKKISEEkllEEVEKAKAIADEAVKLQKEID 695
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
912-1680 |
5.47e-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: 71.54 E-value: 5.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 912 RCDLLIKTKIQLEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDI----DDLEITLAKIEKEKHAIENKVKNLI 987
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 988 EEMAALDETILKLTKEKKALQEAH--QQTLDDLQAEEDKVNALTKAKAKLEQQVDdlegslEQEKKLRMdLERVKRKLEG 1065
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAVLEETQERIN------RARKAAPL-AAHIKAVTQI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1066 DLKlsLESVMDLENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELqaRTEELEEELEADRACRAKVEKQR- 1144
Cdd:TIGR00618 306 EQQ--AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHI--RDAHEVATSIREISCQQHTLTQHi 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1145 SDVARELEDLSERLEEAGGATSaqIEMNKKREAEFLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQK 1224
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCKELD--ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKI 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1225 LEKERSEAKMEADDLASTVEQLSKGKATSEKmcrLYEDQMNEAKAKADELQRQLNEANtQRARAQAESGEVSRKLEERES 1304
Cdd:TIGR00618 460 HLQESAQSLKEREQQLQTKEQIHLQETRKKA---VVLARLLELQEEPCPLCGSCIHPN-PARQDIDNPGPLTRRMQRGEQ 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1305 MVSQLQRaknsfsqnveelkkqleeenkaknalahSLQSSRHDCDLLREQYEEEQEAKGELQRALSKanaeVAQWRTKYe 1384
Cdd:TIGR00618 536 TYAQLET----------------------------SEEDVYHQLTSERKQRASLKEQMQEIQQSFSI----LTQCDNRS- 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1385 tdaiqrTEELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLErANAAAAALDKKQRNFDKVLAEW 1464
Cdd:TIGR00618 583 ------KEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH-LQQCSQELALKLTALHALQLTL 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1465 KQKYEECQSELEISQKESRGLSTE--LFKLKNSYEETLDHLETIKRENKNLQEEITdltdQISQGAKTIHELEKMKKGLE 1542
Cdd:TIGR00618 656 TQERVREHALSIRVLPKELLASRQlaLQKMQSEKEQLTYWKEMLAQCQTLLRELET----HIEEYDREFNEIENASSSLG 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1543 MEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDVDRKLAEKDEELDNLRRKHQRSLESMQaTLDAEAKSRNEAVRL 1622
Cdd:TIGR00618 732 SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLRE-EDTHLLKTLEAEIGQ 810
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1623 KKKMEGDLNEMEVQLNhANRLASESQKLLRN--LQIQIKDVQLELDETVHQNEELKEQVA 1680
Cdd:TIGR00618 811 EIPSDEDILNLQCETL-VQEEEQFLSRLEEKsaTLGEITHQLLKYEECSKQLAQLTQEQA 869
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1392-1903 |
6.03e-12 |
|
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: 70.82 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1392 EELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDK---VLAEWKQKY 1468
Cdd:TIGR04523 134 KENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELllsNLKKKIQKN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1469 EECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEI 1548
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1549 QAALEEAEGTLEHEESKTLRIQLELNQmksdvdrklaEKDEELDNLRRKHQRSLESMQATLDAEAKSRNEAVRLKKKMEG 1628
Cdd:TIGR04523 294 KSEISDLNNQKEQDWNKELKSELKNQE----------KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1629 DLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQNDRARK 1708
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1709 LAEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDAVQECRNAE---EKAKKAITDAAMMAEELKKEQDTSA 1785
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEkelKKLNEEKKELEEKVKDLTKKISSLK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1786 H----LERMKKNMEQTIKDLQMRLDEAEQIALKGG-KKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKE--- 1857
Cdd:TIGR04523 524 EkiekLESEKKEKESKISDLEDELNKDDFELKKENlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDlik 603
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1529987947 1858 -----------LSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSK 1903
Cdd:TIGR04523 604 eieekekkissLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
927-1533 |
6.93e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.10 E-value: 6.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 927 VKELMERLEDEEEMSSNVLAKKRKLEDECaELKKDIDDLEITLAKIEKEKHAIEnkVKNLIEEMAALDETILKLTKEKKA 1006
Cdd:COG4913 230 LVEHFDDLERAHEALEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1007 LQEA---HQQTLDDLQAEEDKVNAL-----TKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLEsvmDLE 1078
Cdd:COG4913 307 LEAElerLEARLDALREELDELEAQirgngGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE---EFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1079 NDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARteeleeeleadracRAKVEKQRSDVARELEDLSERL 1158
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE--------------IASLERRKSNIPARLLALRDAL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1159 EEAGGATSAQIemnkKREAEFLKMRRDLE------EAMLHHEATTAALRKKHADSVAELSEQIDSLQRVK-QKLEKERSE 1231
Cdd:COG4913 450 AEALGLDEAEL----PFVGELIEVRPEEErwrgaiERVLGGFALTLLVPPEHYAAALRWVNRLHLRGRLVyERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1232 AKMEADDLASTVEQLS-KGKATSEKMCRLYEDQMNEAK-AKADELQRQ--------LNEANTQRARAQAESGEVSR---- 1297
Cdd:COG4913 526 PERPRLDPDSLAGKLDfKPHPFRAWLEAELGRRFDYVCvDSPEELRRHpraitragQVKGNGTRHEKDDRRRIRSRyvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1298 -----KLEERESMVSQLQRAKNSFSQNVEELKKQLEEENKAKNALAHSLQSSRHDCDLlrEQYEEEQEAKGELQRALSKA 1372
Cdd:COG4913 606 fdnraKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV--ASAEREIAELEAELERLDAS 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1373 NAEVaqwrtkyetdaiqrtEELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAA--- 1449
Cdd:COG4913 684 SDDL---------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelr 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1450 ---------------LDKKQRNFDKVLAEWKQKYEECQSELEISQKE--------SRGLSTELfklkNSYEETLDHLETI 1506
Cdd:COG4913 749 alleerfaaalgdavERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaeTADLDADL----ESLPEYLALLDRL 824
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1529987947 1507 KRE-------------NKNLQEEITDLTDQISQGAKTIHE 1533
Cdd:COG4913 825 EEDglpeyeerfkellNENSIEFVADLLSKLRRAIREIKE 864
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
855-1263 |
1.10e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.80 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 855 KELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQD--NLADAEDRCDLLIKTKIQLEAKVKELME 932
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 933 RLEDEEEMSSNVLAKKRKLEDECAEL----KKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALQ 1008
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1009 EAHQ------------------QTLDDLQAEEDKVNA---------------LTKAKAKLEQQVDDLEGSLEQEKKLRMD 1055
Cdd:COG4717 241 LEERlkearlllliaaallallGLGGSLLSLILTIAGvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1056 LERVKRKLEGDLKLSLESVMDLENDKQQLEEKLKKKdfemnelstRIEDEQALVNQLQKKIKELQARTEELEEELEADRA 1135
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREA---------EELEEELQLEELEQEIAALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1136 CRAKvekQRSDVARELEDLSERLEEAGGATSAQIEMNKKREAEflKMRRDLEEAMLHHEATTAALRKKHADSVAELS--E 1213
Cdd:COG4717 392 EQAE---EYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAELEqlE 466
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1214 QIDSLQRVKQKLEKERSEAKMEADDLAStveqLSKGKATSEKMCRLYEDQ 1263
Cdd:COG4717 467 EDGELAELLQELEELKAELRELAEEWAA----LKLALELLEEAREEYREE 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1496-1941 |
2.03e-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: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1496 YEETLDHLETIKRENKNLqEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLElnq 1575
Cdd:COG4913 237 LERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELE--- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1576 mksDVDRKLAEKDEELDNLRRKHQRS----LESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQLNHA----NRLASES 1647
Cdd:COG4913 313 ---RLEARLDALREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeefAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1648 QKLLRNLQIQIKDVQLELDETV-------HQNEELKEQVAVTERRNNLLAAEVEELRALLEQN-----DRARKLAehELL 1715
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEaalrdlrRELRELEAEIASLERRKSNIPARLLALRDALAEAlgldeAELPFVG--ELI 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1716 E----------ASERVnlLHSQNTGL-------------INQKK-----------------------------KLENDLS 1743
Cdd:COG4913 468 EvrpeeerwrgAIERV--LGGFALTLlvppehyaaalrwVNRLHlrgrlvyervrtglpdperprldpdslagKLDFKPH 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1744 MLSNEVDDAVQE------CRNAEE--KAKKAITDAAMMAEELKK-EQDTSAHLER---MKKNMEQTIKDLQMRLDEAEQi 1811
Cdd:COG4913 546 PFRAWLEAELGRrfdyvcVDSPEElrRHPRAITRAGQVKGNGTRhEKDDRRRIRSryvLGFDNRAKLAALEAELAELEE- 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1812 alkggkkQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQA-----EEDKKNLVRLQDLIDKLQVKVKSY 1886
Cdd:COG4913 625 -------ELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEReiaelEAELERLDASSDDLAALEEQLEEL 697
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 1887 KRQTEEAEEQANTNLSKYRKLQHELDDAEERADTAETQVNKLRVRTRDQVSKLAE 1941
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
923-1440 |
2.92e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 923 LEAKVKELMERLEDEEEmssnvlakkrklEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETIlkltk 1002
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIE------------EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVL----- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1003 ekkalqEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLS-------LESVM 1075
Cdd:PRK02224 244 ------EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDdadaeavEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1076 DLENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLS 1155
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1156 ERLEEA----GGATS------AQIEMNKKREAEFLKMRRDLEEAMLHHEATTAALR----------KKHADSVAELSEQI 1215
Cdd:PRK02224 398 ERFGDApvdlGNAEDfleelrEERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegSPHVETIEEDRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1216 DSLQRVKQKLEKERS--EAKME-ADDLASTVEQLSKGKATSEKMCRLYEDQ---MNEAKAKADELQRQLN----EANTQR 1285
Cdd:PRK02224 478 EELEAELEDLEEEVEevEERLErAEDLVEAEDRIERLEERREDLEELIAERretIEEKRERAEELRERAAeleaEAEEKR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1286 ARAQAESGEVSRKLEERESMVSQLQRAKNSFSQ--NVEELKKQLEEENKAKNALAHSLQSSRHDCDLLREQYEEEQEAKG 1363
Cdd:PRK02224 558 EAAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKR 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1364 ELQRALSKANAEVAQWR----TKYETDAIQRTEELEEAKKKL----------VTRLQESEEIMEASNAKCSSLEkTKHRL 1429
Cdd:PRK02224 638 ELEAEFDEARIEEAREDkeraEEYLEQVEEKLDELREERDDLqaeigaveneLEELEELRERREALENRVEALE-ALYDE 716
|
570
....*....|.
gi 1529987947 1430 QTEIEDLIIDL 1440
Cdd:PRK02224 717 AEELESMYGDL 727
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1475-1938 |
2.92e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1475 LEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEE 1554
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1555 AEGtLEHEESKTLRIQLELNQMKSDVDRKLAEKDEELDNLRRKHQRSLEsmqatLDAEAKSRNEAVRLKKKMEGDLNEME 1634
Cdd:PRK03918 240 IEE-LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-----LKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1635 VQLNHANRLASESQKLLRNLQiqikDVQLELDETVHQNEELKEQVAVTERRNNLLaaevEELRALLEQNDRARK-LAEHE 1713
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEKRLEELEERHELY----EEAKAKKEELERLKKrLTGLT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1714 LLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVddavQECRNAEEKAKKAITDAAMMAEELKKEqdtsaHLERMKKN 1793
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISKITARIGELKKEI----KELKKAIEELKKAKGKCPVCGRELTEE-----HRKELLEE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1794 MEQTIKDLQMRLDEAEqialkggkKQVQKLEARVKELETELDAEQKKSQEYQ--KVVRKYERRIKELSYQ-AEEDKKNLV 1870
Cdd:PRK03918 457 YTAELKRIEKELKEIE--------EKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEeLEKKAEEYE 528
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1529987947 1871 RLQDLIDKLQVKVKSYKRQTEEAEEQANtnlsKYRKLQHELDDAEERADTAETQVNKLRVRTRDQVSK 1938
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKK----KLAELEKKLDELEEELAELLKELEELGFESVEELEE 592
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
980-1808 |
4.41e-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: 68.12 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 980 ENKVKNLIEEMAALDETILKLTKEKKALQeahqqtlDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERV 1059
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLD-------KNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1060 KRKLEGDLKLSLESVMDLENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELqarteeleeeleadracrak 1139
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDL-------------------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1140 vEKQRSDVARELEDLSERLEeaggatsaqiemNKKREAEFLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQ 1219
Cdd:TIGR04523 165 -KKQKEELENELNLLEKEKL------------NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1220 RVKQKLEKERSEAKMEaddLASTVEQLSKGKATSEKMCRLYED---QMNEAKAKADELQRQLNEANTQ--RARAQAESGE 1294
Cdd:TIGR04523 232 DNIEKKQQEINEKTTE---ISNTQTQLNQLKDEQNKIKKQLSEkqkELEQNNKKIKELEKQLNQLKSEisDLNNQKEQDW 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1295 VSRKLEERESMVSQLQRAKNSFSQNveelkkqleeeNKAKNALAHSLQSSRHDCDLLREQYEEEQEAKGELQRALSKANA 1374
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQN-----------NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1375 EVAQWRtkyetdaiQRTEELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQ 1454
Cdd:TIGR04523 378 ENQSYK--------QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1455 RNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHEL 1534
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1535 EKmkkglemEKTEIqaaleeaegtleheESKTLRIQLELNQMKSDVDRKLAEKdeELDNLrrkhQRSLESMQATLDAeak 1614
Cdd:TIGR04523 530 ES-------EKKEK--------------ESKISDLEDELNKDDFELKKENLEK--EIDEK----NKEIEELKQTQKS--- 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1615 srneavrLKKKMEgdlnemevqlnhanrlasESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVE 1694
Cdd:TIGR04523 580 -------LKKKQE------------------EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK 634
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1695 ELRALLEQNDRARKLAEHELLEASERVNllhsqntGLINQKKKLENDLSMLSNEVDDAVQECRNAEEKA---KKAITDAA 1771
Cdd:TIGR04523 635 NIKSKKNKLKQEVKQIKETIKEIRNKWP-------EIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYitrMIRIKDLP 707
|
810 820 830
....*....|....*....|....*....|....*..
gi 1529987947 1772 MMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEA 1808
Cdd:TIGR04523 708 KLEEKYKEIEKELKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
847-1554 |
6.35e-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: 67.69 E-value: 6.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 847 LLRSAATEKELaalkveLAKLkEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDnlaDAEDRCDLLIKTKIQLEAK 926
Cdd:TIGR00618 158 LKAKSKEKKEL------LMNL-FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTL---CTPCMPDTYHERKQVLEKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 927 VKELMERLEDEEEmSSNVLAKKR-------KLEDECAELKKDIDDLEITLAKIEKEKHAIE--NKVKNLIEEMAALDE-- 995
Cdd:TIGR00618 228 LKHLREALQQTQQ-SHAYLTQKReaqeeqlKKQQLLKQLRARIEELRAQEAVLEETQERINraRKAAPLAAHIKAVTQie 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 996 ----TILKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSl 1071
Cdd:TIGR00618 307 qqaqRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQ- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1072 esvMDLENDKQQLEEKLKKKDFEMNELST---RIEDEQALVNQLQKKIKELQARTEELEEELEADrACRAKVEKQRSDVA 1148
Cdd:TIGR00618 386 ---QQKTTLTQKLQSLCKELDILQREQATidtRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI-TCTAQCEKLEKIHL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1149 REL--------------EDLSERLEEAGGATSAQIEMNKKREAEFLKMRRDLEEA-------------MLHHEATTAALR 1201
Cdd:TIGR00618 462 QESaqslkereqqlqtkEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPArqdidnpgpltrrMQRGEQTYAQLE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1202 KKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEADDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNEA 1281
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1282 NTQRARAQ--AESGEVSRKLEERESMVSQLQraknsfsqnveelkkqleeENKAKNALAHSLQSSRHDCDLLREQYEEEQ 1359
Cdd:TIGR00618 622 QPEQDLQDvrLHLQQCSQELALKLTALHALQ-------------------LTLTQERVREHALSIRVLPKELLASRQLAL 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1360 EAKGELQRALSKANAEVAQWRTKyetdaiqrteeLEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLiiD 1439
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMLAQCQTL-----------LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKEL--M 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1440 LERANAAAAALDKKQRNFDKVLAEWK--QKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKR-ENKNLQEE 1516
Cdd:TIGR00618 750 HQARTVLKARTEAHFNNNEEVTAALQtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQE 829
|
730 740 750
....*....|....*....|....*....|....*...
gi 1529987947 1517 ITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEE 1554
Cdd:TIGR00618 830 EEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQE 867
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
851-1280 |
1.10e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.99 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 851 AATEKELAALKVELAKLKEALEKSEIKRKE--------------LEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLL 916
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDllaeaglddadaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 917 IKTKIQLEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDET 996
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 997 ILKLT----------KEKKALQEA--------------HQQTLDDlqaEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKL 1052
Cdd:PRK02224 428 EAELEatlrtarervEEAEALLEAgkcpecgqpvegspHVETIEE---DRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1053 RmDLERVKRKLEGDLKLSLESVMDLENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEA 1132
Cdd:PRK02224 505 V-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1133 DRACRAKVEKQRSDVArELEDLSERLEEAGGATSAQIEMNKKRE---AEFLKMRRDLEEAmlHHEATTAALRKKHA---- 1205
Cdd:PRK02224 584 LKERIESLERIRTLLA-AIADAEDEIERLREKREALAELNDERRerlAEKRERKRELEAE--FDEARIEEAREDKEraee 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1206 ------DSVAELSEQIDSLQR----VKQKLEkERSEAKMEADDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAK-ADEL 1274
Cdd:PRK02224 661 yleqveEKLDELREERDDLQAeigaVENELE-ELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRnVETL 739
|
....*.
gi 1529987947 1275 QRQLNE 1280
Cdd:PRK02224 740 ERMLNE 745
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
922-1121 |
1.68e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.17 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 922 QLEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLT 1001
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1002 KEKK----ALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDL 1077
Cdd:COG4942 104 EELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1529987947 1078 ENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQA 1121
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
854-1551 |
1.81e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 66.53 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 854 EKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRcdlliktkIQLEAKVKELMER 933
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESER--------LSSAAKLKEEELE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 934 LEDEEEMSSNVLakkrkledecAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALQEAHQQ 1013
Cdd:pfam02463 399 LKSEEEKEAQLL----------LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1014 TLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVmDLENDKQQLEEKLKKKDF 1093
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHG-RLGDLGVAVENYKVAIST 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1094 EMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSERLEEAGGATSAQIEMNK 1173
Cdd:pfam02463 548 AVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEG 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1174 KREAEFLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERsEAKMEADDLASTVEQLSKGKATS 1253
Cdd:pfam02463 628 ILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQE-KAESELAKEEILRRQLEIKKKEQ 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1254 EKMCRLYEDQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKQLEEENKA 1333
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKL 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1334 KNALAHSLQSSRHDcDLLREQYEEEQEAKGELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQESEEIME 1413
Cdd:pfam02463 787 KVEEEKEEKLKAQE-EELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITK 865
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1414 ASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLK 1493
Cdd:pfam02463 866 EELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEA 945
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1529987947 1494 NSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAA 1551
Cdd:pfam02463 946 DEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1262-1745 |
2.00e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1262 DQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQnveelkkqleeenkaknaLAHSL 1341
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED------------------LRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1342 QSSRHDCDLLREQYEEEQEAKGELQRALSKANAEVAQWRTKYETDAiQRTEELEEAKKKLVTRLQESEEIMEASNAKCSS 1421
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVE-ARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1422 LEKTKHRLQTEIEDLiidleranaaaaalDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLD 1501
Cdd:PRK02224 347 LREDADDLEERAEEL--------------REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1502 HLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKK-------GLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELN 1574
Cdd:PRK02224 413 FLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1575 QMKSDVDR------------KLAEKDEELDNLRRKHQRSLESMQ----------ATLDAEAKSRNEAVRLK--------- 1623
Cdd:PRK02224 493 EVEERLERaedlveaedrieRLEERREDLEELIAERRETIEEKReraeelreraAELEAEAEEKREAAAEAeeeaeeare 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1624 --KKMEGDLNEMEVQLNHANRLAsESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLE 1701
Cdd:PRK02224 573 evAELNSKLAELKERIESLERIR-TLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEA 651
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1529987947 1702 QNDRARklAEHELLEASERVNLLHSQNTGLINQKKKLENDLSML 1745
Cdd:PRK02224 652 REDKER--AEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL 693
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1350-1696 |
2.13e-10 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 65.30 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1350 LLREQYEEEQEAKGELQRALSKANAEVAQWRTKYETDA----IQRTE---ELEEAKKKLVTRLQESEEIM---------- 1412
Cdd:pfam07888 31 LLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDReqweRQRRElesRVAELKEELRQSREKHEELEekykelsass 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1413 ----EASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEE---CQSELEISQKESRGL 1485
Cdd:pfam07888 111 eelsEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAErkqLQAKLQQTEEELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1486 STELFKLKNSYEETLDHLETikrenknLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEheesk 1565
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGE----- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1566 tlriqlELNQMKSDVDRKLAEkdeeldnlrrKHQRSLESMQATL---DAEAKSRNEAVRLKKKMEGDLNEMEVQLNHANR 1642
Cdd:pfam07888 259 ------ELSSMAAQRDRTQAE----------LHQARLQAAQLTLqlaDASLALREGRARWAQERETLQQSAEADKDRIEK 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1529987947 1643 LASESQKLLRNLQ-------------IQIKDVQL-ELDETVHQNEELKEQVAVTERRNNLLAAEVEEL 1696
Cdd:pfam07888 323 LSAELQRLEERLQeermereklevelGREKDCNRvQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
843-1243 |
3.45e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 843 KIKPLLRSAATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSlqlQAEQDNLADaEDRCDLLIKTKIQ 922
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK---KAEEAKKAE-EDKNMALRKAEEA 1586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 923 L---EAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDiddlEITLAKIEKEKHAIENKVKNLIEEMAALDETILK 999
Cdd:PTZ00121 1587 KkaeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1000 LTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQvddlegslEQEKKLRMDLERVKRKLEGDLKLSLESVMDLEN 1079
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA--------KKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1080 DKQQLEEKLKKKDfemnelSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDL---SE 1156
Cdd:PTZ00121 1735 AKKEAEEDKKKAE------EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIfdnFA 1808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1157 RLEEAGGATSAQIEMNKKREAEFLK-------MRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKER 1229
Cdd:PTZ00121 1809 NIIEGGKEGNLVINDSKEMEDSAIKevadsknMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEAD 1888
|
410
....*....|....
gi 1529987947 1230 SEAKMEADDLASTV 1243
Cdd:PTZ00121 1889 EIEKIDKDDIEREI 1902
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1351-1911 |
3.91e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1351 LREQYEEEQEAkgELQRALSKANAEVAqwrtkyETDAIqrTEELEEAKKKLVTRLQESEEIMEASNAKCSSLEktkhRLQ 1430
Cdd:PRK02224 192 LKAQIEEKEEK--DLHERLNGLESELA------ELDEE--IERYEEQREQARETRDEADEVLEEHEERREELE----TLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1431 TEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKREN 1510
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1511 KNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDVDRKLAEKDEE 1590
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1591 LDNLRRKHQRsLESMQATLDAEAKSRNEAVRLKKkmEGDLNEMEVQLN---HANRLASESQKL--LRNLQIQIKDVQLEL 1665
Cdd:PRK02224 418 REERDELRER-EAELEATLRTARERVEEAEALLE--AGKCPECGQPVEgspHVETIEEDRERVeeLEAELEDLEEEVEEV 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1666 DETVHQNEELKEQVAVTER---RNNLLAAEVEELRALLEQ--------NDRARKLaEHELLEASERVNLLHSQNTGLINQ 1734
Cdd:PRK02224 495 EERLERAEDLVEAEDRIERleeRREDLEELIAERRETIEEkreraeelRERAAEL-EAEAEEKREAAAEAEEEAEEAREE 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1735 KKKLENDLSmlsnEVDDAVQECRNAEEKAKkAITDAAMMAEELKKEQDTSAHLERMKKNMEQT----IKDLQMRLDEAeq 1810
Cdd:PRK02224 574 VAELNSKLA----ELKERIESLERIRTLLA-AIADAEDEIERLREKREALAELNDERRERLAEkrerKRELEAEFDEA-- 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1811 iALKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELsyqaEEDKKNLVRLQDLIDKLQVkvksykrQT 1890
Cdd:PRK02224 647 -RIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL----EELRERREALENRVEALEA-------LY 714
|
570 580
....*....|....*....|.
gi 1529987947 1891 EEAEEQANTnlskYRKLQHEL 1911
Cdd:PRK02224 715 DEAEELESM----YGDLRAEL 731
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
860-1461 |
5.61e-10 |
|
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: 64.66 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 860 LKVELAKLKEALEK---------SEIKRKE------------LEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCD---- 914
Cdd:TIGR04523 122 LEVELNKLEKQKKEnkknidkflTEIKKKEkeleklnnkyndLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLklel 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 915 --LLIKTKIQLEAK-VKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENK--------- 982
Cdd:TIGR04523 202 llSNLKKKIQKNKSlESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKqkeleqnnk 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 983 -VKNLIEEMAALDETILKLTKEKKalQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKR 1061
Cdd:TIGR04523 282 kIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENS 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1062 KLEGDLKLSLESVMDLENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVE 1141
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNN 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1142 KQRSDVARELEDLSERLEEAGGATSAQIEMNKKREAEFLKMRRDLEEamlhheaTTAALRKKhadsvaelSEQIDSLQRV 1221
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ-------KQKELKSK--------EKELKKLNEE 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1222 KQKLEKERSEAKMEADDLASTVEQLSKGKATSEKMCRLYEDQMNEAKA--KADELQRQLNEANTQRARAQAESGEVSRKL 1299
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFelKKENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1300 EERESMVSQLQRAKNSFSQNVEELKKQLEEENKaknalahslqssrhDCDLLREQYEEEQEAKGELQRALSKANAEVAQW 1379
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK--------------ELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1380 RTKYETdAIQRTEELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLiIDLERANAAAAALDKKQRNFDK 1459
Cdd:TIGR04523 651 KETIKE-IRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRIKDL-PKLEEKYKEIEKELKKLDEFSK 728
|
..
gi 1529987947 1460 VL 1461
Cdd:TIGR04523 729 EL 730
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
898-1312 |
6.32e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 898 QLQAEQDNLADAEDRCDLLIKTKIQ-LEAKVKELMERLEDEEEmssnVLAKKRKLEDECAELKKDIDDLEITLAKIEKEK 976
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKeLEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 977 HAIEnkvknLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLegSLEQEKKLRMDL 1056
Cdd:COG4717 126 QLLP-----LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1057 ERVKRklegdlklslesvmdLENDKQQLEEKLKKKDFEMNELSTRIED--EQALVNQLQKKIKELQA------------- 1121
Cdd:COG4717 199 EELEE---------------LQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLllliaaallallg 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1122 ----------------------------RTEELEEELEADRACRAKVEKQRSDVARELEDLSERLEEAGGATSAQIEMNK 1173
Cdd:COG4717 264 lggsllsliltiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1174 KREAEFLKMRRDLEEAM------LHHEATTAALRKKHADSVAELSEQIDSLQRvKQKLEKERSEAKMEADDLASTVEQLS 1247
Cdd:COG4717 344 DRIEELQELLREAEELEeelqleELEQEIAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELL 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1529987947 1248 KGKATSEkmcrlYEDQMNEAKAKADELQRQLNEANTQRARAQAE------SGEVSRKLEERESMVSQLQRA 1312
Cdd:COG4717 423 EALDEEE-----LEEELEELEEELEELEEELEELREELAELEAEleqleeDGELAELLQELEELKAELREL 488
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1381-1928 |
6.43e-10 |
|
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: 64.27 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1381 TKYETDAIQRTEELEEAKKKLVTRLQESEEIMEASNAKcsslEKTKHRLQTEIEDLiidleraNAAAAALDKKQRNFDKV 1460
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKD----EEKINNSNNKIKIL-------EQQIKDLNDKLKKNKDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1461 LAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKG 1540
Cdd:TIGR04523 98 INKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1541 LEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDVDR--KLAEKDEELDNLRRKHQRSLESMQATLDAEAKSRNE 1618
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQisELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1619 AVRLKKKMEGDLNEMEVQLNHANRLASESQKLLRNLQIQI------------KDVQLELDETVHQNEELKEQVAVTERRN 1686
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIsdlnnqkeqdwnKELKSELKNQEKKLEEIQNQISQNNKII 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1687 NLLAAEVEELRALLEQNDRARKLAEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDAVQECRNAEEKAKKA 1766
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1767 ITDAammaEELKKEQDtsaHLERMKKNMEQTIKDLQmrldeaEQIALKggKKQVQKLEARVKELETELDAeqkksqeyqk 1846
Cdd:TIGR04523 418 QQEK----ELLEKEIE---RLKETIIKNNSEIKDLT------NQDSVK--ELIIKNLDNTRESLETQLKV---------- 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1847 vvrkYERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADTAETQVN 1926
Cdd:TIGR04523 473 ----LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
..
