|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
152-827 |
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: 1481.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVAALGDTPAKKAQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 311
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENMDDGQELMATDH 391
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 392 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 471
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 472 QNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMF 551
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 552 ILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPDKKRKY 631
Cdd:cd14927 401 ILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 632 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGSDAAFDSKTGSKEKRKKAASFQTVSQV 711
Cdd:cd14927 481 EAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEDPKSGVKEKRKKAASFQTVSQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 712 HKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPHAI 791
Cdd:cd14927 561 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAI 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 2108526737 792 PDDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14927 641 PDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
152-827 |
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: 1345.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVAALGdtpakKAQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 311
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASS-----KKKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENMDDGQELMATDH 391
Cdd:cd01377 156 TGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 392 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 471
Cdd:cd01377 236 AFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 472 QNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMF 551
Cdd:cd01377 316 QNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 552 ILEQEEYKREGIEWTFIDFGLDLQACIDLIEKP-LGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPrpdKKRK 630
Cdd:cd01377 396 VLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKP---KPKK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 631 YEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGSDaafdskTGSKEKRKKAASFQTVSQ 710
Cdd:cd01377 473 SEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESG------GGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 711 VHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPHA 790
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*..
gi 2108526737 791 IPDDkFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
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 ... |
152-827 |
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: 1165.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVAALGDtPAKKAqgpatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 311
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIE-SKKKL--------GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKpELLDMLLVSSNPYDYHFCSQGVTTVENMDDGQELMATDH 391
Cdd:cd14929 152 RGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 392 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 471
Cdd:cd14929 231 AMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 472 QNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMF 551
Cdd:cd14929 311 QNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 552 ILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPDKKrKY 631
Cdd:cd14929 391 VLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKK-KF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 632 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGSDAAfdSKTGSKeKRKKAASFQTVSQV 711
Cdd:cd14929 470 EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSA--IQFGEK-KRKKGASFQTVASL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 712 HKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPHAI 791
Cdd:cd14929 547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTF 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 2108526737 792 PDDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14929 627 PKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
153-827 |
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: 1150.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 153 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 232
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 233 SGAGKTVNTKRVIQYFAIVAALGDtPAKKAQgpaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 312
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGD-LAKKKD---SKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 313 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENMDDGQELMATDHA 392
Cdd:cd14913 158 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 393 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 472
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 473 NVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 552
Cdd:cd14913 318 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 553 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPDKKRKyE 632
Cdd:cd14913 398 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRA-E 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 633 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGSDAAFDSKTGSKekrKKAASFQTVSQVH 712
Cdd:cd14913 477 AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAK---KKGSSFQTVSALF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 713 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPHAIP 792
Cdd:cd14913 554 RENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIP 633
|
650 660 670
....*....|....*....|....*....|....*
gi 2108526737 793 DDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
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 ... |
153-827 |
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: 1105.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 153 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 232
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 233 SGAGKTVNTKRVIQYFAIVAALGDTpAKKAQGPATktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 312
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDR-SKKDQTPGK---GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 313 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENMDDGQELMATDHA 392
Cdd:cd14917 158 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 393 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 472
Cdd:cd14917 238 FDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 473 NVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 552
Cdd:cd14917 318 NVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 553 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRpDKKRKYE 632
Cdd:cd14917 398 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPR-NIKGKPE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 633 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGSDAAFDSKTGskeKRKKAASFQTVSQVH 712
Cdd:cd14917 477 AHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKGKG---KAKKGSSFQTVSALH 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 713 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPHAIP 792
Cdd:cd14917 554 RENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 633
|
650 660 670
....*....|....*....|....*....|....*
gi 2108526737 793 DDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14917 634 EGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
153-827 |
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: 1074.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 153 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 232
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 233 SGAGKTVNTKRVIQYFAIVAALGDTPAKKAqgpATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 312
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKKEN---PNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 313 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENMDDGQELMATDHA 392
Cdd:cd14916 159 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 393 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 472
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 473 NVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 552
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 553 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRpDKKRKYE 632
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPR-NVKGKQE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 633 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGSDAAFDSKtgSKEKRKKAASFQTVSQVH 712
Cdd:cd14916 478 AHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGK--GKGGKKKGSSFQTVSALH 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 713 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPHAIP 792
Cdd:cd14916 556 RENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 635
|
650 660 670
....*....|....*....|....*....|....*
gi 2108526737 793 DDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14916 636 EGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
153-827 |
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: 1048.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 153 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 232
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 233 SGAGKTVNTKRVIQYFAIVAALGDtpaKKAQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 312
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGD---KKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 313 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENMDDGQELMATDHA 392
Cdd:cd14923 159 GKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 393 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 472
Cdd:cd14923 239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 473 NVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 552
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 553 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPdKKRKYE 632
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKP-AKGKAE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 633 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGSDAAfDSKTGSKEKRKKAASFQTVSQVH 712
Cdd:cd14923 478 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAG-DSGGSKKGGKKKGSSFQTVSAVF 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 713 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPHAIP 792
Cdd:cd14923 557 RENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIP 636
|
650 660 670
....*....|....*....|....*....|....*
gi 2108526737 793 DDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14923 637 EGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
140-827 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1039.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 140 IEDMAMLTHLNEASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDML 219
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 220 RNRENQSMLITGESGAGKTVNTKRVIQYFAIVAAlgdtpakkaQGPATKtGGTLEDQIIEANPAMEAFGNAKTLRNDNSS 299
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSG---------SGSAGN-VGRLEEQILQSNPILEAFGNAKTVRNNNSS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 300 RFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVsSNPYDYHFCSQ-GVTTVE 378
Cdd:pfam00063 151 RFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TNPKDYHYLSQsGCYTID 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 379 NMDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLH 458
Cdd:pfam00063 230 GIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 459 PRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINF 537
Cdd:pfam00063 310 RRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLdVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 538 TNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNHiGK 616
Cdd:pfam00063 390 VNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 617 SPNFQKPRPdkkrKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENY-VGSDAAFDSKTGS 695
Cdd:pfam00063 468 HPHFQKPRL----QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYeTAESAAANESGKS 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 696 KEKRKKAASFQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLL 775
Cdd:pfam00063 544 TPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRIT 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2108526737 776 YAEFKQRYRILNPHAIPDDkFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:pfam00063 624 FQEFVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
154-827 |
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: 1030.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 154 VLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGES 233
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 234 GAGKTVNTKRVIQYFAIVAALGDtpakKAQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTG 313
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGE----KKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 314 KLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENMDDGQELMATDHAM 393
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 394 DILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQN 473
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 474 VEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFIL 553
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 554 EQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPdKKRKYEA 633
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKV-VKGKAEA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 634 HFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGSDAAFDSKTGSKekrKKAASFQTVSQVHK 713
Cdd:cd14918 478 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAK---KKGSSFQTVSALFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 714 ENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPHAIPD 793
Cdd:cd14918 555 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE 634
|
650 660 670
....*....|....*....|....*....|....
gi 2108526737 794 DKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
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 ... |
153-827 |
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: 1026.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 153 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 232
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 233 SGAGKTVNTKRVIQYFAIVAALGDTpaKKAQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 312
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 313 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENMDDGQELMATDHA 392
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 393 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 472
Cdd:cd14910 240 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 473 NVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 552
Cdd:cd14910 320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 553 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPdKKRKYE 632
Cdd:cd14910 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKVE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 633 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGSDAafDSKTGSKEKRKKAASFQTVSQVH 712
Cdd:cd14910 479 AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEA--EEGGGKKGGKKKGSSFQTVSALF 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 713 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPHAIP 792
Cdd:cd14910 557 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 636
|
650 660 670
....*....|....*....|....*....|....*
gi 2108526737 793 DDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14910 637 EGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
153-827 |
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: 1023.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 153 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 232
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 233 SGAGKTVNTKRVIQYFAIVAALGDTpaKKAQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 312
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 313 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENMDDGQELMATDHA 392
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 393 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 472
Cdd:cd14915 240 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 473 NVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 552
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 553 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPdKKRKYE 632
Cdd:cd14915 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 633 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENyvGSDAAFDSKTGSKEKRKKAASFQTVSQVH 712
Cdd:cd14915 479 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG--GQTAEAEGGGGKKGGKKKGSSFQTVSALF 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 713 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPHAIP 792
Cdd:cd14915 557 RENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 636
|
650 660 670
....*....|....*....|....*....|....*
gi 2108526737 793 DDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14915 637 EGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
152-827 |
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: 1021.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVaalGDTPAKKAQGPatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 311
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANI---GGTGKQSSDGK-----GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENMDDGQELMATDH 391
Cdd:cd14934 153 TGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 392 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 471
Cdd:cd14934 233 AFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 472 QNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMF 551
Cdd:cd14934 313 QNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 552 ILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPDKKRKY 631
Cdd:cd14934 393 VLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKGP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 632 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENyvgsdaafDSKTGSKEKRKKAASFQTVSQV 711
Cdd:cd14934 473 EAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKE--------EEAPAGSKKQKRGSSFMTVSNF 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 712 HKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPHAI 791
Cdd:cd14934 545 YREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVI 624
|
650 660 670
....*....|....*....|....*....|....*.
gi 2108526737 792 PDDkFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14934 625 PQG-FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
153-827 |
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: 1016.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 153 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 232
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 233 SGAGKTVNTKRVIQYFAIVAALGDTpaKKAQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 312
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 313 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENMDDGQELMATDHA 392
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 393 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 472
Cdd:cd14912 240 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 473 NVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 552
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 553 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPdKKRKYE 632
Cdd:cd14912 400 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKV-VKGKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 633 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGSDAAFDSKTGSKEKRKKAASFQTVSQVH 712
Cdd:cd14912 479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAKKGGKKKGSSFQTVSALF 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 713 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPHAIP 792
Cdd:cd14912 559 RENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 638
|
650 660 670
....*....|....*....|....*....|....*
gi 2108526737 793 DDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14912 639 EGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
152-827 |
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: 1011.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVAAlgdtpaKKAQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 311
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGA------SKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENMDDGQELMATDH 391
Cdd:cd14909 155 TGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 392 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 471
Cdd:cd14909 235 AFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 472 QNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMF 551
Cdd:cd14909 315 RNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 552 ILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPDKKRKY 631
Cdd:cd14909 395 VLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 632 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGSDAafDSKTGSKEKRKKAASFQTVSQV 711
Cdd:cd14909 475 AAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSG--GGEQAKGGRGKKGGGFATVSSA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 712 HKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPHAI 791
Cdd:cd14909 553 YKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGI 632
|
650 660 670
....*....|....*....|....*....|....*.
gi 2108526737 792 PDDKfvDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14909 633 QGEE--DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
133-839 |
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: 1003.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 133 NPPKFDMIEDMAMLTHLNEASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIAD 212
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 213 NAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAivaalgdtpakkAQGPATKTGGTLEDQIIEANPAMEAFGNAKT 292
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLA------------SVSGSNTEVGSVEDQILESNPILEAFGNAKT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 293 LRNDNSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQ 372
Cdd:smart00242 149 LRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 373 GVT-TVENMDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEA-DGTESADKASYLMGVSSA 450
Cdd:smart00242 228 GGClTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTvKDKEELSNAAELLGVDPE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 451 DLIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSF 530
Cdd:smart00242 308 ELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 531 EQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKM 609
Cdd:smart00242 388 EQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 610 YDNHiGKSPNFQKPRpdkkRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLyenyvgsdaaF 689
Cdd:smart00242 467 NQHH-KKHPHFSKPK----KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASL----------F 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 690 DSKTGSKEKRKKaasFQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKG 769
Cdd:smart00242 532 PSGVSNAGSKKR---FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAG 608
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 770 FPNRLLYAEFKQRYRILNPHAIPDDKFvDSRKAAEKLLASLDIDHNQYKFGHTKVFFKAGLLGHLEELRD 839
Cdd:smart00242 609 FPYRLPFDEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
80-1176 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 878.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 80 HTIASDGKkRAWIPDEKEAYIEIEIKELSGDKVIV----ETKDGKTLTVK--DCDIQQMNPPKFDMIEDMAMLTHLNEAS 153
Cdd:COG5022 3 TTNAEVGS-GCWIPDEEKGWIWAEIIKEAFNKGKVteegKKEDGESVSVKkkVLGNDRIKLPKFDGVDDLTELSYLNEPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 154 VLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGES 233
Cdd:COG5022 82 VLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 234 GAGKTVNTKRVIQYFAIVaalgdtpakkaQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTG 313
Cdd:COG5022 162 GAGKTENAKRIMQYLASV-----------TSSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 314 KLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQG-VTTVENMDDGQELMATDHA 392
Cdd:COG5022 231 EICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQ-NPKDYIYLSQGgCDKIDGIDDAKEFKITLDA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 393 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQrQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 472
Cdd:COG5022 310 LKTIGIDEEEQDQIFKILAAILHIGNIEFKE-DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 473 NVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 552
Cdd:COG5022 389 NLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 553 LEQEEYKREGIEWTFIDFgLDLQACIDLIEK--PLGIMSILEEECMFPKATDNSFKAKMYDN-HIGKSPNFQKPR-PDKK 628
Cdd:COG5022 469 LEQEEYVKEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRfRDNK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 629 rkyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYvgsdaafdsktgskEKRKKAASFQTV 708
Cdd:COG5022 548 ------FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE--------------ENIESKGRFPTL 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 709 SQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNP 788
Cdd:COG5022 608 GSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSP 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 789 HAIPDDKFV---DSRKAAEKLLASLDIDHNQYKFGHTKVFFKAGLLGHLEELRDERLAKVLTLLQAAARGKIMRMELLKL 865
Cdd:COG5022 688 SKSWTGEYTwkeDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQA 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 866 MERREALMIIQWNIRAFNAVKHWPWMKLFFKIKPLLRSATTEKELVSLKEELAKLKEALEKsEVKRKELEERQVSLIQEK 945
Cdd:COG5022 768 LKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKR-EKKLRETEEVEFSLKAEV 846
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 946 NDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEIMErLEDEEEMSANVLAKKRKLEDECAELKKDID-----DLEI 1020
Cdd:COG5022 847 LIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQE-LKIDVKSISSLKLVNLELESEIIELKKSLSsdlieNLEF 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1021 TLA--------------KVEKEKHATENKVKN-LIEEMAALDETilklTKEKKALLEAHQQTLDDLQAEEDKVNILTKAK 1085
Cdd:COG5022 926 KTEliarlkkllnnidlEEGPSIEYVKLPELNkLHEVESKLKET----SEEYEDLLKKSTILVREGNKANSELKNFKKEL 1001
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1086 AKLEQQVDDLEGSLEQEKKLRMDLervrrklegdlkLSLESVMdlendkqqldeklkKKDFEMNEMSTRIEDEQALVNQL 1165
Cdd:COG5022 1002 AELSKQYGALQESTKQLKELPVEV------------AELQSAS--------------KIISSESTELSILKPLQKLKGLL 1055
|
1130
....*....|.
gi 2108526737 1166 QKKIKELQART 1176
Cdd:COG5022 1056 LLENNQLQARY 1066
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
152-827 |
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: 826.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRR-SEVPPHIYSIADNAYNDMLRNRENQSMLIT 230
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 231 GESGAGKTVNTKRVIQYFAIVAALGDTPAKKAQGpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 310
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSAS-------SIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 311 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHF----CSQGVTTVENMDDGQEL 386
Cdd:cd00124 154 PTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDDAEEF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 387 MATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREE--QAEADGTESADKASYLMGVSSADLIKGLLHPRVKVG 464
Cdd:cd00124 234 QELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 465 NEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQ--YFIGVLDIAGFEIFELNSFEQLCINFTNEKL 542
Cdd:cd00124 314 GETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 543 QQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQ 621
Cdd:cd00124 394 QQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 622 KPRPDKKrkyeaHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSnkllaslyenyvgsdaafdsktgskekrkk 701
Cdd:cd00124 473 KKRKAKL-----EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS------------------------------ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 702 aasfqtvsqVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQ 781
Cdd:cd00124 518 ---------QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLK 588
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2108526737 782 RYRILNPHAiPDDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
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 ... |
152-827 |
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: 791.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVAAL----GDTPAKKAQGPATKTGGtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 307
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgSGAVPHPAVNPAVLIGE-LEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 308 HFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS-----QKKPELLDmllvssNPYDYHFCSQGVTTVENMDD 382
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAgatpeQREKFILD------DVKSYAFLSNGSLPVPGVDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 383 GQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVK 462
Cdd:cd14911 234 YAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 463 VGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEK 541
Cdd:cd14911 314 VGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLdRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 542 LQQFFNHHMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQ 621
Cdd:cd14911 394 LQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFM 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 622 KprpdKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENY----VGSDAAFDSKTGSke 697
Cdd:cd14911 473 K----TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAeivgMAQQALTDTQFGA-- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 698 kRKKAASFQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYA 777
Cdd:cd14911 547 -RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2108526737 778 EFKQRYRILNPHAIPdDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
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 ... |
152-827 |
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: 774.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVAalgdtpAKKAQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 311
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVA------SSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPEL-LDMLLVSSNpyDYHFCSQGVTTVENMDDGQELMATD 390
Cdd:cd14920 155 TGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 391 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVK 470
Cdd:cd14920 233 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 471 GQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLyTSLPRQ--YFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNH 548
Cdd:cd14920 313 AQTKEQADFAVEALAKATYERLFRWLVHRINKAL-DRTKRQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 549 HMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKPRp 625
Cdd:cd14920 392 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPR- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 626 dkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYEN---YVGSD---AAFDSKTGSKEKR 699
Cdd:cd14920 470 --QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrIVGLDqvtGMTETAFGSAYKT 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 700 KKAAsFQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEF 779
Cdd:cd14920 548 KKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2108526737 780 KQRYRILNPHAIPdDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14920 627 RQRYEILTPNAIP-KGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
152-827 |
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: 732.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVAAlgDTPAKKAQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 311
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVAS--SFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVsSNPYDYHFCSQGVTTVENMDDGQELMATDH 391
Cdd:cd14932 159 NGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCL-EDYSKYRFLSNGNVTIPGQQDKELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 392 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 471
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 472 QNVEQVTYAVGALAKATYDRMFKWLVIRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHM 550
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALdKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 551 FILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKPrpdK 627
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQ-GNNPKFQKP---K 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 628 KRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENY---VGSD---AAFDSKTGSKEKRKk 701
Cdd:cd14932 474 KLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdriVGLDkvaGMGESLHGAFKTRK- 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 702 aASFQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQ 781
Cdd:cd14932 553 -GMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2108526737 782 RYRILNPHAIPDDkFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14932 632 RYEILTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
152-827 |
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 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVAAlgdtpAKKAQGPATKTgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 311
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVAS-----SHKGKKDTSIT-GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELL-DMLLVSSNpyDYHFCSQGVTTVENMDDGQELMATD 390
Cdd:cd14921 155 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 391 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVK 470
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 471 GQNVEQVTYAVGALAKATYDRMFKWLVIRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHH 549
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKALdKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 550 MFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKPrpd 626
Cdd:cd14921 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKP--- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 627 KKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENY---VGSD--AAFDSKTGSKEKRKK 701
Cdd:cd14921 469 KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdriVGLDqmAKMTESSLPSASKTK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 702 AASFQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQ 781
Cdd:cd14921 549 KGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2108526737 782 RYRILNPHAIPDDkFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14921 629 RYEILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
152-827 |
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: 695.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVAALGDTpaKKAQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 311
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKT--KKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVsSNPYDYHFCSQGVTTVENMDDGQELMATDH 391
Cdd:cd15896 159 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL-ENYNNYRFLSNGNVTIPGQQDKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 392 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 471
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 472 QNVEQVTYAVGALAKATYDRMFKWLVIRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHM 550
Cdd:cd15896 318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALdKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 551 FILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKPrpdK 627
Cdd:cd15896 398 FILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKP---K 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 628 KRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENyVGSDAAFDSKTGSKEK----RKKAA 703
Cdd:cd15896 474 KLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKD-VDRIVGLDKVSGMSEMpgafKTRKG 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 704 SFQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRY 783
Cdd:cd15896 553 MFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2108526737 784 RILNPHAIPDDkFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd15896 633 EILTPNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
152-827 |
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: 692.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVAalgdTPAKKAQGPATKtgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 311
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVA----SSPKGRKEPGVP--GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYdYHFCSQGVTTvenmDDGQE---LMA 388
Cdd:cd14930 155 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSS----SPGQErelFQE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 389 TDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 468
Cdd:cd14930 230 TLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 469 VKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSlPRQ--YFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFF 546
Cdd:cd14930 310 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRS-PRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 547 NHHMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKP 623
Cdd:cd14930 389 NHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 624 RpdkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLY---ENYVGSDAAFDSKTGSKEKRK 700
Cdd:cd14930 468 R---HLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRP 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 701 KAASFQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFK 780
Cdd:cd14930 545 RRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFR 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2108526737 781 QRYRILNPHAIPDDkFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14930 625 QRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
153-827 |
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: 689.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 153 SVLYNLRRRYS-AWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVaalgdtpakkaQGPATKTGGTlEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 311
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATV-----------GGSSSGETQV-EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQK-KPELLDMLLVSSNpyDYHFCSQG-VTTVENMDDGQELMAT 389
Cdd:cd01380 150 NYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKELHLGSAE--DFFYTNQGgSPVIDGVDDAAEFEET 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 390 DHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVV 469
Cdd:cd01380 228 RKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 470 KGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLP--RQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFN 547
Cdd:cd01380 308 KPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 548 HHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGK-SPNFQKPRPD 626
Cdd:cd01380 388 QHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 627 KKRkyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNkllaslyenyvgsdaafdsktgskekRKKaasfq 706
Cdd:cd01380 467 NTA-----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN--------------------------RKK----- 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 707 TVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRIL 786
Cdd:cd01380 511 TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVL 590
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2108526737 787 NP--HAIPDDKfvdsRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd01380 591 LPskEWLRDDK----KKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
152-827 |
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: 689.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVAAlgDTPAKKAQgpatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 311
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVAS--SHKSKKDQ-------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsnPYD-YHFCSQGVTTVENMDDGQELMATD 390
Cdd:cd14919 152 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE--PYNkYRFLSNGHVTIPGQQDKDMFQETM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 391 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVK 470
Cdd:cd14919 230 EAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 471 GQNVEQVTYAVGALAKATYDRMFKWLVIRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHH 549
Cdd:cd14919 310 AQTKEQADFAIEALAKATYERMFRWLVLRINKALdKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 550 MFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKPrpd 626
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKP--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 627 KKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENyVGSDAAFDSKTGSKEK------RK 700
Cdd:cd14919 466 KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD-VDRIIGLDQVAGMSETalpgafKT 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 701 KAASFQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFK 780
Cdd:cd14919 545 RKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFR 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2108526737 781 QRYRILNPHAIPDDkFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14919 625 QRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
153-827 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 653.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 153 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 232
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 233 SGAGKTVNTKRVIQYFAIVAalgdtpakkaqGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 312
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVS-----------GGSESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 313 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENMDDGQELMATDHA 392
Cdd:cd01378 151 GEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 393 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADgTESADKASYLMGVSSADLIKGLLHPRVKVGNEY---VV 469
Cdd:cd01378 231 MKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 470 KGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQ-YFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFfnh 548
Cdd:cd01378 310 VPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQI--- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 549 hmFIL-----EQEEYKREGIEWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFP-KATDNSFKAKMydNHIGKSPNFQ 621
Cdd:cd01378 387 --FIEltlkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL--NQLFSNHPHF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 622 KPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENyvgsdaafDSKTGSKeKRKK 701
Cdd:cd01378 462 ECPSGHFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE--------GVDLDSK-KRPP 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 702 AASFQTvsqvhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQ 781
Cdd:cd01378 533 TAGTKF-----KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLE 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2108526737 782 RYRILNPHAIPDDKFvDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd01378 608 RYKLLSPKTWPAWDG-TWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
152-827 |
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: 648.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVAALGDtpakkaqgpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 311
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS---------------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVsSNPYDYHFCSQG-VTTVENMDDGQELMATD 390
Cdd:cd01381 146 NGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLEL-GDASDYYYLTQGnCLTCEGRDDAAEFADIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 391 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQRE--EQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 468
Cdd:cd01381 225 SAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 469 VKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYF---IGVLDIAGFEIFELNSFEQLCINFTNEKLQQF 545
Cdd:cd01381 305 VSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 546 FNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLI-EKPLGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKPr 624
Cdd:cd01381 385 FVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 625 pdkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGSDAafdsktgskEKRKKAas 704
Cdd:cd01381 462 ---KSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGS---------ETRKKS-- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 705 fQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYR 784
Cdd:cd01381 528 -PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYR 606
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2108526737 785 ILNPhAIPDDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd01381 607 VLVP-GIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
153-827 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 629.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 153 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 232
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 233 SGAGKTVNTKRVIQYFAIVaalgdtpakkaqgpaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 312
Cdd:cd14883 82 SGAGKTETTKLILQYLCAV---------------TNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDAS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 313 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS--QKKPELLDMLLVSSnPYDYHFCSQ-GVTTVENMDDGQELMAT 389
Cdd:cd14883 147 GHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAgaKHSKELKEKLKLGE-PEDYHYLNQsGCIRIDNINDKKDFDHL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 390 DHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAE-ADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 468
Cdd:cd14883 226 RLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 469 VKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNH 548
Cdd:cd14883 306 EIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 549 HMFILEQEEYKREGIEWTFIDFGlDLQACIDLIEK-PLGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKPrpdK 627
Cdd:cd14883 386 YVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKP---D 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 628 KRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASL--YENYVGSDAAFDSKTGSKEKRKKAASF 705
Cdd:cd14883 461 RRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELftYPDLLALTGLSISLGGDTTSRGTSKGK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 706 QTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRI 785
Cdd:cd14883 541 PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLC 620
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2108526737 786 LNPHAI-PDDKfvDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14883 621 LDPRARsADHK--ETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
153-827 |
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: 615.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 153 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYkGKRRSEvPPHIYSIADNAYNDMLRNRENQSMLITGE 232
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY-RQKLLD-SPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 233 SGAGKTVNTKRVIQYfaiVAALGDTpakkaqgpatktGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 312
Cdd:cd01383 80 SGAGKTETAKIAMQY---LAALGGG------------SSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 313 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQ-GVTTVENMDDGQELMATDH 391
Cdd:cd01383 145 GKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQsNCLTIDGVDDAKKFHELKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 392 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 471
Cdd:cd01383 224 ALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 472 QNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTS-LPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHM 550
Cdd:cd01383 304 LTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGkRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 551 FILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMyDNHIGKSPNFQKPRpdkkr 629
Cdd:cd01383 384 FKLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER----- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 630 kyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGSD--AAFDSKTGSKEKRKkaasfQT 707
Cdd:cd01383 457 --GGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASrkALPLTKASGSDSQK-----QS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 708 VSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILN 787
Cdd:cd01383 530 VATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLL 609