gi 1529987947 1927 KL 1928
Cdd:TIGR04523 549 KD 550
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
924-1679 |
9.19e-10 |
|
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: 63.89 E-value: 9.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 924 EAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKE 1003
Cdd:TIGR04523 53 EKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1004 KKALQEAHQQTLDDLQaeedkvnaltkakaKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDLENDKQQ 1083
Cdd:TIGR04523 133 KKENKKNIDKFLTEIK--------------KKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1084 LEEKL---KKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEadracraKVEKQRSDVARELEDLSERLEE 1160
Cdd:TIGR04523 199 LELLLsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIS-------NTQTQLNQLKDEQNKIKKQLSE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1161 aggaTSAQIEMNKKREAEflkmrrdLEEAMLHHEATTAALRK-KHADSVAELSEQIDSLQRVKQKLEKERSEAKMEADDL 1239
Cdd:TIGR04523 272 ----KQKELEQNNKKIKE-------LEKQLNQLKSEISDLNNqKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1240 ASTVEQLSKGKATSEkmcrlyedqmneakakadelqrqlneantqraraqAESGEVSRKLEERESMVSQLQRAKNSFSQN 1319
Cdd:TIGR04523 341 NEQISQLKKELTNSE-----------------------------------SENSEKQRELEEKQNEIEKLKKENQSYKQE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1320 VEelkkqleeenkaknalahSLQSSRHDcdlLREQYEEEQEAKGELQralskanaevaqwrtkyetdaiQRTEELEEAKK 1399
Cdd:TIGR04523 386 IK------------------NLESQIND---LESKIQNQEKLNQQKD----------------------EQIKKLQQEKE 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1400 KLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDliidleranaaaaaLDKKQRNFDKVLAEWKQKYEECQSELEISQ 1479
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN--------------LDNTRESLETQLKVLSRSINKIKQNLEQKQ 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1480 KEsrglstelFKLKNSyeetldHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTL 1559
Cdd:TIGR04523 489 KE--------LKSKEK------ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1560 EHEESKT--LRIQLELNQMKSD---VDRKLAEKDEELDNLrRKHQRSLESMQATLDAEAKSRNEAVRLKKKMEGDLNEME 1634
Cdd:TIGR04523 555 KKENLEKeiDEKNKEIEELKQTqksLKKKQEEKQELIDQK-EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1529987947 1635 VQLNHAnrlASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQV 1679
Cdd:TIGR04523 634 KNIKSK---KNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
847-1051 |
9.52e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 9.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 847 LLRSAATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAK 926
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 927 VKELMERLEDEEEMSSNVLAKKRKLEDE-------------------------CAELKKDIDDLEITLAKIEKEKHAIEN 981
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQpplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 982 KVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKK 1051
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
848-1220 |
1.10e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 848 LRSAATEK--ELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEA 925
Cdd:PRK02224 354 LEERAEELreEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 926 KVKELMERLEDEEEM---------------SSNVLA------KKRKLEDECAELKKDIDDLE------ITLAKIEKEKHA 978
Cdd:PRK02224 434 TLRTARERVEEAEALleagkcpecgqpvegSPHVETieedreRVEELEAELEDLEEEVEEVEerleraEDLVEAEDRIER 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 979 IENKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLER 1058
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1059 VKRklegdlklSLESVMDLENDKQQLEEKLKKKDfEMNElstriedeqalvnQLQKKIKELQARTEELEEELEADRACRA 1138
Cdd:PRK02224 594 IRT--------LLAAIADAEDEIERLREKREALA-ELND-------------ERRERLAEKRERKRELEAEFDEARIEEA 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1139 KVEKQRS-----DVARELEDLSER----LEEAGGATSAQIEMNKKREA-EFLKMRRDLEEAmLHHEATTaaLRKKHADSV 1208
Cdd:PRK02224 652 REDKERAeeyleQVEEKLDELREErddlQAEIGAVENELEELEELRERrEALENRVEALEA-LYDEAEE--LESMYGDLR 728
|
410
....*....|...
gi 1529987947 1209 AELSEQ-IDSLQR 1220
Cdd:PRK02224 729 AELRQRnVETLER 741
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1435-1931 |
1.52e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1435 DLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEEtldhLETIKRENKNLQ 1514
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE----LEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1515 EEITDLTDQISQGAKTIHELEKMKKGLEMEKTEiqaaLEEAEGTLEHEESKTLRIqLELNQMKSDVDRKLAEKDEELDNL 1594
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEE----LEEKVKELKELKEKAEEY-IKLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1595 RRKhqrsLESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVqLNHANRLASESQKLLRNLQiqikdvQLELDETVHQNEE 1674
Cdd:PRK03918 320 EEE----INGIEERIKELEEKEERLEELKKKLKELEKRLEE-LEERHELYEEAKAKKEELE------RLKKRLTGLTPEK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1675 LKEQVAVTERRNNLLAAEVEELRAL---LEQNDRARKLAEHELLEASERVNLLHSQNTGliNQKKKLENDLSMLSNEVDD 1751
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARigeLKKEIKELKKAIEELKKAKGKCPVCGRELTE--EHRKELLEEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1752 AVQECRNAEEKAKKAitdaammAEELKKEQDTSAHLERMKKNMEQtIKDLQMRLDEAEQIALKGGKKQVQKLEARVKELE 1831
Cdd:PRK03918 467 ELKEIEEKERKLRKE-------LRELEKVLKKESELIKLKELAEQ-LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLK 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1832 TE---LDAEQKKSQEYQKVVRKYERRIKELSYQAEEDKKNLVRL-----QDLIDKLQVKVKSYKRQTE--EAEEQANTNL 1901
Cdd:PRK03918 539 GEiksLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesvEELEERLKELEPFYNEYLElkDAEKELEREE 618
|
490 500 510
....*....|....*....|....*....|
gi 1529987947 1902 SKYRKLQHELDDAEERADTAETQVNKLRVR 1931
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKE 648
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1072-1292 |
1.88e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1072 ESVMDLENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVAREL 1151
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1152 EDLSERLEE-------AGGATSAQIEMNKKREAEFLKMRRDLEEAMLHHEATTAALRKKhadsVAELSEQIDSLQRVKQK 1224
Cdd:COG4942 100 EAQKEELAEllralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1529987947 1225 LEKERSEAKMEADDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNEANTQRARAQAES 1292
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1389-1836 |
2.78e-09 |
|
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: 62.01 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1389 QRTEELE-------EAKKKLV---TRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFD 1458
Cdd:pfam05622 14 QRCHELDqqvsllqEEKNSLQqenKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1459 KVLAEWKQKYEECQSELEisqkESRGLSTELFKLKNS-------------YEETLDHLETIKRENKNLQEEITDLTDQIS 1525
Cdd:pfam05622 94 KEVLELQHRNEELTSLAE----EAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNAEYMQRTL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1526 QGAKTIHELEKMKKGLEMEKTEIQaaleEAEGTLEHEESKTLRIQLELNQMKSDVDRKLAEKD---EELDNLRRK----- 1597
Cdd:pfam05622 170 QLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKErliIERDTLRETneelr 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1598 ----HQRSLESMQATLDAEAKSRNEAVrlKKKMEGDLNEMEVQLNHANRLASESQKLlrNLQIQIKDVQLELDETVHQNE 1673
Cdd:pfam05622 246 caqlQQAELSQADALLSPSSDPGDNLA--AEIMPAEIREKLIRLQHENKMLRLGQEG--SYRERLTELQQLLEDANRRKN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1674 ELKEQVAVTERRNNLLAAEVEELRALLEQNDrarklaehelleaservnllhSQNTGLINQKKKLENDLSMLsNEVDDAV 1753
Cdd:pfam05622 322 ELETQNRLANQRILELQQQVEELQKALQEQG---------------------SKAEDSSLLKQKLEEHLEKL-HEAQSEL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1754 QECRNA-EEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQ---TIKDLQMRLDEAEQIALKGGKKQVQKLE 1824
Cdd:pfam05622 380 QKKKEQiEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksVIKTLDPKQNPASPPEIQALKNQLLEKD 459
|
490
....*....|..
gi 1529987947 1825 ARVKELETELDA 1836
Cdd:pfam05622 460 KKIEHLERDFEK 471
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1508-1924 |
3.34e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1508 RENKNLQEEITDLTDQISQgaktIHELEKMKKGLEMEKTEIQAALEEAEGtlEHEESKTLRIQLELNQMKSDVDRKLAEK 1587
Cdd:COG4717 71 KELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELRE--ELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1588 DEELDNLRRKHQRSLESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELDE 1667
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1668 TVHQNEELKEQVAVTERRNNLLAAEVE-----ELRALLEQNDRARKLAEHELLEASERVNLLHSQNTGLINQKKKLENDL 1742
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLlliaaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1743 SMLsnevdDAVQECRNAEEKAKKAITDAAMMAEELKKEqdtsaHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQK 1822
Cdd:COG4717 305 EEL-----QALPALEELEEEELEELLAALGLPPDLSPE-----ELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1823 LEARVK-ELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEEDKKNLVRLQDliDKLQVKVKSYKRQTEEAEEQANTNL 1901
Cdd:COG4717 375 LLAEAGvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELR 452
|
410 420
....*....|....*....|...
gi 1529987947 1902 SKYRKLQHELDDAEERADTAETQ 1924
Cdd:COG4717 453 EELAELEAELEQLEEDGELAELL 475
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
923-1610 |
5.00e-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: 61.78 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 923 LEAKVKELMERLEDEEEMSSNVLAKKRKledecaELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTK 1002
Cdd:pfam12128 263 LHFGYKSDETLIASRQEERQETSAELNQ------LLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLD 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1003 EKKALQEAHQQTLDDLQAE----EDKVNALTKAKAKLEQQVDDLEGSLEQEkkLRMDLERVKRKL----EGDLKLSLESV 1074
Cdd:pfam12128 337 ADIETAAADQEQLPSWQSElenlEERLKALTGKHQDVTAKYNRRRSKIKEQ--NNRDIAGIKDKLakirEARDRQLAVAE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1075 MDLENDKQQLEEKLKKKDFEMNE----LSTRIEDEQALVNQLQKKIKELQARTEELEEELEADR---ACRAKVE------ 1141
Cdd:pfam12128 415 DDLQALESELREQLEAGKLEFNEeeyrLKSRLGELKLRLNQATATPELLLQLENFDERIERAREeqeAANAEVErlqsel 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1142 ---KQRSDVA-RELEDLSERLEEAGGATSAQIEMNKKREA---EFLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQ 1214
Cdd:pfam12128 495 rqaRKRRDQAsEALRQASRRLEERQSALDELELQLFPQAGtllHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSV 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1215 IDSLQRVKQKLEKERSEAKMEA---DDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNEAntQRARAQAE 1291
Cdd:pfam12128 575 GGELNLYGVKLDLKRIDVPEWAaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFA--RTALKNAR 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1292 SgEVSRKLEERESMVSQLQRAKNSFSQNVeelKKQLEEENKAKNALAHSLQS-SRHDCDLLREQYEEEQEAKGELQRALS 1370
Cdd:pfam12128 653 L-DLRRLFDEKQSEKDKKNKALAERKDSA---NERLNSLEAQLKQLDKKHQAwLEEQKEQKREARTEKQAYWQVVEGALD 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1371 KANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQESEEimeasnakcsslekTKHRLQTEIEDLIIDLERAnaaaaal 1450
Cdd:pfam12128 729 AQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPD--------------VIAKLKREIRTLERKIERI------- 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1451 dkkqRNFDKVLAEWKQKYEECQSeleiSQKESRGLStelfklknsyeetldhLETIKRENKNLQEEItdltdqisqgAKT 1530
Cdd:pfam12128 788 ----AVRRQEVLRYFDWYQETWL----QRRPRLATQ----------------LSNIERAISELQQQL----------ARL 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1531 IHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRI-QLELNQMKSDVDRKLAEKDEELDNLRRKHQRSLESMQATL 1609
Cdd:pfam12128 834 IADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLaTLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYV 913
|
.
gi 1529987947 1610 D 1610
Cdd:pfam12128 914 E 914
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
866-1374 |
9.17e-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: 60.51 E-value: 9.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 866 KLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELMERLEDEE------- 938
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKaahsfvv 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 939 -EMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALQEAHQ--QTL 1015
Cdd:pfam05483 352 tEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfeKIA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1016 DDLQAEEDKVNALTKAKAK----LEQQVDDLEGS----LEQEKKLRMDLERVKRKlegDLKLSLESVMDLENDKQQLEEk 1087
Cdd:pfam05483 432 EELKGKEQELIFLLQAREKeihdLEIQLTAIKTSeehyLKEVEDLKTELEKEKLK---NIELTAHCDKLLLENKELTQE- 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1088 lkKKDFEMnELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSERLEEAGGATSA 1167
Cdd:pfam05483 508 --ASDMTL-ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLK 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1168 QIEMNKKREAEFLKMRRDLEEAMLHHEATTAALRKKHADSVAElSEQIDSLQRVKQKLEKERSEAKMEADDLASTVEQLS 1247
Cdd:pfam05483 585 KEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAE-NKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEI 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1248 KGKATSEKmcRLYEdQMNEAKAKADELQRQLNEANTqraRAQAESGEVSRKLEERESMVSQLQRAKNSfsqNVEELKKQL 1327
Cdd:pfam05483 664 EDKKISEE--KLLE-EVEKAKAIADEAVKLQKEIDK---RCQHKIAEMVALMEKHKHQYDKIIEERDS---ELGLYKNKE 734
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1529987947 1328 EEENKAKNALAHSLQSSRHDCDLLREQYEEEQEAKGELQRALSKANA 1374
Cdd:pfam05483 735 QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTA 781
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1478-1685 |
9.76e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1478 SQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEG 1557
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1558 TLEhEESKTLRIQLELNQMKSDVDRK--LAEKDEELDNLRRKH---------QRSLESMQATLDAEAKSRNEAVRLKKKM 1626
Cdd:COG4942 98 ELE-AQKEELAELLRALYRLGRQPPLalLLSPEDFLDAVRRLQylkylaparREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1529987947 1627 EGDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERR 1685
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1451-1920 |
1.10e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.44 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1451 DKKQRNFDKVLAEWKQKYEECQSELEISQKEsrglstelfklKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKT 1530
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQ-----------REQARETRDEADEVLEEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1531 IHELEKMKKGLEMEKTEIQAALEEAEgtlehEESKTLRIQLELnqmkSDVDRK-LAEKDEELDNLRRKHQRSLEsmQATL 1609
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELE-----EERDDLLAEAGL----DDADAEaVEARREELEDRDEELRDRLE--ECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1610 DAEAKsRNEAVRLKKKmegdlnemevqlnhANRLASESQKLlrnlQIQIKDVQLELDETvhqneelkeQVAVTERRNnll 1689
Cdd:PRK02224 336 AAQAH-NEEAESLRED--------------ADDLEERAEEL----REEAAELESELEEA---------REAVEDRRE--- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1690 aaEVEELRALLEQNDRARKLAEHELLEASERVNLLHSQNTGLINQKKKLENDLSmlsnEVDDAVQECRNAEEKAK----- 1764
Cdd:PRK02224 385 --EIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR----TARERVEEAEALLEAGKcpecg 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1765 KAITDAAmMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQiaLKGGKKQVQKLEARVKELETELDAEQKKSQEY 1844
Cdd:PRK02224 459 QPVEGSP-HVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED--LVEAEDRIERLEERREDLEELIAERRETIEEK 535
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1529987947 1845 QKVVRKYERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEAEEQANtNLSKYRKLQHELDDAEERADT 1920
Cdd:PRK02224 536 RERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLERIRTLLAAIADAEDEIER 610
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1534-1815 |
1.35e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 60.31 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1534 LEKMKKG--LEMEKTEIQAALEEAEGTLEheesKTLRIQLELNQMKsdvdRKLAEKDEELdnlrRKHQRSLESMQATLDA 1611
Cdd:PRK11281 45 LDALNKQklLEAEDKLVQQDLEQTLALLD----KIDRQKEETEQLK----QQLAQAPAKL----RQAQAELEALKDDNDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1612 EAKSRNEAVRLKKkMEGDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELK--------EQVAVTE 1683
Cdd:PRK11281 113 ETRETLSTLSLRQ-LESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRnllkggkvGGKALRP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1684 RRNNLLAAEVEEL-------RALLEQNDRARKLAEHELLEASERVNLLHSQNT---GLINQkKKLEndlsmLSNEVddaV 1753
Cdd:PRK11281 192 SQRVLLQAEQALLnaqndlqRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQllqEAINS-KRLT-----LSEKT---V 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1529987947 1754 QECRNAEEKAKkaITDAAMMAEELKKEQDTSAHL-ERMKKNMEQTIKDLQMR--LDEA--------EQI-ALKG 1815
Cdd:PRK11281 263 QEAQSQDEAAR--IQANPLVAQELEINLQLSQRLlKATEKLNTLTQQNLRVKnwLDRLtqsernikEQIsVLKG 334
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1205-1421 |
1.55e-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: 59.01 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1205 ADSVAELSEQIDSLQRVKQKLEKERSEAKMEADDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNEANTQ 1284
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1285 RARAQAESGEVSRKLEERESM-----------VSQLQRAKNSFSQNVEELKKQLEEENKAKNALAHSLQSSRHDCDLLRE 1353
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1529987947 1354 QYEEEQEAKGELQRALSKANAEVAQWRTKYETDAiQRTEELEEAKKKLVTRLQESEEIMEASNAKCSS 1421
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1184-1879 |
1.60e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1184 RDLEEAmlHHEATTA-----ALR--KKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEAddLASTVEQLSKGKATSEKM 1256
Cdd:COG4913 235 DDLERA--HEALEDAreqieLLEpiRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1257 CRLYEDQMNEAKAKADELQRQLNEANTQR-ARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKQLEEENKAKN 1335
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1336 ALAHSLQSSRHDcdlLREQYEEEQEAKGELQRALSKANAEVAQWRTK---YETDAIQRTEELEEAkkklvTRLQESE--- 1409
Cdd:COG4913 391 ALLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASLERRksnIPARLLALRDALAEA-----LGLDEAElpf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1410 --EIMEAsnakcssleKTKHRL-QTEIE--------DLIIDLERANAAAAALDK---KQR-NFDKVlaewkqkyEECQSE 1474
Cdd:COG4913 463 vgELIEV---------RPEEERwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1475 LEISQKESRGLSTELFKLKNSYEETLDHletikrenknlqeEITDLTDQISqgAKTIHELEKMKKGLemekTeiQAALEE 1554
Cdd:COG4913 526 PERPRLDPDSLAGKLDFKPHPFRAWLEA-------------ELGRRFDYVC--VDSPEELRRHPRAI----T--RAGQVK 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1555 AEGTL-EHEESKTLRiqlELNQMKSDVDRKLAEKDEELDNLRRKH---QRSLESMQATLDAEAKSRNEAVRLKKKMEGDL 1630
Cdd:COG4913 585 GNGTRhEKDDRRRIR---SRYVLGFDNRAKLAALEAELAELEEELaeaEERLEALEAELDALQERREALQRLAEYSWDEI 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1631 NEMEVQ-----LNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQNDR 1705
Cdd:COG4913 662 DVASAEreiaeLEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1706 ARKLAEHELLEAsERVNLLHSQNTGLInqKKKLENDLSMLSNEVDDAVQECRNAEEKAKK--------------AITDAA 1771
Cdd:COG4913 742 LARLELRALLEE-RFAAALGDAVEREL--RENLEERIDALRARLNRAEEELERAMRAFNRewpaetadldadleSLPEYL 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1772 MMAEELkKEQDTSAHLERMK----KNMEQTIKDLQMRLDEAEQIAlkggKKQVQKLEARVKELE------TELDAEQKKS 1841
Cdd:COG4913 819 ALLDRL-EEDGLPEYEERFKellnENSIEFVADLLSKLRRAIREI----KERIDPLNDSLKRIPfgpgryLRLEARPRPD 893
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1529987947 1842 QEyqkvVRKYERRIKELS-----YQAEEDKKNLVRLQDLIDKL 1879
Cdd:COG4913 894 PE----VREFRQELRAVTsgaslFDEELSEARFAALKRLIERL 932
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1657-1893 |
1.60e-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: 59.01 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1657 QIKDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQNDRARKLAEHELLEASERVNLLHSQNTGLINQKK 1736
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1737 KLENDLSMLsneVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQialkgg 1816
Cdd:COG4942 101 AQKEELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA------ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1529987947 1817 kkQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEA 1893
Cdd:COG4942 172 --ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1508-1941 |
2.56e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1508 RENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKtlriqlelnqmKSDVDRKLAEK 1587
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR-----------KAEDARKAEEA 1145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1588 DEELDNLRRKHQRSLEsmQATLDAEAKSRNEAvrlkKKMEGDLNEMEVQLNHANRLASESqkllRNLQIQIKDVQLELDE 1667
Cdd:PTZ00121 1146 RKAEDAKRVEIARKAE--DARKAEEARKAEDA----KKAEAARKAEEVRKAEELRKAEDA----RKAEAARKAEEERKAE 1215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1668 TVHQNEELKEQVAVTerrnnllaaEVEELRALLEQNDRARKLAEHELLEASERVNLLH-SQNTGLINQKKKLENDLSMLS 1746
Cdd:PTZ00121 1216 EARKAEDAKKAEAVK---------KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHfARRQAAIKAEEARKADELKKA 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1747 NEVDDAvQECRNAEEKAKkaITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQ--MRLDEAEQIALKGGKKQVQKLE 1824
Cdd:PTZ00121 1287 EEKKKA-DEAKKAEEKKK--ADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEeaKKAAEAAKAEAEAAADEAEAAE 1363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1825 ARVKELETELDAEQKKSQEYQKVVRKyERRIKELSYQAEEDKKNLVRLQDlIDKLQVKVKSYKRQTEEAE--EQANTNLS 1902
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEE-KKKADEAKKKAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKkaDEAKKKAE 1441
|
410 420 430
....*....|....*....|....*....|....*....
gi 1529987947 1903 KYRKLQHELDDAEERADTAETQVNKLRVRTRDQVSKLAE 1941
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1535-1913 |
2.99e-08 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 59.15 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1535 EKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQM----KSDVDRKLAEKDEELDNLRRKHQRSLESMQATLD 1610
Cdd:PLN02939 48 KKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKstssDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1611 AEAKSRNEAVRLKKKMEGDLNEMEVQ-LNHANRLASESQKLlrnlQIQIKDVQLELDETVHQNEELKEQVAVTErrnnLL 1689
Cdd:PLN02939 128 FQLEDLVGMIQNAEKNILLLNQARLQaLEDLEKILTEKEAL----QGKINILEMRLSETDARIKLAAQEKIHVE----IL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1690 AAEVEELRALLEQNDRARKLAEHELleaSERVNLLHSQNTglinqkkKLENDLSMLSNEVDdavqecrnaeekakkaitd 1769
Cdd:PLN02939 200 EEQLEKLRNELLIRGATEGLCVHSL---SKELDVLKEENM-------LLKDDIQFLKAELI------------------- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1770 aammaeELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVR 1849
Cdd:PLN02939 251 ------EVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLD 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1529987947 1850 KY---ERRIKELSYQAEEdkKNLVRLQ-DLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDD 1913
Cdd:PLN02939 325 QNqdlRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQD 390
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
854-1311 |
3.64e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 854 EKELAALKVELAKLKEAL---EKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAE-----------DRCDLLIKT 919
Cdd:TIGR04523 186 QKNIDKIKNKLLKLELLLsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTteisntqtqlnQLKDEQNKI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 920 KIQLEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDID-DLEITLAKIEKEKHAIENKVKNLIEEMAALDETIL 998
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 999 KLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSleqekklrmdlervKRKLEGDLKlslesvmDLE 1078
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ--------------INDLESKIQ-------NQE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1079 NDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSERL 1158
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1159 EEaggaTSAQIEMNKKREAEFLKMRRDLEEamlhheattaalrkkhadSVAELSEQIDSLQRVKQKLEKERSEAKMEADD 1238
Cdd:TIGR04523 485 EQ----KQKELKSKEKELKKLNEEKKELEE------------------KVKDLTKKISSLKEKIEKLESEKKEKESKISD 542
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 1239 LASTVEQLSKGKATS--EKMCRLYEDQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQR 1311
Cdd:TIGR04523 543 LEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
848-1064 |
4.11e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 848 LRSAATEKELAALKVELAKLKEALEKSEIKRKELEERQ--VSLIQEKNDLSLQLQAEQDNLADAEDRcdlliktKIQLEA 925
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAE-------LAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 926 KVKELMERLEDEEEMSSNVLAkkrklEDECAELKKDIDDLEITLAKIEK---EKHAienKVKNLIEEMAALDETIlkltk 1002
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSArytPNHP---DVIALRAQIAALRAQL----- 307
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1529987947 1003 eKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLE 1064
Cdd:COG3206 308 -QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYE 368
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
922-1307 |
4.13e-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: 57.98 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 922 QLEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLT 1001
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1002 KEKKAL---QEAHQQTLDDLqaeEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDLE 1078
Cdd:pfam07888 115 EEKDALlaqRAAHEARIREL---EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1079 NDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQArtEELEEELEADRACRAKvekqrsdvaRELEDLSERL 1158
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEA--LLEELRSLQERLNASE---------RKVEGLGEEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1159 EEAGGATS-AQIEMNKKR-EAEFLKMR-RDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKME 1235
Cdd:pfam07888 261 SSMAAQRDrTQAELHQARlQAAQLTLQlADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERME 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 1236 ADDLASTVEQlskgkatsEKMCRLYedQMNEAKAKADELQRQLNEANTQRARAQAESGEV---SRKLEERESMVS 1307
Cdd:pfam07888 341 REKLEVELGR--------EKDCNRV--QLSESRRELQELKASLRVAQKEKEQLQAEKQELleyIRQLEQRLETVA 405
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
977-1189 |
5.04e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 977 HAIENKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSL----EQEKKL 1052
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1053 RMDLERVKRKLEGDL----KLSLESVMDL---ENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEE 1125
Cdd:COG4942 96 RAELEAQKEELAELLralyRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1529987947 1126 LEEELEADRACRAKVEKQRSDVARELEDLSERLEEAGGATSAQIEMNKKREAEFLKMRRDLEEA 1189
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
843-1025 |
6.45e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 55.70 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 843 KIKPLLRSAATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRcdlliktkiq 922
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 923 lEAKVKELMERLEDEEEMSSnvlakkrkLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTK 1002
Cdd:COG1579 75 -IKKYEEQLGNVRNNKEYEA--------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
170 180
....*....|....*....|...