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2108526737 788 PHAIPDDKFVDSRKAAekLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd01383 610 PEDVSASQDPLSTSVA--ILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
152-827 |
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: 584.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLIT 230
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 231 GESGAGKTVNTKRVIQYFAIVAalgdtpakkaqGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 310
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG-----------GRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 311 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQGVT-TVENMDDGQELMAT 389
Cdd:cd01384 150 DAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLK-DPKQFHYLNQSKCfELDGVDDAEEYRAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 390 DHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKqrqreEQAEADGTESADKASY--------LMGVSSADLIKGLLHPRV 461
Cdd:cd01384 229 RRAMDVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEKSEfhlkaaaeLLMCDEKALEDALCKRVI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 462 KVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEK 541
Cdd:cd01384 304 VTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 542 LQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNhIGKSPNF 620
Cdd:cd01384 384 LQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 621 QKPrpdkKRKYEAhFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYEnyvgSDAAFDSKTGSKekrk 700
Cdd:cd01384 462 SKP----KLSRTD-FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFP----PLPREGTSSSSK---- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 701 kaasFQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFK 780
Cdd:cd01384 529 ----FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2108526737 781 QRYRILNPHAipDDKFVDSRKAAEKLLASLDIdhNQYKFGHTKVFFK 827
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 ... |
152-827 |
7.53e-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: 544.54 E-value: 7.53e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLIT 230
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 231 GESGAGKTVNTKRVIQYfaIVAALGdtpakkaqgpatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 310
Cdd:cd01382 81 GESGAGKTESTKYILRY--LTESWG------------SGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 311 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLvssnpydyhfcsqgvtTVENMDDGQELMATD 390
Cdd:cd01382 147 EKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 391 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFkqrqrEEQAE---------ADGTESADKASYLMGVSSADLIKGLLHpRV 461
Cdd:cd01382 211 KAMKKIGLSDEEKLDIFRVVAAVLHLGNIEF-----EENGSdsgggcnvkPKSEQSLEYAAELLGLDQDELRVSLTT-RV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 462 KVGNEYVVKGQ------NVEQVTYAVGALAKATYDRMFKWLVIRINRtlytSLPRQ---YFIGVLDIAGFEIFELNSFEQ 532
Cdd:cd01382 285 MQTTRGGAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQ----CIPFEtssYFIGVLDIAGFEYFEVNSFEQ 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 533 LCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYD 611
Cdd:cd01382 361 FCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 612 NHiGKSPNFQKPRPDKKRKY------EAhFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYEnyvgs 685
Cdd:cd01382 440 KH-KNHFRLSIPRKSKLKIHrnlrddEG-FLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFE----- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 686 dAAFDSKTGSKEKRKKaASFQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRI 765
Cdd:cd01382 513 -SSTNNNKDSKQKAGK-LSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDL 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108526737 766 CRKGFPNRLLYAEFKQRYRILNPHAIPDdkfVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd01382 591 MQGGFPSRTSFHDLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
152-827 |
1.21e-172 |
|
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: 540.90 E-value: 1.21e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVAalGDTpakkaqgpatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 311
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVA--GST-------------NGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnpyDYHFCSQ-GVTTVENMDDGQELMATD 390
Cdd:cd14872 146 RGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA---AYGYLSLsGCIEVEGVDDVADFEEVV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 391 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASY---LMGVSSADLIKGLLHPRVKvgney 467
Cdd:cd14872 223 LAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLME----- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 468 vVKGQNV-------EQVTYAVGALAKATYDRMFKWLVIRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTN 539
Cdd:cd14872 298 -IKGCDPtripltpAQATDACDALAKAAYSRLFDWLVKKINESMrPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 540 EKLQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIEK-PLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSp 618
Cdd:cd14872 377 EKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 619 NFQkprPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGsdaafdsktgsKEK 698
Cdd:cd14872 455 TFV---YAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEG-----------DQK 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 699 RKKAasfqTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAE 778
Cdd:cd14872 521 TSKV----TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHER 596
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2108526737 779 FKQRYRILnPHAIPDDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14872 597 FLKRYRFL-VKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
152-827 |
2.23e-169 |
|
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: 532.81 E-value: 2.23e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLIT 230
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 231 GESGAGKTVNTKRVIQYFAIVAA-LGDTPAKKaqgpatktggtledqIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 309
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGgLNDSTIKK---------------IIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 310 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDmLLVSSNPYDYHFcSQGVTTVENMDDGQELMAT 389
Cdd:cd14903 146 DKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERL-FLDSANECAYTG-ANKTIKIEGMSDRKHFART 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 390 DHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAE--ADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEY 467
Cdd:cd14903 224 KEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 468 VVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFN 547
Cdd:cd14903 304 YTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 548 HHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFQKPRPDK 627
Cdd:cd14903 384 QDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 628 krkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGSDAAFDSKT--GSKEKRKKAASF 705
Cdd:cd14903 463 -----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLarGARRRRGGALTT 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 706 QTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRI 785
Cdd:cd14903 538 TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2108526737 786 LNPHAipDDKFVDSRKAAEKLLASLDIDH-NQYKFGHTKVFFK 827
Cdd:cd14903 618 FLPEG--RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
152-827 |
1.22e-164 |
|
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: 520.02 E-value: 1.22e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAVYKGKRRSEvPPHIYSIADNAYNDMLRNRENQSMLIT 230
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSISK-SPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 231 GESGAGKTVNTKRVIQYFAIVAAlgdtpakkaqgPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF- 309
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGS-----------EDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFs 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 310 --------GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS-----------------------QKKPELLDML 358
Cdd:cd14888 149 klkskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 359 LVSS-NPYDYHFCSqGVTTVENMDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQA---EADG 434
Cdd:cd14888 229 SFEPhLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASC 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 435 TESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTL-YTSLPRQYF 513
Cdd:cd14888 308 TDDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIgYSKDNSLLF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 514 IGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLI-EKPLGIMSILE 592
Cdd:cd14888 388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 593 EECMFPKATDNSFKAKMYDNHIGKSpnfqkpRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSN 672
Cdd:cd14888 467 EECFVPGGKDQGLCNKLCQKHKGHK------RFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKN 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 673 KLLASLYENYvgsdaaFDSKTGSKEKRKKaasFQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLH 752
Cdd:cd14888 541 PFISNLFSAY------LRRGTDGNTKKKK---FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNE 611
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526737 753 QLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPhaipddkfvdsrkaaekllASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14888 612 QLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN-------------------GEGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
153-827 |
1.56e-164 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 518.37 E-value: 1.56e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 153 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 232
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 233 SGAGKTVNTKRVIQYfaiVAALGDTPAKkaqgpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 312
Cdd:cd01379 82 SGAGKTESANLLVQQ---LTVLGKANNR-----------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 313 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIM----SQKKpeLLDMLLVSSNPYDY-HFCSQGVTTVENMDDGQE-L 386
Cdd:cd01379 148 GAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYaglaEDKK--LAKYKLPENKPPRYlQNDGLTVQDIVNNSGNREkF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 387 MATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQ----AEADGTESADKASYLMGVSSADLIKGLLHPRVK 462
Cdd:cd01379 226 EEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 463 VGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLY---TSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTN 539
Cdd:cd01379 306 TRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKpdrSASDEPLSIGILDIFGFENFQKNSFEQLCINIAN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 540 EKLQQFFNHHMFILEQEEYKREGIEWTFIDFG-----LDLqacidLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHi 614
Cdd:cd01379 386 EQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 615 gKSPNFQKPRPDkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLAslyenyvgsdaafdsktg 694
Cdd:cd01379 460 -KSKYYWRPKSN-----ALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 695 skekrkkaasfQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRL 774
Cdd:cd01379 516 -----------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRI 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 2108526737 775 LYAEFKQRYRILNPHAipDDKFVDSRKAAEKLLASLDIDHnqYKFGHTKVFFK 827
Cdd:cd01379 585 LFADFLKRYYFLAFKW--NEEVVANRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
152-827 |
1.96e-164 |
|
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: 520.40 E-value: 1.96e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYfaiVAALgdtpakkaqgpATKTGGT-LEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 310
Cdd:cd01385 81 ESGSGKTESTNFLLHH---LTAL-----------SQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 311 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSqKKPELLDMLLVSSNPYDYHFCSQGVT-TVENMDDGQELMAT 389
Cdd:cd01385 147 ENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLA-GASEEERKELHLKQPEDYHYLNQSDCyTLEGEDEKYEFERL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 390 DHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQR--QREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEY 467
Cdd:cd01385 226 KQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGET 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 468 VVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTL----YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQ 543
Cdd:cd01385 306 LILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 544 QFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKmYDNHIGKSPNFQK 622
Cdd:cd01385 386 YYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 623 PrpdkkRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLyenyVGSD---------------A 687
Cdd:cd01385 464 P-----QVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL----IGIDpvavfrwavlraffrA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 688 AFDSKTGSKEKRKKAASFQ---------------------TVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMD 746
Cdd:cd01385 535 MAAFREAGRRRAQRTAGHSltlhdrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFD 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 747 PFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPHAIpdDKFVDSRKaaeKLLASLDIDHNQYKFGHTKVFF 826
Cdd:cd01385 615 DELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGL--ISSKEDIK---DFLEKLNLDRDNYQIGKTKVFL 689
|
.
gi 2108526737 827 K 827
Cdd:cd01385 690 K 690
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
152-827 |
3.78e-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: 518.56 E-value: 3.78e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLR----NRENQS 226
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 227 MLITGESGAGKTVNTKRVIQYFAIVA------ALGDTPAKKAQGPATKtgGTLEDQIIEANPAMEAFGNAKTLRNDNSSR 300
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITsgfaqgASGEGEAASEAIEQTL--GSLEDRVLSSNPLLESFGNAKTLRNDNSSR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 301 FGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQGVTTVENM 380
Cdd:cd14890 159 FGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQ-TPVEYFYLRGECSSIPSC 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 381 DDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGT-ESADKASYLMGVSSADLIKGLLHP 459
Cdd:cd14890 238 DDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 460 RVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTN 539
Cdd:cd14890 318 QLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 540 EKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPLGIMSIL------------EEECMFPKATDNSFK 606
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFitlddcwrfkgeEANKKFVSQLHASFG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 607 AKMYDNHIGKS----PNFQKPRPDKKRkyeaHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNkllaSLYENY 682
Cdd:cd14890 477 RKSGSGGTRRGssqhPHFVHPKFDADK----QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRR----SIREVS 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 683 VGsdaafdsktgskekrkkaASFqtvsqvhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEG 762
Cdd:cd14890 549 VG------------------AQF-------RTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEA 603
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526737 763 IRICRKGFPNRLLYAEFKQRYRILNPHAipddkfvDSRKAAEKLLAS-LDIDHNQYKFGHTKVFFK 827
Cdd:cd14890 604 IQIRQQGFALREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKmLGLGKADWQIGSSKIFLK 662
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
907-1984 |
4.22e-163 |
|
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: 530.13 E-value: 4.22e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 907 EKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEIMER 986
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 987 LEDEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALLEAHQQ 1066
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1067 TLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQLDEKLKKKDF 1146
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1147 EMNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEELSERLEEAGGATSAQIEMNK 1226
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1227 KREADFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATS 1306
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1307 EKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKA 1386
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1387 KNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAiQRTEELEEAKKKLVTRLQEAEETVE 1466
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1467 TSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLK 1546
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1547 NSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLEL 1626
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1627 NQIKADVDRKLAEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRN 1706
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1707 LQVQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRALLEQSDRARKLAEHELLEATERVNLLNSQNTGLIN 1786
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1787 QKKKLESDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIAL 1866
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1867 KGGKKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEA 1946
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 2108526737 1947 EEQANTNLSKYRKLQHELDDAEERADMAESQANKLRAR 1984
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
152-825 |
2.41e-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: 510.87 E-value: 2.41e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVY------KGKRRSEVPPHIYSIADNAYNDMLRNRE-- 223
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 224 --NQSMLITGESGAGKTVNTKRVIQYFAIVAAlgdtpaKKAQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 301
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS------ATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 302 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKP-ELLDMLLVSSNPYDYHFCSQGVTTVENM 380
Cdd:cd14901 155 GKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSdELHALGLTHVEEYKYLNSSQCYDRRDGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 381 DDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTES-ADKASYLMGVSSADLIKGLLHP 459
Cdd:cd14901 235 DDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLAnVRAACDLLGLDMDVLEKTLCTR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 460 RVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTL-YTSLPRQY-FIGVLDIAGFEIFELNSFEQLCINF 537
Cdd:cd14901 315 EIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaYSESTGASrFIGIVDIFGFEIFATNSLEQLCINF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 538 TNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGLDlQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNhIGK 616
Cdd:cd14901 395 ANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 617 SPNFQKprpDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASlyenyvgsdaafdsktgsk 696
Cdd:cd14901 473 HASFSV---SKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 697 ekrkkaasfqTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLY 776
Cdd:cd14901 531 ----------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPH 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 2108526737 777 AEFKQRYRILNPHAIPDDKFVDSRKAAEKLLASLDI----DHNQYKFGHTKVF 825
Cdd:cd14901 601 DAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSElnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
152-827 |
1.94e-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: 508.14 E-value: 1.94e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVAALGDTPakkaqgpatktggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 311
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNL--------------VTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-E 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS------QKKPELLDmllvssnPYDYHFCSQGVTT-VENMDDGQ 384
Cdd:cd01387 146 GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAglpaqlRQKYGLQE-------AEKYFYLNQGGNCeIAGKSDAD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 385 ELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQRE---EQAEADGTESADKASYLMGVSSADLIKGLLHPRV 461
Cdd:cd01387 219 DFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 462 KVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEK 541
Cdd:cd01387 299 ETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANEN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 542 LQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLI-EKPLGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNF 620
Cdd:cd01387 379 LQYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELY 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 621 QKPRPDkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVgsdaafdSKTGSKEKRK 700
Cdd:cd01387 457 SKPRMP-----LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHR-------AQTDKAPPRL 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 701 KAASF-------QTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNR 773
Cdd:cd01387 525 GKGRFvtmkprtPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVR 604
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2108526737 774 LLYAEFKQRYRILNPHAIPDDKFVDSRKAAEKLLASLDIDhNQYKFGHTKVFFK 827
Cdd:cd01387 605 LPFQVFIDRYRCLVALKLPRPAPGDMCVSLLSRLCTVTPK-DMYRLGATKVFLR 657
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
152-827 |
1.11e-157 |
|
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: 500.48 E-value: 1.11e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLIT 230
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 231 GESGAGKTVNTKRVIQYFAIVAAlgdtpaKKAQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 310
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQ------QSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNIC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 311 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQ-GVTTVENMDDGQELMAT 389
Cdd:cd14873 155 QKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST-PENYHYLNQsGCVEDKTISDQESFREV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 390 DHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFkqrqreeqAEADGTESADK-----ASYLMGVSSADLIKGLLHPRVKVG 464
Cdd:cd14873 234 ITAMEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 465 NEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSlPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQ 544
Cdd:cd14873 306 GEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGK-EDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 545 FFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQKPR 624
Cdd:cd14873 385 YFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 625 PDkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYEnYVGSDAAFDS-KTGSKEKRKkaa 703
Cdd:cd14873 463 VA-----VNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFE-HVSSRNNQDTlKCGSKHRRP--- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 704 sfqTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRY 783
Cdd:cd14873 534 ---TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRY 610
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2108526737 784 RILNPHAIPDDkfvDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14873 611 KVLMRNLALPE---DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
152-827 |
4.48e-152 |
|
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: 485.42 E-value: 4.48e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAVYKG--KRRSEVPPHIYSIADNAYNDMLRNR----EN 224
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 225 QSMLITGESGAGKTVNTKRVIQYFAIVAALGDTPAKKAQgpATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKF 304
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKG--AANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 305 IRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKpELLDMLLVSSNPYDYHFCSQG-VTTVENMDDG 383
Cdd:cd14892 159 IQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGnCVEVDGVDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 384 QELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQR--QREEQAEADGTESADKASYLMGVSSADLIKGLLhPRV 461
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENadDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLV-TQT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 462 KVGNeyvvKGQNVE------QVTYAVGALAKATYDRMFKWLVIRINR----------TLYTSLPRQYFIGVLDIAGFEIF 525
Cdd:cd14892 317 TSTA----RGSVLEikltarEAKNALDALCKYLYGELFDWLISRINAchkqqtsgvtGGAASPTFSPFIGILDIFGFEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 526 ELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIEK-PLGIMSILEEECMFP-KATDN 603
Cdd:cd14892 393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 604 SFKAKMYDNHIGKSPNFQKPRPDKKrkyeaHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNkllaslyenyv 683
Cdd:cd14892 472 QLLTIYHQTHLDKHPHYAKPRFECD-----EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK----------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 684 gsdaafdsktgskekrkkaasFQTvsqvhkeNLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGI 763
Cdd:cd14892 536 ---------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVV 587
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2108526737 764 RICRKGFPNRLLYAEFKQRYRIL-----NPHAIPDDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14892 588 RIRREGFPIRRQFEEFYEKFWPLarnkaGVAASPDACDATTARKKCEEIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
152-827 |
2.86e-143 |
|
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: 459.93 E-value: 2.86e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKR-RSEVPPHIYSIADNAYNDMLRNRENQSMLIT 230
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 231 GESGAGKTVNTKRVIQYFAIVAALGDTpakkaqgpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 310
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDS--------------DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 311 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVsSNPYDYHFCSQGVTTVENMDDGQEL---- 386
Cdd:cd14897 147 ENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELeyyr 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 387 -MATDHA--MDILGFLPDEKYGCYKIVGAIMHFGNMKFkqrqrEEQAEADGTESADK-----ASYLMGVSSADLIKGLLH 458
Cdd:cd14897 226 qMFHDLTniMKLIGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALIS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 459 PRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYF-----IGVLDIAGFEIFELNSFEQL 533
Cdd:cd14897 301 NVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 534 CINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLI-EKPLGIMSILEEECMFPKATDNSFKAKMyDN 612
Cdd:cd14897 381 CINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 613 HIGKSPNFQKPRPDKkrkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVgsdaafdsk 692
Cdd:cd14897 459 YCGESPRYVASPGNR-----VAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSYF--------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 693 tgskekrkkaasfqtvsqvhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPN 772
Cdd:cd14897 525 --------------------KRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPI 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 2108526737 773 RLLYAEFKQRYRILNPHaiPDDKFVDSRKAAEKLLASLDIDhnQYKFGHTKVFFK 827
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 ... |
152-827 |
1.49e-141 |
|
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: 456.41 E-value: 1.49e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAVYKGK--------RRSEVPPHIYSIADNAYNDMLRNR 222
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 223 ENQSMLITGESGAGKTVNTKRVIQYFAIVAA--------LGDTPAKKAQGPATKTggtLEDQIIEANPAMEAFGNAKTLR 294
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevLTLTSSIRATSKSTKS---IEQKILSCNPILEAFGNAKTVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 295 NDNSSRFGKFIRIHFG-PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYD-YHFCS 371
Cdd:cd14907 158 NDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDrYDYLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 372 QGVT-TVENMDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQ--REEQAEADGTESADKASYLMGVS 448
Cdd:cd14907 238 KSNCyEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGID 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 449 SADLIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTL--YTSLPRQYF------IGVLDIA 520
Cdd:cd14907 318 EEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpKDEKDQQLFqnkylsIGLLDIF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 521 GFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTF--IDFgLDLQACIDLIEK-PLGIMSILEEECMF 597
Cdd:cd14907 398 GFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 598 PKATDNSFKAKMYDNHiGKSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLAS 677
Cdd:cd14907 477 ATGTDEKLLNKIKKQH-KNNSKLIFPNKINKDT----FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 678 LYENYVGSDAAFDSKTGSKEKRKKaasfqTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCN 757
Cdd:cd14907 552 IFSGEDGSQQQNQSKQKKSQKKDK-----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYL 626
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 758 GVLEGIRICRKGFPNRLLYAEFKQRYRILNphaipddkfvdsrkaaekllasldidhNQYKFGHTKVFFK 827
Cdd:cd14907 627 GVLESIRVRKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
153-790 |
5.31e-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: 450.53 E-value: 5.31e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 153 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAVY-----------KGKRRSEVPPHIYSIADNAYNDMLR 220
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 221 NR----ENQSMLITGESGAGKTVNTKRVIQYFAIVaalGDTPAKkAQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRND 296
Cdd:cd14900 82 GLngvmSDQSILVSGESGSGKTESTKFLMEYLAQA---GDNNLA-ASVSMGKSTSGIAAKVLQTNILLESFGNARTLRND 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 297 NSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLdmllvssnpydyhfcsqgvtt 376
Cdd:cd14900 158 NSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAAR--------------------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 377 veNMDDGQELMAtdhAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTE-------SADKASYLMGVSS 449
Cdd:cd14900 217 --KRDMYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDlapssiwSRDAAATLLSVDA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 450 ADLIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTL-----YTSLPRQYFIGVLDIAGFEI 524
Cdd:cd14900 292 TKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 525 FELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLI-EKPLGIMSILEEECMFPKATDN 603
Cdd:cd14900 372 FPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECVMPKGSDT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 604 SFKAKMYdNHIGKSPNFQKPRPDKKRkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACfrkssnkllaslyenyv 683
Cdd:cd14900 451 TLASKLY-RACGSHPRFSASRIQRAR---GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDL----------------- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 684 gsdaafdsktgskekrkkaasFQTVSQVhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGI 763
Cdd:cd14900 510 ---------------------FVYGLQF-KEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAV 567
|
650 660 670
....*....|....*....|....*....|.
gi 2108526737 764 RICRKGFPNRLLYAEFKQRYRIL----NPHA 790
Cdd:cd14900 568 RVARAGFPIRLLHDEFVARYFSLarakNRLL 598
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
152-827 |
3.36e-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: 446.41 E-value: 3.36e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNL--RRRYSAWMIYTYSGLFCVTVNPYKWLPvytAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRE---NQS 226
Cdd:cd14891 1 AGILHNLeeRSKLDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 227 MLITGESGAGKTVNTKRVIQYFAIVAALGDTPAKKAQGPATKT----GGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFG 302
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKrklsVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 303 KFIRIHFGPTG-KLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQ-GVTTVENM 380
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLS-PEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 381 DDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKA----SYLMGVSSADLIKGL 456
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEAlataAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 457 LHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTL---YTSLPrqyFIGVLDIAGFEIFEL-NSFEQ 532
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLghdPDPLP---YIGVLDIFGFESFETkNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 533 LCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLI-EKPLGIMSILEEECMFPKATDNSFKAKMYD 611
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 612 NHiGKSPNFqkPRPDKKRKYEAhFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRkSSNKLLASLYEnyvgsdaafds 691
Cdd:cd14891 473 TH-KRHPCF--PRPHPKDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLA-SSAKFSDQMQE----------- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 692 ktgskekrkkaasfqtvsqvhkenlnkLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFP 771
Cdd:cd14891 537 ---------------------------LVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLP 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108526737 772 NRLLYAEFKQRYRILNPHAI------PDDKFVdsrkaaEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14891 590 TRVTYAELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
154-827 |
4.16e-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: 446.66 E-value: 4.16e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 154 VLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDML----RNRENQSMLI 229
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 230 TGESGAGKTVNTKRVIQYFAIVAalgdtpakkaqgpatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 309
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC---------------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 310 gPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI---MSQKKPELLDMLlvssNPYDYHFCSQGVTTVENMDD-GQE 385
Cdd:cd14889 148 -RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLL----DPGKYRYLNNGAGCKREVQYwKKK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 386 LMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREE-QAEADGTESADKASYLMGVSSADLIKGLLHPRVKVG 464
Cdd:cd14889 223 YDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 465 NEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLytsLPRQYF------IGVLDIAGFEIFELNSFEQLCINFT 538
Cdd:cd14889 303 GEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQACINLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 539 NEKLQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDL-IEKPLGIMSILEEECMFPKATDNSFKAKMyDNHIGKS 617
Cdd:cd14889 380 NEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 618 PNFQKPRpDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYenyvgsdAAFDSKTGSKE 697
Cdd:cd14889 458 SYYGKSR-SKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLF-------TATRSRTGTLM 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 698 KRKKAASF----------QTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICR 767
Cdd:cd14889 526 PRAKLPQAgsdnfnstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRR 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108526737 768 KGFPNRLLYAEFKQRYRIL--NPhAIPDDKfvdsrKAAEKLLASLDIdhNQYKFGHTKVFFK 827
Cdd:cd14889 606 EGFSWRPSFAEFAERYKILlcEP-ALPGTK-----QSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
152-827 |
2.25e-134 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 435.91 E-value: 2.25e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLIT 230
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 231 GESGAGKTVNTKRVIQYFAIVAAlgdtpakkaqGPATKTggtlEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 310
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG----------GRKDKT----IAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 311 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNpYDYHFCSQGV--TTVENMDDGQELMA 388
Cdd:cd14904 147 GRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPN-CQYQYLGDSLaqMQIPGLDDAKLFAS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 389 TDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGtESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 468
Cdd:cd14904 226 TQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNG-SQLSQVAKMLGLPTTRIEEALCNRSVVTRNESV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 469 VKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQY-FIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFN 547
Cdd:cd14904 305 TVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 548 HHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNH--IGKSPNFQKPRP 625
Cdd:cd14904 385 TDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 626 DKkrkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGSDAAFDSKTGSKEKRKKAASF 705
Cdd:cd14904 464 KR-----TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEGKSGKGTKAPKSLGS 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 706 QtvsqvHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRI 785
Cdd:cd14904 539 Q-----FKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAI 613
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2108526737 786 LNPHAIPDDkfvDSRKAAEKLLASLDIDHN-QYKFGHTKVFFK 827
Cdd:cd14904 614 MFPPSMHSK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
152-805 |
2.84e-133 |
|
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: 435.09 E-value: 2.84e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAVYK--------GKRRSEVPPHIYSIADNAYNDMLRN- 221
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 222 RENQSMLITGESGAGKTVNTKRVIQYFAIVAAlgDTPAKKAQGPATKTGGTledQIIEANPAMEAFGNAKTLRNDNSSRF 301
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGR--DQSSTEQEGSDAVEIGK---RILQTNPILESFGNAQTIRNDNSSRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 302 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYDYH---FCSQGVTTV 377
Cdd:cd14902 156 GKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLgLQKGGKYELLnsyGPSFARKRA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 378 ENMDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESA---DKASYLMGVSSADLIK 454
Cdd:cd14902 236 VADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLET 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 455 GLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTL-------YTSLPRQYF--IGVLDIAGFEIF 525
Cdd:cd14902 316 LLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEInyfdsavSISDEDEELatIGILDIFGFESL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 526 ELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFPKATDNS 604
Cdd:cd14902 396 NRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGSNQA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 605 FKAKMYDNHIGkspnfqkprpdkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLyenyvG 684
Cdd:cd14902 475 LSTKFYRYHGG----------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAI-----G 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 685 SDAAFDS--KTGSKEKRKKAASFQT--VSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVL 760
Cdd:cd14902 534 ADENRDSpgADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVL 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2108526737 761 EGIRICRKGFPNRLLYAEFKQRYRILNPhaipddkFVDSRKAAEK 805
Cdd:cd14902 614 EAVRIARHGYSVRLAHASFIELFSGFKC-------FLSTRDRAAK 651
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
114-880 |
2.02e-129 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 427.52 E-value: 2.02e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 114 VETKDGKTLTVKDCDI----QQMNPPKFDmieDMAMLTHLNEASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTA 189
Cdd:PTZ00014 71 IDPPTNSTFEVKPEHAfnanSQIDPMTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 190 PVVAVYKGKRRSE-VPPHIYSIADNAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAivaalgdtpakkaQGPATK 268
Cdd:PTZ00014 148 DWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA-------------SSKSGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 269 TGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS 348
Cdd:PTZ00014 215 MDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 349 QKKPELLDML-LVSSNpyDYHFCSQGVTTVENMDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQRE 427
Cdd:PTZ00014 295 GANDEMKEKYkLKSLE--EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEG 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 428 EQAEA-----DGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINR 502
Cdd:PTZ00014 373 GLTDAaaisdESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 503 TLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGI-----EWTfidfglDLQAC 577
Cdd:PTZ00014 453 TIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGIsteelEYT------SNESV 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 578 IDLI-EKPLGIMSILEEECMFPKATDNSFKAKMYdNHIGKSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNK 656
Cdd:PTZ00014 527 IDLLcGKGKSVLSILEDQCLAPGGTDEKFVSSCN-TNLKNNPKYKPAKVDSNKN----FVIKHTIGDIQYCASGFLFKNK 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 657 DPLNETVVACFRKSSNKLLASLYEnyvgsdaafdsktGSKEKRKKAASFQTVSQVHKENLNKLMTNLRSTQPHFVRCIIP 736
Cdd:PTZ00014 602 DVLRPELVEVVKASPNPLVRDLFE-------------GVEVEKGKLAKGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKP 668
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 737 NETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNpHAIPDDKFVDSRKAAEKLLASLDIDHNQ 816
Cdd:PTZ00014 669 NENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD-LAVSNDSSLDPKEKAEKLLERSGLPKDS 747
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526737 817 YKFGHTKVFFKAGLLGHLEELRDERLAK---VLTLLQAAargkIMRMELLKLMERR-EALMIIQWNIR 880
Cdd:PTZ00014 748 YAIGKTMVFLKKDAAKELTQIQREKLAAwepLVSVLEAL----ILKIKKKRKVRKNiKSLVRIQAHLR 811
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
152-827 |
4.29e-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: 407.76 E-value: 4.29e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYK--GKRRSE-------VPPHIYSIADNAYNDMLRN- 221
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 222 RENQSMLITGESGAGKTVNTKRVIQYFAIVAAlGDTPAKKAQGPATKtgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 301
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGN-GEEGAPNEGEELGK--LSIMDRVLQSNPILEAFGNARTLRNDNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 302 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIM------SQKKPELLDMLLVSSN-PYDYHFCSQG- 373
Cdd:cd14908 158 GKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggdeeEHEKYEFHDGITGGLQlPNEFHYTGQGg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 374 VTTVENMDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASY---LMGVSSA 450
Cdd:cd14908 238 APDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 451 DLIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQY--FIGVLDIAGFEIFELN 528
Cdd:cd14908 318 KLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrsSVGVLDIFGFECFAHN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 529 SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFP-KATDNSFK 606
Cdd:cd14908 398 SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 607 AKMYDNHIgksPNFQKPRPDKKR-------KYEAHFELVHYAGVVPYNI-IGWLDKNKDPLNETvvacfrkssnkllasl 678
Cdd:cd14908 477 SRLYETYL---PEKNQTHSENTRfeatsiqKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEIPLT---------------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 679 yenyvgSDAAFDSktgskekrkkaasfqtvSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNG 758
Cdd:cd14908 538 ------ADSLFES-----------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGG 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 759 VLEGIRICRKGFPNRLLYAEFKQRYRILNPhAIPDD----------------KFVDSRKAAEKLLASLDIDHN----QYK 818
Cdd:cd14908 595 VLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVvlswsmerldpqklcvKKMCKDLVKGVLSPAMVSMKNipedTMQ 673
|
....*....