gi 1529987947 1003 EKKALQEAHQQTLDDLQAEEDKV 1025
Cdd:COG1579 146 ELDEELAELEAELEELEAEREEL 168
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1064-1312 |
7.56e-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: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1064 EGDLKLSLESVMDLENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARteeleeeleadracrakVEKQ 1143
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE-----------------IAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1144 RSDVARELEDLSERleeaggATSAQIEMNKKREAEFLKMRRDLEEaMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQ 1223
Cdd:COG3883 78 EAEIEERREELGER------ARALYRSGGSVSYLDVLLGSESFSD-FLDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1224 KLEKERSEAKMEADDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERE 1303
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
....*....
gi 1529987947 1304 SMVSQLQRA 1312
Cdd:COG3883 231 AAAAAAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1108-1600 |
8.53e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1108 LVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSERLEEAggatSAQIEMNKKREAEFLKMRRDLE 1187
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1188 EAMLHHEATTAALRKKhadsvAELSEQIDSLQRVKQKLEkERSEAKMEADDLASTVEQLSKGKATSEKMCRLY-EDQMNE 1266
Cdd:COG4717 123 KLLQLLPLYQELEALE-----AELAELPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLAtEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1267 AKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKqleeenkaknALAHSLQSSRH 1346
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA----------AALLALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1347 DCDLLREQYeeeqeakGELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQESEEImeasnakCSSLEKTK 1426
Cdd:COG4717 267 SLLSLILTI-------AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL-------LAALGLPP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1427 HRLQTEIEDLIIDLERANAAAAALDKKQRNfdkvlAEWKQKYEECQSELEISQKESrglstelfklknsyEETLDHLETI 1506
Cdd:COG4717 333 DLSPEELLELLDRIEELQELLREAEELEEE-----LQLEELEQEIAALLAEAGVED--------------EEELRAALEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1507 KRENKNLQEEITDLTDQISQGAKTIHELEKM--KKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSdvDRKL 1584
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE--DGEL 471
|
490
....*....|....*.
gi 1529987947 1585 AEKDEELDNLRRKHQR 1600
Cdd:COG4717 472 AELLQELEELKAELRE 487
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
926-1541 |
8.96e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.60 E-value: 8.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 926 KVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDEtilkltkekk 1005
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS---------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1006 alqeahqqTLDDLQAEEDKVNALTKAKAKLEqqvDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDLENDKQQLE 1085
Cdd:PRK01156 240 --------ALNELSSLEDMKNRYESEIKTAE---SDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1086 EKlkkkdfemNELSTRIEDEQALVNQLQKKIKELQarteeleeeleADRACRAKVEKQRSDVARELEDLSERLEEAGGAT 1165
Cdd:PRK01156 309 NK--------KQILSNIDAEINKYHAIIKKLSVLQ-----------KDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1166 SAQIEMNKKREAEFLKMRR---DLEEAMLHHEATTAALRKKHAD---SVAELSEQIDSLQR----VKQKLEKERSEAKME 1235
Cdd:PRK01156 370 KSIESLKKKIEEYSKNIERmsaFISEILKIQEIDPDAIKKELNEinvKLQDISSKVSSLNQriraLRENLDELSRNMEML 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1236 ADDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNEANTQRARAQA-ESGEVSRKLEERESMVSQLQRAKN 1314
Cdd:PRK01156 450 NGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKrKEYLESEEINKSINEYNKIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1315 SFSQNVEELKKQLEEENKAKNALAhslQSSRHDCDLLREQYEEeqeakgelqraLSKANAEvaqwRTKYETDAIQ-RTEE 1393
Cdd:PRK01156 530 DLEDIKIKINELKDKHDKYEEIKN---RYKSLKLEDLDSKRTS-----------WLNALAV----ISLIDIETNRsRSNE 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1394 LEEAKKKLVTRLQESEEIMEASNakcSSLEKTKHRLQTEIEDL---IIDLERANAAAAALDKKQRNFDKVLAEwKQKYEE 1470
Cdd:PRK01156 592 IKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLnnkYNEIQENKILIEKLRGKIDNYKKQIAE-IDSIIP 667
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1529987947 1471 CQSELEISQKESrglSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGL 1541
Cdd:PRK01156 668 DLKEITSRINDI---EDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
868-1908 |
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 1529987947 868 KEALEKSEIKRKELEE---RQVSLIQEKNDLSLQLQAEQDN-LADAEDRCDLLIK--TKIQLEAKVKELMERLED-EEEM 940
Cdd:TIGR01612 930 KESIEKFHNKQNILKEilnKNIDTIKESNLIEKSYKDKFDNtLIDKINELDKAFKdaSLNDYEAKNNELIKYFNDlKANL 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 941 SSNvlaKKRKLEDECAELKKDIDDLEITLAKIEKE----KHAIENKVKNLIEEMA--------ALDETILK-----LTKE 1003
Cdd:TIGR01612 1010 GKN---KENMLYHQFDEKEKATNDIEQKIEDANKNipniEIAIHTSIYNIIDEIEkeigknieLLNKEILEeaeinITNF 1086
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1004 KKALQEAHQQTLDDLQAEE-----DKVNALTKAKAKLEQQVDDLEGSLEQ-EKKLRMDLERVK---RKLE--GDLKLSLE 1072
Cdd:TIGR01612 1087 NEIKEKLKHYNFDDFGKEEnikyaDEINKIKDDIKNLDQKIDHHIKALEEiKKKSENYIDEIKaqiNDLEdvADKAISND 1166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1073 SVMDLENDKQQLEEKLKKKDF---EMNEL---STRIEDEQALVNQLqKKIKELQARTEELEEELEADRAcRAKVEKQRSD 1146
Cdd:TIGR01612 1167 DPEEIEKKIENIVTKIDKKKNiydEIKKLlneIAEIEKDKTSLEEV-KGINLSYGKNLGKLFLEKIDEE-KKKSEHMIKA 1244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1147 VARELEDLSERLEEA-GGATSAQIEMNKKREAEFLKMRRDLEEAML----HHEATTAALRKKHADSVAELSEQIDsLQRV 1221
Cdd:TIGR01612 1245 MEAYIEDLDEIKEKSpEIENEMGIEMDIKAEMETFNISHDDDKDHHiiskKHDENISDIREKSLKIIEDFSEESD-INDI 1323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1222 KQKLEKERSEAKMEADDLASTVEQLS----------------KGKATSEKMCRlYEDQMNEAKAKADELQRQLNE-ANTQ 1284
Cdd:TIGR01612 1324 KKELQKNLLDAQKHNSDINLYLNEIAniynilklnkikkiidEVKEYTKEIEE-NNKNIKDELDKSEKLIKKIKDdINLE 1402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1285 RARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKQLEEENK-----------AKNALAHSLQ------SSRHD 1347
Cdd:TIGR01612 1403 ECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNEnvlllfkniemADNKSQHILKikkdnaTNDHD 1482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1348 CDL--LREQYEEEQEAKGELQR--ALSKANAEVAQWRTKYETDAIQRTEELEeAKKKLVTRLQESE----EIMEASNAKC 1419
Cdd:TIGR01612 1483 FNIneLKEHIDKSKGCKDEADKnaKAIEKNKELFEQYKKDVTELLNKYSALA-IKNKFAKTKKDSEiiikEIKDAHKKFI 1561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1420 SSLEKTKHRL------QTEIEDLIIDLERANAAAAALDKKQRNFDKVL---AEWKQKYEECQSELEISQKESRGLS---- 1486
Cdd:TIGR01612 1562 LEAEKSEQKIkeikkeKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFlkiSDIKKKINDCLKETESIEKKISSFSidsq 1641
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1487 -TELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEM------------EKTEIQAALE 1553
Cdd:TIGR01612 1642 dTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIgiiekikeiaiaNKEEIESIKE 1721
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1554 EAEGTLEHEESKTLRIQLElnqmKSDVDRKLAEKDEELDNLRRKHQRSLESMQATLDAEAK--------------SRNEA 1619
Cdd:TIGR01612 1722 LIEPTIENLISSFNTNDLE----GIDPNEKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKepitydeikntrinAQNEF 1797
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1620 VR---LKKKMEGDLNEMEVqlNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERRN---NLLAAEV 1693
Cdd:TIGR01612 1798 LKiieIEKKSKSYLDDIEA--KEFDRIINHFKKKLDHVNDKFTKEYSKINEGFDDISKSIENVKNSTDENllfDILNKTK 1875
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1694 EELRALLEQNDRARKL-AEHELLEASERVNLLH--SQNTGLINQKKKLEND-LSMLSNEVDDAVQECRNAEEKAK----- 1764
Cdd:TIGR01612 1876 DAYAGIIGKKYYSYKDeAEKIFINISKLANSINiqIQNNSGIDLFDNINIAiLSSLDSEKEDTLKFIPSPEKEPEiytki 1955
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1765 ----KAITDAAMMAEEL-KKEQDTsahLERMKKNMEQTIKdlqMRLDEAEQIALKGGKKQVQKLEARVKEL---ETELDA 1836
Cdd:TIGR01612 1956 rdsyDTLLDIFKKSQDLhKKEQDT---LNIIFENQQLYEK---IQASNELKDTLSDLKYKKEKILNDVKLLlhkFDELNK 2029
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1837 EQKKSQEYQKVVR-KYERRIKELSYQAEEDKKNLVRLQDL-------------IDKLQVKVKSYKRQTEEAEEQANTNLS 1902
Cdd:TIGR01612 2030 LSCDSQNYDTILElSKQDKIKEKIDNYEKEKEKFGIDFDVkameekfdndikdIEKFENNYKHSEKDNHDFSEEKDNIIQ 2109
|
....*.
gi 1529987947 1903 KYRKLQ 1908
Cdd:TIGR01612 2110 SKKKLK 2115
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1223-1708 |
1.12e-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: 57.04 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1223 QKLEKERSEAKMEADDLASTVEQL---------SKGKATSEKMCRLYEDQmNEAKAKADELQRQLNEANTQRARAQAESG 1293
Cdd:pfam05483 172 KKYEYEREETRQVYMDLNNNIEKMilafeelrvQAENARLEMHFKLKEDH-EKIQHLEEEYKKEINDKEKQVSLLLIQIT 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1294 EVSRK-------LEERESMVSQLQRAKNSFSQNVEELKKQLEEENKAKNALAHSLQSSRHDCDLLRE----------QYE 1356
Cdd:pfam05483 251 EKENKmkdltflLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEdlqiatkticQLT 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1357 EEQEAKGElqrALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQESEEIMEASNAKCSSLEK-TKHRLQTEIEd 1435
Cdd:pfam05483 331 EEKEAQME---ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmTKFKNNKEVE- 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1436 lIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQE 1515
Cdd:pfam05483 407 -LEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1516 EITDLTDQIS----QGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTL---EHEESKTLRIQLELNQMKSDVDRKLAEKD 1588
Cdd:pfam05483 486 KNIELTAHCDklllENKELTQEASDMTLELKKHQEDIINCKKQEERMLkqiENLEEKEMNLRDELESVREEFIQKGDEVK 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1589 EELDNLRRKHQRSLESMQATLDAEAKSRNEAVRLKKKMEG---DLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLEL 1665
Cdd:pfam05483 566 CKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENknkNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELEL 645
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1529987947 1666 DETVHQNEEL----KEQVAVTERRNNLLAAEVEELRALLEQNDRARK 1708
Cdd:pfam05483 646 ASAKQKFEEIidnyQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1462-1918 |
1.30e-07 |
|
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: 56.90 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1462 AEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLdhletikrenKNLQEEITDLTDQISQGAKTIHELEKMKKGL 1541
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERK----------QVLEKELKHLREALQQTQQSHAYLTQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1542 EmEKTEIQAALEEAEGTLEheESKTLRIQLELNQMKSDVDRK---LAEKDEELDNLRRKHQRSLESMQATLDAEAKSRNE 1618
Cdd:TIGR00618 253 E-EQLKKQQLLKQLRARIE--ELRAQEAVLEETQERINRARKaapLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1619 AVRLKK------KMEGDLNEMEVQLNHaNRLASESQKLLRnlqiQIKDVQLELDETVHQneeLKEQVAVTERRNNLLAAE 1692
Cdd:TIGR00618 330 RAAHVKqqssieEQRRLLQTLHSQEIH-IRDAHEVATSIR----EISCQQHTLTQHIHT---LQQQKTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1693 VEELRALL------------EQNDRARKLAEHELLEASERVNLLHSQNTGLI-NQKKKLENDLSMLSNEVDDAVQECRNA 1759
Cdd:TIGR00618 402 LDILQREQatidtrtsafrdLQGQLAHAKKQQELQQRYAELCAAAITCTAQCeKLEKIHLQESAQSLKEREQQLQTKEQI 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1760 EEKAKKAITDAAMMAEELKKEQdtsahLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQKLEARVKELETELDAEQK 1839
Cdd:TIGR00618 482 HLQETRKKAVVLARLLELQEEP-----CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1840 KSQEY-------QKVVRKYERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELD 1912
Cdd:TIGR00618 557 QRASLkeqmqeiQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ 636
|
....*.
gi 1529987947 1913 DAEERA 1918
Cdd:TIGR00618 637 CSQELA 642
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
857-1304 |
1.62e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 857 LAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDlslQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELMERLED 936
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELK---EAEEKEEEYAELQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 937 EEEMSSN--VLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKalqEAHQQT 1014
Cdd:COG4717 121 LEKLLQLlpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE---EELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1015 LDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDLENDKQQLEEKLKKKDFE 1094
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1095 MneLSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSERLEEAGGATSAQIEMNKK 1174
Cdd:COG4717 278 V--LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1175 REaeflKMRRDLEEAMLHHEATtAALRKKHADSVAELSEQIDSLQRvKQKLEKERSEAKMEADDLASTVEQLSKGKATSE 1254
Cdd:COG4717 356 AE----ELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEE 429
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1255 kmcrlyedqmneAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERES 1304
Cdd:COG4717 430 ------------LEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1619-1857 |
1.63e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1619 AVRLKKKMEGDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELRA 1698
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1699 LLE--QNDRARKLAEHELLEASERVNLLHSQNTGlinqkkkleNDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEE 1776
Cdd:COG4942 98 ELEaqKEELAELLRALYRLGRQPPLALLLSPEDF---------LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1777 LKKEQDTsahLERMKKNMEQTIKDLQMRLDEAEQIalkggkkqVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIK 1856
Cdd:COG4942 169 LEAERAE---LEALLAELEEERAALEALKAERQKL--------LARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
.
gi 1529987947 1857 E 1857
Cdd:COG4942 238 A 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
863-1407 |
3.02e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 863 ELAKLKEALEKSEIKRK---ELEERQVSLIQEKNDLS-LQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELMERLEDEE 938
Cdd:COG4913 236 DLERAHEALEDAREQIEllePIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 939 EMSSNVLAKKRKLEDECAELK-KDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDD 1017
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1018 LQAEEDKV-NALTKAKAKLEQQVDDLEgSLEQE------KKLRMD--LERVKRKLEGDLKLSLESV------MDLENDKQ 1082
Cdd:COG4913 396 LEEELEALeEALAEAEAALRDLRRELR-ELEAEiaslerRKSNIParLLALRDALAEALGLDEAELpfvgelIEVRPEEE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1083 QLE---EKLkkkdfeMNELSTRI--EDEQ-----ALVNQLQKKIK----ELQARTEELEEELEADRACRAKVEKQRSDVA 1148
Cdd:COG4913 475 RWRgaiERV------LGGFALTLlvPPEHyaaalRWVNRLHLRGRlvyeRVRTGLPDPERPRLDPDSLAGKLDFKPHPFR 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1149 RELEDLSERLEEAGGATSAQiemnkkreaEFLKMRRDL-EEAMLHHEATtaalRKKHADSVAELS---------EQIDSL 1218
Cdd:COG4913 549 AWLEAELGRRFDYVCVDSPE---------ELRRHPRAItRAGQVKGNGT----RHEKDDRRRIRSryvlgfdnrAKLAAL 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1219 QRVKQKLEKERSEAKMEADDLASTVEQLSKGKATSEKMcrlyeDQMNEAKAKADELQRQLNEANTQRARAQAESGEVsRK 1298
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRL-----AEYSWDEIDVASAEREIAELEAELERLDASSDDL-AA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1299 LEEResmVSQLQRAKNSFSQNVEELKKQLEEENKAKNALAHSLQSSRHDCDLLREQYEEEQEAKGELQRALSKANAEVAQ 1378
Cdd:COG4913 690 LEEQ---LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
570 580
....*....|....*....|....*....
gi 1529987947 1379 WRTKYETDAIQRTEELEEAKKKLVTRLQE 1407
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
865-1911 |
3.24e-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: 55.83 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 865 AKLKEALEKSEIKRKELEERQVSLiQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELMERLEDEEEMSSNV 944
Cdd:TIGR01612 544 AGLKESYELAKNWKKLIHEIKKEL-EEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDKNEYIKKA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 945 LAKKRKLEDECA---ELKKdIDDLEIT--LAKIEKEKHAIENKVKNLIE-EMAALDETILKLTKEKKALQEAHQQTLDDL 1018
Cdd:TIGR01612 623 IDLKKIIENNNAyidELAK-ISPYQVPehLKNKDKIYSTIKSELSKIYEdDIDALYNELSSIVKENAIDNTEDKAKLDDL 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1019 QAEEDKVnaLTKAKAKLEQQVDDLEGSLEQEK-KLRMDLERVKRKLEGDLKLSLESVM-DLENDKQQLEEKLKKKDFEMN 1096
Cdd:TIGR01612 702 KSKIDKE--YDKIQNMETATVELHLSNIENKKnELLDIIVEIKKHIHGEINKDLNKILeDFKNKEKELSNKINDYAKEKD 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1097 ELstriedeqalvNQLQKKIKELQARTEELEEELEAdracRAKVEKQRSDVARE-LEDLSERLEEaggaTSAQIEMNKKR 1175
Cdd:TIGR01612 780 EL-----------NKYKSKISEIKNHYNDQINIDNI----KDEDAKQNYDKSKEyIKTISIKEDE----IFKIINEMKFM 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1176 EAEFLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQI--DSLQRVKQKLEKERSEAKMEADDLASTVEQLSKGKATS 1253
Cdd:TIGR01612 841 KDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEIsdDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVD 920
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1254 E--KMCRLYEDQMNEAKAKADELQRQLNEaNTQRARaQAESGEVSRKLEERESMVSQLQRAKNSFSQ-NVEELKKQLEEE 1330
Cdd:TIGR01612 921 EyiKICENTKESIEKFHNKQNILKEILNK-NIDTIK-ESNLIEKSYKDKFDNTLIDKINELDKAFKDaSLNDYEAKNNEL 998
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1331 NKAKNALAHSLQSSRHDcdLLREQYEEEQEAKGELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLqeSEE 1410
Cdd:TIGR01612 999 IKYFNDLKANLGKNKEN--MLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELL--NKE 1074
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1411 IMEASNAKCSSLEKTKHRLqteiedliidleranaaaaaldkKQRNFDKVLAEWKQKYEEcqseleisqkESRGLSTELF 1490
Cdd:TIGR01612 1075 ILEEAEINITNFNEIKEKL-----------------------KHYNFDDFGKEENIKYAD----------EINKIKDDIK 1121
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1491 KLKNSYEETLDHLETIKRENKNLQEEI-TDLTDQISQGAKTIHELEKmkKGLEMEKTEIQAALEEAEGTLEheesktlri 1569
Cdd:TIGR01612 1122 NLDQKIDHHIKALEEIKKKSENYIDEIkAQINDLEDVADKAISNDDP--EEIEKKIENIVTKIDKKKNIYD--------- 1190
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1570 qlELNQMKSDVDRklAEKD----EELDNLRRKHQRSLESM-QATLDAEaksrneavrlKKKMEGDLNEMEVQLNHANRLA 1644
Cdd:TIGR01612 1191 --EIKKLLNEIAE--IEKDktslEEVKGINLSYGKNLGKLfLEKIDEE----------KKKSEHMIKAMEAYIEDLDEIK 1256
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1645 SESQKLLRNLQIQIkDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQNDRA------RKLAEHELLEAS 1718
Cdd:TIGR01612 1257 EKSPEIENEMGIEM-DIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIEDFSEEsdindiKKELQKNLLDAQ 1335
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1719 ER---VNLLHSQNTGLINQKKklendLSMLSNEVDDaVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNME 1795
Cdd:TIGR01612 1336 KHnsdINLYLNEIANIYNILK-----LNKIKKIIDE-VKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIE 1409
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1796 QTIKDLQmrldeaeqiaLKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVV-----------RKYERRIKELSYQAEE 1864
Cdd:TIGR01612 1410 STLDDKD----------IDECIKKIKELKNHILSEESNIDTYFKNADENNENVlllfkniemadNKSQHILKIKKDNATN 1479
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*...
gi 1529987947 1865 DKK-NLVRLQDLIDklqvKVKSYKRQTEEAEEQANTNLSKYRKLQHEL 1911
Cdd:TIGR01612 1480 DHDfNINELKEHID----KSKGCKDEADKNAKAIEKNKELFEQYKKDV 1523
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
919-1248 |
3.35e-07 |
|
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: 55.53 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 919 TKIQLEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITL-----AKIEKEKHAIENKVKNLIEemaAL 993
Cdd:pfam09731 76 TGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKekaleEVLKEAISKAESATAVAKE---AK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 994 DETILKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEK-------------KLRMDLERVK 1060
Cdd:pfam09731 153 DDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAapplldaapetppKLPEHLDNVE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1061 RKLE--GDLKLSLESVMDLEND-----KQQLEEKL--------KKKDFEMNELSTRIEDEQALVNQLQKKIKELQARtee 1125
Cdd:pfam09731 233 EKVEkaQSLAKLVDQYKELVASerivfQQELVSIFpdiipvlkEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKR--- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1126 leeeleADRACRAKVEKQRSDVARELEDLSERLEEAGGATSAQIEmnKKREAEFLKMRRDLEEAM---LHHEATTAALRK 1202
Cdd:pfam09731 310 ------EEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLR--LEFEREREEIRESYEEKLrteLERQAEAHEEHL 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1529987947 1203 KHADSVAELSEQIDSLQRVKQKLEKERSEAKMEADDLASTVEQLSK 1248
Cdd:pfam09731 382 KDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNELLANLKGLEK 427
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
985-1187 |
4.76e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 985 NLIEEMAALDETILKLTKE----KKALQEAhQQTLDDLQAEEDKVNALTKAKAkLEQQVDDLEGSLEQEKKLRMDLERVK 1060
Cdd:COG3206 165 NLELRREEARKALEFLEEQlpelRKELEEA-EAALEEFRQKNGLVDLSEEAKL-LLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1061 RKLEGDLKLSLESVMDLENDK--QQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADracra 1138
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS----- 317
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1529987947 1139 kVEKQRSDVARELEDLSERLEEAggatSAQIEMNKKREAEFLKMRRDLE 1187
Cdd:COG3206 318 -LEAELEALQAREASLQAQLAQL----EARLAELPELEAELRRLEREVE 361
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
861-1267 |
6.11e-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: 54.73 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 861 KVELAKLKEALEKSEI---KRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELMERLEDE 937
Cdd:pfam05483 404 EVELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKE 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 938 EEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDD 1017
Cdd:pfam05483 484 KLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDE 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1018 LQAEEDKVnaltkakakleqqvddlegsleqekklrmdlERVKRKLEGDLKLSLESVMDLENDKQQLEEKLKKKDFEMNE 1097
Cdd:pfam05483 564 VKCKLDKS-------------------------------EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1098 LStriEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSERLEEAGGatsaQIEMNKKREA 1177
Cdd:pfam05483 613 LH---QENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLE----EVEKAKAIAD 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1178 EFLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEAD--------DLASTVEQLSKG 1249
Cdd:pfam05483 686 EAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEielsnikaELLSLKKQLEIE 765
|
410
....*....|....*...
gi 1529987947 1250 KATSEKMCRlyEDQMNEA 1267
Cdd:pfam05483 766 KEEKEKLKM--EAKENTA 781
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1159-1939 |
6.43e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 54.67 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1159 EEAGGATSAQIEMNKKREAEFLKMRRDLEEAMLhheattaalrkkhaDSVAELSEQIDSLQRVKQKLEKERSEakmeadd 1238
Cdd:TIGR00606 229 KEAQLESSREIVKSYENELDPLKNRLKEIEHNL--------------SKIMKLDNEIKALKSRKKQMEKDNSE------- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1239 LASTVEQLSKGkaTSEKMCRLYEDQMNEAKAKADEL---QRQLNEANTqraraqaESGEVSRKLEERESMVSQLQrakns 1315
Cdd:TIGR00606 288 LELKMEKVFQG--TDEQLNDLYHNHQRTVREKERELvdcQRELEKLNK-------ERRLLNQEKTELLVEQGRLQ----- 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1316 FSQNVEELKKQLEEENKAKNALAHSLQSSRHDCDLLReQYEEEQEAKGELQRALSKANAEVAQWRTKYETDAIQRTEELE 1395
Cdd:TIGR00606 354 LQADRHQEHIRARDSLIQSLATRLELDGFERGPFSER-QIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIR 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1396 EAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNfdkVLAEWKQKYEECQSEL 1475
Cdd:TIGR00606 433 DEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKN---SLTETLKKEVKSLQNE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1476 EISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQIS--------------QGAKTIHELEKMKKGL 1541
Cdd:TIGR00606 510 KADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSdeltsllgyfpnkkQLEDWLHSKSKEINQT 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1542 EMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDVDRKLAEKDEELDnlrrkhqrsLESMQATLDAEAKSRNEAVR 1621
Cdd:TIGR00606 590 RDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESD---------LERLKEEIEKSSKQRAMLAG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1622 LKKKMEGDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLE 1701
Cdd:TIGR00606 661 ATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIID 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1702 qndrarkLAEHELLEASERvnlLHSQNTGLINQKKKLENDLSMLsnevddavqECRNAEEK-AKKAITDAAMMaEELKKE 1780
Cdd:TIGR00606 741 -------LKEKEIPELRNK---LQKVNRDIQRLKNDIEEQETLL---------GTIMPEEEsAKVCLTDVTIM-ERFQME 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1781 qdtsahLERMKKNMEQTIKDLQ-MRLDEAEQIAlkggKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELS 1859
Cdd:TIGR00606 801 ------LKDVERKIAQQAAKLQgSDLDRTVQQV----NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELK 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1860 YQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADTAETQVNKLRVRTRDQVSKL 1939
Cdd:TIGR00606 871 SEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKV 950
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1350-1941 |
6.59e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.59 E-value: 6.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1350 LLREQYEEEQEAKGELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRL 1429
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1430 QTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKR- 1508
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKk 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1509 ---ENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDVDRKLA 1585
Cdd:pfam02463 326 aekELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1586 EKDEELDNLRRK--HQRSLESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQLNHANRL-ASESQKLLRNLQIQIKDVQ 1662
Cdd:pfam02463 406 EAQLLLELARQLedLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELeLKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1663 LELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQNDRARKLAEHELLEASERVNLLHSQN----------TGLI 1732
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVevsatadeveERQK 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1733 NQKKKLENDLSMLSNEV---DDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAE 1809
Cdd:pfam02463 566 LVRALTELPLGARKLRLlipKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1810 -----QIALKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRI-------KELSYQAEEDKKNLVRLQDLID 1877
Cdd:pfam02463 646 sglrkGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRrqleikkKEQREKEELKKLKLEAEELLAD 725
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1529987947 1878 KLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADTAETQVNKLRVRTRDQVSKLAE 1941
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVE 789
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
853-1281 |
6.65e-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: 54.64 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 853 TEKELAALKVELAKLKEALEKseiKRKELEERQVSLIQEKNDLS--------LQLQAEQDNLADAEDRCDLLIKTKIQLE 924
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSE---KQKELEQNNKKIKELEKQLNqlkseisdLNNQKEQDWNKELKSELKNQEKKLEEIQ 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 925 AKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEK 1004
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1005 KALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDLENDKQQL 1084
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1085 EEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEEleadracRAKVEKQRSDVARELEDLSERLeeagga 1164
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE-------KKEKESKISDLEDELNKDDFEL------ 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1165 TSAQIEMNKKREAEFLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEADDLASTVE 1244
Cdd:TIGR04523 555 KKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK 634
|
410 420 430
....*....|....*....|....*....|....*..