gi 2108526737 819 FGHTKVFFK 827
Cdd:cd14908 674 LGKSKVFMR 682
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
158-827 |
1.15e-121 |
|
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: 401.64 E-value: 1.15e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 158 LRRRYSAWMIYTYSGLFCVTVNPYKWLPvytapvvAVYK-GKRRSEVP------PHIYSIADNAYNDMLR-------NRE 223
Cdd:cd14895 7 LAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDlHKYREEMPgwtalpPHVFSIAEGAYRSLRRrlhepgaSKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 224 NQSMLITGESGAGKTVNTKRVIQYFAIVAAlgdtpAKKAQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGK 303
Cdd:cd14895 80 NQTILVSGESGAGKTETTKFIMNYLAESSK-----HTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 304 FIRIHFGP-----TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYDYHFCSQGVTTV 377
Cdd:cd14895 155 FVRMFFEGheldtSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELqLELLSAQEFQYISGGQCYQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 378 --ENMDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESA----------------- 438
Cdd:cd14895 235 rnDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqh 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 439 -DKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRIN----RTLYTSLPRQY- 512
Cdd:cd14895 315 lDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNsaspQRQFALNPNKAa 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 513 ------FIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGLDlQACIDLIE-KPL 585
Cdd:cd14895 395 nkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEqRPS 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 586 GIMSILEEECMFPKATDNSFKAKMYDNHIGKSpNFQKPRPDKKrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVA 665
Cdd:cd14895 474 GIFSLLDEECVVPKGSDAGFARKLYQRLQEHS-NFSASRTDQA---DVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFS 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 666 CFRKSSNKLLASLYENYVGSDAAFDSKTGSKEKRKKA--ASFQTVSQVhKENLNKLMTNLRSTQPHFVRCIIPNETKTPG 743
Cdd:cd14895 550 VLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSvlSSVGIGSQF-KQQLASLLDVVQQTQTHYIRCIKPNDESASD 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 744 IMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPHAIPDDkfvdsrKAAEKLLASLDIDHNQykFGHTK 823
Cdd:cd14895 629 QFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASD------ATASALIETLKVDHAE--LGKTR 700
|
....
gi 2108526737 824 VFFK 827
Cdd:cd14895 701 VFLR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
152-827 |
7.14e-120 |
|
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: 394.53 E-value: 7.14e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVaalgdtpakkAQGPATKTGGTLEDQIieanPAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 311
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL----------YQDQTEDRLRQPEDVL----PILESFGHAKTILNANASRFGQVLRLHL-Q 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQG-VTTVENMDDGQELMATD 390
Cdd:cd14896 146 HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQG-PETYYYLNQGgACRLQGKEDAQDFEGLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 391 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESAD--KASYLMGVsSADLIKGLLHPRVKVGN-EY 467
Cdd:cd14896 225 KALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQV-PPERLEGAVTHRVTETPyGR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 468 VVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLytSLPRQY----FIGVLDIAGFEIFELNSFEQLCINFTNEKLQ 543
Cdd:cd14896 304 VSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWL--APPGEAesdaTIGVVDAYGFEALRVNGLEQLCINLASERLQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 544 QFFNHHMFILEQEEYKREGIEWTFIDfGLDLQACIDLI-EKPLGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFQK 622
Cdd:cd14896 382 LFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 623 PR---PdkkrkyeaHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENyvgsdaaFDSKTGSKEKR 699
Cdd:cd14896 460 PQlplP--------VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE-------AEPQYGLGQGK 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 700 KKAAS-FQtvsqvhkENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAE 778
Cdd:cd14896 525 PTLASrFQ-------QSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQA 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2108526737 779 FKQRYRILNPHAIPDdkFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14896 598 FLARFGALGSERQEA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
152-796 |
3.75e-117 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 389.07 E-value: 3.75e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAVYKGKRRSEV----------PPHIYSIADNAYNDMLR 220
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAYDHNSQFgdrvtstdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 221 NRENQSMLITGESGAGKTVNTKRVIQYFAIVAALGDTPAKKAQG---PATKTGGTLEDQIIEANPAMEAFGNAKTLRNDN 297
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESispPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 298 SSRFGKFIRIHF-GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQK----KPELLDMLLVSSNPYDYHFCSQ 372
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 373 GVTTV--ENMDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQ--RQREEQAEADGTESA---------- 438
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 439 DKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQY------ 512
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 513 ---------FIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE- 582
Cdd:cd14899 401 vddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEh 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 583 KPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKS--PNFqkpRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLN 660
Cdd:cd14899 480 RPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNshPHF---RSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFC 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 661 ETVVACFRKSSNKLLASLYENYVGSDAAFDSKTGSKEKR-----KKAASFQTVSQVHKENLNKLMTNLRSTQPHFVRCII 735
Cdd:cd14899 557 ESAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRtrrraKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIK 636
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2108526737 736 PNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYR--ILNPHAIPDDKF 796
Cdd:cd14899 637 PNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRrvLLSLYKWGDNDF 699
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
152-827 |
1.29e-114 |
|
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: 379.33 E-value: 1.29e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKG-KRRSEVPPHIYSIADNAYNDMLRNRENQSMLIT 230
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 231 GESGAGKTVNTKRVIQYFAivaalgdtpakkaqgpATKTG---GTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 307
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA----------------SAKSGnmdLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 308 HFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS------QKKPELLDMllvssnpYDYHFCSQGVTTVENMD 381
Cdd:cd14876 145 DVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKgadsemKSKYHLLGL-------KEYKFLNPKCLDVPGID 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 382 DGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADK-----ASYLMGVSSADLIKGL 456
Cdd:cd14876 218 DVADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVDDAAAISNESLevfkeACSLLFLDPEALKREL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 457 LHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCIN 536
Cdd:cd14876 298 TVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFIN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 537 FTNEKLQQFFNHHMFILEQEEYKREGI-----EWTfidfglDLQACID-LIEKPLGIMSILEEECMFPKATDNSFKAKMY 610
Cdd:cd14876 378 ITNEMLQKNFIDIVFERESKLYKDEGIptaelEYT------SNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 611 DNhIGKSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVgsdaafd 690
Cdd:cd14876 452 SK-LKSNGKFKPAKVDSNIN----FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVV------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 691 sktgsKEKRKKAASFQTVSQVHKeNLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGF 770
Cdd:cd14876 520 -----VEKGKIAKGSLIGSQFLK-QLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGY 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2108526737 771 PNRLLYAEFKQRYRILNPhAIPDDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14876 594 SYRRPFEEFLYQFKFLDL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
152-825 |
5.91e-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: 360.70 E-value: 5.91e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAVYKGKRRSE-VPPHIYSIADNAYNDMLRNRE--NQSM 227
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQkLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 228 LITGESGAGKTVNTKRVIQYFAIVAALGDTPAKKaqgpatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 307
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESH------KIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 308 HFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS-QKKPELLDMLLVSSNPYDYhfcsqgVTTVENMDDGQEL 386
Cdd:cd14880 155 QLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKgASADERLQWHLPEGAAFSW------LPNPERNLEEDCF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 387 MATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQA---EADGTESADKASYLMGVSSADLIKGLLHPRVKV 463
Cdd:cd14880 229 EVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 464 GNEYVV--KGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPR-QYFIGVLDIAGFEIFELNSFEQLCINFTNE 540
Cdd:cd14880 309 GKQQQVfkKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 541 KLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPN 619
Cdd:cd14880 389 KLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPC 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 620 FQKPRPDKkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYEnyvgsdAAFDSKTGSKEKR 699
Cdd:cd14880 468 LGHNKLSR----EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFP------ANPEEKTQEEPSG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 700 KKAASFQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEF 779
Cdd:cd14880 538 QSRAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNF 617
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2108526737 780 KQRYRILNPHAIPDDKFVDSRKAAEKLLASLDIdhnqykfGHTKVF 825
Cdd:cd14880 618 VERYKLLRRLRPHTSSGPHSPYPAKGLSEPVHC-------GRTKVF 656
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
152-787 |
6.45e-107 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 359.68 E-value: 6.45e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAVYKGKRR-SEVPPHIYSIADNAYNDMLRNRENQSMLI 229
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 230 TGESGAGKTVNTKRVIQYfaivaaLGDTPAKKAQGPAT--KTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 307
Cdd:cd14906 81 SGESGSGKTEASKTILQY------LINTSSSNQQQNNNnnNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 308 HFGPT-GKLASADIDIYLLEKSRvIFQQPGER--SYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVE------ 378
Cdd:cd14906 155 EFRSSdGKIDGASIETYLLEKSR-ISHRPDNInlSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISsfksqs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 379 ---------NMDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQ---REEQAEADGTESADKASYLMG 446
Cdd:cd14906 234 snknsnhnnKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 447 VSSADLIKGLLHPRVKVGNEYVV--KGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTL-----------YTSLPRQYF 513
Cdd:cd14906 314 YIESVFKQALLNRNLKAGGRGSVycRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFnqntqsndlagGSNKKNNLF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 514 IGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPLGIMSILE 592
Cdd:cd14906 394 IGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 593 EECMFPKATDNSFKAK---MYDNhigkspnfqKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRK 669
Cdd:cd14906 473 DECIMPKGSEQSLLEKynkQYHN---------TNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLA 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 670 SSNKLLASLYENyvgsdaafdSKTGSKEKRKKAASFQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFM 749
Cdd:cd14906 544 SSNFLKKSLFQQ---------QITSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVH 614
|
650 660 670
....*....|....*....|....*....|....*...