gi 1529987947 1245 QLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNEA 1281
Cdd:TIGR04523 635 NIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1627-1864 |
6.97e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1627 EGDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEqnDRA 1706
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1707 RKLAEHELLEASERVnLLHSQNTG-LINQkkklENDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTsa 1785
Cdd:COG3883 93 RALYRSGGSVSYLDV-LLGSESFSdFLDR----LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE-- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1529987947 1786 hLERMKKNMEQTIKDLQMRLDEAEQialkggkkQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEE 1864
Cdd:COG3883 166 -LEAAKAELEAQQAEQEALLAQLSA--------EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1208-1848 |
7.94e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.36 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1208 VAELSEQIDSLQRVKQKLEKERSEAKMEADDLASTveqlskgkatSEKMCRLYEDQMNEAKAKADELQRQLNEANTQRaR 1287
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASA----------LKRQLDRESDRNQELQKRIRLLEKREAEAEEAL-R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1288 AQAE--------SGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKQLEEENKAKNALAHSLQSSRHDCDLLREQYEEEQ 1359
Cdd:pfam05557 73 EQAElnrlkkkyLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1360 EAKGELQRALSKANAEVAQWRT------KYETDAiqrtEELEEAKKKL--VTRLQESEEIMEASNAKCSSLEKTKHRLQT 1431
Cdd:pfam05557 153 QLRQNLEKQQSSLAEAEQRIKElefeiqSQEQDS----EIVKNSKSELarIPELEKELERLREHNKHLNENIENKLLLKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1432 EIEDLIIDLERANAAAAALDKKQRNFDKVLAewkqkyeECQSELEISQKESRGLstelfklkNSYEETLDHLETIKRENK 1511
Cdd:pfam05557 229 EVEDLKRKLEREEKYREEAATLELEKEKLEQ-------ELQSWVKLAQDTGLNL--------RSPEDLSRRIEQLQQREI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1512 NLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDVDrklaEKDEEL 1591
Cdd:pfam05557 294 VLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILE----SYDKEL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1592 DNlrrkhqrSLESMQATLDAEaksrnEAVRLKKKMEGDLNEMEVQLNHANRLASESQKLLRNLQIQIKdvqleldeTVHQ 1671
Cdd:pfam05557 370 TM-------SNYSPQLLERIE-----EAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQ--------ALRQ 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1672 NEELKEQVAVTERRNNlLAAEVEELRAlleQNDRARKlaEHELLEAS-ERVNLlhsqnTGLINQKKKLENDLSMlsNEVD 1750
Cdd:pfam05557 430 QESLADPSYSKEEVDS-LRRKLETLEL---ERQRLRE--QKNELEMElERRCL-----QGDYDPKKTKVLHLSM--NPAA 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1751 DAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHL-ERMKKNMEQTIKDLQMRLDEAEqialkggkKQVQKLEarvke 1829
Cdd:pfam05557 497 EAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLpETTSTMNFKEVLDLRKELESAE--------LKNQRLK----- 563
|
650
....*....|....*....
gi 1529987947 1830 letelDAEQKKSQEYQKVV 1848
Cdd:pfam05557 564 -----EVFQAKIQEFRDVC 577
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
849-1010 |
8.75e-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: 53.23 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 849 RSAATEKELAALKVELAKLKEALEKseiKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLL------IKTKI- 921
Cdd:COG4942 77 ELAALEAELAELEKEIAELRAELEA---QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLkylapaRREQAe 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 922 QLEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLT 1001
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*....
gi 1529987947 1002 KEKKALQEA 1010
Cdd:COG4942 234 AEAAAAAER 242
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
656-683 |
9.05e-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: 50.81 E-value: 9.05e-07
10 20
....*....|....*....|....*...
gi 1529987947 656 SQLHKENLNKLMTNLRSTQPHFVRCIIP 683
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1581-1941 |
1.07e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.03 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1581 DRKLAEKDEELDNLRRKHQRS------LESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVqlnhanRLASESQKLLRNL 1654
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAeselkeLEKKHQQLCEEKNALQEQLQAETELCAEAEEMRA------RLAARKQELEEIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1655 QIQIKDVQLELDETVH-QNEELKEQVAVTERRNNLLAAEVEELRALLEQNDRARKLAEHElleasERVNLLHSQNTGLIN 1733
Cdd:pfam01576 78 HELESRLEEEEERSQQlQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLE-----EDILLLEDQNSKLSK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1734 QKKKLENDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAeQIAL 1813
Cdd:pfam01576 153 ERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAEL-QAQI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1814 KGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEA 1893
Cdd:pfam01576 232 AELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDT 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1529987947 1894 EEQANTNLSKYRKLQHELDD----AEERADTAETQVNKLRVRTRDQVSKLAE 1941
Cdd:pfam01576 312 LDTTAAQQELRSKREQEVTElkkaLEEETRSHEAQLQEMRQKHTQALEELTE 363
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1335-1934 |
1.11e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1335 NALAHSLQSSRHDCDLLREQYEEEQEAKGELQRALSKANAEVAQWRTKYE--TDAIQRTEELEEAKKKLVTRLQESEEIM 1412
Cdd:PRK01156 186 DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDMKNRYESEIKTAESDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1413 EASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWK---QKYEECQSELEISQKEsrglstel 1489
Cdd:PRK01156 266 SMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDaeiNKYHAIIKKLSVLQKD-------- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1490 fklKNSYEETldhletiKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRI 1569
Cdd:PRK01156 338 ---YNDYIKK-------KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1570 QLELNQMKSDVDR---KLAEKDEELDNLRrKHQRSLESMQATLDAEAKSRNEAVRLKKKMEGDLnemevqLNHANRLASE 1646
Cdd:PRK01156 408 KKELNEINVKLQDissKVSSLNQRIRALR-ENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHI------INHYNEKKSR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1647 SQKLLRNLQIQIKDVqleldetvhqNEELKEQVAVTERrnnLLAAEVEELrallEQNDRARKLAEHELleaservnllhs 1726
Cdd:PRK01156 481 LEEKIREIEIEVKDI----------DEKIVDLKKRKEY---LESEEINKS----INEYNKIESARADL------------ 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1727 qntglinqkKKLENDLSMLsnevddavqecRNAEEKAKKAITDAAMMAEELKKEQDTSaHLERMKKNMEQTIKDLQMRLD 1806
Cdd:PRK01156 532 ---------EDIKIKINEL-----------KDKHDKYEEIKNRYKSLKLEDLDSKRTS-WLNALAVISLIDIETNRSRSN 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1807 EAeqialkggKKQVQKLEARVKELETELdaeqkksQEYQKVVRKYERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSY 1886
Cdd:PRK01156 591 EI--------KKQLNDLESRLQEIEIGF-------PDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNY 655
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 1887 KRQTEEAEE----------QANTNLSKYRKLQHELDDA-------EERADTAETQVNKLRVRTRD 1934
Cdd:PRK01156 656 KKQIAEIDSiipdlkeitsRINDIEDNLKKSRKALDDAkanrarlESTIEILRTRINELSDRIND 720
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1757-1898 |
1.12e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.63 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1757 RNAEEKAKKAITDAAMMAEELKKEQDTSA---------HLERMKKNMEQTIKDLQMRLDEAEQIaLKGGKKQVQKLEARV 1827
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAkeeihklrnEFEKELRERRNELQKLEKRLLQKEEN-LDRKLELLEKREEEL 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1529987947 1828 KELETELDAEQ----KKSQEYQKVVRKYERRIKELS-YQAEEDKKNLvrLQDLIDKLQVKVKSYKRQTE-EAEEQAN 1898
Cdd:PRK12704 113 EKKEKELEQKQqeleKKEEELEELIEEQLQELERISgLTAEEAKEIL--LEKVEEEARHEAAVLIKEIEeEAKEEAD 187
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
967-1168 |
1.14e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 967 ITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSL 1046
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1047 E------QEKKLRMD-----------------LERVKRKLEGDLKLslesVMDLENDKQQLEEKLKKKDFEMNELSTRIE 1103
Cdd:COG3883 89 GeraralYRSGGSVSyldvllgsesfsdfldrLSALSKIADADADL----LEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 1104 DEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSERLEEAGGATSAQ 1168
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
969-1468 |
1.15e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 969 LAKIEKEKHAIENK-VKNLIEEMAALDETILKLtKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLE---- 1043
Cdd:COG4717 48 LERLEKEADELFKPqGRKPELNLKELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllq 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1044 --GSLEQEKKLRMDLERVKRKLEgDLKLSLESVMDLENDKQQLEEKLKKKDFEMNELstRIEDEQALVNQLQKKIKELQA 1121
Cdd:COG4717 127 llPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEEL--LEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1122 RTEELEEELEADRACRAKVEKQRSDVAR-----ELEDLSERLEEAGGATSAQIEMnkkreAEFLKMRRDLEEAMLHHEAT 1196
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQlenelEAAALEERLKEARLLLLIAAAL-----LALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1197 TAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEADDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQR 1276
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1277 QLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAknsfsqnveelkkqleeenkaknalahslqssrhdcdllrEQYE 1356
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA----------------------------------------EEYQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1357 EEQEAKGELQRALSKANAEVAQWRTKYETDAI-QRTEELEEAKKKLVTRLQESEEIMEASNAKCSSLEK--TKHRLQTEI 1433
Cdd:COG4717 399 ELKEELEELEEQLEELLGELEELLEALDEEELeEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQEL 478
|
490 500 510
....*....|....*....|....*....|....*
gi 1529987947 1434 EDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKY 1468
Cdd:COG4717 479 EELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
851-1033 |
1.17e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 851 AATEKELAALKVELAKLKEALEKseiKRKELEERQVSLIQEKNDLS-LQLQAEQDNLADAEDRCDLLIktkiQLEAKVKE 929
Cdd:COG3883 61 EALQAEIDKLQAEIAEAEAEIEE---RREELGERARALYRSGGSVSyLDVLLGSESFSDFLDRLSALS----KIADADAD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 930 LMERLEDEEEmssNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALQE 1009
Cdd:COG3883 134 LLEELKADKA---ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
170 180
....*....|....*....|....
gi 1529987947 1010 AHQQTLDDLQAEEDKVNALTKAKA 1033
Cdd:COG3883 211 AAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1671-1853 |
1.24e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1671 QNEELKEQVAVTERRNNLLAAEVEELRALLEQNDRARK--LAEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNE 1748
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1749 VDdAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNMEQTIKDLQMRLDEAEQIALKGGKK 1818
Cdd:COG3206 242 LA-ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEA 320
|
170 180 190
....*....|....*....|....*....|....*
gi 1529987947 1819 QVQKLEARVKELETELDAEQKKSQEYQKVVRKYER 1853
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1593-1841 |
1.35e-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: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1593 NLRRKHQRSLESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQLnhanrlaSESQKLLRNLQIQIKDVQLELDETVHQN 1672
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------AALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1673 EELKEQvavterrnnlLAAEVEELRALLEQNDRARKLAEHELL-------EASERVNLLHSQNTGLINQKKKLENDLsml 1745
Cdd:COG4942 93 AELRAE----------LEAQKEELAELLRALYRLGRQPPLALLlspedflDAVRRLQYLKYLAPARREQAEELRADL--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1746 snevdDAVQECRNAEEKAKKAITDAAMMAEELKKEqdtsahLERMKKNMEQTIKDLQMRLDEAEQiALKGGKKQVQKLEA 1825
Cdd:COG4942 160 -----AELAALRAELEAERAELEALLAELEEERAA------LEALKAERQKLLARLEKELAELAA-ELAELQQEAEELEA 227
|
250
....*....|....*.
gi 1529987947 1826 RVKELETELDAEQKKS 1841
Cdd:COG4942 228 LIARLEAEAAAAAERT 243
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1257-1924 |
1.39e-06 |
|
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: 53.69 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1257 CRLYEDQMNEAkAKADELQRQLNEANTQRARAQAESGEV---SRKLEERESMVSQLQRAKNS-FSQNVEELKKQLEEENK 1332
Cdd:pfam12128 230 IQAIAGIMKIR-PEFTKLQQEFNTLESAELRLSHLHFGYksdETLIASRQEERQETSAELNQlLRTLDDQWKEKRDELNG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1333 AKNALAHSLQSSRHDCDLLREQ---YEEE--QEAKGELQRALS-KANAEVAQWRTKYETDAIQRTEELEEAKKKLVTrlQ 1406
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQhgaFLDAdiETAAADQEQLPSwQSELENLEERLKALTGKHQDVTAKYNRRRSKIK--E 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1407 ESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLE-----RANAAAAALDKKQRNFDKVLAEWK---------------- 1465
Cdd:pfam12128 387 QNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALEselreQLEAGKLEFNEEEYRLKSRLGELKlrlnqatatpelllql 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1466 -QKYEEC---QSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGL 1541
Cdd:pfam12128 467 eNFDERIeraREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1542 emekteiqaaLEEAEGTLEHEEsKTLRIQLelnqmksdvdrklaekDEELDNLRRKHQRSLESMqaTLDAEAKSRNEAVR 1621
Cdd:pfam12128 547 ----------WEQSIGKVISPE-LLHRTDL----------------DPEVWDGSVGGELNLYGV--KLDLKRIDVPEWAA 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1622 LKKKMEGDLNEME--VQLNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERRNnllaaeveELRAL 1699
Cdd:pfam12128 598 SEEELRERLDKAEeaLQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQS--------EKDKK 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1700 LEQNDRARKLAEHELleaservnllhsqnTGLINQKKKLENDLSMLSNEVDDAVQECRNAEEKAKKAI---TDAAMMAEE 1776
Cdd:pfam12128 670 NKALAERKDSANERL--------------NSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVegaLDAQLALLK 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1777 LKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIAlkggkkqvqKLEARVKELETELDAEQKKSQEyqkvVRKYERRIK 1856
Cdd:pfam12128 736 AAIAARRSGAKAELKALETWYKRDLASLGVDPDVIA---------KLKREIRTLERKIERIAVRRQE----VLRYFDWYQ 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1857 E--------LSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQ-------TEEAEEQANTNLSKYRKLQHELDDAEERADTA 1921
Cdd:pfam12128 803 EtwlqrrprLATQLSNIERAISELQQQLARLIADTKLRRAKlemerkaSEKQQVRLSENLRGLRCEMSKLATLKEDANSE 882
|
...
gi 1529987947 1922 ETQ 1924
Cdd:pfam12128 883 QAQ 885
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1382-1941 |
1.57e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1382 KYETDAIQRTEELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDKVL 1461
Cdd:TIGR00618 177 QYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1462 aEWKQKYEECQSELEISQKESRGLS--TELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKK 1539
Cdd:TIGR00618 257 -KKQQLLKQLRARIEELRAQEAVLEetQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1540 ----GLEMEKTEIQAALEEAEGTLEHEESKTLRIQLElnQMKSDVDRKLA-----EKDEELDNLRRKHQRSLESMQATLD 1610
Cdd:TIGR00618 336 qqssIEEQRRLLQTLHSQEIHIRDAHEVATSIREISC--QQHTLTQHIHTlqqqkTTLTQKLQSLCKELDILQREQATID 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1611 AEAKSRN----EAVRLKKKMEGDLNEMEVQLNHA----------NRLASESQKLLRNLQIQIKDVqleldETVHQNEELK 1676
Cdd:TIGR00618 414 TRTSAFRdlqgQLAHAKKQQELQQRYAELCAAAItctaqcekleKIHLQESAQSLKEREQQLQTK-----EQIHLQETRK 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1677 EQVavterrnnllaaeveELRALLEQNDRARKLAEHELLEASERVNLLHSQNT-----GLINQKKKLENDLSMLSNEVDD 1751
Cdd:TIGR00618 489 KAV---------------VLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLtrrmqRGEQTYAQLETSEEDVYHQLTS 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1752 AVQECRNAEEKAKKAITDAAMMAEelkKEQDTSAHLERMKkNMEQTIKDLQMRLDEAEQIALKGGKKQVQKLEARVKELE 1831
Cdd:TIGR00618 554 ERKQRASLKEQMQEIQQSFSILTQ---CDNRSKEDIPNLQ-NITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1832 TELDaEQKKSQEYQKVVRKYERRIKELSYQAEEDKKNLVRL---------QDLIDKLQVKVKSYK------RQTEEAEEQ 1896
Cdd:TIGR00618 630 VRLH-LQQCSQELALKLTALHALQLTLTQERVREHALSIRVlpkellasrQLALQKMQSEKEQLTywkemlAQCQTLLRE 708
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1529987947 1897 ANTNLSKYRKLQHELDDA--------EERADTAETQVNKLRVRTRDQVSKLAE 1941
Cdd:TIGR00618 709 LETHIEEYDREFNEIENAssslgsdlAAREDALNQSLKELMHQARTVLKARTE 761
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
921-1228 |
2.24e-06 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 52.93 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 921 IQLEAKVKELMERLEDEEEMSSNvlAKKRKLEDECAELKKDIDdLEITLAKIEKekhAIENKVKNLIEEMA--------- 991
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSK--PSELALNEMIEKLKKEID-LEYTEAVIAM---GLQERLENLREEFSkansqdqlm 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 992 --ALDETILKLTKE-KKALQEAHQQTldDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLR--MDLERVKRKLEG- 1065
Cdd:PLN03229 506 hpVLMEKIEKLKDEfNKRLSRAPNYL--SLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKevMDRPEIKEKMEAl 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1066 -----DLKLSLESVMDlENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKElqarteeleeeLEADRACRAKV 1140
Cdd:PLN03229 584 kaevaSSGASSGDELD-DDLKEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKDTAE-----------QTPPPNLQEKI 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1141 EKQRSDVARELEDLSE-----------RLEEAGGATSAQIEMNKKREAEFLKMRRDLEEAMlhheaTTAALRKKHADSVA 1209
Cdd:PLN03229 652 ESLNEEINKKIERVIRssdlkskiellKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEAL-----NSSELKEKFEELEA 726
|
330
....*....|....*....
gi 1529987947 1210 ELSEQIDSLQRVKQKLEKE 1228
Cdd:PLN03229 727 ELAAARETAAESNGSLKND 745
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
926-1185 |
2.34e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 52.62 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 926 KVKELMERLEDEeeMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEkhaienkVKNLIEEMAALDETILKLTKEKK 1005
Cdd:PRK05771 54 KLSEALDKLRSY--LPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1006 ALQ--EAHQQTLDDLQAEED---KVNALTKAKAKLEQQVDDLEGSLEqekklrmdlerVKRKLEGDLKLslesVMDLEND 1080
Cdd:PRK05771 125 RLEpwGNFDLDLSLLLGFKYvsvFVGTVPEDKLEELKLESDVENVEY-----------ISTDKGYVYVV----VVVLKEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1081 KQQLEEKLKKKDFEMNELSTrIEDEQALVNQLQKKIKELqarteeleeeleadracrakvEKQRSDVARELEDLSERLEE 1160
Cdd:PRK05771 190 SDEVEEELKKLGFERLELEE-EGTPSELIREIKEELEEI---------------------EKERESLLEELKELAKKYLE 247
|
250 260
....*....|....*....|....*
gi 1529987947 1161 AGGATSAQIEMNKKREAEFLKMRRD 1185
Cdd:PRK05771 248 ELLALYEYLEIELERAEALSKFLKT 272
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
978-1163 |
2.75e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 978 AIENKVKNLIEeMAALDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLrmdLE 1057
Cdd:COG1579 1 AMPEDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---IK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1058 RVKRKLEG--------DLKLSLESvmdLENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEE 1129
Cdd:COG1579 77 KYEEQLGNvrnnkeyeALQKEIES---LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180 190
....*....|....*....|....*....|....*
gi 1529987947 1130 LEADRA-CRAKVEKQRSDVARELEDLSERLEEAGG 1163
Cdd:COG1579 154 LEAELEeLEAEREELAAKIPPELLALYERIRKRKN 188
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1479-1928 |
2.79e-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: 52.52 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1479 QKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQI-SQGAKTIHELEKMKKGLEMekTEIQAALEEAEG 1557
Cdd:pfam10174 122 QSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLqSKGLPKKSGEEDWERTRRI--AEAEMQLGHLEV 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1558 TLEHEESKTLRIQLEL---NQMKSDVDRKLA------EKDEELDNLRRKHqRSLESMQATLDAEAKSRNEavrlkkKMEG 1628
Cdd:pfam10174 200 LLDQKEKENIHLREELhrrNQLQPDPAKTKAlqtvieMKDTKISSLERNI-RDLEDEVQMLKTNGLLHTE------DREE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1629 DLNEMEVQLNHANRLASESQKLLRNLQ---IQIKDVQLELDETVHQN-------EELKEQVAVTERRNNLLAAEVEELRA 1698
Cdd:pfam10174 273 EIKQMEVYKSHSKFMKNKIDQLKQELSkkeSELLALQTKLETLTNQNsdckqhiEVLKESLTAKEQRAAILQTEVDALRL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1699 LLEQ-----NDRARKLAE---------------HELLEASER-VNLLHsqntglinqkKKLENdlsmLSNEVDDAVQECR 1757
Cdd:pfam10174 353 RLEEkesflNKKTKQLQDlteekstlageirdlKDMLDVKERkINVLQ----------KKIEN----LQEQLRDKDKQLA 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1758 NAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNM-EQTIKDLQMRLDEAEQI--ALKGGKKQVQKLEARVKELETEL 1834
Cdd:pfam10174 419 GLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESLkkENKDLKEKVSALQPELTEKESSL 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1835 DAEQKKSQEYQKVVRKYERRIKELSYQAEEDKKNLVRLQDlidklqvkvKSYKRQTEEAEEQANTNLS-KYRKLQHELDD 1913
Cdd:pfam10174 499 IDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLEN---------QLKKAHNAEEAVRTNPEINdRIRLLEQEVAR 569
|
490
....*....|....*
gi 1529987947 1914 AEERADTAETQVNKL 1928
Cdd:pfam10174 570 YKEESGKAQAEVERL 584
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
906-1067 |
3.30e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 906 LADAEDRCDLLIKTKIQLEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIE---------KEK 976
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvrnnKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 977 HAIENKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNALtkaKAKLEQQVDDLEgslEQEKKLRMDL 1056
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELE---AELEELEAER 165
|
170
....*....|.
gi 1529987947 1057 ERVKRKLEGDL 1067
Cdd:COG1579 166 EELAAKIPPEL 176
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1501-1740 |
3.41e-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: 51.69 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1501 DHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKsdv 1580
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1581 dRKLAEKDEELDNLRRKHQRSLESMQATLDAEAKSRNEAVRLKKKMegdlnemevqlnhaNRLASESQKLLRNLQIQIKD 1660
Cdd:COG4942 97 -AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL--------------KYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1661 VQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQNDRARKLAEHELLEASERVNLLHSQNTGLINQKKKLEN 1740
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
858-1519 |
4.26e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 858 AALKVELAKLKEALEKSEIKRKELEERQVSliQEKNDLSLQLQAEQDNLADAEDR-----CDLLIKTKIQLEAKVKELME 932
Cdd:pfam05483 99 AELKQKENKLQENRKIIEAQRKAIQELQFE--NEKVSLKLEEEIQENKDLIKENNatrhlCNLLKETCARSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 933 RLEDEEEMSSN----------------VLAKKRKLEDEcAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDET 996
Cdd:pfam05483 177 EREETRQVYMDlnnniekmilafeelrVQAENARLEMH-FKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENK 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 997 ILKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKlrmdlerVKRKLEGDLKLSLESVMD 1076
Cdd:pfam05483 256 MKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMS-------TQKALEEDLQIATKTICQ 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1077 LENDKQ-QLEEKLKKK---DFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELE 1152
Cdd:pfam05483 329 LTEEKEaQMEELNKAKaahSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1153 DLSERLEEaggatsAQIEMNKKREAEflkmrrDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEA 1232
Cdd:pfam05483 409 ELKKILAE------DEKLLDEKKQFE------KIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1233 KMEADDlastvEQLSKGKATSEKMCRLYEDQ--MNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQ 1310
Cdd:pfam05483 477 KTELEK-----EKLKNIELTAHCDKLLLENKelTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELE 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1311 RAKNSFSQN-------VEELKKQLEEENKAKNALAHSLQSSRHDCDLLREQYEEEQEAKGELQ---RALSKANAEVAQWR 1380
Cdd:pfam05483 552 SVREEFIQKgdevkckLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHqenKALKKKGSAENKQL 631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1381 TKYETDAIQRTEELEEAKKKL------------VTRLQESEEIMEASNAKCSSLEKTKhrLQTEIEDLIidLERANAAAA 1448
Cdd:pfam05483 632 NAYEIKVNKLELELASAKQKFeeiidnyqkeieDKKISEEKLLEEVEKAKAIADEAVK--LQKEIDKRC--QHKIAEMVA 707
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1529987947 1449 ALDKKQRNFDKVLAE-------WKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITD 1519
Cdd:pfam05483 708 LMEKHKHQYDKIIEErdselglYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
847-1246 |
4.61e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 847 LLRSAAT-EKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEdrcdlliktKI-QLE 924
Cdd:PRK04863 284 HLEEALElRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQE---------KIeRYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 925 AKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAK-----IEKEKHAIE-NKVKNLIEEMAALDEtIL 998
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADyqqalDVQQTRAIQyQQAVQALERAKQLCG-LP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 999 KLTKEKkaLQEAHQQtlddLQAEEDkvnALTKAKAKLEQQVDDLEGSLEQEKKLrmdLERVkRKLEGDlklslesvMDLE 1078
Cdd:PRK04863 434 DLTADN--AEDWLEE----FQAKEQ---EATEELLSLEQKLSVAQAAHSQFEQA---YQLV-RKIAGE--------VSRS 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1079 NDKQQLEEKLkkKDFEmnelSTRIEDEQalVNQLQKKIKELQARTEELEEELEA-DRACraKVEKQRSDVARELEDLSER 1157
Cdd:PRK04863 493 EAWDVARELL--RRLR----EQRHLAEQ--LQQLRMRLSELEQRLRQQQRAERLlAEFC--KRLGKNLDDEDELEQLQEE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1158 LEEAGGATSAQIEMNKKREAEflkMRRDLEEamlhHEATTAALRKK----HA--DSVAELSEQ----IDSLQRV----KQ 1223
Cdd:PRK04863 563 LEARLESLSESVSEARERRMA---LRQQLEQ----LQARIQRLAARapawLAaqDALARLREQsgeeFEDSQDVteymQQ 635
|
410 420
....*....|....*....|...
gi 1529987947 1224 KLEKERsEAKMEADDLASTVEQL 1246
Cdd:PRK04863 636 LLERER-ELTVERDELAARKQAL 657
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1585-1816 |
5.14e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1585 AEKDEELDNLRRKHQRSLESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLE 1664
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1665 LDEtvhQNEELKEQVAVTERRNN------LLAAE----VEELRALLEQNDRARKLAEHELLEASERvnlLHSQNTGLINQ 1734
Cdd:COG4942 99 LEA---QKEELAELLRALYRLGRqpplalLLSPEdfldAVRRLQYLKYLAPARREQAEELRADLAE---LAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1735 KKKLENDLsmlsnevdDAVQECRNAEEKAKKAITDA-AMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIAL 1813
Cdd:COG4942 173 RAELEALL--------AELEEERAALEALKAERQKLlARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
...
gi 1529987947 1814 KGG 1816
Cdd:COG4942 245 AAG 247
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
952-1168 |
5.41e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 952 EDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALQEAhqqtLDDLQAEEDKVNALTKA 1031
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1032 KAKLEQQVDDLEGSLE-----------------------QEKKLRMDLERVKRKLEgDLKLSLESVM-DLENDKQQLEEK 1087
Cdd:COG3883 91 RARALYRSGGSVSYLDvllgsesfsdfldrlsalskiadADADLLEELKADKAELE-AKKAELEAKLaELEALKAELEAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1088 LKkkdfemnELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSERLEEAGGATSA 1167
Cdd:COG3883 170 KA-------ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
.