gi 2108526737 750 VLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILN 787
Cdd:cd14906 615 VLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIV 652
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
152-827 |
7.69e-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: 354.19 E-value: 7.69e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAVYKGKRRS-----EVPPHIYSIADNAYNDMLRNRENQ 225
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 226 SMLITGESGAGKTVNTKRVIQYFAIVAALGDTPAKKAqgpatktggtledqIIEANPAMEAFGNAKTLRNDNSSRFGKFI 305
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSSTDVQSL--------------ILGSNPLLESFGNAKTLRNNNSSRFGKFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 306 RIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYdYHFCSQG-VTTVENMDDGQ 384
Cdd:cd14886 147 KLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASkCYDAPGIDDQK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 385 ELMATDHAMDILgFLPDEKYGCYKIVGAIMHFGNMKFKQRQR---EEQAEADGTESADKASYLMGVSSADLIKGLLHPRV 461
Cdd:cd14886 226 EFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 462 KVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEK 541
Cdd:cd14886 305 VINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANER 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 542 LQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIEKP-LGIMSILEEECMFPKATDNSFKAKMyDNHIgKSPNF 620
Cdd:cd14886 385 LQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 621 QkprPDKKRkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENyvgsdaaFDSKTGSKEKRK 700
Cdd:cd14886 462 I---PGKGS--QCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSD-------IPNEDGNMKGKF 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 701 KAASFQTvsqvhkeNLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFK 780
Cdd:cd14886 530 LGSTFQL-------SIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFF 602
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2108526737 781 QRYRILNPHA-IPDDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14886 603 HRNKILISHNsSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
152-827 |
9.99e-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: 354.50 E-value: 9.99e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMI-YTYSGLFCVTVNPYKWLPVYTAPVVAVY-KGKRRSEVPPHIYSIADNAYNDM-LRNRENQSML 228
Cdd:cd14875 1 ATLLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 229 ITGESGAGKTVNTKRVIQYfaivaaLGDTPAKKAQGPATKTggtLEDQIIE----ANPAMEAFGNAKTLRNDNSSRFGKF 304
Cdd:cd14875 81 ISGESGSGKTENAKMLIAY------LGQLSYMHSSNTSQRS---IADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 305 IRIHFGPT-GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTV------ 377
Cdd:cd14875 152 IKLYFDPTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 378 ENMDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESAdKASYLMGVSSADLIKGLL 457
Cdd:cd14875 232 KTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLRECFL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 458 hprVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLY--TSLPRQYFIGVLDIAGFEIFELNSFEQLCI 535
Cdd:cd14875 311 ---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpqGDCSGCKYIGLLDIFGFENFTRNSFEQLCI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 536 NFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNHI 614
Cdd:cd14875 388 NYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 615 GKSPNFQKPrpdkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGSDaafdsktg 694
Cdd:cd14875 467 NKSPYFVLP----KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLA-------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 695 skeKRKkaasfQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRL 774
Cdd:cd14875 535 ---RRK-----QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRR 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526737 775 LYAEF-KQRYRILNPHAIPDDKFVDSRKAAEKLLASLDIDHN----QYKFGHTKVFFK 827
Cdd:cd14875 607 PIEQFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYYQRLYGwakpNYAVGKTKVFLR 664
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
152-827 |
1.96e-104 |
|
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: 351.61 E-value: 1.96e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAIVAALGDTPAKKaqgpatktggtleDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 311
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSV-------------EKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML----LVSSNPYDYHFCSQGvttVENMDDGQELM 387
Cdd:cd01386 148 AGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELhlnqLAESNSFGIVPLQKP---EDKQKAAAAFS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 388 ATDHAMDILGFLPDEKYGCYKIVGAIMHFGN---MKFKQRQREEQAEadgTESADKASYLMGVSSADLIKGLLHPRVKVG 464
Cdd:cd01386 225 KLQAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFAR---PEWAQRAAYLLGCTLEELSSAIFKHHLSGG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 465 NEYVVKGQNVEQVTY------------AVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELN---- 528
Cdd:cd01386 302 PQQSTTSSGQESPARsssggpkltgveALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqr 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 529 --SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPL---------------GIMSIL 591
Cdd:cd01386 382 gaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPqqalvrsdlrdedrrGLLWLL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 592 EEECMFPKATDNSFKAKMYdNHIGKSPNFQKPRPDKKRKYEAHFELVHYAGV--VPYNIIGWLDKNK-DPLNETVVACFR 668
Cdd:cd01386 462 DEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQ 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 669 KSSNKLLASlyenyvgsdaafdsktgskekRKKAASFQTVSQVhkenlNKLMTNLRSTQPHFVRCIIPN------ETKTP 742
Cdd:cd01386 541 ESQKETAAV---------------------KRKSPCLQIKFQV-----DALIDTLRRTGLHFVHCLLPQhnagkdERSTS 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 743 GIMDPFMVLH------QLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPH----AIPDDKFVDSRKAAEKLLASLDI 812
Cdd:cd01386 595 SPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPltkkLGLNSEVADERKAVEELLEELDL 674
|
730
....*....|....*
gi 2108526737 813 DHNQYKFGHTKVFFK 827
Cdd:cd01386 675 EKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
152-827 |
1.40e-93 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 318.68 E-value: 1.40e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVY---KGKRRSEVPPHIYSIADNAYNDMLRNRENQSML 228
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 229 ITGESGAGKTVNTKRVIQYFAivaalgdtpakkaqGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 308
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLT--------------CRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 309 FGPTGK-LASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQG----VTTVENMDDG 383
Cdd:cd14878 147 FCERKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQTmredVSTAERSLNR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 384 QELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKV 463
Cdd:cd14878 226 EKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 464 GNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTL-----YTSLPrQYFIGVLDIAGFEIFELNSFEQLCINFT 538
Cdd:cd14878 306 KGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdeQKSMQ-TLDIGILDIFGFEEFQKNEFEQLCVNMT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 539 NEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGLDLQACIDLI-EKPLGIMSILEEECMFPKATDNSFKAKMY------D 611
Cdd:cd14878 385 NEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDFFfQKPSGFLSLLDEESQMIWSVEPNLPKKLQsllessN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 612 NHIGKSPNFQKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLyenyvgsdaaFDS 691
Cdd:cd14878 465 TNAVYSPMKDGNGNVALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL----------FQS 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 692 KtgskekrkkaasFQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFP 771
Cdd:cd14878 535 K------------LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYP 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2108526737 772 NRLLYAEFKQRYRILNPHAIPDDKfvdSRKAAEKL-LASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14878 603 VRLSFSDFLSRYKPLADTLLGEKK---KQSAEERCrLVLQQCKLQGWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
152-827 |
2.94e-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: 2.94e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYtapvVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFAivaalgdtpakkaqgPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 311
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL---------------SGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPyDYHFCSQGVTTVENMDDGQE---LMA 388
Cdd:cd14937 142 YQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDfgnLMI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 389 TDHAMDilgfLPDEKYGCYKIVGAIMHFGNMKFKQRQRE-----EQAEADGTESADKASYLMGVSSADLIKGLLHPRVKV 463
Cdd:cd14937 221 SFDKMN----MHDMKDDLFLTLSGLLLLGNVEYQEIEKGgktncSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 464 GNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQ 543
Cdd:cd14937 297 ANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIH 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 544 QFFNHHMFILEQEEYKREGIEWTFIDFGLDlQACIDLIEKPLGIMSILEEECMFPKATDNSFkAKMYDNHIGKSPNFQKp 623
Cdd:cd14937 377 SIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYAS- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 624 rpdKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYEnyvgsdaafDSKTGSKEKRKKAA 703
Cdd:cd14937 454 ---TKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYE---------DVEVSESLGRKNLI 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 704 SFQtvsqvHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRIcRKGFPNRLLYAEFKQRY 783
Cdd:cd14937 522 TFK-----YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2108526737 784 RILNPHAIPDDKFVDSRKAAEKLLASLDIDhnQYKFGHTKVFFK 827
Cdd:cd14937 596 EYLDYSTSKDSSLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
153-790 |
5.30e-91 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 308.75 E-value: 5.30e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 153 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKwlPVYTAPVVAVYKgKRRSEVPPHIYSIADNAYNDMLRNrENQSMLITGE 232
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 233 SGAGKTVNTKRVIQYFAivaalgdtpakkaqgPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgpT 312
Cdd:cd14898 78 SGSGKTENAKLVIKYLV---------------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 313 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKpelldmLLVSSNPYDYHFCSQGVTTVENMDdgQELMATDHA 392
Cdd:cd14898 141 GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESIVQLS--EKYKMTCSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 393 MDILGFLPDEKYGcyKIVGAIMHFGNMKFKQrqrEEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 472
Cdd:cd14898 213 MKSLGIANFKSIE--DCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 473 NVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPRQyfIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 552
Cdd:cd14898 288 TLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 553 LEQEEYKREGIEWTFIDFgLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKM--YDNHigkspnFQKPRPDKKRK 630
Cdd:cd14898 366 AKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNG------FINTKARDKIK 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 631 yeahfeLVHYAGVVPYNIIGWLDKNKDPLNetvvacFRKSSNKLLASlyenyvgsdaafdskTGSKEkrkkaasfqTVSQ 710
Cdd:cd14898 439 ------VSHYAGDVEYDLRDFLDKNREKGQ------LLIFKNLLIND---------------EGSKE---------DLVK 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 711 VHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPHA 790
Cdd:cd14898 483 YFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
152-827 |
1.80e-86 |
|
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: 300.03 E-value: 1.80e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSA--------WMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRE 223
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 224 NQSMLITGESGAGKTVNTKRVIQYFAIVAalgdtpaKKAQGPATKTggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGK 303
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVS-------DRRHGADSQG---LEARLLQSGPVLEAFGNAHTVLNANSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 304 FIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI-MSQKKPELLDMLLVSSNPYDYhfcsqgvttvenmdd 382
Cdd:cd14887 151 MLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALcNAAVAAATQKSSAGEGDPEST--------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 383 gqELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQREEQAEADGT--------ESADKASYLMGVSS----- 449
Cdd:cd14887 216 --DLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvgceETAADRSHSSEVKClssgl 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 450 ---ADLIKGLLHPRVKVGNEYVVKGQN-------------------VEQVTYAVGALAKATYDRMFKWLVIRINRTLYTS 507
Cdd:cd14887 294 kvtEASRKHLKTVARLLGLPPGVEGEEmlrlalvsrsvretrsffdLDGAAAARDAACKNLYSRAFDAVVARINAGLQRS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 508 LPRQY--------------FIGVLDIAGFEIFE---LNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREG--IEWTFI 568
Cdd:cd14887 374 AKPSEsdsdedtpsttgtqTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQDCS 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 569 DFGLDLQACIDLIEKP------------------------LGIMSILEEE-CMFPKATDNSFKA----KMYDNHIGKSPN 619
Cdd:cd14887 454 AFPFSFPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSdlfyEKLNKNIINSAK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 620 FQKPRPDKKRKyEAHFELVHYAGVVPYNIIGWLDKNKDPLnetvvacfrksSNKLlaslyENYVGSDAAFDSKTGSKEKR 699
Cdd:cd14887 534 YKNITPALSRE-NLEFTVSHFACDVTYDARDFCRANREAT-----------SDEL-----ERLFLACSTYTRLVGSKKNS 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 700 KKAA---SFQTVSQVHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLY 776
Cdd:cd14887 597 GVRAissRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPY 676
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 2108526737 777 AEFKQRYRILNPHAIpdDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFFK 827
Cdd:cd14887 677 VELWRRYETKLPMAL--REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
149-826 |
1.07e-73 |
|
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: 260.17 E-value: 1.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 149 LNEASVLYNLRRRYSAWMIYTY---SGLfcVTVNPYKWLPVYTAPVVAVYK-------GKRRSEVPPHIYSIADNAYNDM 218
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 219 LRNRENQSMLITGESGAGKTVNTKRVIQyfaivaALGD--TPAKKAqgpaTKtggtLEDQIIEANPAMEAFGNAKTLRND 296
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLR------QLLRlsSHSKKG----TK----LSSQISAAEFVLDSFGNAKTLTNP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 297 NSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYDYHFCSQGVT 375
Cdd:cd14879 145 NASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLgLDDPSDYALLASYGCHP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 376 TVENM--DDG---QELMAtdhAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQ--REEQAEADGTESADKASYLMGVS 448
Cdd:cd14879 225 LPLGPgsDDAegfQELKT---ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 449 SADLiKGLLHPRVKvgneYVVKgqnvEQVTY---AVGA------LAKATYDRMFKWLVIRINRTLytSLPRQY---FIGV 516
Cdd:cd14879 302 PEDL-ETSLTYKTK----LVRK----ELCTVfldPEGAaaqrdeLARTLYSLLFAWVVETINQKL--CAPEDDfatFISL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 517 LDIAGFEIF---ELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLI-EKPLGIMSILE 592
Cdd:cd14879 371 LDFPGFQNRsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 593 EEC-MFPKATDNSFKAKMYDNHIGKSPnFQKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRkss 671
Cdd:cd14879 450 DQTrRMPKKTDEQMLEALRKRFGNHSS-FIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLR--- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 672 nkllaslyenyvgsdaafdsktgskekrkkaasfqTVSQvHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVL 751
Cdd:cd14879 526 -----------------------------------GATQ-LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVK 569
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526737 752 HQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYrilnphaIPDDKFVDSRKAAEKLLASLDIDHNQYKFGHTKVFF 826
Cdd:cd14879 570 AQIRSLGLPELAARLRVEYVVSLEHAEFCERY-------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
153-826 |
2.63e-72 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 255.81 E-value: 2.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 153 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAvykgkRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 232
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVGNPLTLTST-----RSSPLAPQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 233 SGAGKTVNTKRVI-QYFAIVAALGDTPAKKaqgpatktggtledQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 311
Cdd:cd14881 77 SGSGKTYASMLLLrQLFDVAGGGPETDAFK--------------HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-T 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 312 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYDYHFCSQGVTTVENMDDGQELMATD 390
Cdd:cd14881 142 DGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLhLDGYSPANLRYLSHGDTRQNEAEDAARFQAWK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 391 HAMDILG--FLpdekyGCYKIVGAIMHFGNMKFKQRQREEQAEADGTESADKASyLMGVSSADLIKGLlHPRVKVGNEYV 468
Cdd:cd14881 222 ACLGILGipFL-----DVVRVLAAVLLLGNVQFIDGGGLEVDVKGETELKSVAA-LLGVSGAALFRGL-TTRTHNARGQL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 469 VKGQNVEQVTYAV-GALAKATYDRMFKWLVIRINrtlytSLPRQY----------FIGVLDIAGFEIFELNSFEQLCINF 537
Cdd:cd14881 295 VKSVCDANMSNMTrDALAKALYCRTVATIVRRAN-----SLKRLGstlgthatdgFIGILDMFGFEDPKPSQLEHLCINL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 538 TNEKLQQFFNHHMFILEQEEYKREGIEwTFIDFG-LDLQACIDLIEK-PLGIMSILEEECMfPKATDNSFKAKMYDNHIG 615
Cdd:cd14881 370 CAETMQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQ 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 616 kSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSnkllaslyenyvgsdAAFDSKTGS 695
Cdd:cd14881 448 -NPRLFEAKPQDDRM----FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN---------------CNFGFATHT 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 696 KEkrkkaasFQTvsqvhkeNLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLL 775
Cdd:cd14881 508 QD-------FHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMR 573
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 2108526737 776 YAEFKQRYRILNPHAIP---DDKFVDSRKAAEKLLASLDIDHN-----QYKFGHTKVFF 826
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 ... |
152-778 |
1.28e-70 |
|
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: 252.13 E-value: 1.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAVYKGKRRSE-------VPPHIYSIADNAYNDMLRNRE 223
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 224 NQSMLITGESGAGKTVNTKRVIQYFAIVaalgdtpakkaQGPATKTggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGK 303
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI-----------QTDSQMT--ERIDKLIYINNILESMSNATTIKNNNSSRCGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 304 FIRIHF---------GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGV 374
Cdd:cd14884 148 INLLIFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 375 ------------TTVENMDDGQELMATD--------HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQrqreeqaeadg 434
Cdd:cd14884 228 shqkrsvkgtlrLGSDSLDPSEEEKAKDeknfvallHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA----------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 435 tesadkASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPR---- 510
Cdd:cd14884 297 ------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKdesd 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 511 --------QYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDF--GLDLQACIDL 580
Cdd:cd14884 371 nediysinEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVApsYSDTLIFIAK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 581 IEKPLGIMSILeEECMFPKATDNSFK-----AKMY----DNHIGKSPNFQKPRPDKKRKYEAH-FELVHYAGVVPYNIIG 650
Cdd:cd14884 451 IFRRLDDITKL-KNQGQKKTDDHFFRyllnnERQQqlegKVSYGFVLNHDADGTAKKQNIKKNiFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 651 WLDKNKDPLNETVVACFRKSSNKLLAslyENYVGsdaafdsktgskekrKKAASFQTVSQVHKENLNKLMTNLRSTQPHF 730
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLR---EANNG---------------GNKGNFLSVSKKYIKELDNLFTQLQSTDMYY 591
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2108526737 731 VRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAE 778
Cdd:cd14884 592 IRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
152-791 |
9.63e-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: 9.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 152 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYkgkrrsevppHIYSIADNAYNDMLRNRENQSMLI-T 230
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNAESIVfG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 231 GESGAGKTVNTKRVIQYfaivaaLGDTPAKKAqgpATKTGGTLEDQIieanpamEAFGNAKTLRNDNSSRFGKFIRIHFG 310
Cdd:cd14874 71 GESGSGKSYNAFQVFKY------LTSQPKSKV---TTKHSSAIESVF-------KSFGCAKTLKNDEATRFGCSIDLLYK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 311 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNpYDYHFCSQGVTTVENMDDGQELMATD 390
Cdd:cd14874 135 RNVLTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL-QKFFYINQGNSTENIQSDVNHFKHLE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 391 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQRQR---EEQAEADGTESADK-ASYLMGVSSADLIKGLLhPRVKVGNE 466
Cdd:cd14874 214 DALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnvEQDVVEIGNMSEVKwVAFLLEVDFDQLVNFLL-PKSEDGTT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 467 YvvkgqNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLpRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFF 546
Cdd:cd14874 293 I-----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPL-HTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 547 NHHMFILEQEEYKREGIEwtfIDFglDLQACID-------LIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSpN 619
Cdd:cd14874 367 VKHSFHDQLVDYAKDGIS---VDY--KVPNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRS-S 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 620 FQKPRpdKKRKYEahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENYVGSdaafdsktgskekr 699
Cdd:cd14874 441 YGKAR--NKERLE--FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSN-------------- 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 700 kkaASFQTVSQVHKEN--LNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYA 777
Cdd:cd14874 503 ---TSDMIVSQAQFILrgAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKT 579
|
650
....*....|....