gi 1529987947 1168 Q 1168
Cdd:COG3883 243 A 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1688-1927 |
6.39e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1688 LLAAEVEELRALLEQNDRARKLAEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDAVQECRNAEEKAKKAI 1767
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1768 TDAAMMAEELKKEQDTSAHLER-MKKNMEQTIKDLQMRLDEAEQIA---------LKGGKKQVQKLEARVKELETELDAE 1837
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRaLYRLGRQPPLALLLSPEDFLDAVrrlqylkylAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1838 QKKSQEYQKVVRKYERRIKELsyQAEEDKKnlvrlQDLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEER 1917
Cdd:COG4942 170 EAERAELEALLAELEEERAAL--EALKAER-----QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|
gi 1529987947 1918 ADTAETQVNK 1927
Cdd:COG4942 243 TPAAGFAALK 252
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1079-1245 |
6.45e-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: 49.54 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1079 NDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSERL 1158
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1159 EEAGG-----ATSAQIEMNKKREAEFLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAK 1233
Cdd:COG1579 83 GNVRNnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|..
gi 1529987947 1234 MEADDLASTVEQ 1245
Cdd:COG1579 163 AEREELAAKIPP 174
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1262-1715 |
6.51e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1262 DQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNveelkkqleeenKAKNALAHSL 1341
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY------------QELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1342 QSSRHDCDLLREQYEEEQEakgeLQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQESEEIMEASNAKCSS 1421
Cdd:COG4717 142 AELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1422 LEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFD-----KVLAEWKQKYEECQSELEISQ-------KESRGLSTEL 1489
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARLLLLIaaallALLGLGGSLLSLILTIAGVLFlvlgllaLLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1490 FKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLri 1569
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL-- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1570 qLELNQMKSDVD-RKLAEKDEELDNLRRKhqrsLESMQATLDAEAKSRNEAVRlkkkmEGDLNEMEVQLNHANRLASESQ 1648
Cdd:COG4717 376 -LAEAGVEDEEElRAALEQAEEYQELKEE----LEELEEQLEELLGELEELLE-----ALDEEELEEELEELEEELEELE 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1529987947 1649 KLLRNLQIQIKDVQLELD--ETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQNDRARKLAEHELL 1715
Cdd:COG4717 446 EELEELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1560-1935 |
6.51e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1560 EHEESKTLRIQLELNQMKSDVDRKLAEKDEELDNLRRK---HQRSLESMQATLDAeAKSR----NEAVRLKKKME---GD 1629
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARElaeLNEAESDLEQDYQA-ASDHlnlvQTALRQQEKIEryqAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1630 LNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELDEtvhqneeLKEQVAVTERrnnllAAEVEELRALLEQN-----D 1704
Cdd:PRK04863 357 LEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDE-------LKSQLADYQQ-----ALDVQQTRAIQYQQavqalE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1705 RARKLAEHELLEASERVNLLHSqntgLINQKKKLENDLSMLSNEVDDAvQECRNAEEKAKKAIT---------DAAMMAE 1775
Cdd:PRK04863 425 RAKQLCGLPDLTADNAEDWLEE----FQAKEQEATEELLSLEQKLSVA-QAAHSQFEQAYQLVRkiagevsrsEAWDVAR 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1776 ELKKEQDTSAHLErmkknmeQTIKDLQMRLDEAEQialkgGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRI 1855
Cdd:PRK04863 500 ELLRRLREQRHLA-------EQLQQLRMRLSELEQ-----RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARL 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1856 KELSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQtEEAEEQANTNLSKYRKLQHE-LDDAEE----RADTAE----TQVN 1926
Cdd:PRK04863 568 ESLSESVSEARERRMALRQQLEQLQARIQRLAAR-APAWLAAQDALARLREQSGEeFEDSQDvteyMQQLLErereLTVE 646
|
....*....
gi 1529987947 1927 KLRVRTRDQ 1935
Cdd:PRK04863 647 RDELAARKQ 655
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1761-1941 |
6.99e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1761 EKAKKAITdaamMAEELKKEQDTSAHLERmkKNMEQTIKDLQMRLDEAEQiALKGGKKQVQKLEARVKELETELDAEQKK 1840
Cdd:COG1196 210 EKAERYRE----LKEELKELEAELLLLKL--RELEAELEELEAELEELEA-ELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1841 SQEYQKVVRKYERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADT 1920
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180
....*....|....*....|.
gi 1529987947 1921 AETQVNKLRVRTRDQVSKLAE 1941
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEE 383
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1480-1930 |
7.09e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1480 KESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQ--GAKTIHELEKMKKGLEMEKTEIQAALEEAEG 1557
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1558 TLEHEESKtlriQLELNQMKSDVDRKLAEKDEELDNLRRKHQRSLESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQL 1637
Cdd:COG4717 154 RLEELREL----EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1638 NHAN---RLASESQKLLRNLQIQ-IKDVQLELDETVHQNEELKEQVAvterrnNLLAAEVEELRALLEQNDRARKLAEHE 1713
Cdd:COG4717 230 EQLEnelEAAALEERLKEARLLLlIAAALLALLGLGGSLLSLILTIA------GVLFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1714 LLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDAVQECRNAEEKAKKaitdaammAEELKKEQDTSAHLERMKKN 1793
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE--------AEELEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1794 MEQTIKDlqmrlDEAEQIALKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKyerriKELSYQAEEDKKNLVRLQ 1873
Cdd:COG4717 376 LAEAGVE-----DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELEELE 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1529987947 1874 DLIDKLQVKVKSYKRQTEEAEEQAntnlsKYRKLQHELDDAEERADTAETQVNKLRV 1930
Cdd:COG4717 446 EELEELREELAELEAELEQLEEDG-----ELAELLQELEELKAELRELAEEWAALKL 497
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
848-1314 |
7.66e-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: 7.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 848 LRSAATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSL----QLQAEQDNLADAEDRC--------DL 915
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdrleQLEREIERLERELEERerrrarleAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 916 LIKTKIQLEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALde 995
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL-- 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 996 tilkltkeKKALQEAHQQTLDDLQ--------AEEDKV--NALTKA--KAKL-----EQQVDDLEGSLEQEK-KLRMDLE 1057
Cdd:COG4913 446 --------RDALAEALGLDEAELPfvgelievRPEEERwrGAIERVlgGFALtllvpPEHYAAALRWVNRLHlRGRLVYE 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1058 RVKRKLEGDLKLSLesvmdlenDKQQLEEKLKKKD--------FEMNELSTRI--EDEQALvNQLQKKI-KELQARTEEL 1126
Cdd:COG4913 518 RVRTGLPDPERPRL--------DPDSLAGKLDFKPhpfrawleAELGRRFDYVcvDSPEEL-RRHPRAItRAGQVKGNGT 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1127 EEELEADRACR-------------AKVEKQRSDVARELEDLSERLEEAGGATSAqieMNKKREA-----EFLKMRRDLEE 1188
Cdd:COG4913 589 RHEKDDRRRIRsryvlgfdnraklAALEAELAELEEELAEAEERLEALEAELDA---LQERREAlqrlaEYSWDEIDVAS 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1189 AMLHHEATTAALRKKHADS--VAELSEQIDSLQRVKQKLEKERSEAKMEADDLASTVEQLskgkatsEKMCRLYEDQMNE 1266
Cdd:COG4913 666 AEREIAELEAELERLDASSddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA-------EEELDELQDRLEA 738
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1529987947 1267 AKAKADELQRQLNEANTQRARAQAESGEVSRKLE-ERESMVSQLQRAKN 1314
Cdd:COG4913 739 AEDLARLELRALLEERFAAALGDAVERELRENLEeRIDALRARLNRAEE 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1359-1590 |
7.74e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1359 QEAKGELQRALSKANAEVAQwrtkyetdAIQRTEELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLII 1438
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAE--------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1439 DLERANAAaaaLDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIT 1518
Cdd:COG4942 91 EIAELRAE---LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1529987947 1519 DLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDVDRKLAEKDEE 1590
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1101-1675 |
8.50e-06 |
|
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: 50.91 E-value: 8.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1101 RIEDEQALVNQ--LQKKIKeLQARTEELEEELEADRACRAKVEKQRSDVARElEDLSERLEEAGgatsaqiemnkkreae 1178
Cdd:pfam07111 77 RLEEEVRLLREtsLQQKMR-LEAQAMELDALAVAEKAGQAEAEGLRAALAGA-EMVRKNLEEGS---------------- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1179 flkmRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLE-------KERSEAKMEAD----DLASTVEQLS 1247
Cdd:pfam07111 139 ----QRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkrageaKQLAEAQKEAEllrkQLSKTQEELE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1248 KGKATSEKMCRLYEDQM-NEAKAKADELQRQ-----LNEANTQRARAQA------------------ESGEVSRKLEERE 1303
Cdd:pfam07111 215 AQVTLVESLRKYVGEQVpPEVHSQTWELERQelldtMQHLQEDRADLQAtvellqvrvqslthmlalQEEELTRKIQPSD 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1304 SMVSQLQRAKNSFSQNVEELKKQLEEENKAKNaLAH--SLQSSRHDCDLLREQYEEEQEAKGELQRALSKANAEVAQWRT 1381
Cdd:pfam07111 295 SLEPEFPKKCRSLLNRWREKVFALMVQLKAQD-LEHrdSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERM 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1382 KYETDAIQrTEELEEAKKKLVTRLQESEE----IMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNF 1457
Cdd:pfam07111 374 SAKGLQME-LSRAQEARRRQQQQTASAEEqlkfVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLM 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1458 DKVLAEWKQKYEEC-------------QSELEISQKESRGLSTEL-FKLKNSYEETLDHLETIKRENKNLQEEITDLTDQ 1523
Cdd:pfam07111 453 ARKVALAQLRQESCpppppappvdadlSLELEQLREERNRLDAELqLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1524 ISQGAKTI----HELEKMKKGlEMEKTEIQAALEEaEGTLEHE------ESKTLRIQLELNQMKSDVDRKLAEKdeeldn 1593
Cdd:pfam07111 533 LQRAQESLasvgQQLEVARQG-QQESTEEAASLRQ-ELTQQQEiygqalQEKVAEVETRLREQLSDTKRRLNEA------ 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1594 lRRKHQRSLESMQATLDAEAKSRNEAVRLKKKMEgdlnemEVQLNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNE 1673
Cdd:pfam07111 605 -RREQAKAVVSLRQIQHRATQEKERNQELRRLQD------EARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQQ 677
|
..
gi 1529987947 1674 EL 1675
Cdd:pfam07111 678 RL 679
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
860-1226 |
8.77e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.98 E-value: 8.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 860 LKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLiktkiqlEAKVKELMERLEDEEE 939
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL-------QTEVDALRLRLEEKES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 940 MSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALQEAHQQ------ 1013
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtalt 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1014 TLDDLQAEEDKV-NALTKAKAKLEQQVDDlegSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDLENDKQQLEEKLKKKD 1092
Cdd:pfam10174 440 TLEEALSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKD 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1093 FEMN----ELSTRIEDEQALVNQLQK--------KIKE---LQARTEELEEELEADRACRAKVEKQR-----SDVARELE 1152
Cdd:pfam10174 517 SKLKsleiAVEQKKEECSKLENQLKKahnaeeavRTNPeinDRIRLLEQEVARYKEESGKAQAEVERllgilREVENEKN 596
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1529987947 1153 DLSERLEEAGGATSAQIEMNKKREAEF----LKMRRDLEEAMLHHEATTAALRKKHADSvaELSEQIDSLQRVKQKLE 1226
Cdd:pfam10174 597 DKDKKIAELESLTLRQMKEQNKKVANIkhgqQEMKKKGAQLLEEARRREDNLADNSQQL--QLEELMGALEKTRQELD 672
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1465-1825 |
9.09e-06 |
|
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: 50.73 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1465 KQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKREN----KNLQEEITDLTDQISQGAKTIHELEK---M 1537
Cdd:COG5185 228 IINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENaessKRLNENANNLIKQFENTKEKIAEYTKsidI 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1538 KKGLEMEKTEIQAALEEAEGT--LEHEESKTLRIQLELNQMKSDVDRKLAEKDEELDNLRRKHQRSlesmqatlDAEAKS 1615
Cdd:COG5185 308 KKATESLEEQLAAAEAEQELEesKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELS--------KSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1616 RNEAVRLKKKMEGDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQV--AVTERRNNLLAAEV 1693
Cdd:COG5185 380 DSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLneLISELNKVMREADE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1694 EELRALLEQNDRARKLAEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMM 1773
Cdd:COG5185 460 ESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIL 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1529987947 1774 AEElKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQKLEA 1825
Cdd:COG5185 540 ALE-NLIPASELIQASNAKTDGQAANLRTAVIDELTQYLSTIESQQAREDPI 590
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1639-1866 |
1.30e-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: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1639 HANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQndrarklAEHELLEAS 1718
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-------AEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1719 ERVN--LLHSQNTGLINqkkkleNDLSML--SNEVDDAVQECrnaeEKAKKAITDAAMMAEELKKEQDTsahLERMKKNM 1794
Cdd:COG3883 86 EELGerARALYRSGGSV------SYLDVLlgSESFSDFLDRL----SALSKIADADADLLEELKADKAE---LEAKKAEL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1529987947 1795 EQTIKDLQMRLDEAEQiALKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEEDK 1866
Cdd:COG3883 153 EAKLAELEALKAELEA-AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
847-1702 |
1.36e-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: 50.34 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 847 LLRSAAT-EKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAE--DRC-----DLLIK 918
Cdd:COG3096 283 LSERALElRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEkiERYqedleELTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 919 TKIQLEAkVKELMERLEDEEEmssnvlaKKRKLEDECAELKKDIDDL-------------------------------EI 967
Cdd:COG3096 363 LEEQEEV-VEEAAEQLAEAEA-------RLEAAEEEVDSLKSQLADYqqaldvqqtraiqyqqavqalekaralcglpDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 968 TLAKIEKEKHAIENKVKNLIEEMAALdETILKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQ---------- 1037
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLEL-EQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRyrsqqalaqr 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1038 ------QVDDLEGSLEQEKKLRMDLERVKRKLEGDLklslESVMDLENDKQQLEEKLKkkdfemnELSTRIEDEQALVNQ 1111
Cdd:COG3096 514 lqqlraQLAELEQRLRQQQNAERLLEEFCQRIGQQL----DAAEELEELLAELEAQLE-------ELEEQAAEAVEQRSE 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1112 LQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSErleeaggaTSAQIEMNKKREAEFLKMRRDLEEAml 1191
Cdd:COG3096 583 LRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQE--------VTAAMQQLLEREREATVERDELAAR-- 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1192 hHEATTAALRKKHADSVAELSEqidsLQRVKQKLEKER-SE----------AKMEA-----------DDLASTVEQLSKG 1249
Cdd:COG3096 653 -KQALESQIERLSQPGGAEDPR----LLALAERLGGVLlSEiyddvtledaPYFSAlygparhaivvPDLSAVKEQLAGL 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1250 KATSEKmcrLY-----EDQMNEAKAKADEL---------QRQLN------------EANTQRARA-QAESGEVSRKLEER 1302
Cdd:COG3096 728 EDCPED---LYliegdPDSFDDSVFDAEELedavvvklsDRQWRysrfpevplfgrAAREKRLEElRAERDELAEQYAKA 804
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1303 ESMVSQLQRAKNSFSQNVeelkkqleeenkaknalahslqsSRHDCDLLREQYEEE----QEAKGELQRALSKANAEVAQ 1378
Cdd:COG3096 805 SFDVQKLQRLHQAFSQFV-----------------------GGHLAVAFAPDPEAElaalRQRRSELERELAQHRAQEQQ 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1379 WRTKY---------------------ETDAIQRTEELEEAkkklVTRLQESEEIMEASNAKCSSLEKTKHRLQT---EIE 1434
Cdd:COG3096 862 LRQQLdqlkeqlqllnkllpqanllaDETLADRLEELREE----LDAAQEAQAFIQQHGKALAQLEPLVAVLQSdpeQFE 937
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1435 DLIIDLERANAAAAALdkKQRNFdkVLAEWKQK-----YEECQSELEisqkESRGLSTELfklknsyEETLDHLETIKRE 1509
Cdd:COG3096 938 QLQADYLQAKEQQRRL--KQQIF--ALSEVVQRrphfsYEDAVGLLG----ENSDLNEKL-------RARLEQAEEARRE 1002
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1510 NKNLQEEITDLTDQISQ---------GAK--TIHELEKmkkglEMEKTEIQAAlEEAEGTlEHEESKTLRIQLELN-QMK 1577
Cdd:COG3096 1003 AREQLRQAQAQYSQYNQvlaslkssrDAKqqTLQELEQ-----ELEELGVQAD-AEAEER-ARIRRDELHEELSQNrSRR 1075
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1578 SDVDRKLAEKDEELDNLRRKHQRSLESMQA--TLDAEAKSRNEAV-RLKKK--MEGDLNEMEVQLNHANRLASESQKLLR 1652
Cdd:COG3096 1076 SQLEKQLTRCEAEMDSLQKRLRKAERDYKQerEQVVQAKAGWCAVlRLARDndVERRLHRRELAYLSADELRSMSDKALG 1155
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1653 NLQIQIKDvqlelDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQ 1702
Cdd:COG3096 1156 ALRLAVAD-----NEHLRDALRLSEDPRRPERKVQFYIAVYQHLRERIRQ 1200
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1049-1476 |
1.93e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1049 EKKLRMDLERVKRKLEGDLKLSLESVMDLENDKQQLEEKLKkkdfEMNELSTRIEDEQALVNQLQKKIKELQARTEELEE 1128
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1129 ELEAdracrAKVEKQRSDVARELEDLSERLEEAggatSAQIEMNKKREAEFLKMRRDLEEAMLHHEATTAALRKKHADSV 1208
Cdd:COG4717 124 LLQL-----LPLYQELEALEAELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1209 AELSEQIDSLQRVKQKLEKERSEAKMEADDLASTVEQLSKGKATSEKMCRLYEDQ------------------------- 1263
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallglggsllslilt 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1264 ------MNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMvSQLQRAKNSFSQNVEELKKQLEEENKAKNAL 1337
Cdd:COG4717 275 iagvlfLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELE-ELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1338 AhslQSSRHDCDLLREQYEEEQEAKgeLQRALSKANAEVAQWRTKYEtDAIQRTEELEEAKKKLVTRLQESEEIMEASNA 1417
Cdd:COG4717 354 R---EAEELEEELQLEELEQEIAAL--LAEAGVEDEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALDE 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1529987947 1418 KcsSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNF--DKVLAEWKQKYEECQSELE 1476
Cdd:COG4717 428 E--ELEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAELR 486
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1009-1181 |
2.20e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1009 EAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRM-------DLERVKRKLEGDLKlslESVMDLENDK 1081
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEaakteleDLEKEIKRLELEIE---EVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1082 QQLEEKLKKKdfEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELeadracrAKVEKQRSDVARELEDLSERLEEA 1161
Cdd:COG1579 80 EQLGNVRNNK--EYEALQKEIESLKRRISDLEDEILELMERIEELEEEL-------AELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|
gi 1529987947 1162 GGATSAQIEMNKKREAEFLK 1181
Cdd:COG1579 151 LAELEAELEELEAEREELAA 170
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1424-1864 |
2.77e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1424 KTKHRLQTEIEDLIIDLERANAAAAALDKKQRNfdkvLAEWKQKYEECQSELEISQKESRGLSTELfklknSYEETLDHL 1503
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEE----LEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1504 ETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDVDRK 1583
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1584 LAEKDEELDNLRRKHQRSLESMQATLDAEAKSRNEAVRLkkkmegDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQL 1663
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL------IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1664 ELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQNDRARKLAEHELLEASERVNLLHSqntgLINQKKKLENDLs 1743
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE----LLREAEELEEEL- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1744 mlsnEVDDAVQECRNAEEKAK-KAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKggkKQVQK 1822
Cdd:COG4717 364 ----QLEELEQEIAALLAEAGvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE---EELEE 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 1823 LEARVKELETELDAEQKK-------------SQEYQKVVRKYERRIKELSYQAEE 1864
Cdd:COG4717 437 LEEELEELEEELEELREElaeleaeleqleeDGELAELLQELEELKAELRELAEE 491
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1038-1708 |
2.78e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1038 QVDDL-EGSLEQEKKLRMDLERVKRKLEGDLKLS--LESVMDLENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQK 1114
Cdd:PRK01156 139 EMDSLiSGDPAQRKKILDEILEINSLERNYDKLKdvIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1115 KIKELQArteeleeeleadracrakvekQRSDVARELEDLSERLEEaggaTSAQIEMNKKREAEFLKMRRDL---EEAML 1191
Cdd:PRK01156 219 EIERLSI---------------------EYNNAMDDYNNLKSALNE----LSSLEDMKNRYESEIKTAESDLsmeLEKNN 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1192 HHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERseakmeaDDLASTVEQLSKGKATSEKMCRLYED--QMNEAKA 1269
Cdd:PRK01156 274 YYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKK-------QILSNIDAEINKYHAIIKKLSVLQKDynDYIKKKS 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1270 KADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKQLEEENKAKNALAHSLQSSRHDCD 1349
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVS 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1350 LLREQYEEEQEAKGELQRalskaNAEVAQWRTKYETDAIQRTEEleeakkklvtrlqESEEIMEASNAKCSSLEKTKHRL 1429
Cdd:PRK01156 427 SLNQRIRALRENLDELSR-----NMEMLNGQSVCPVCGTTLGEE-------------KSNHIINHYNEKKSRLEEKIREI 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1430 QTEIEDLiidleranaaaaalDKKQRNFDKVLaEWKQKYEECQSELEISQKESRGLSTELFKLK-NSYEETLDHLETIKR 1508
Cdd:PRK01156 489 EIEVKDI--------------DEKIVDLKKRK-EYLESEEINKSINEYNKIESARADLEDIKIKiNELKDKHDKYEEIKN 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1509 ENKNLQEEITDltdqisqgAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDVDRKLAEKD 1588
Cdd:PRK01156 554 RYKSLKLEDLD--------SKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIE 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1589 EELDNLRRKHQ--RSLESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQLNHANRlasesqkllrnlqiQIKDVQLELD 1666
Cdd:PRK01156 626 NEANNLNNKYNeiQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIED--------------NLKKSRKALD 691
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1529987947 1667 ETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQNDRARK 1708
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1800-1941 |
3.23e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1800 DLQMRLDEAEQiALKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEEDKKNL--VRLQDLID 1877
Cdd:COG1579 14 ELDSELDRLEH-RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNKEYE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1529987947 1878 KLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADTAETQVNKLRVRTRDQVSKLAE 1941
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
898-1161 |
3.25e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 48.54 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 898 QLQAEQDNLADAEdrcdlliKTKIQLEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKH 977
Cdd:PRK11637 48 QLKSIQQDIAAKE-------KSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 978 AIEnkvKNLIEEMAAL--------DETILKLTKEKKA---------LQEAHQQTLDDLQaeedkvnaltKAKAKLEQQVD 1040
Cdd:PRK11637 121 AQE---RLLAAQLDAAfrqgehtgLQLILSGEESQRGerilayfgyLNQARQETIAELK----------QTREELAAQKA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1041 DLEGSLEQEKKLRMDLERVKRKLEGDLK------LSLESvmDLENDKQQLEEklkkkdFEMNElsTRIEDEQAlvnqlqk 1114
Cdd:PRK11637 188 ELEEKQSQQKTLLYEQQAQQQKLEQARNerkktlTGLES--SLQKDQQQLSE------LRANE--SRLRDSIA------- 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1529987947 1115 kikelqarteeleeelEADRACRAKVEKQrsdvARELEDLSERLEEA 1161
Cdd:PRK11637 251 ----------------RAEREAKARAERE----AREAARVRDKQKQA 277
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1646-1851 |
3.29e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1646 ESQKLLRNLQiqikDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQNDRARKLAEHELLEASERVNLLH 1725
Cdd:COG1579 4 EDLRALLDLQ----ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1726 SQNTGLINQKkklenDLSMLSNEVDDAVQECRNAEEKAKKAItdaammaEELKKEQDTSAHLERMKKNMEQTIKDLQMRL 1805
Cdd:COG1579 80 EQLGNVRNNK-----EYEALQKEIESLKRRISDLEDEILELM-------ERIEELEEELAELEAELAELEAELEEKKAEL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1529987947 1806 DEAEQIAlkggKKQVQKLEARVKELETELDAEQKKsqEYQKVVRKY 1851
Cdd:COG1579 148 DEELAEL----EAELEELEAEREELAAKIPPELLA--LYERIRKRK 187
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1019-1237 |
4.68e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1019 QAEEDKVNALTKAKAKLEQQVDDLEGSLEQ-EKKlrmdLERVKRK-----LEGDLKLSLESVMDLENDKQQLEEKLKKKD 1092
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEaEAA----LEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1093 FEMNELSTRIED---------EQALVNQLQKKIKELQARTEELEEELEAD----RACRAKVEKQRSDVARELEDLSERLE 1159
Cdd:COG3206 240 ARLAALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1529987947 1160 eaggatsAQIEMNKKREAEFLKMRRDLEEAMLHHEATTAALRkkhadsvaELSEQIDSLQRVKQKLEKERSEAKMEAD 1237
Cdd:COG3206 320 -------AELEALQAREASLQAQLAQLEARLAELPELEAELR--------RLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1622-1937 |
5.01e-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: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1622 LKKKMEGDLNEMEVQLNHANRLASESQKLLRnLQIQIKDV---QLEL-DETVHQNE---ELKEQVAVTERRNNLLAAEVE 1694
Cdd:TIGR01612 546 LKESYELAKNWKKLIHEIKKELEEENEDSIH-LEKEIKDLfdkYLEIdDEIIYINKlklELKEKIKNISDKNEYIKKAID 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1695 eLRALLEQN----DRARKLAEHELLEASERVNLLHSQNTGLINQKkkLENDLSMLSNEVDDAVQE--CRNAEEKAKKAIT 1768
Cdd:TIGR01612 625 -LKKIIENNnayiDELAKISPYQVPEHLKNKDKIYSTIKSELSKI--YEDDIDALYNELSSIVKEnaIDNTEDKAKLDDL 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1769 DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVV 1848
Cdd:TIGR01612 702 KSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAKEKDEL 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1849 RKYERRIKELSYQ-----------AEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEER 1917
Cdd:TIGR01612 782 NKYKSKISEIKNHyndqinidnikDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEK 861
|
330 340
....*....|....*....|
gi 1529987947 1918 ADTAETQVNKLRVRTRDQVS 1937
Cdd:TIGR01612 862 IDSEHEQFAELTNKIKAEIS 881
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1170-1913 |
5.14e-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: 48.51 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1170 EMNKKREAEFLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDS-----LQRVKQKLEKERSEAKMEADDLASTVE 1244
Cdd:TIGR01612 700 DLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGeinkdLNKILEDFKNKEKELSNKINDYAKEKD 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1245 QLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAKNSFsqnveelk 1324
Cdd:TIGR01612 780 ELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKF-------- 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1325 kqleeENKAKNAlahslqssrhdcdllREQYEEEQEAKGELqraLSKANAEVAQWR-TKYETDA------IQRTEELEEA 1397
Cdd:TIGR01612 852 -----INFENNC---------------KEKIDSEHEQFAEL---TNKIKAEISDDKlNDYEKKFndskslINEINKSIEE 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1398 KKKLVTRLQESEEIMEASNAKCSSLEKTKHRlQTEIEDLIIDLERANAAAAALDKKQRN-FDKVLAEWKQKYEECQSELE 1476
Cdd:TIGR01612 909 EYQNINTLKKVDEYIKICENTKESIEKFHNK-QNILKEILNKNIDTIKESNLIEKSYKDkFDNTLIDKINELDKAFKDAS 987
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1477 ISQKESRglSTELFKLKNSYEETL---------DHLETIKRENKNLQEEITDLTDQISQGAKTIH--------ELEK-MK 1538
Cdd:TIGR01612 988 LNDYEAK--NNELIKYFNDLKANLgknkenmlyHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHtsiyniidEIEKeIG 1065
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1539 KGLEMEKTEIqaaLEEAEGTLEHEESKTLRIQLelnqmkSDVDRKLAEKDEELDNLRRKHQRSLESMQATLDaeaKSRNE 1618
Cdd:TIGR01612 1066 KNIELLNKEI---LEEAEINITNFNEIKEKLKH------YNFDDFGKEENIKYADEINKIKDDIKNLDQKID---HHIKA 1133
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1619 AVRLKKKMEGDLNEMEVQLNHANRLASE--SQKLLRNLQIQIKDVQLELDETVHQNEELKEqvavterrnnlLAAEVEEL 1696
Cdd:TIGR01612 1134 LEEIKKKSENYIDEIKAQINDLEDVADKaiSNDDPEEIEKKIENIVTKIDKKKNIYDEIKK-----------LLNEIAEI 1202
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1697 ralleQNDRARklaehelLEASERVNLLHSQNTGLI------NQKKKLENDLSMLSNEVD--DAVQECRNAEEKAKKAIT 1768
Cdd:TIGR01612 1203 -----EKDKTS-------LEEVKGINLSYGKNLGKLflekidEEKKKSEHMIKAMEAYIEdlDEIKEKSPEIENEMGIEM 1270
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1769 DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRldeaeQIALKGGKKQVQKLEARVKELETELDAEQKKSQEyqkvV 1848
Cdd:TIGR01612 1271 DIKAEMETFNISHDDDKDHHIISKKHDENISDIREK-----SLKIIEDFSEESDINDIKKELQKNLLDAQKHNSD----I 1341
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 1849 RKYERRIKELSyqaeedkkNLVRLQDlIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDD 1913
Cdd:TIGR01612 1342 NLYLNEIANIY--------NILKLNK-IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD 1397
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1204-1418 |
5.32e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1204 HADS-VAELSEQIDSLQRVKQKLEKERSEAKMEADDLASTVEQLSKGKATSEKmcrlyedQMNEAKAKADELQRQLNEAN 1282
Cdd:COG3883 13 FADPqIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA-------EIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1283 TQ---RARAQAESGEVSRKLE------------ERESMVSQLQRAKNSFSQNVeelkkqleeeNKAKNALAHSLQSSRHD 1347
Cdd:COG3883 86 EElgeRARALYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEEL----------KADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1529987947 1348 CDLLREQYEEEQEAKGELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQESEEIMEASNAK 1418
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
853-1091 |
5.76e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 853 TEKELAAL---KVELAKLKEALEKSEIKRKELEERQVSliqeknDLSLQLQAEQDN---LADAEDRCDlliktkiQLEAK 926
Cdd:PRK01156 488 IEIEVKDIdekIVDLKKRKEYLESEEINKSINEYNKIE------SARADLEDIKIKineLKDKHDKYE-------EIKNR 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 927 VKEL-MERLEDEEEMSSNVLAKKRKLEDEC-----AELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEM---AALDETI 997
Cdd:PRK01156 555 YKSLkLEDLDSKRTSWLNALAVISLIDIETnrsrsNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIeneANNLNNK 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 998 LKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDL 1077
Cdd:PRK01156 635 YNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINEL 714
|
250
....*....|....