gi 2108526737 778 EFKQRYRILNPHAI 791
Cdd:cd14874 580 TFARQYRCLLPGDI 593
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
153-827 |
3.46e-64 |
|
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: 231.94 E-value: 3.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 153 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGE 232
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 233 SGAGKTVNTKRVIQYFAIvaaLGDTPAKKAQgpatktggtledQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 312
Cdd:cd14882 82 SYSGKTTNARLLIKHLCY---LGDGNRGATG------------RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGST 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 313 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS--QKKPELLDMLLVSSNPYDYHFCSQGVTTV----------ENM 380
Cdd:cd14882 147 GKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEVPPSklkyrrddpeGNV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 381 DDGQELMATDHAMDilgFLPDEKYGCYKIVGAIMHFGNMKFkqRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPR 460
Cdd:cd14882 227 ERYKEFEEILKDLD---FNEEQLETVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 461 VKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLytSLPR-----QYFIGVLDIAGFEIFELNSFEQLCI 535
Cdd:cd14882 302 LIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKM--SFPRavfgdKYSISIHDMFGFECFHRNRLEQLMV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 536 NFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILeeecmfpkatDNSFKAKMYDNHIG 615
Cdd:cd14882 380 NTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYII----------DDASRSCQDQNYIM 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 616 KSPNfQKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLYENyvgsdaafdSKTgs 695
Cdd:cd14882 450 DRIK-EKHSQFVKKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN---------SQV-- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 696 KEKRKKAASFQTVSQvhkENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLL 775
Cdd:cd14882 518 RNMRTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIP 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2108526737 776 YAEFKQRYRILnphAIPDDKFVDSRKAAEKLLAsLDIDHNQYKFGHTKVFFK 827
Cdd:cd14882 595 FQEFLRRYQFL---AFDFDETVEMTKDNCRLLL-IRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
155-826 |
2.66e-62 |
|
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: 228.70 E-value: 2.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 155 LYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRR----------SEVPPHIYSIADNAYNDMLRNREN 224
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 225 QSMLITGESGAGKTVNTKRVIQYFAIVAAlGDTPAKKAQGpATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKF 304
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGD-ETEPRPDSEG-ASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 305 IRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS--QKKPELLDMLLVSSNPYDYHFCSQGVTTVENMD- 381
Cdd:cd14893 162 ISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAgvQHDPTLRDSLEMNKCVNEFVMLKQADPLATNFAl 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 382 ---DGQELMATDHAMDIlgfLPDEKYGCYKIVGAIMHFGNMKF--KQRQREEQAEADGTESADKAS-YLMGVSSADLIKG 455
Cdd:cd14893 242 darDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFvpDPEGGKSVGGANSTTVSDAQScALKDPAQILLAAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 456 LL--HPRV------------KVGNEYV--VKGQNVEQVTYAVGALAKATYDRMFKWLVIRINRTLYTSLPR--------- 510
Cdd:cd14893 319 LLevEPVVldnyfrtrqffsKDGNKTVssLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksnivin 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 511 QYFIGVLDIAGFEIFE--LNSFEQLCINFTNEKLQQFFNHHMF-----ILEQEEYKREG--IEWTFIDFGLDLQACIDLI 581
Cdd:cd14893 399 SQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLainfsFLEDESQQVENrlTVNSNVDITSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 582 E-KPLGIMSILEEECMFPKATDNSFKAKMY--DNHIG--KSPN----FQKPRPDKKRKYEAHFELVHYAGVVPYNIIGWL 652
Cdd:cd14893 479 EdKPFGIFDLLTENCKVRLPNDEDFVNKLFsgNEAVGglSRPNmgadTTNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 653 DKNKDPLNETVVACFRKSSNKLLASLYENYVGSDAAFDSKTGSKEKRKKAASFQTVSQVHKENLN--------------K 718
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 719 LMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPHaipddkfvd 798
Cdd:cd14893 639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVCGH--------- 709
|
730 740 750
....*....|....*....|....*....|..
gi 2108526737 799 sRKAAEKLLASLD----IDHNQYKFGHTKVFF 826
Cdd:cd14893 710 -RGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
158-779 |
4.18e-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: 220.73 E-value: 4.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 158 LRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAVYKGKRrsEVPPHIYSIADNAYNDMLRNRENQSMLITGESGAG 236
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 237 KTVNTKRVIQYfaivaaLGDTPAKKAQgpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLA 316
Cdd:cd14905 85 KSENTKIIIQY------LLTTDLSRSK--------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 317 SADIDIYLLEKSRVIFQQPGERSYHIYYQIM---SQKKPELLDMLLVSSnpydYHFCSQGVT-TVENMDDGQELMATDHA 392
Cdd:cd14905 151 GAKLYSYFLDENRVTYQNKGERNFHIFYQFLkgiTDEEKAAYQLGDINS----YHYLNQGGSiSVESIDDNRVFDRLKMS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 393 MDILGFlPDEKYG-CYKIVGAIMHFGNMKFkqRQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVvkg 471
Cdd:cd14905 227 FVFFDF-PSEKIDlIFKTLSFIIILGNVTF--FQKNGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAV--- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 472 QNVEqvtyavgALAKATYDRMFKWLVIRINRTLYtslPRQY--FIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHH 549
Cdd:cd14905 301 ENRD-------SLARSLYSALFHWIIDFLNSKLK---PTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 550 MFILEQEEYKREGIEW-TFIDFGlDLQACIDLIEKplgIMSILEEECMFPKATDNSFKAKMyDNHIGKSPNFQKpRPDKk 628
Cdd:cd14905 371 VLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL-QNFLSRHHLFGK-KPNK- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 629 rkyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLAS------LYENYVGSDAAFDSKTGSKE----- 697
Cdd:cd14905 444 ------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSrdgvfnINATVAELNQMFDAKNTAKKsplsi 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 698 -KRKKAASFQTVSQVHKENLN------------------KLMTNLRSTQP---------HFVRCIIPNETKTPGIMDPFM 749
Cdd:cd14905 518 vKVLLSCGSNNPNNVNNPNNNsgggggggnsgggsgsggSTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVKS 597
|
650 660 670
....*....|....*....|....*....|....
gi 2108526737 750 VLHQLRCNGVLEGIRICRKGFP----NRLLYAEF 779
Cdd:cd14905 598 VNEQIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
174-307 |
1.61e-54 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 187.94 E-value: 1.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 174 FCVTVNPYKWLPVYTAPVVAV-YKGKRRSEVPPHIYSIADNAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAIVA 252
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVfYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2108526737 253 ALGDtPAKKAQG--PATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 307
Cdd:cd01363 81 FNGI-NKGETEGwvYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
153-825 |
2.37e-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: 2.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 153 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAVYKGKRRSE-VPPHIYSIADNAYNDMLRNRENQSMLITG 231
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 232 ESGAGKTVNTKRVIQYFA---------IVAALGDTPAKKAQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFG 302
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAyqvkgsrrlPTNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 303 KFIRIHFgPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQGVTTVENMDD 382
Cdd:cd14938 162 KFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLK-NIENYSMLNNEKGFEKFSDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 383 GQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMK-----------FKQRQREEQAEADGTESADKASYLMGVSSAD 451
Cdd:cd14938 240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEivkafrkksllMGKNQCGQNINYETILSELENSEDIGLDENV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 452 ----LIKGLLHPRVKVGNEY-----------VVKGQNVEQVTYAVGALAKATYDRMFKWLVIRINrTLYTSLPR----QY 512
Cdd:cd14938 320 knllLACKLLSFDIETFVKYfttnyifndsiLIKVHNETKIQKKLENFIKTCYEELFNWIIYKIN-EKCTQLQNininTN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 513 FIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPL--GIMSI 590
Cdd:cd14938 399 YINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFSL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 591 LEEECMfPKATDNSFKAKMYDNHIGKSPNFQKPRPDKKRKyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKS 670
Cdd:cd14938 479 LENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNK--KTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 671 SNKLLASLYENYvgsdaAFDSkTGSKEKRKKAASFQTVSQVHKE---------------NLNKLMTNLRSTQPHFVRCII 735
Cdd:cd14938 556 ENEYMRQFCMFY-----NYDN-SGNIVEEKRRYSIQSALKLFKRrydtknqmavsllrnNLTELEKLQETTFCHFIVCMK 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 736 PNETKTP-GIMDPFMVLHQLRCNGVLEGIRICRKGFPNRLLYAEFKQRYRILNPhaipddkfvDSRKAAEKLLASLDIDH 814
Cdd:cd14938 630 PNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISN 700
|
730
....*....|.
gi 2108526737 815 NQYKFGHTKVF 825
Cdd:cd14938 701 YEWMIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1233-1994 |
5.03e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 130.56 E-value: 5.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1233 LKLRRDLEEAMLHHEATTAALrKKHADSVAELSEQIDSLQRVKQKLEKERseakmevdDLASTVEQLSKgkatsekmcRL 1312
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERYK--------ELKAELRELEL---------AL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1313 YEDQMNEAKAKADELQRQLNETNTQRAraqaesgELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAH 1392
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELE-------ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1393 ALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKK------LVTRLQEAEETVE 1466
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELeaeleeLESRLEELEEQLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1467 TSNAKCSSLEKTKHRLQTEIEDLVIDLERanaaaavLDKKQRNFDKVLAEWRQKYEEcqSELETSQKESRGLSTELFKLK 1546
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLER-------LEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1547 NSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEG------------TLEH 1614
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlseliSVDE 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1615 EESKSLRIQLELNqIKADVDRKLAEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRKKMEG------DLNEMEV 1688
Cdd:TIGR02168 534 GYEAAIEAALGGR-LQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGflgvakDLVKFDP 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1689 QLS-----------------HANRQASESQKFLR---------------------------NLQVQIKDIQLELDETIHQ 1724
Cdd:TIGR02168 613 KLRkalsyllggvlvvddldNALELAKKLRPGYRivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEK 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1725 NEELKEQVAVTERRNNLLAAEVEELRALLEQSDRARKLAEHELLEA-------TERVNLLNSQNTGLINQKKKLESDLSM 1797
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeveqlEERIAQLSKELTELEAEIEELEERLEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1798 LSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQD-------TSAHLERMKKNMEQTIKDLQMRLDEAEQIA----- 1865
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeltllneEAANLRERLESLERRIAATERRLEDLEEQIeelse 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1866 -LKGGKKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTE 1944
Cdd:TIGR02168 853 dIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 2108526737 1945 EAEEQANTNLSKYR-KLQHELDDAEERADMAESQANKLRARTRDQGSKLAE 1994
Cdd:TIGR02168 933 GLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1221-1994 |
9.95e-26 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 116.32 E-value: 9.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1221 QIEMNKKREadFLKLRRDLEEAmlhhEATTAALRKKHAD-SVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQL 1299
Cdd:TIGR02169 204 RREREKAER--YQALLKEKREY----EGYELLKEKEALErQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1300 SKgkatseKMCRLYEDQMNEakakadeLQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQ 1379
Cdd:TIGR02169 278 NK------KIKDLGEEEQLR-------VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1380 LEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSkanaevaqwrtkyetdaiQRTEELEEAKKKLvtrlq 1459
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK------------------DYREKLEKLKREI----- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1460 eaeetvetsnakcSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLS 1539
Cdd:TIGR02169 402 -------------NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1540 TELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKG-------LDMEKSEIQAALEEAEG-- 1610
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGvhgtvaqLGSVGERYATAIEVAAGnr 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1611 ----TLEHEESKSLRIQ------------LELNQIKA--------------DVDRKLAEKDEEIDSLRRNHQR---ILES 1657
Cdd:TIGR02169 549 lnnvVVEDDAVAKEAIEllkrrkagratfLPLNKMRDerrdlsilsedgviGFAVDLVEFDPKYEPAFKYVFGdtlVVED 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1658 MQAtldaeAKSRNEAVRLrKKMEGDLnemeVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIhqnEELKeqvavteR 1737
Cdd:TIGR02169 629 IEA-----ARRLMGKYRM-VTLEGEL----FEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERL---EGLK-------R 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1738 RNNLLAAEVEELRALLEQSDRARKLAEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLSnevddavQECRNAEEKAK 1817
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE-------QEIENVKSELK 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1818 KAITDAAMMAEELKKEQDTSAHLERMKKnmEQTIKDLQMRLDEAEQIaLKGGKKQVLKLEARVKELENELESEQKKSQEY 1897
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEE-VSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1898 QKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADMAESQ 1977
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
810
....*....|....*..