gi 1529987947 1078 ENDKQQLEEKLKKK 1091
Cdd:PRK01156 715 SDRINDINETLESM 728
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1132-1560 |
5.93e-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: 48.41 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1132 ADRACRAKVEKQRsdVARELEDLSERLEEAGGATSAqiemnkkreAEFLkmrRDLEEAMLHHEATtAALRKKHADSVAEL 1211
Cdd:COG3096 237 ALRENRMTLEAIR--VTQSDRDLFKHLITEATNYVA---------ADYM---RHANERRELSERA-LELRRELFGARRQL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1212 SEQIDSLQRVKQKL-EKERSEAKMEADdLASTVEQLSK---GKATSEKMCRlYEDQMNEAKAKADELQRQLNEANTQRAR 1287
Cdd:COG3096 302 AEEQYRLVEMARELeELSARESDLEQD-YQAASDHLNLvqtALRQQEKIER-YQEDLEELTERLEEQEEVVEEAAEQLAE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1288 AQAESGEVSrklEERESMVSQL---QRAKNSFSQNVEELKKQLEEENKAKNALAHSLQSSRHDCDLLREQYEEEQEAKG- 1363
Cdd:COG3096 380 AEARLEAAE---EEVDSLKSQLadyQQALDVQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEe 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1364 --ELQRALSKANAEVAQWRTKYE-----TDAIQRTEELEEAKKKLVT--RLQESEEIMEASNAKCSSLEKTKHRLQteie 1434
Cdd:COG3096 457 vlELEQKLSVADAARRQFEKAYElvckiAGEVERSQAWQTARELLRRyrSQQALAQRLQQLRAQLAELEQRLRQQQ---- 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1435 dliiDLERANAAAAALDKKQRN----FDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEEtldhLETIKREN 1510
Cdd:COG3096 533 ----NAERLLEEFCQRIGQQLDaaeeLEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE----LAARAPAW 604
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1529987947 1511 KNLQEEITDLTDQISQGAKTIHEL-EKMKKGLE------MEKTEIQAALEEAEGTLE 1560
Cdd:COG3096 605 LAAQDALERLREQSGEALADSQEVtAAMQQLLErereatVERDELAARKQALESQIE 661
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
841-1295 |
6.44e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.91 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 841 FFKIKPLLRSA-----ATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEkndlslqLQAEQDNLADAEDrcdl 915
Cdd:PRK04778 100 FRKAKHEINEIeslldLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKS-------LLANRFSFGPALD---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 916 liktkiQLEAKVKELMERLEDEEEMSSN---VLAKK--RKLEDECAELKKDIDDLEITLAKIEKEKHA----IENKVKNL 986
Cdd:PRK04778 169 ------ELEKQLENLEEEFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDqlqeLKAGYREL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 987 IEEMAALDEtiLKLTKEKKALQEAHQQTLDDLqaEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGD 1066
Cdd:PRK04778 243 VEEGYHLDH--LDIEKEIQDLKEQIDENLALL--EELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1067 LKLSLEsvmdlENDKQQLEEKLKKKDFEMNElstrieDEQALVNQLQKKIKELQARTEELeeeleadracRAKVEKQR-- 1144
Cdd:PRK04778 319 LEHAKE-----QNKELKEEIDRVKQSYTLNE------SELESVRQLEKQLESLEKQYDEI----------TERIAEQEia 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1145 -SDVARELEDLSERLEEAggatsaqiemnkkrEAEFLKMRRDLeeamlhheattAALRKkhADSVAElseqiDSLQRVKQ 1223
Cdd:PRK04778 378 ySELQEELEEILKQLEEI--------------EKEQEKLSEML-----------QGLRK--DELEAR-----EKLERYRN 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1529987947 1224 KLEKERSeaKMEADDLAST-VEQLSKGKATSEKMCRLyEDQMNEAKAKADELQRQLNEANTQRARAQAESGEV 1295
Cdd:PRK04778 426 KLHEIKR--YLEKSNLPGLpEDYLEMFFEVSDEIEAL-AEELEEKPINMEAVNRLLEEATEDVETLEEETEEL 495
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1363-1804 |
7.63e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.89 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1363 GELQRALSKANAEVAQWRTKYETDAIQRTEELeeakkklvtrlQESEEIMEASNAKcsslEKTKHRLQTEIEDLIIDLER 1442
Cdd:pfam10174 292 DQLKQELSKKESELLALQTKLETLTNQNSDCK-----------QHIEVLKESLTAK----EQRAAILQTEVDALRLRLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1443 anaaaaaldkKQRNFDKvlaewKQKYeecqseLEISQKESRGLSTELFKLKnsyeetlDHLETIKRENKNLQEEITDLTD 1522
Cdd:pfam10174 357 ----------KESFLNK-----KTKQ------LQDLTEEKSTLAGEIRDLK-------DMLDVKERKINVLQKKIENLQE 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1523 QISQGAKTIHELEKMKKGLEMEK-------TEIQAALEEAEGTLEH-------------EESKTLRIQL-ELNQMKSDVD 1581
Cdd:pfam10174 409 QLRDKDKQLAGLKERVKSLQTDSsntdtalTTLEEALSEKERIIERlkeqreredrerlEELESLKKENkDLKEKVSALQ 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1582 RKLAEKDEELDNLrRKHQRSLESMQATLDAEAKSRNEAVRLKKKmegDLNEMEVQLNHANRLASESQKllrNLQIQIKDV 1661
Cdd:pfam10174 489 PELTEKESSLIDL-KEHASSLASSGLKKDSKLKSLEIAVEQKKE---ECSKLENQLKKAHNAEEAVRT---NPEINDRIR 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1662 QLELDETVHQNEELKEQvavterrnnllaAEVEELRALL-----EQNDRARKLAEHELLEASErvnlLHSQNTGLINQKK 1736
Cdd:pfam10174 562 LLEQEVARYKEESGKAQ------------AEVERLLGILrevenEKNDKDKKIAELESLTLRQ----MKEQNKKVANIKH 625
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1529987947 1737 KLENDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQdtsahLERMKKNMEQTIKDLQMR 1804
Cdd:pfam10174 626 GQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQE-----LDATKARLSSTQQSLAEK 688
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
846-1010 |
7.71e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 846 PLLRSAATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEA 925
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 926 KVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDL-------EITLAKIEKEKHAIENKVKNLIEEMAALDETIL 998
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaIEEYEELEERYDFLSEQREDLEEARETLEEAIE 819
|
170
....*....|...
gi 1529987947 999 KLTKEKK-ALQEA 1010
Cdd:COG1196 820 EIDRETReRFLET 832
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1351-1636 |
9.35e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.43 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1351 LREQYEE---EQEAKGELQRALSKANAEVAQWRTKY---ETDAIQRTEELE----EAKKKLVTRLQESEEIMEASnaKCS 1420
Cdd:pfam17380 301 LRQEKEEkarEVERRRKLEEAEKARQAEMDRQAAIYaeqERMAMERERELErirqEERKRELERIRQEEIAMEIS--RMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1421 SLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEEcqseleisQKESRglSTELFKLKnsyEETL 1500
Cdd:pfam17380 379 ELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE--------QEEAR--QREVRRLE---EERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1501 DHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKK----GLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQM 1576
Cdd:pfam17380 446 REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRdrkrAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEER 525
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1529987947 1577 KSDV----DRKLAEKDEELDNLRRKHQRSLESMQATldAEAKSRNEAVRLKKKMEGDLNEMEVQ 1636
Cdd:pfam17380 526 QKAIyeeeRRREAEEERRKQQEMEERRRIQEQMRKA--TEERSRLEAMEREREMMRQIVESEKA 587
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1461-1859 |
1.01e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1461 LAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETikrENKNLQEEITDLTDQISQGAKTIHELEKMKKG 1540
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKE---ELRQSREKHEELEEKYKELSASSEELSEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1541 LEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDVDRKLAEKDEELDNlRRKHQRSLESMQAtldaeaksrnEAV 1620
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAE-RKQLQAKLQQTEE----------ELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1621 RLKKKMEGDLNEMEVQLNHANRLASESQKLLRNL-QIQIKDVQLELdeTVHQNEELKEQVAVTERRNNLLAaevEELRAL 1699
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLtTAHRKEAENEA--LLEELRSLQERLNASERKVEGLG---EELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1700 LEQNDRARKLAEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVD---DAVQECRNAEEKAKKAITDAAMMAEE 1776
Cdd:pfam07888 264 AAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEadkDRIEKLSAELQRLEERLQEERMEREK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1777 LKKEqdtsahLERMKknmeqtikdlqmrldEAEQIALKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIK 1856
Cdd:pfam07888 344 LEVE------LGREK---------------DCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
...
gi 1529987947 1857 ELS 1859
Cdd:pfam07888 403 TVA 405
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
917-1226 |
1.03e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.43 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 917 IKTKIQLEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDID--------------DLEITLAKIEKEKHAIENK 982
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDrqaaiyaeqermamERERELERIRQEERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 983 vKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAEEdKVNALTKAKA-KLEQQVDDLEGSLEQEKKLRmdlERVKR 1061
Cdd:pfam17380 364 -RIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR-KVKILEEERQrKIQQQKVEMEQIRAEQEEAR---QREVR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1062 KLEGDLKLSLESVMDLENDKQQLEEKLKKKDFEMNELSTRIEDEQalvnQLQKKIKELqaRTEELEEELEADRACRAKVE 1141
Cdd:pfam17380 439 RLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK----RDRKRAEEQ--RRKILEKELEERKQAMIEEE 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1142 KQRSDVARELEDLSERLEEAGGATSAQIEMNKKREAEflkMRRDLEEAMLhhEATTAALRKKHADSVAELSEQIDSLQRV 1221
Cdd:pfam17380 513 RKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEME---ERRRIQEQMR--KATEERSRLEAMEREREMMRQIVESEKA 587
|
....*
gi 1529987947 1222 KQKLE 1226
Cdd:pfam17380 588 RAEYE 592
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
847-1120 |
1.06e-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: 47.48 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 847 LLRSAATEKELAALKVELAKLKEALEKSEIKRKELEerqvsliQEKNDLslqlqaeQDNLADAEDRCDLLIKTKIQLEAK 926
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQ-------QERDEL-------ADEIASGASGKSALQDEKRRLEAR 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 927 VKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETIlkLTKEKKA 1006
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTV--KSKFKSS 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1007 LqeahqqtlddlqaeedkvnaltkakAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDLENDKQQLEE 1086
Cdd:pfam01576 969 I-------------------------AALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKD 1023
|
250 260 270
....*....|....*....|....*....|....
gi 1529987947 1087 KLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQ 1120
Cdd:pfam01576 1024 QAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQ 1057
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1595-1931 |
1.22e-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: 47.36 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1595 RRKHQRSLESMQATLDaeaksrneavrlkkKMEGDLNEMEVQLNHANRLASESQKLlRNLQIQIKDVQLELdetvhqnee 1674
Cdd:TIGR02168 174 RKETERKLERTRENLD--------------RLEDILNELERQLKSLERQAEKAERY-KELKAELRELELAL--------- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1675 lkeqvavterrnnlLAAEVEELRALLEQNDRARKLAEHELLEASERVNLLHSQntglinqkkklendlsmlSNEVDDAVQ 1754
Cdd:TIGR02168 230 --------------LVLRLEELREELEELQEELKEAEEELEELTAELQELEEK------------------LEELRLEVS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1755 ECRNAEEKAKKAItdaammaEELKKEQDTsahlermkknMEQTIKDLQMRLDEAEQialkggkkQVQKLEARVKELETEL 1834
Cdd:TIGR02168 278 ELEEEIEELQKEL-------YALANEISR----------LEQQKQILRERLANLER--------QLEELEAQLEELESKL 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1835 DaeqkksqeyqkvvrKYERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDA 1914
Cdd:TIGR02168 333 D--------------ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
330
....*....|....*..
gi 1529987947 1915 EERADTAETQVNKLRVR 1931
Cdd:TIGR02168 399 NNEIERLEARLERLEDR 415
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1728-1925 |
1.29e-04 |
|
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: 45.87 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1728 NTGLINQKKKLENDLSMLSNEVDDAvqecrnaeEKAKKAITDAAMMAEEL-KKEQDTSAHLERMKKNMEQTIKDLQMRLD 1806
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENAHKIQI--------EILEKELSSLAQETEELqKKATQTLAKAQQVNAESERTLGHAKELAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1807 EAEQIAlkggkKQVQKLEARVKELETELDAE-----QKKSQEYQKVVRkyERRIKELSYQAEEDKKNLVRLQDLIDKLQV 1881
Cdd:pfam06008 90 AIKNLI-----DNIKEINEKVATLGENDFALpssdlSRMLAEAQRMLG--EIRSRDFGTQLQNAEAELKAAQDLLSRIQT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1529987947 1882 KVKSYKRQTEEAEEQANTNLSKYrklQHELDDAEERADTAETQV 1925
Cdd:pfam06008 163 WFQSPQEENKALANALRDSLAEY---EAKLSDLRELLREAAAKT 203
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1694-1916 |
1.80e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1694 EELRALLEQNDRARKlAEHELLEASERVNLLhSQNTGLINQKKKLENDLSMLsNEVDDAVQecrnaeekAKKAITDAAMM 1773
Cdd:COG4913 225 EAADALVEHFDDLER-AHEALEDAREQIELL-EPIRELAERYAAARERLAEL-EYLRAALR--------LWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1774 AEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAE-QIALKGGkkqvqkleARVKELETELDAEQKKSQEYQKVVRKYE 1852
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEaQIRGNGG--------DRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1529987947 1853 RRIKELSYQAEEDKKNLVRLQDLIDKLqvkVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEE 1916
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1631-1868 |
1.89e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 46.59 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1631 NEMEVQLNHANRLASESQKLLRNLQIQIKDVqlelDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQNdraRKla 1710
Cdd:pfam13166 279 DEFTEFQNRLQKLIEKVESAISSLLAQLPAV----SDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAK---RK-- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1711 ehellEASERVNLLHSQNTGL-INQKKKLENDLSMLSNEVDDavqecrNAEEKAKKAITD-AAMMAEELKKEQDTsahLE 1788
Cdd:pfam13166 350 -----DPFKSIELDSVDAKIEsINDLVASINELIAKHNEITD------NFEEEKNKAKKKlRLHLVEEFKSEIDE---YK 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1789 RMKKNMEQTIKDLQMRLDEAEqialkggkKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRikELSYQAEEDKKN 1868
Cdd:pfam13166 416 DKYAGLEKAINSLEKEIKNLE--------AEIKKLREEIKELEAQLRDHKPGADEINKLLKAFGFG--ELELSFNEEGKG 485
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
781-1060 |
1.96e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 781 LEELRDERLAKVLTLLQAVARGKIMRLELQRMMERREALMIIQwnirafnavkhwpwmKLFFKIkplLRSAATEKELAAL 860
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA---------------EYSWDE---IDVASAEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 861 KVELAKLKEA---LEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVK-ELMERLED 936
Cdd:COG4913 674 EAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 937 --EEEMSSNVLAKKRK-LEDECAELKKDIDDLEITLAKIEKE-KHAIENKVKNLIEEMAALDETILKLTK---------E 1003
Cdd:COG4913 754 rfAAALGDAVERELREnLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALLDRleedglpeyE 833
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1529987947 1004 KKALQEAHQQTLDDLqaeEDKVNALTKAKAKLEQQVDDLEGSLEQ-----EKKLRMDLERVK 1060
Cdd:COG4913 834 ERFKELLNENSIEFV---ADLLSKLRRAIREIKERIDPLNDSLKRipfgpGRYLRLEARPRP 892
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1387-1620 |
2.18e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1387 AIQRTEELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQ 1466
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1467 KYEECQSELE----ISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKGLE 1542
Cdd:COG4942 98 ELEAQKEELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1543 MEKTEIQ---AALEEAegtleheesktlriQLELNQMKSDVDRKLAEKDEELDNLRRKhQRSLESMQATLDAEAKSRNEA 1619
Cdd:COG4942 178 ALLAELEeerAALEAL--------------KAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAER 242
|
.
gi 1529987947 1620 V 1620
Cdd:COG4942 243 T 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1761-1935 |
2.26e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1761 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIalkggkKQVQKLEARVKELETELDAEQKK 1840
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1841 SQEyqkvVRKYERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQT-EEAEEQANTNLSKYRKLQHELDDAEERAD 1919
Cdd:COG4717 148 LEE----LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*.
gi 1529987947 1920 TAETQVNKLRVRTRDQ 1935
Cdd:COG4717 224 ELEEELEQLENELEAA 239
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1489-1911 |
2.48e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 46.00 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1489 LFKLKNSYEEtLDHLETIKRE--NKNLQEEITDLtDQISQGAKTIHELEKMKKG----LEMEKTEIQAALEEAEGTLE-H 1561
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELNDkY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1562 EESKTLRIQLELNQMKSDVDRKLAEKDEELDNLRRKHQRSLESMQATLDAEAKSRNE--AVRLK-----KKMEGDLNEME 1634
Cdd:pfam06160 80 RFKKAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTllANRFSygpaiDELEKQLAEIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1635 VQLNHANRLASESQkllrnlQIQIKDVQLELDETVHQNEELKEQV-AVTERRNNLLAAEVEELRA----LLEQNdraRKL 1709
Cdd:pfam06160 160 EEFSQFEELTESGD------YLEAREVLEKLEEETDALEELMEDIpPLYEELKTELPDQLEELKEgyreMEEEG---YAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1710 AEHELLEASERVNLLHSQNTGLINQK--KKLENDLSMLSNEVDdAVQECRNAEEKAKKaitdaammaeELKKEQDT-SAH 1786
Cdd:pfam06160 231 EHLNVDKEIQQLEEQLEENLALLENLelDEAEEALEEIEERID-QLYDLLEKEVDAKK----------YVEKNLPEiEDY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1787 LERMKKNMEQTIKDLQM-----RLDEAEQIALKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKElsyq 1861
Cdd:pfam06160 300 LEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEE---- 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1862 aeedkknlvrlqdlIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHEL 1911
Cdd:pfam06160 376 --------------IEEEQEEFKESLQSLRKDELEAREKLDEFKLELREI 411
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1394-1595 |
2.65e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1394 LEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQrnfdkvlAEWKQKYEECQS 1473
Cdd:PHA02562 204 IEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAA-------AKIKSKIEQFQK 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1474 ELEISQKesrglSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKmkkgLEMEKTEIQAALE 1553
Cdd:PHA02562 277 VIKMYEK-----GGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNE----QSKKLLELKNKIS 347
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1529987947 1554 EAEGTLEHEESKTLRIQLELNQMKSDVdrklAEKDEELDNLR 1595
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEF----VDNAEELAKLQ 385
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1418-1578 |
2.69e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.39 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1418 KCSSLEKTKHRLQTEIEDLIIDLERanaaaaaLDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGL----STELFKLK 1493
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKL-------LMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELedcdPTELDRAK 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1494 NSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEkmkkglemekTEIQAALEEAEGTLEHEESKTLRIQLEL 1573
Cdd:smart00787 211 EKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELN----------TEIAEAEKKLEQCRGFTFKEIEKLKEQL 280
|
....*
gi 1529987947 1574 NQMKS 1578
Cdd:smart00787 281 KLLQS 285
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1657-1927 |
3.22e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1657 QIKDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALL-EQNDRARKLAEhELLEASERVNLLHSQNTGLINQK 1735
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRdELNAQVKELRE-EAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1736 KKLENDLSMLSNEVDDAVQEcRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIAlkg 1815
Cdd:COG1340 81 DELNEKLNELREELDELRKE-LAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKAL--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1816 gkkqvqKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEAEE 1895
Cdd:COG1340 157 ------EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHE 230
|
250 260 270
....*....|....*....|....*....|..
gi 1529987947 1896 QANTNLSKYRKLQHELDDAEERADTAETQVNK 1927
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
856-1121 |
3.24e-04 |
|
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: 45.45 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 856 ELAALKVELAKLKEALEKS-------EIKRKELEE-----RQVSLIQEKNDLSLQlqaeqdNLADAEDRCDLLIKTKIQL 923
Cdd:pfam05622 112 EAQALKDEMDILRESSDKVkkleatvETYKKKLEDlgdlrRQVKLLEERNAEYMQ------RTLQLEEELKKANALRGQL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 924 EA---KVKELMERLEDE--------------EEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHA------IE 980
Cdd:pfam05622 186 ETykrQVQELHGKLSEEskkadklefeykklEEKLEALQKEKERLIIERDTLRETNEELRCAQLQQAELSQAdallspSS 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 981 NKVKNLIEEM--AALDETILKLTKEKKALQEA----HQQTLDDLQAEEDKVNA--------LTKAKAK---LEQQVDDLE 1043
Cdd:pfam05622 266 DPGDNLAAEImpAEIREKLIRLQHENKMLRLGqegsYRERLTELQQLLEDANRrkneletqNRLANQRileLQQQVEELQ 345
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1529987947 1044 GSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDLENDKQQLEEKlkkkdfemnelstriedEQALVNQLQKKIKELQA 1121
Cdd:pfam05622 346 KALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEEL-----------------EPKQDSNLAQKIDELQE 406
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
906-1050 |
3.27e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 906 LADAEDRCDLLIK-TKIQLEAKVKELMerLEDEEEmssnVLAKKRKLEDECAELKKDIDDLEITLAK----IEKEKHAIE 980
Cdd:PRK12704 33 IKEAEEEAKRILEeAKKEAEAIKKEAL--LEAKEE----IHKLRNEFEKELRERRNELQKLEKRLLQkeenLDRKLELLE 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 981 NKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQaeedKVNALTKAKAKlEQQVDDLEGSLEQEK 1050
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE----RISGLTAEEAK-EILLEKVEEEARHEA 171
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
854-1023 |
3.28e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 854 EKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKvkelMER 933
Cdd:pfam07888 79 ESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE----LER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 934 LEDEEEMSsnvLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEkkaLQEAHQQ 1013
Cdd:pfam07888 155 MKERAKKA---GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK---LTTAHRK 228
|
170
....*....|
gi 1529987947 1014 TLDDLQAEED 1023
Cdd:pfam07888 229 EAENEALLEE 238
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1596-1771 |
3.47e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1596 RKHQRSLESMQAtLDAEAksrNEAVRLKKKMEGDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNEEL 1675
Cdd:COG1579 3 PEDLRALLDLQE-LDSEL---DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1676 KEQVAvtERRNNllaaevEELRAL---LEQNDRARKLAEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDA 1752
Cdd:COG1579 79 EEQLG--NVRNN------KEYEALqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170
....*....|....*....
gi 1529987947 1753 VQECRNAEEKAKKAITDAA 1771
Cdd:COG1579 151 LAELEAELEELEAEREELA 169
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1672-1868 |
3.49e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1672 NEELKEQVAVTERRNNLLAAEVEELRALLeqndRARKLAEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVdd 1751
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1752 AVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQKLEARVKELE 1831
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|....*..
gi 1529987947 1832 TELDAEQKKSQEYQKVVRKYERRIKELSYQAEEDKKN 1868
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1430-1649 |
3.52e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1430 QTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRE 1509
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1510 NKN------------LQEEITDLTDQIS-------QGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEheesktlriq 1570
Cdd:COG3883 95 LYRsggsvsyldvllGSESFSDFLDRLSalskiadADADLLEELKADKAELEAKKAELEAKLAELEALKA---------- 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1529987947 1571 lELNQMKSDVDRKLAEKDEELDNLRRKhQRSLESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQLNHANRLASESQK 1649
Cdd:COG3883 165 -ELEAAKAELEAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
969-1307 |
3.99e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 45.81 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 969 LAKIEKEKHAIENKVKNLieEMAALDETILKLTKEKKALQEAHQQTLD------DLQAEEDKVNALTKAKAKLEQQVDDL 1042
Cdd:PTZ00108 1001 LGKLERELARLSNKVRFI--KHVINGELVITNAKKKDLVKELKKLGYVrfkdiiKKKSEKITAEEEEGAEEDDEADDEDD 1078
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1043 EGSLEQEKK----LRMDLervkrklegdLKLSLESVMDLEND---KQQLEEKLKKKDF------EMNELSTRIED----E 1105
Cdd:PTZ00108 1079 EEELGAAVSydylLSMPI----------WSLTKEKVEKLNAElekKEKELEKLKNTTPkdmwleDLDKFEEALEEqeevE 1148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1106 QALVNQ--------------LQKKIKELQARTEELEEELEADRACRaKVEKQRSDVARELEDLSERLEEAGGATSAQIEM 1171
Cdd:PTZ00108 1149 EKEIAKeqrlksktkgkaskLRKPKLKKKEKKKKKSSADKSKKASV-VGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQED 1227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1172 NKKREAEFLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQI-----------DSLQRVKQKLEKERSEAKMEADDLA 1240
Cdd:PTZ00108 1228 DEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPknapkrvsavqYSPPPPSKRPDGESNGGSKPSSPTK 1307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1529987947 1241 STVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVS 1307
Cdd:PTZ00108 1308 KKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVD 1374
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1262-1481 |
4.10e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1262 DQMNEAKAKADELQRQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKQLEEENKAKNALAHSL 1341
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1342 QSSRHD-CDLLREQYEEEQEakGELQRALSKANAEVAQWRTKYETDAIQ----RTEELEEAKKKLVTRLQESEEIMEAsn 1416
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQ--PPLALLLSPEDFLDAVRRLQYLKYLAParreQAEELRADLAELAALRAELEAERAE-- 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 1417 akcssLEKTKHRLQTEIEDLIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELEISQKE 1481
Cdd:COG4942 176 -----LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1458-1625 |
4.12e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1458 DKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKT------- 1530
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1531 --IHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDVDRKLAEKDEELDNLRRKhqrsLESMQAT 1608
Cdd:COG1579 96 keIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE----REELAAK 171
|
170
....*....|....*..
gi 1529987947 1609 LDAEAKSRNEAVRLKKK 1625
Cdd:COG1579 172 IPPELLALYERIRKRKN 188
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
845-1436 |
4.59e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 845 KPLLRSAATEKELA----ALKVELAKLKEALEKSEIKRKELEERQVSLIQEkndlslqlqaeqdnLADAEDrcdlliktk 920
Cdd:COG3096 498 RELLRRYRSQQALAqrlqQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQ--------------LDAAEE--------- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 921 iqLEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDdleiTLAKIEKEKHAIENKVKNLIEEM-AALDETilk 999
Cdd:COG3096 555 --LEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIK----ELAARAPAWLAAQDALERLREQSgEALADS--- 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1000 ltkekKALQEAHQQTLDD---LQAEEDKVNAltkAKAKLEQQVDDLE--GSLEQEKKLRM-------------------- 1054
Cdd:COG3096 626 -----QEVTAAMQQLLERereATVERDELAA---RKQALESQIERLSqpGGAEDPRLLALaerlggvllseiyddvtled 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1055 ------------------DLERVKRKLEGdLKLSLESVMDLENDKQQLEEKLkkkdFEMNELSTRIedeqaLVnqlqkKI 1116
Cdd:COG3096 698 apyfsalygparhaivvpDLSAVKEQLAG-LEDCPEDLYLIEGDPDSFDDSV----FDAEELEDAV-----VV-----KL 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1117 KELQARTEELEEELEADRACRakvEKQRSDVARELEDLSERLeeaggATSAqiemnkkreAEFLKMRR---DLEEAMLHH 1193
Cdd:COG3096 763 SDRQWRYSRFPEVPLFGRAAR---EKRLEELRAERDELAEQY-----AKAS---------FDVQKLQRlhqAFSQFVGGH 825
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1194 ---------EATTAALRKKHADSVAELSEQIDSLQRVKQKLEkersEAKMEADDLASTVEQLSkgkatsekmcrLYEDqm 1264
Cdd:COG3096 826 lavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLD----QLKEQLQLLNKLLPQAN-----------LLAD-- 888
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1265 NEAKAKADELQRQLNEANtqraRAQAESGEVSRKLEERESMVSQLQRAKNSFSQNVEELKKQLEEENKAKN---ALAHSL 1341
Cdd:COG3096 889 ETLADRLEELREELDAAQ----EAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQqifALSEVV 964
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1342 QSSRH------------DCDL---LREQYEEEQEAKGELQRALSKANAEVAQW-----------RTKYET--DAIQRTEE 1393
Cdd:COG3096 965 QRRPHfsyedavgllgeNSDLnekLRARLEQAEEARREAREQLRQAQAQYSQYnqvlaslkssrDAKQQTlqELEQELEE 1044
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1529987947 1394 LE-----EAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTEIEDL 1436
Cdd:COG3096 1045 LGvqadaEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSL 1092
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1752-1941 |
4.75e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1752 AVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQiALKGGKKQVQKLEARVKELE 1831
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-ELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1832 TELDAEQkksQEYQKVVRKY---------------------ERRIKELSY-------QAEEDKKNLVRLQDLIDKLQVKV 1883
Cdd:COG4942 97 AELEAQK---EELAELLRALyrlgrqpplalllspedfldaVRRLQYLKYlaparreQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1529987947 1884 KSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADTAETQVNKLRVRTRDQVSKLAE 1941
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
847-1091 |
5.07e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 44.67 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 847 LLRSAATEKELAALKVELAKLKEALEKSEIKRKELEE-----RQVSL----IQEKNDLSLQLQAEQDNLADaedrcdllI 917
Cdd:pfam15742 99 VLKQAQSIKSQNSLQEKLAQEKSRVADAEEKILELQQklehaHKVCLtdtcILEKKQLEERIKEASENEAK--------L 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 918 KTKIQLEAKVKELMERLEDEEEMS-SNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEemaaLDET 996
Cdd:pfam15742 171 KQQYQEEQQKRKLLDQNVNELQQQvRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQE----LSEK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 997 ILKLTKEKKALQEAHQQTLDDLQAEEDKVNaltkakakleqqvddlEGSLEQEKKLRmdleRVKRKLEGDLKLSLESVMD 1076
Cdd:pfam15742 247 LSSLQQEKEALQEELQQVLKQLDVHVRKYN----------------EKHHHHKAKLR----RAKDRLVHEVEQRDERIKQ 306
|
250
....*....|....*
gi 1529987947 1077 LENDKQQLEEKLKKK 1091
Cdd:pfam15742 307 LENEIGILQQQSEKE 321
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1717-1941 |
5.86e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1717 ASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNMEQ 1796
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1797 TIKDLQMRLDEAEQIALKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEEdkknlvrLQDLI 1876
Cdd:COG3883 91 RARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-------LEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 1877 DKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADTAETQVNKLRVRTRDQVSKLAE 1941
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
851-1003 |
5.88e-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: 45.05 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 851 AATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLL------IKTKIQ-L 923
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELreklaqLELRLEgL 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 924 EAKVKELMERL--------EDEEEMSSNVLAKKRKLEDECAELKKDIDDL-EITLAKIE-------------KEKHAIEN 981
Cdd:TIGR02168 935 EVRIDNLQERLseeysltlEEAEALENKIEDDEEEARRRLKRLENKIKELgPVNLAAIEeyeelkerydfltAQKEDLTE 1014
|
170 180
....*....|....*....|..
gi 1529987947 982 KVKNLIEEMAALDETILKLTKE 1003
Cdd:TIGR02168 1015 AKETLEEAIEEIDREARERFKD 1036
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1640-1911 |
5.97e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1640 ANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVAVT-----ERRNNLLA---------AEVEE-LRALLEQND 1704
Cdd:PRK04778 103 AKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLkdlyrELRKSLLAnrfsfgpalDELEKqLENLEEEFS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1705 RARKLAEH-ELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDAVQECRNAEEKAKKA---ITDAAMMAE--ELK 1778
Cdd:PRK04778 183 QFVELTESgDYVEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEgyhLDHLDIEKEiqDLK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1779 KE-QDTSAHLERMK-KNMEQTIKDLQMRLD------EAEQIALKGGKK-------QVQKLEARVKELETELDAEQKK--- 1840
Cdd:PRK04778 263 EQiDENLALLEELDlDEAEEKNEEIQERIDqlydilEREVKARKYVEKnsdtlpdFLEHAKEQNKELKEEIDRVKQSytl 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1841 SQEYQKVVRKYERRIKELSYQAEEDKKNLV-----------RLQDL------IDKLQVKVKSYKRQTEEAEEQANTNLSK 1903
Cdd:PRK04778 343 NESELESVRQLEKQLESLEKQYDEITERIAeqeiayselqeELEEIlkqleeIEKEQEKLSEMLQGLRKDELEAREKLER 422
|
....*...
gi 1529987947 1904 YRKLQHEL 1911
Cdd:PRK04778 423 YRNKLHEI 430
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1464-1935 |
6.18e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.04 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1464 WKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIheleKMKKGLEM 1543
Cdd:TIGR01612 556 WKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDKNEYIKKAI----DLKKIIEN 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1544 EKTEI-QAALEEAEGTLEHEESKTL---RIQLELNQM-KSDVDRKLAE-----KDEELDNLRRKHQrsLESMQATLDAE- 1612
Cdd:TIGR01612 632 NNAYIdELAKISPYQVPEHLKNKDKiysTIKSELSKIyEDDIDALYNElssivKENAIDNTEDKAK--LDDLKSKIDKEy 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1613 ------------------AKSRNE----AVRLKKKMEGDLNE-----------MEVQL-NHANRLASESQKLLR------ 1652
Cdd:TIGR01612 710 dkiqnmetatvelhlsniENKKNElldiIVEIKKHIHGEINKdlnkiledfknKEKELsNKINDYAKEKDELNKykskis 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1653 ------NLQIQIKDVQlelDETVHQN-EELKEQVAVTERRNNLLAAEVEELRALleQNDRARKLAEHELLEAS--ERVNL 1723
Cdd:TIGR01612 790 eiknhyNDQINIDNIK---DEDAKQNyDKSKEYIKTISIKEDEIFKIINEMKFM--KDDFLNKVDKFINFENNckEKIDS 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1724 LHSQNTGLINQKK------------KLENDLSMLSNEVDDAVQE-----------------CRNAEEKAKKAITDAAMMA 1774
Cdd:TIGR01612 865 EHEQFAELTNKIKaeisddklndyeKKFNDSKSLINEINKSIEEeyqnintlkkvdeyikiCENTKESIEKFHNKQNILK 944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1775 EELKKEQDT---SAHLERMKKN-MEQTIKDLQMRLDEA-EQIALKGGKKQVQKLEARVKELETELdAEQKKSQEYQKVVR 1849
Cdd:TIGR01612 945 EILNKNIDTikeSNLIEKSYKDkFDNTLIDKINELDKAfKDASLNDYEAKNNELIKYFNDLKANL-GKNKENMLYHQFDE 1023
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1850 KyERRIKELSYQAEEDKKNLVRLQ--------DLIDKLQVKV-KSYKRQTEEAEEQANTNLSKYRKLQHEL------DDA 1914
Cdd:TIGR01612 1024 K-EKATNDIEQKIEDANKNIPNIEiaihtsiyNIIDEIEKEIgKNIELLNKEILEEAEINITNFNEIKEKLkhynfdDFG 1102
|
570 580
....*....|....*....|...
gi 1529987947 1915 EERADTAETQVNKLR--VRTRDQ 1935
Cdd:TIGR01612 1103 KEENIKYADEINKIKddIKNLDQ 1125
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1724-1912 |
6.55e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1724 LHSQNTGLINQKKKLENDLSMLSNEVDDAVQECRNAE---EKAKKAITDAAMMAEelkkeqDTSAHLE-------RMKKN 1793
Cdd:PHA02562 197 IKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKaeiEELTDELLNLVMDIE------DPSAALNklntaaaKIKSK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1794 MEQTIKDLQMRLDEAE----QIALKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKY---ERRIKELSYQAEEDK 1866
Cdd:PHA02562 271 IEQFQKVIKMYEKGGVcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFneqSKKLLELKNKISTNK 350
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1529987947 1867 KNLV-------RLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELD 1912
Cdd:PHA02562 351 QSLItlvdkakKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKY 403
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1356-1488 |
7.06e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1356 EEEQEAKGELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKklvtRLQESEEIMEasnAKCSSLEKTKHRLQTEIED 1435
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEK----RLLQKEENLD---RKLELLEKREEELEKKEKE 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1529987947 1436 liidleranaaaaaLDKKQRNFDKVLAEWKQKYEECQSELE-ISqkesrGLSTE 1488
Cdd:PRK12704 119 --------------LEQKQQELEKKEEELEELIEEQLQELErIS-----GLTAE 153
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
847-1189 |
7.21e-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: 44.73 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 847 LLRSAATEKELAALKVELAKLKEALEKSEIKRKELE------ERQVSLIQEKNDLSLQLQAEQDNLAD----AEDRCdLL 916
Cdd:pfam05557 196 LARIPELEKELERLREHNKHLNENIENKLLLKEEVEdlkrklEREEKYREEAATLELEKEKLEQELQSwvklAQDTG-LN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 917 IKTKIQLEAKVKEL-------MERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEE 989
Cdd:pfam05557 275 LRSPEDLSRRIEQLqqreivlKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 990 MAALDEtILKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKK----LRMDLERVKRKLE- 1064
Cdd:pfam05557 355 RDGYRA-ILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQqaqtLERELQALRQQESl 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1065 GDLKLSLESVMDLENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQR 1144
Cdd:pfam05557 434 ADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEI 513
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1529987947 1145 SDVARELEDLSERLEEAGGATSAQIEMNKKreaEFLKMRRDLEEA 1189
Cdd:pfam05557 514 ERLKRLLKKLEDDLEQVLRLPETTSTMNFK---EVLDLRKELESA 555
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1040-1248 |
7.32e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1040 DDLEGSLEQ-EKKL--RMDLERVK-RKLEGdlkLSLESV-MDLENDKQQLEEKLKKKDFEMNElsTRIEDEQALVNQLQK 1114
Cdd:COG2433 346 DAYKNKFERvEKKVppDVDRDEVKaRVIRG---LSIEEAlEELIEKELPEEEPEAEREKEHEE--RELTEEEEEIRRLEE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1115 KIKELQARTEELeeeleadracRAKVEKQRsdvaRELEDLSERLEEAggatsaqiemnkkREAEFLKMRRDLEEAMLhhE 1194
Cdd:COG2433 421 QVERLEAEVEEL----------EAELEEKD----ERIERLERELSEA-------------RSEERREIRKDREISRL--D 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1529987947 1195 ATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMeaddLASTVEQLSK 1248
Cdd:COG2433 472 REIERLERELEEERERIEELKRKLERLKELWKLEHSGELV----PVKVVEKFTK 521
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1459-1730 |
8.41e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1459 KVLAEWKQKYEECQSEL--EISQKESRGLSTELFKLKNSYEETLDHLETIKRENK--NLQEEITDLTDQISQgaktihel 1534
Cdd:COG3206 152 AVANALAEAYLEQNLELrrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSE-------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1535 ekmkkgLEMEKTEIQAALEEAEGTLEheeskTLRIQLELNQMKSDVdrklAEKDEELDNLRRKHQRsLESMQATLDAEAK 1614
Cdd:COG3206 224 ------LESQLAEARAELAEAEARLA-----ALRAQLGSGPDALPE----LLQSPVIQQLRAQLAE-LEAELAELSARYT 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1615 SRN-EAVRLKKKMEgDLNEmevqlnhanRLASESQKLLRNLQIQIKDVQleldetvHQNEELKEQVAVTERRNNLLAAEV 1693
Cdd:COG3206 288 PNHpDVIALRAQIA-ALRA---------QLQQEAQRILASLEAELEALQ-------AREASLQAQLAQLEARLAELPELE 350
|
250 260 270
....*....|....*....|....*....|....*..
gi 1529987947 1694 EELRALLEQNDRARKLAEhELLEASERVNLLHSQNTG 1730
Cdd:COG3206 351 AELRRLEREVEVARELYE-SLLQRLEEARLAEALTVG 386
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
915-1051 |
9.38e-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: 43.47 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 915 LLIKTKIQLEAKV------KELMERLEDeeemssnVLAKKRK-LEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLI 987
Cdd:smart00787 120 QLVKTFARLEAKKmwyewrMKLLEGLKE-------GLDENLEgLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 988 E---EMAALDETILKLTKEKKALQEAH----QQTLDDLQAE----EDKVNALTKAKAKLEQQVDDLEGSLEQEKK 1051
Cdd:smart00787 193 QledELEDCDPTELDRAKEKLKKLLQEimikVKKLEELEEElqelESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
900-1237 |
9.58e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.12 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 900 QAEQDNLADAEDRCDLLIKTKIQLEAKVKELMERLEDEEEMSSNVL---------AKKRKLEDECAELKKdIDDLEitla 970
Cdd:PLN02939 85 ELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLedlvgmiqnAEKNILLLNQARLQA-LEDLE---- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 971 KIEKEKHAIENKVKNLIEEMAALDETIlKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKA-KAKLEQQVDDLEgslEQE 1049
Cdd:PLN02939 160 KILTEKEALQGKINILEMRLSETDARI-KLAAQEKIHVEILEEQLEKLRNELLIRGATEGLcVHSLSKELDVLK---EEN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1050 KKLRMDLERVKRKLEgDLKLSLESVMDLENDKQQLEEKLKkkdfemnELSTRIEDEQALVNQLQ--------KKIKELQA 1121
Cdd:PLN02939 236 MLLKDDIQFLKAELI-EVAETEERVFKLEKERSLLDASLR-------ELESKFIVAQEDVSKLSplqydcwwEKVENLQD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1122 rtEELEEELEADRAcrAKVEKQRSDVARELEDLSERLEEAGGA--TSAQIEMNKKReaefLKMrrdLEEAMLHHEATTAA 1199
Cdd:PLN02939 308 --LLDRATNQVEKA--ALVLDQNQDLRDKVDKLEASLKEANVSkfSSYKVELLQQK----LKL---LEERLQASDHEIHS 376
|
330 340 350
....*....|....*....|....*....|....*...
gi 1529987947 1200 LRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEAD 1237
Cdd:PLN02939 377 YIQLYQESIKEFQDTLSKLKEESKKRSLEHPADDMPSE 414
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
861-1021 |
9.86e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 9.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 861 KVELAKLKEALEKSEI----KRKELEERQVSLIQEKNDLSLQLQAEQDNlaDAEDRcdlliktkiqlEAKVKELMERLED 936
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRileeAKKEAEAIKKEALLEAKEEIHKLRNEFEK--ELRER-----------RNELQKLEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 937 EEEMSSNvlaKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMaaldETILKLTKEkkalqEAHQQTLD 1016
Cdd:PRK12704 94 KEENLDR---KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL----ERISGLTAE-----EAKEILLE 161
|
....*
gi 1529987947 1017 DLQAE 1021
Cdd:PRK12704 162 KVEEE 166
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
991-1121 |
1.04e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 991 AALDETILK-LTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERvkrklegdlkl 1069
Cdd:COG2433 380 EALEELIEKeLPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLER----------- 448
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1529987947 1070 SLESVMDLENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQA 1121
Cdd:COG2433 449 ELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1087-1240 |
1.09e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1087 KLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEeleadracRAKVEKQRSDVARELEDLSERLEEAGGATS 1166
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKL--------RNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1167 AQIEMNKKREAEFLKMRRDLEEAMLHHEATTAALRKKHADSVAELsEQIDSL----------QRVKQKLEKERS------ 1230
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLtaeeakeillEKVEEEARHEAAvlikei 178
|
170
....*....|..
gi 1529987947 1231 --EAKMEADDLA 1240
Cdd:PRK12704 179 eeEAKEEADKKA 190
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
997-1178 |
1.16e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 997 ILKLTKEKKaLQEAHQQTLDDLQAEEDKVNALTKaKAKLEQQvddlegslEQEKKLRMDLERVKRKLEGDLKlslesvmD 1076
Cdd:PRK12704 24 VRKKIAEAK-IKEAEEEAKRILEEAKKEAEAIKK-EALLEAK--------EEIHKLRNEFEKELRERRNELQ-------K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1077 LENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARteeleeeleadraCRAKVEKQR----------SD 1146
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEE-------------LEELIEEQLqelerisgltAE 153
|
170 180 190
....*....|....*....|....*....|....
gi 1529987947 1147 VARE--LEDLSERLEEAGGATSAQIEMNKKREAE 1178
Cdd:PRK12704 154 EAKEilLEKVEEEARHEAAVLIKEIEEEAKEEAD 187
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
1463-1536 |
1.30e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 42.79 E-value: 1.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1529987947 1463 EWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEK 1536
Cdd:COG4026 132 ELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLK 205
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1031-1313 |
1.38e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.05 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1031 AKAKLEQQVDDLEGSLEQEKKLRMDLERvKRKLEGDLKLslesvmdLENDKQQLEEKLKKKDFEMNelSTrieDEQALVN 1110
Cdd:NF012221 1536 ATSESSQQADAVSKHAKQDDAAQNALAD-KERAEADRQR-------LEQEKQQQLAAISGSQSQLE--ST---DQNALET 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1111 QLQKKikelqarteeleeeleadracRAKVEKQRSDVARELEDLSERLEEAGGATSAQIEMNKKREAEFL-----KMRRD 1185
Cdd:NF012221 1603 NGQAQ---------------------RDAILEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAgglldRVQEQ 1661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1186 LEEAMLHHEATTAALRKKHadsvaelseqIDSLQRVKQKLEKerSEAkmeaddlastveqlskGKATSEKMCRLYEDQMN 1265
Cdd:NF012221 1662 LDDAKKISGKQLADAKQRH----------VDNQQKVKDAVAK--SEA----------------GVAQGEQNQANAEQDID 1713
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1529987947 1266 EAKAKADelQRQLnEANTQRARA-QAES-----GEVSRKLEERESMVSQLQRAK 1313
Cdd:NF012221 1714 DAKADAE--KRKD-DALAKQNEAqQAESdanaaANDAQSRGEQDASAAENKANQ 1764
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1710-1926 |
1.67e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1710 AEHELLEASERVNLLHSQNTGLINQKKKLENDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDT-SAHLE 1788
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1789 RMKKNMEQT-----------IKDLQMRLD------EAEQIALKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKY 1851
Cdd:COG3883 94 ALYRSGGSVsyldvllgsesFSDFLDRLSalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 1852 ERRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADTAETQVN 1926
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1570-1931 |
1.70e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.66 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1570 QLELNQMKSDVDRKLAEKDEELDNLRRKHQRSLESMQATLDAEAKSR-----NEAVRLKKKMEGDLNEmEVQLNHANRLA 1644
Cdd:NF041483 82 QIQADQLRADAERELRDARAQTQRILQEHAEHQARLQAELHTEAVQRrqqldQELAERRQTVESHVNE-NVAWAEQLRAR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1645 SESQKllRNLqiqikdvqleLDETVHQNEEL-----KEQVAVTERRNNLLAAEVEELRALLEQN-DRARKLAEHEL---- 1714
Cdd:NF041483 161 TESQA--RRL----------LDESRAEAEQAlaaarAEAERLAEEARQRLGSEAESARAEAEAIlRRARKDAERLLnaas 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1715 ---LEASERVNLLHSQNTGLINQKKKLENDLSMLS----NEVDDAVQECRNAEEKAKKAITDAA---MMAEELKKEQDTS 1784
Cdd:NF041483 229 tqaQEATDHAEQLRSSTAAESDQARRQAAELSRAAeqrmQEAEEALREARAEAEKVVAEAKEAAakqLASAESANEQRTR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1785 AHLERMKKNMEQTIKDLQMRLDEAEQiALKGGKKQVQKLEARVKELETELDAEQKKSQeyqkvVRKYERRIKELSYQAEE 1864
Cdd:NF041483 309 TAKEEIARLVGEATKEAEALKAEAEQ-ALADARAEAEKLVAEAAEKARTVAAEDTAAQ-----LAKAARTAEEVLTKASE 382
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1529987947 1865 DKKNLVRlqdlidklqVKVKSYKRQTEEAEEQANTNLSKYRKLQHEL-----DDAEE-RADTAETQVNKLRVR 1931
Cdd:NF041483 383 DAKATTR---------AAAEEAERIRREAEAEADRLRGEAADQAEQLkgaakDDTKEyRAKTVELQEEARRLR 446
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
847-1121 |
1.78e-03 |
|
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: 43.57 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 847 LLRSAATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLslqLQAEQDNLADAEDrcdlLIKTKIQLEAK 926
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL---VNAGSERLRAVKD----IKQERDQLLNE 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 927 VK----ELMERLEDEEEMSSNVLAKKRKLEDECAELKkdiddLEITLAKIEKEkhaienKVKNLIEEMAALDETILKLTK 1002
Cdd:pfam15921 662 VKtsrnELNSLSEDYEVLKRNFRNKSEEMETTTNKLK-----MQLKSAQSELE------QTRNTLKSMEGSDGHAMKVAM 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1003 EKKALQEAHQQTLDDLQAeedKVNALTKAKAKLEQQVDDLEgslEQEKKLRMDLERV---KRKLEGDLKLslesvmdLEN 1079
Cdd:pfam15921 731 GMQKQITAKRGQIDALQS---KIQFLEEAMTNANKEKHFLK---EEKNKLSQELSTVateKNKMAGELEV-------LRS 797
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1529987947 1080 DKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKK-----------IKELQA 1121
Cdd:pfam15921 798 QERRLKEKVANMEVALDKASLQFAECQDIIQRQEQEsvrlklqhtldVKELQG 850
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
773-1118 |
1.81e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 43.40 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 773 FKAGLLGHLEELRDERLAKVLTLLQAvarGKIMrLELQRMMERREALM-----IIQWNIRAFNAVKHWPWMKLFF----K 843
Cdd:pfam15818 5 FKTSLLEALEELRMRREAETQYEEQI---GKII-VETQELKWQKETLQnqketLAKQHKEAMAVFKKQLQMKMCAleeeK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 844 IKPLLRSAATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQL 923
Cdd:pfam15818 81 GKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLHLLAKEDHHKQLNEIEKYYATITGQFGLVKENHGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 924 EAKVKELMErledeeeMSSNVLAKKRKLEDECAELKKDIDDLEITLAK--------IEKEKHAI---ENKVKNLIEEMAA 992
Cdd:pfam15818 161 EQNVQEAIQ-------LNKRLSALNKKQESEICSLKKELKKVTSDLIKskvtcqykMGEENINLtikEQKFQELQERLNM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 993 LDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEgslEQEKKLRMDLERVKRKLegdlKLSLE 1072
Cdd:pfam15818 234 ELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALK---ENNQTLERDNELQREKV----KENEE 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1529987947 1073 SVMDLENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKE 1118
Cdd:pfam15818 307 KFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQE 352
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1516-1702 |
1.88e-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: 43.09 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1516 EITDLTDQISQGAKTIHELEKMKKGLEMEK----TEIQAALEEAEGTLEHEESKTLRIQLELNQMK---SDVDRKLAEKD 1588
Cdd:pfam05667 276 DLAELLSSFSGSSTTDTGLTKGSRFTHTEKlqftNEAPAATSSPPTKVETEEELQQQREEELEELQeqlEDLESSIQELE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1589 EELDNLRRKHQRSLESMQaTLDAEAKSRNEAVRLKKKMEGDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELdet 1668
Cdd:pfam05667 356 KEIKKLESSIKQVEEELE-ELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPL--- 431
|
170 180 190
....*....|....*....|....*....|....
gi 1529987947 1669 VHQNEELKEQVAVTERRNNLLAAEVEELRALLEQ 1702
Cdd:pfam05667 432 IEEYRALKEAKSNKEDESQRKLEEIKELREKIKE 465
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1787-1941 |
2.27e-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: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1787 LERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEEDk 1866
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERRE- 460
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 1867 knlVRLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQhELDDAEERADTaeTQVNKLRVRTRDQVSKLAE 1941
Cdd:COG2433 461 ---IRKDREISRLDREIERLERELEEERERIEELKRKLERLK-ELWKLEHSGEL--VPVKVVEKFTKEAIRRLEE 529
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1630-1924 |
2.29e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 42.75 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1630 LNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLEL-------DETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQ 1702
Cdd:pfam05622 40 LQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENfrletarDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1703 NDrarklaehELLEASERVNLLHSQntgLINQKKKLEnDLSMLSNEVddavqecRNAEEKAKKAITDAAMMAEELKKEQD 1782
Cdd:pfam05622 120 MD--------ILRESSDKVKKLEAT---VETYKKKLE-DLGDLRRQV-------KLLEERNAEYMQRTLQLEEELKKANA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1783 TSAHLERMKKNmeqtIKDLQMRLDEAEQIALK---GGKKQVQKLEARVKELET---------ELDAEQKKSQEYQKVVRK 1850
Cdd:pfam05622 181 LRGQLETYKRQ----VQELHGKLSEESKKADKlefEYKKLEEKLEALQKEKERliierdtlrETNEELRCAQLQQAELSQ 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1529987947 1851 YERRIKELSYQAEEDKKNLV--RLQDLIDKLQVKVKSYKRQTEEAEEQantnlsKYRKLQHELDDAEERADTAETQ 1924
Cdd:pfam05622 257 ADALLSPSSDPGDNLAAEIMpaEIREKLIRLQHENKMLRLGQEGSYRE------RLTELQQLLEDANRRKNELETQ 326
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
947-1161 |
2.37e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 41.66 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 947 KKRKLEDECAELKKDIDDLEITLAKIEKEKHAIE-----NKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAE 1021
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESveallKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1022 EDKVNALTKA-KAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEgdlKLSLESVMDLENDKQQLEEKLKKKDfemnELST 1100
Cdd:cd00176 81 LEELNQRWEElRELAEERRQRLEEALDLQQFFRDADDLEQWLEE---KEAALASEDLGKDLESVEELLKKHK----ELEE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1529987947 1101 RIEDEQALVNQLQKKIKELQARteELEEELEADRACRAKVEKQRSDVARELEDLSERLEEA 1161
Cdd:cd00176 154 ELEAHEPRLKSLNELAEELLEE--GHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1461-1737 |
2.60e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1461 LAEWKQKYEECQSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIHELEKMKKG 1540
Cdd:COG4372 61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1541 LEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMksdvdrKLAEKDEELDNLRRKHQRSLESMQATLDAEAKSRNEAV 1620
Cdd:COG4372 141 LQSEIAEREEELKELEEQLESLQEELAALEQELQAL------SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1621 RLKKKMEGDLNEMEVQLNHANRLASESQKLLRNLQIQIKDVQLELDEtvhqnEELKEQVAVTERRNNLLAAEVEELRALL 1700
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE-----ELELAILVEKDTEEEELEIAALELEALE 289
|
250 260 270
....*....|....*....|....*....|....*..
gi 1529987947 1701 EQNDRARKLAEHELLEASERVNLLHSQNTGLINQKKK 1737
Cdd:COG4372 290 EAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
958-1119 |
2.61e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.05 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 958 LKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKalqeahqqtlddlQAEEDKVnALTKAKAKLEQ 1037
Cdd:pfam13851 31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLE-------------NYEKDKQ-SLKNLKARLKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1038 QVDDLEgSLEQEKK-LRMDLERVKRKLEGDLKLSLESVMD-----------LENDKQQLEEKLKKKDFEMNELSTRIEDE 1105
Cdd:pfam13851 97 LEKELK-DLKWEHEvLEQRFEKVERERDELYDKFEAAIQDvqqktglknllLEKKLQALGETLEKKEAQLNEVLAAANLD 175
|
170
....*....|....
gi 1529987947 1106 QALVNQLQKKIKEL 1119
Cdd:pfam13851 176 PDALQAVTEKLEDV 189
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
953-1063 |
2.69e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 953 DE-CAELK-------KDIDDLEITLAKIEKEKHAIENkvknliEEMAALDETILKLTKEKKALQEAHQQTLDDLQAEEDK 1024
Cdd:COG0542 396 DEaAARVRmeidskpEELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKEL 469
|
90 100 110
....*....|....*....|....*....|....*....
gi 1529987947 1025 VNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKL 1063
Cdd:COG0542 470 IEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLL 508
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
727-1153 |
2.80e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 727 KQRYRILNPHAIPDDKFVDSRKAAEKLLASLDIDHNQYRfghtkvffkaGLLGHLEELRD--ERLAKVLTLLQAVARGKI 804
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYA----------ELQEELEELEEelEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 805 MRLELQRMMERREAL-MIIQWNIRAFNAVKHwpwmklffKIKPLlrsAATEKELAALKVELAKLKEALEKSEIKRKELEE 883
Cdd:COG4717 123 KLLQLLPLYQELEALeAELAELPERLEELEE--------RLEEL---RELEEELEELEAELAELQEELEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 884 RQVS-LIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELMERLEDEEEMSSNVLA---------------- 946
Cdd:COG4717 192 EELQdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAaallallglggsllsl 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 947 ------------------------KKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTK 1002
Cdd:COG4717 272 iltiagvlflvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1003 EKKALQEAHQQtLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDLenDKQ 1082
Cdd:COG4717 352 LLREAEELEEE-LQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL--DEE 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1529987947 1083 QLEEKLkkkdfemNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRAcRAKVEKQRSDVARELED 1153
Cdd:COG4717 429 ELEEEL-------EELEEELEELEEELEELREELAELEAELEQLEEDGELAEL-LQELEELKAELRELAEE 491
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
982-1265 |
2.81e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 982 KVKNLIEEMAALDETIL----KLTKEKKALQEAHQQTLDDLQaeeDKVNALTKAKAKLEQQVDdlegsleqekKLRMDLE 1057
Cdd:pfam00038 19 KVRFLEQQNKLLETKISelrqKKGAEPSRLYSLYEKEIEDLR---RQLDTLTVERARLQLELD----------NLRLAAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1058 RVKRKLEGDLKLSLESVMDLENDKQQL-EEKLKKKDFEMnELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRAC 1136
Cdd:pfam00038 86 DFRQKYEDELNLRTSAENDLVGLRKDLdEATLARVDLEA-KIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1137 RAKVEKQRSDVARELEDLSER-LEEAGGATSAQIEmNKKREAEflkmrRDLEEAMLHHEATTAALRKkhadsVAELSEQI 1215
Cdd:pfam00038 165 KLDLTSALAEIRAQYEEIAAKnREEAEEWYQSKLE-ELQQAAA-----RNGDALRSAKEEITELRRT-----IQSLEIEL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1529987947 1216 DSLQRVKQKLEKERSEAK----MEADDLASTV----EQLSKGKATSEKMCRLYEDQMN 1265
Cdd:pfam00038 234 QSLKKQKASLERQLAETEeryeLQLADYQELIseleAELQETRQEMARQLREYQELLN 291
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1787-1905 |
2.95e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1787 LERMKK-NMEQTIKDLQMRLDEAE------QIALKGGKKQVQKLEARVKELETELDAEQKKSQEYQkvvrkyeRRIKELS 1859
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEaersrlQALLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1529987947 1860 YQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEE-------AEEQANTNLSKYR 1905
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADlgrrlnvALAQRVQELNRYR 196
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
847-1178 |
3.23e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 847 LLRSAATEKELAALKVELAKLKEALEKSEIKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAK 926
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 927 VKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKA 1006
Cdd:COG4372 117 LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1007 LQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDLENDKQQLEE 1086
Cdd:COG4372 197 EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1087 KLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRAcrAKVEKQRSDVARELEDLSERLEEAGGATS 1166
Cdd:COG4372 277 ELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA--KKLELALAILLAELADLLQLLLVGLLDND 354
|
330
....*....|..
gi 1529987947 1167 AQIEMNKKREAE 1178
Cdd:COG4372 355 VLELLSKGAEAG 366
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
923-1184 |
3.86e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 923 LEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTK 1002
Cdd:COG1340 6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1003 EKKALQEahqqTLDDLQAEEDKVNALTKAKAKLEQQVDDLEG-------SLEQEKKLRMDLERVKRKLEGDLKLSLES-- 1073
Cdd:COG1340 86 KLNELRE----ELDELRKELAELNKAGGSIDKLRKEIERLEWrqqtevlSPEEEKELVEKIKELEKELEKAKKALEKNek 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1074 --------------VMDLENDKQQLEEKLKKKDFEMNELSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAK 1139
Cdd:COG1340 162 lkelraelkelrkeAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1529987947 1140 VEKQRSDVARELEDLSERLEEAggatsaqiEMNKKREAEFLKMRR 1184
Cdd:COG1340 242 LRKELKKLRKKQRALKREKEKE--------ELEEKAEEIFEKLKK 278
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1483-1624 |
3.91e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1483 RGLSTE--LFKLKNsyEETLDHLETIKRENKNLQEEITDLTDQISQgaktiheLEKMKKGLEMEKTEIQAALEEAEGTLE 1560
Cdd:COG2433 374 RGLSIEeaLEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRR-------LEEQVERLEAEVEELEAELEEKDERIE 444
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1529987947 1561 HEESKTLRIQLELNQmKSDVDRKLAEKDEELDNLRRKhqrsLESMQATLDaEAKSRNEavRLKK 1624
Cdd:COG2433 445 RLERELSEARSEERR-EIRKDREISRLDREIERLERE----LEEERERIE-ELKRKLE--RLKE 500
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
918-1250 |
4.11e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 918 KTKIQLEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETI 997
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 998 LKLTKEKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEQekklrmdLERVKRKLEGDLKLSLESVMDL 1077
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ-------LEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1078 ENDKQQLEEKLKKKDFEMNELSTRiEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEDLSER 1157
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEA-EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1158 LEEAGGATSAQIEMNKKREAEFLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEAD 1237
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330
....*....|...
gi 1529987947 1238 DLASTVEQLSKGK 1250
Cdd:COG4372 315 DALLAALLELAKK 327
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
988-1097 |
4.29e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 988 EEMAALDETILKLTKEKKAL----QEAHQQTLDDLQAEEdkvnaltkakAKLEQQVDDLEGSLEQEKKLRMDLERVKRKL 1063
Cdd:COG0542 411 EELDELERRLEQLEIEKEALkkeqDEASFERLAELRDEL----------AELEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|....
gi 1529987947 1064 EGDlklsLESVMDLENDKQQLEEKLKKKDFEMNE 1097
Cdd:COG0542 481 EQR----YGKIPELEKELAELEEELAELAPLLRE 510
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1348-1563 |
4.77e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1348 CDLLREQYEEEQEAKGELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKH 1427
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1428 RLQTEIEDLI------IDLERANAAAAAL----DKKQRNFDKVLAEWKQKYEECQSELE-------ISQKESRGLSTELF 1490
Cdd:PRK05771 118 ELEQEIERLEpwgnfdLDLSLLLGFKYVSvfvgTVPEDKLEELKLESDVENVEYISTDKgyvyvvvVVLKELSDEVEEEL 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1529987947 1491 KlKNSYEE-TLDHLETIKRENKNLQEEITDLTDQISqgaKTIHELEKMKKGLEmekTEIQAALEEAEGTLEHEE 1563
Cdd:PRK05771 198 K-KLGFERlELEEEGTPSELIREIKEELEEIEKERE---SLLEELKELAKKYL---EELLALYEYLEIELERAE 264
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
939-1266 |
4.81e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 939 EMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKALQEahqqtldDL 1018
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNE-------KV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1019 QAEEDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSLESVMDLENDKQQLEeklkkkdfEMNEL 1098
Cdd:COG1340 74 KELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVE--------KIKEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1099 STRIEDEQALvNQLQKKIKELQARTeeleeeleadracrAKVEKQRSDVARELEDLSERLEEAggatSAQIEMNKKREAE 1178
Cdd:COG1340 146 EKELEKAKKA-LEKNEKLKELRAEL--------------KELRKEAEEIHKKIKELAEEAQEL----HEEMIELYKEADE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1179 FLKMRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEK-ERSEAKMEADDLASTVEQ--LSKGKATSEK 1255
Cdd:COG1340 207 LRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRAlKREKEKEELEEKAEEIFEklKKGEKLTTEE 286
|
330
....*....|.
gi 1529987947 1256 MCRLYEDQMNE 1266
Cdd:COG1340 287 LKLLQKSGLLE 297
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
918-1086 |
4.94e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 41.76 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 918 KTKIQLEAKVKELMERLEDEEEMSsnvlAKKRKLEDECAELKKDIDDleITLAKIEKEKHAIENKVKNLIEEMAaLDETI 997
Cdd:PLN03229 558 KLKAEINKKFKEVMDRPEIKEKME----ALKAEVASSGASSGDELDD--DLKEKVEKMKKEIELELAGVLKSMG-LEVIG 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 998 LKltkeKKALQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGSLEqEKKLRM-------DLERVK--RKLEGDLK 1068
Cdd:PLN03229 631 VT----KKNKDTAEQTPPPNLQEKIESLNEEINKKIERVIRSSDLKSKIE-LLKLEVakasktpDVTEKEkiEALEQQIK 705
|
170
....*....|....*...
gi 1529987947 1069 LSLESVMDLENDKQQLEE 1086
Cdd:PLN03229 706 QKIAEALNSSELKEKFEE 723
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1740-1941 |
5.13e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1740 NDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLErmkknmeQTIKDLQMRLDEAEQiALKGGKKQ 1819
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLE-------AEIEDLRETIAETER-EREELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1820 VQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELSYQAEEdkknlvrLQDLIDKLQVKVksykrqtEEAEEQANT 1899
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE-------LRDRLEECRVAA-------QAHNEEAES 346
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1529987947 1900 NLSKYRKLQHELDDAEERADTAETQVNKLRVRTRDQVSKLAE 1941
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
857-1006 |
5.31e-03 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 41.28 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 857 LAALKVELAKLKeaLEKSEIKRKELEerqvsLIQEKNDLSLQLQAEQDNLADAEdrcdlLIKTKI-QLEAKVKELMERLE 935
Cdd:pfam10186 21 LYELRVDLARLL--SEKDSLKKKVEE-----ALEGKEEGEQLEDNIGNKKLKLR-----LLKSEVaISNERLNEIKDKLD 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1529987947 936 -DEEEMSsnvlAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNLIEEMAALDETILKLTKEKKA 1006
Cdd:pfam10186 89 qLRREIA----EKKKKIEKLRSSLKQRRSDLESASYQLEERRASQLAKLQNSIKRIKQKWTALHSKTAESRS 156
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1174-1436 |
5.48e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 41.82 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1174 KREAEFLKMRRDLEEAMLHHEATTAalRKKHADSVAELSEQIDSLQRVKQKLEKERSEAkmeADDLASTVEQLSKGKATS 1253
Cdd:pfam15964 373 EKELASQQEKRAQEKEALRKEMKKE--REELGATMLALSQNVAQLEAQVEKVTREKNSL---VSQLEEAQKQLASQEMDV 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1254 EKMCRLYEDQMNEAKAKADELQRQLNEANTQraraqaesgeVSRKLEERESMVSQLQRAKNSFSQNVEELKKQLEEENKA 1333
Cdd:pfam15964 448 TKVCGEMRYQLNQTKMKKDEAEKEHREYRTK----------TGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREE 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1334 KNALAHSLQSSRHDCDLLREQYEEEQEAKGElqraLSKANAEVAQWRTKYETDAIQRTEELEE-----------AKKKLV 1402
Cdd:pfam15964 518 CLKLTELLGESEHQLHLTRLEKESIQQSFSN----EAKAQALQAQQREQELTQKMQQMEAQHDktvneqyslltSQNTFI 593
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1529987947 1403 TRLQES--------EEIMEASNAKCSSLEKTKHRLQTEIEDL 1436
Cdd:pfam15964 594 AKLKEEcctlakklEEITQKSRSEVEQLSQEKEYLQDRLEKL 635
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1795-1938 |
5.98e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1795 EQTIKDLQMRLDEAEQiALKGGKKQVQKLEARVKELETELDAEQKKSQEYQKVVRKYERRIKELS----YQA-----EED 1865
Cdd:COG1579 23 EHRLKELPAELAELED-ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeYEAlqkeiESL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1529987947 1866 KKNLVRLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADTAETQVNKLRVRTRDQVSK 1938
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
888-1048 |
6.94e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.82 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 888 LIQEKNDLSLQLQAEQdNLADAEDRCDLLIKTKIQLEAKVKELMERLedeeemssnvlakkRKLEDECAELKKDIDDLEI 967
Cdd:cd22656 99 LIDDLADATDDEELEE-AKKTIKALLDDLLKEAKKYQDKAAKVVDKL--------------TDFENQTEKDQTALETLEK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 968 TL-AKIEKEKHAIENK-VKNLIEEMAALDETILKLTKEKkalQEAHQQTLDDLQAEEDKVNALTKAKAKLEQQVDDLEGS 1045
Cdd:cd22656 164 ALkDLLTDEGGAIARKeIKDLQKELEKLNEEYAAKLKAK---IDELKALIADDEAKLAAALRLIADLTAADTDLDNLLAL 240
|
...
gi 1529987947 1046 LEQ 1048
Cdd:cd22656 241 IGP 243
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
854-1006 |
7.85e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 854 EKELAAlKVELAKLKEALEK-SEIKRKELEERQVSLIQEKNDLslqlqaeqdnladaEDRCDLLIKTKIQLEAKVKELME 932
Cdd:PRK12704 57 EALLEA-KEEIHKLRNEFEKeLRERRNELQKLEKRLLQKEENL--------------DRKLELLEKREEELEKKEKELEQ 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1529987947 933 RLEDEEEMSSNVLAKKRKLEDE---CAELKKDiDDLEITLAKIEKE-KHAIENKVKNlIEEMAaldetilKLTKEKKA 1006
Cdd:PRK12704 122 KQQELEKKEEELEELIEEQLQElerISGLTAE-EAKEILLEKVEEEaRHEAAVLIKE-IEEEA-------KEEADKKA 190
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1276-1711 |
7.90e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1276 RQLNEANTQRARAQAESGEVSRKLEERESMVSQLQRAKnsfsQNVEELKKQLEEENKAKNALAHSLQSSRhdcdlLREQY 1355
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELE----AELEELREELEKLEKLLQLLPLYQELEA-----LEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1356 EEEQEAKGELQRALskanAEVAQWRTKYEtdaiQRTEELEEAKKKLVTRLQESEEIMEAsnakcsslektkhrlqtEIED 1435
Cdd:COG4717 142 AELPERLEELEERL----EELRELEEELE----ELEAELAELQEELEELLEQLSLATEE-----------------ELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1436 LIIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELEISQKESRGLSTELFKLKNSyeeTLDHLETIKRENKNLQE 1515
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA---ALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1516 EITDLTdQISQGAKTIHELEKMKKGLEMEKTEIQAALEEAEGTLEHEESKTLRIQLELNQMKS---------------DV 1580
Cdd:COG4717 274 TIAGVL-FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpeellelldrieelqEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1581 DRKLAEKDEELDNLRRKHQRS--LESMQATLDAEAKSRNEAVRLKKKMEGDLNEMEVQLNHANRLASESQKLL--RNLQI 1656
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEE 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 1657 QIKDVQLELDETVHQNEELKEQVAVTERRNNLLAAEVEELRALLEQNDRARKLAE 1711
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1392-1927 |
7.95e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.17 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1392 EELEEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHrlqtEIEDLIIDLERANaaaaaLDKKQRNFDKVLAEWKQKyeec 1471
Cdd:pfam05701 42 LELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKR----LIEELKLNLERAQ-----TEEAQAKQDSELAKLRVE---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1472 QSELEISQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEITDLTDQISQGAKTIH-------ELEKMKKGLEME 1544
Cdd:pfam05701 109 EMEQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEeavsaskEIEKTVEELTIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1545 KTEIQAALEEAEGTLEHEESKTLRIQLELNQMKSDVDRKLAEKDEELDNLrRKHQRSLESMQATLDAeaksrneAVRLKK 1624
Cdd:pfam05701 189 LIATKESLESAHAAHLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKLET-------ASALLL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1625 KMEGDLNE-MEVQLNHANRLASESQKLLRNLQIQIKDVQLELDETVHQNEELKEQVavterrnNLLAAEVEELRALLEQn 1703
Cdd:pfam05701 261 DLKAELAAyMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEV-------NCLRVAAASLRSELEK- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1704 drarklaehellEASERVNLLHSQNTGLINqkkklendLSMLSNEVDDAVQECRNAEEKAKKAitdAAMMAEELKKEQDT 1783
Cdd:pfam05701 333 ------------EKAELASLRQREGMASIA--------VSSLEAELNRTKSEIALVQAKEKEA---REKMVELPKQLQQA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1784 SAHLERMKKNMEQTIKDLQMRLDEAEQialkgGKKQVQKLEARVKELETELDAEqkksqeyqkvvrKYERRIKELSYQAE 1863
Cdd:pfam05701 390 AQEAEEAKSLAQAAREELRKAKEEAEQ-----AKAAASTVESRLEAVLKEIEAA------------KASEKLALAAIKAL 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1864 EDKKNLVRLQDLID---KLQVKVKSY---KRQTEEAEEQANTNLSKYRKLQHELDDAEERADTAETQVNK 1927
Cdd:pfam05701 453 QESESSAESTNQEDsprGVTLSLEEYyelSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNR 522
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
868-1436 |
8.02e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 868 KEALEKSEiKRKELEERQVSLIQEKNDLSLQLQAEQDN---LADAEDRCDLLIKTKIQLEAKVKELMERLEDEEEMSSNV 944
Cdd:PRK04863 499 RELLRRLR-EQRHLAEQLQQLRMRLSELEQRLRQQQRAerlLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEA 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 945 LAKKRKLEDECAELKKDIDdleiTLAKIEKEKHAIENKVKNLIEEMAALDETilkltkeKKALQEAHQQTLDDLQAEEDK 1024
Cdd:PRK04863 578 RERRMALRQQLEQLQARIQ----RLAARAPAWLAAQDALARLREQSGEEFED-------SQDVTEYMQQLLERERELTVE 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1025 VNALTKAKAKLEQQVDDLE----GSLEQEKKLR------------------------------------MDLERVKRKLE 1064
Cdd:PRK04863 647 RDELAARKQALDEEIERLSqpggSEDPRLNALAerfggvllseiyddvsledapyfsalygparhaivvPDLSDAAEQLA 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1065 GdLKLSLESVMDLENDKQQLEEKLkkkdFEMNELstriedEQALVNQLQKKikelQARTEELEEELEADRACR----AKV 1140
Cdd:PRK04863 727 G-LEDCPEDLYLIEGDPDSFDDSV----FSVEEL------EKAVVVKIADR----QWRYSRFPEVPLFGRAARekriEQL 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1141 EKQRSDVARELEDLS------ERLEEAGG---ATSAQIEMNKKREAEFLKMRRDLEEAmlhhEATTAALRKKHAdsvaEL 1211
Cdd:PRK04863 792 RAEREELAERYATLSfdvqklQRLHQAFSrfiGSHLAVAFEADPEAELRQLNRRRVEL----ERALADHESQEQ----QQ 863
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1212 SEQIDSLQRVKQKLEKERSEAKMEADD-LASTVEQLSkgkatsEKMcrlyeDQMNEAKAKADELQRQLNEANTQRARAQA 1290
Cdd:PRK04863 864 RSQLEQAKEGLSALNRLLPRLNLLADEtLADRVEEIR------EQL-----DEAEEAKRFVQQHGNALAQLEPIVSVLQS 932
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1291 ESGEVSRKLEERESMVSQLQRAKN------SFSQNVEELKKQLEEENKAKNA-----LAHSLQSSRHDCDLLREQYEEEQ 1359
Cdd:PRK04863 933 DPEQFEQLKQDYQQAQQTQRDAKQqafaltEVVQRRAHFSYEDAAEMLAKNSdlnekLRQRLEQAEQERTRAREQLRQAQ 1012
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1360 EAKGELQRALSKANAEvaqWRTKYET--DAIQRTEEL-----EEAKKKLVTRLQESEEIMEASNAKCSSLEKTKHRLQTE 1432
Cdd:PRK04863 1013 AQLAQYNQVLASLKSS---YDAKRQMlqELKQELQDLgvpadSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAE 1089
|
....
gi 1529987947 1433 IEDL 1436
Cdd:PRK04863 1090 MDNL 1093
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1784-1918 |
8.27e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1784 SAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQKL----EARVKELETELDAEQKKSQEYQKVVRKYERRIKELS 1859
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLrnefEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1529987947 1860 YQAEEDKKNLVRLQDLIDKLQVKVksykrqtEEAEEQANTNLSKYRKLQHE------LDDAEERA 1918
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEEL-------EELIEEQLQELERISGLTAEeakeilLEKVEEEA 167
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
854-1113 |
9.23e-03 |
|
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: 40.98 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 854 EKELAALKVELAKLKEALEKSEIKRKEL-EERQVSLIQEKNDLSLQLQA----------------EQDNLADAEDRCDLL 916
Cdd:pfam12128 652 RLDLRRLFDEKQSEKDKKNKALAERKDSaNERLNSLEAQLKQLDKKHQAwleeqkeqkreartekQAYWQVVEGALDAQL 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 917 IKTKIQLEAKVKELMERLEDEEEMSSNVLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHA------------------ 978
Cdd:pfam12128 732 ALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEvlryfdwyqetwlqrrpr 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 979 -------IENKVKNLIEEMAALDET----ILKLTKEKKALQEAHQQTLDDLQAEEDKVNALtkAKAKLEQQVDDLEGSLE 1047
Cdd:pfam12128 812 latqlsnIERAISELQQQLARLIADtklrRAKLEMERKASEKQQVRLSENLRGLRCEMSKL--ATLKEDANSEQAQGSIG 889
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1529987947 1048 QEKKLRMDLERVKRKLEGDLKLSLESVMDLENDKQQLE-----EKLKKKDFEMNELSTRIEDEQALVNQLQ 1113
Cdd:pfam12128 890 ERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGlaetwESLREEDHYQNDKGIRLLDYRKLVPYLE 960
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1775-1906 |
9.54e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1775 EELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQiALKGGKKQVQKLEARVKELET--ELDAEQKKSQEYQKVVRKYE 1852
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLEL-EIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESLKRRISDLE 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1529987947 1853 RRIKELSYQAEEDKKNLVRLQDLIDKLQVKVKSYKRQTEEAEEQANTNLSKYRK 1906
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
907-1161 |
9.58e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 907 ADAEDRCDLLIKTKiQLEAKVKELMERLEDEEEMssnvLAKKRKLEDECAELKKDIDDLEITLAKIEKEKHAIENKVKNL 986
Cdd:PRK11281 39 ADVQAQLDALNKQK-LLEAEDKLVQQDLEQTLAL----LDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 987 IEEMAA---LDETILKLTKEKKALQEAhQQTLDDLQAE--------EDKVNALTKAKAKLEQQVDDLEGSLEQEKKLRMD 1055
Cdd:PRK11281 114 TRETLStlsLRQLESRLAQTLDQLQNA-QNDLAEYNSQlvslqtqpERAQAALYANSQRLQQIRNLLKGGKVGGKALRPS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1056 LervKRKLEGDLKLslesvMDLENDKQ--------QLEEKLKKKDFEMNELSTRIEDE----QALVN-----QLQKKIKE 1118
Cdd:PRK11281 193 Q---RVLLQAEQAL-----LNAQNDLQrkslegntQLQDLLQKQRDYLTARIQRLEHQlqllQEAINskrltLSEKTVQE 264
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1529987947 1119 LQArteeleeeleADRACRAkveKQRSDVARELE---DLSERLEEA 1161
Cdd:PRK11281 265 AQS----------QDEAARI---QANPLVAQELEinlQLSQRLLKA 297
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1427-1651 |
9.90e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 40.09 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1427 HRLQTEIEDLIIDLERANaaaaaldkKQRNFDKVLAEWKQKY-EECQSELEISQKESRGLSTELFKLKNSYEETLDHLET 1505
Cdd:pfam06008 15 YKINYNLENLTKQLQEYL--------SPENAHKIQIEILEKElSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1506 IKRENKNLQEEITDLTDQISQGAKTIHE----------------LEKMK-KGLEMEKTEIQAALEEAEGTLEHEESKTLR 1568
Cdd:pfam06008 87 LAEAIKNLIDNIKEINEKVATLGENDFAlpssdlsrmlaeaqrmLGEIRsRDFGTQLQNAEAELKAAQDLLSRIQTWFQS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1529987947 1569 IQLELNQMKSDVDRKLAEKDEELDNLRRKHQRslesmqatldAEAKSRnEAVRLKKKMEGDLNEMEVQLNHANRLASESQ 1648
Cdd:pfam06008 167 PQEENKALANALRDSLAEYEAKLSDLRELLRE----------AAAKTR-DANRLNLANQANLREFQRKKEEVSEQKNQLE 235
|
...
gi 1529987947 1649 KLL 1651
Cdd:pfam06008 236 ETL 238
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