gi 2108526737 1978 ANKLRARTRDQGSKLAE 1994
Cdd:TIGR02169 919 LSELKAKLEALEEELSE 935
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
907-1589 |
1.12e-24 |
|
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: 113.23 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 907 EKELVSLKEELAKLKEALEKSEVKRKELEERQV-------SLIQEKNDLSLQLQAEQDNLADAED--------------R 965
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERqleeleaqleelesK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 966 CDLLIKTKIQLEAKVKEIMERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAA 1045
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1046 LDETILKLTKEKKALL-EAHQQTLDDLQAEEDKVNiltKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSL 1124
Cdd:TIGR02168 412 LEDRRERLQQEIEELLkKLEEAELKELQAELEELE---EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1125 ESVMDLENDKQQLDEKLKKKDFEMNE--------------MSTRIEDEQALVNQLQKKikeLQARTEELEEELEADRACR 1190
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGVKALLKNqsglsgilgvlselISVDEGYEAAIEAALGGR---LQAVVVENLNAAKKAIAFL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1191 AKVEKQRSDVARELEELSERLEEAGGATSAQIEMNKKREADFLKLRRDLEEAM----------------------LHHEA 1248
Cdd:TIGR02168 566 KQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvvddldnalelakkLRPGY 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1249 TTAAL----------------------------RKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLS 1300
Cdd:TIGR02168 646 RIVTLdgdlvrpggvitggsaktnssilerrreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1301 -------KGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNV 1373
Cdd:TIGR02168 726 rqisalrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1374 EDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRT------EEL 1447
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallnerASL 885
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1448 EEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAaaavldKKQRNFDKVLAEWRQKYEECQSE 1527
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV------RIDNLQERLSEEYSLTLEEAEAL 959
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2108526737 1528 LETSQKESRGLSTELFKLKNSYEE----TLDHLETIKRENK---NLQEEIADLSDQISQGVKTIHELEK 1589
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKIKElgpvNLAAIEEYEELKErydFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
978-1793 |
1.84e-24 |
|
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: 112.46 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 978 AKVKEIMERLED---EEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKhatenkvknLIEEMAALDETILKLT 1054
Cdd:TIGR02168 182 ERTRENLDRLEDilnELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEE---------LREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1055 KEKKALLEAhqqtlddLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDK 1134
Cdd:TIGR02168 253 EELEELTAE-------LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1135 QQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQArteELEEELEADRACRAKVEKQRSDVARELEELSerleea 1214
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEA---ELEELESRLEELEEQLETLRSKVAQLELQIA------ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1215 ggATSAQIEMNKKREADfLKLRRDLEeamlhHEATTAALRKKHADSVAELSEQIDslqrvkqKLEKERSEAKMEVDDLAS 1294
Cdd:TIGR02168 397 --SLNNEIERLEARLER-LEDRRERL-----QQEIEELLKKLEEAELKELQAELE-------ELEEELEELQEELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1295 TVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLN--ETNTQRARAQAESGElsrKLEEREAMVSQLQRAKNSFSQN 1372
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlEGFSEGVKALLKNQS---GLSGILGVLSELISVDEGYEAA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1373 VE-DLKKQL-----EEENKAKNALAHALQSSRHDC-----DLLREQYDEEQEAKA------------------------- 1416
Cdd:TIGR02168 539 IEaALGGRLqavvvENLNAAKKAIAFLKQNELGRVtflplDSIKGTEIQGNDREIlkniegflgvakdlvkfdpklrkal 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1417 -----------DLQRALSKANAEVAQWR-------------------TKYETDAIQRTEELEEAKKKLvtrlQEAEETVE 1466
Cdd:TIGR02168 619 syllggvlvvdDLDNALELAKKLRPGYRivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKI----EELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1467 TSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELfklk 1546
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL---- 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1547 nsyEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMkkgLDMEKSEIQAALEEAEGTLEHEESKSLRIQlEL 1626
Cdd:TIGR02168 771 ---EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE---LTLLNEEAANLRERLESLERRIAATERRLE-DL 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1627 NQIKADVDRKLAEKDEEIDSLRRNhqriLESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRN 1706
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEEL----IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1707 LQVQIKDIQLELDET----IHQNEELKEQVAVT----ERRNNLLAAEVEELRALLEQSDRARK-------LAEHELLEAT 1771
Cdd:TIGR02168 920 LREKLAQLELRLEGLevriDNLQERLSEEYSLTleeaEALENKIEDDEEEARRRLKRLENKIKelgpvnlAAIEEYEELK 999
|
890 900
....*....|....*....|..
gi 2108526737 1772 ERVNLLNSQNTGLINQKKKLES 1793
Cdd:TIGR02168 1000 ERYDFLTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
906-1855 |
3.50e-24 |
|
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: 111.30 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 906 TEKELVSLKEELAKLKEALeksevkrKELEERQVsliqekndlSLQLQAEQdnladAEdrcdlliktkiqleaKVKEIME 985
Cdd:TIGR02168 177 TERKLERTRENLDRLEDIL-------NELERQLK---------SLERQAEK-----AE---------------RYKELKA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 986 RLED-EEEMSANVLakkRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEkkalLEAH 1064
Cdd:TIGR02168 221 ELRElELALLVLRL---EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE----LYAL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1065 QQTLDDLQAEedkvniltkaKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQLDEKLKKK 1144
Cdd:TIGR02168 294 ANEISRLEQQ----------KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1145 DFEMNEMSTRIEDEQALVNQLQKKIKELqarteeleeeleadracRAKVEKQRSDVAREleelserleeaggatSAQIEM 1224
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQL-----------------ELQIASLNNEIERL---------------EARLER 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1225 NKKREADFLKLRRDLEEAMLHHEattaalrkkhadsVAELSEQIDslqrvkqKLEKERSEAKMEVDDLASTVEQLSKGKA 1304
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAE-------------LKELQAELE-------ELEEELEELQEELERLEEALEELREELE 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1305 TSEKMCRLYEDQMNEAKAKADELQRQLNEtntqraraqaesgelsrkLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEEN 1384
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQEN------------------LEGFSEGVKALLKNQSGLSGILGVLSELISVDE 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1385 KAKNALAHALQSSRhdcdllreQY---DEEQEAKADLQrALSKANAEVAQWrtkYETDAIQRTeeleeakkKLVTRLQEA 1461
Cdd:TIGR02168 534 GYEAAIEAALGGRL--------QAvvvENLNAAKKAIA-FLKQNELGRVTF---LPLDSIKGT--------EIQGNDREI 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1462 EETVETSNAKCSSLEKTKHRLQTEIEDL------VIDLERANAAAAVLDKKQRNF----DKVLAEW-------------- 1517
Cdd:TIGR02168 594 LKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvVDDLDNALELAKKLRPGYRIVtldgDLVRPGGvitggsaktnssil 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1518 --RQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKREN--------------KNLQEEIADLSDQISQGV 1581
Cdd:TIGR02168 674 erRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELeelsrqisalrkdlARLEAEVEQLEERIAQLS 753
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1582 KTIHELEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLELNQIKADVDRKLAEKDEEIDSLRRNHQRiLESMQAT 1661
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-LESLERR 832
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1662 LDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRNNL 1741
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1742 LAAEVEELRALLEQSDRARKLAEHELLEATERVNllnsqntgliNQKKKLESDLSMLSNEVDDAVQECRNAEEKAKKAIT 1821
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLS----------EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
970 980 990 1000
....*....|....*....|....*....|....*....|
gi 2108526737 1822 D------AAMmaEELKKEQDTSAHLERMKKNMEQTIKDLQ 1855
Cdd:TIGR02168 983 ElgpvnlAAI--EEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
913-1489 |
7.94e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.94 E-value: 7.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 913 LKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEIMERLEDEEE 992
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 993 MSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALLEAHQQTLDDLQ 1072
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1073 AEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQLDEKLKKKDFEMNEMS 1152
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1153 TRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQR--SDVARELEELSERLEEAGGATSAQIEMNKKREA 1230
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlaGAVAVLIGVEAAYEAALEAALAAALQNIVVEDD 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1231 DFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMC 1310
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1311 RLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKnsfsQNVEDLKKQLEEENKAKNAL 1390
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE----LELEEALLAEEEEERELAEA 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1391 AHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLvTRL-----------Q 1459
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI-EALgpvnllaieeyE 791
|
570 580 590
....*....|....*....|....*....|
gi 2108526737 1460 EAEETVETSNAKCSSLEKTKHRLQTEIEDL 1489
Cdd:COG1196 792 ELEERYDFLSEQREDLEEARETLEEAIEEI 821
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1277-1889 |
8.64e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.56 E-value: 8.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1277 KLEKERSEAKME--------VDDLASTVE-QLSKGKATSEKmCRLYEDQMNEAK-AKADELQRQLNETNTQRARAQAESG 1346
Cdd:COG1196 171 KERKEEAERKLEateenlerLEDILGELErQLEPLERQAEK-AERYRELKEELKeLEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1347 ELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKAN 1426
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1427 AEVAQwrtkyetdAIQRTEELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKK 1506
Cdd:COG1196 330 EELEE--------LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1507 QRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHE 1586
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1587 LEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLELNQIKADVDR---KLAEKDEEIDSLRRNHQRILESMQAtlD 1663
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveAAYEAALEAALAAALQNIVVEDDEV--A 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1664 AEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLqVQIKDIQLELDETIHQNEELkEQVAVTERRNNlla 1743
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL-VASDLREADARYYVLGDTLL-GRTLVAARLEA--- 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1744 aeVEELRALLEQSDRARKLAEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLSNEVDDAVQECRNAEEKAKKAITDA 1823
Cdd:COG1196 635 --ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526737 1824 AMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVLKLEARVKELENELES 1889
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1039-1894 |
3.78e-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: 101.30 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1039 LIEEMAALDETILKLTKEKKALLEAHQQtLDDLQAEEDKVNiltkakakleQQVDDLEGslEQEKKLR-MDLERVRRKLE 1117
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEEN-IERLDLIIDEKR----------QQLERLRR--EREKAERyQALLKEKREYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1118 GDLKLSleSVMDLENDKQQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEadRACRAKVEKqr 1197
Cdd:TIGR02169 225 GYELLK--EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ--LRVKEKIGE-- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1198 sdvareleelserleeaggaTSAQIEMNKKREADFLKLRRDLEEamlhHEATTAALRKKHADSVAELSEQIDSLQRVKQK 1277
Cdd:TIGR02169 299 --------------------LEAEIASLERSIAEKERELEDAEE----RLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1278 LEKERSEAKMEVDDLASTVEQLSKGKATSEkmcrlyeDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREA 1357
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETR-------DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1358 MVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYE 1437
Cdd:TIGR02169 428 AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1438 TDAIQRTE-------------ELEEAKKKLVT--------RLQEAEETVETSNAKCSSLEK----------------TKH 1480
Cdd:TIGR02169 508 GGRAVEEVlkasiqgvhgtvaQLGSVGERYATaievaagnRLNNVVVEDDAVAKEAIELLKrrkagratflplnkmrDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1481 RLQTEI-EDLVID-------------------------LERANAAAAVLDK----------------------KQRNFDK 1512
Cdd:TIGR02169 588 RDLSILsEDGVIGfavdlvefdpkyepafkyvfgdtlvVEDIEAARRLMGKyrmvtlegelfeksgamtggsrAPRGGIL 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1513 VLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKK 1592
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1593 GLDMEKSEIQAALEEAEGTLEHEESKSLRIQLELNQIKADVDR-KLAEKDEEIDSLRRNHQRIlesmqatldaeaksrne 1671
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsRIPEIQAELSKLEEEVSRI----------------- 810
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1672 avrlrkkmEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRA 1751
Cdd:TIGR02169 811 --------EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1752 LLEQSDRARKLAEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELK 1831
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQR 962
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108526737 1832 KEQDTSAhLERMKKNMEQTIKDLQMRLDEAEqialkgGKKQVLKLEAR-VKELENELESEQKKS 1894
Cdd:TIGR02169 963 VEEEIRA-LEPVNMLAIQEYEEVLKRLDELK------EKRAKLEEERKaILERIEEYEKKKREV 1019
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
907-1668 |
4.75e-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: 101.30 E-value: 4.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 907 EKELVSLKEELAKLKEALEKSEVKRKELEERQVSLI-QEKNDLSLQLQAEQDNLADAEDRcdlLIKTKIQLEAKVKEIME 985
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQALLKEKREYEGYELlKEKEALERQKEAIERQLASLEEE---LEKLTEEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 986 RLEDEEEMSANVlakKRKLEDECAELKKDIDDLEITLAKVEK-------EKHATENKVKNLIEEMAALDETILKLTKE-- 1056
Cdd:TIGR02169 270 IEQLLEELNKKI---KDLGEEEQLRVKEKIGELEAEIASLERsiaekerELEDAEERLAKLEAEIDKLLAEIEELEREie 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1057 -KKALLEAHQQTLDDLQAEED----KVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLE 1131
Cdd:TIGR02169 347 eERKRRDKLTEEYAELKEELEdlraELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1132 NDKQQLDEKLkkkdfemNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVAR---ELEELS 1208
Cdd:TIGR02169 427 AAIAGIEAKI-------NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRelaEAEAQA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1209 ERLEEAGGATSAQIEMNKKREADFLKLRRDLEEAMLHHEAT--TAALRKKHA-----DSVAElsEQIDSLQRVK------ 1275
Cdd:TIGR02169 500 RASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAieVAAGNRLNNvvvedDAVAK--EAIELLKRRKagratf 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1276 ------QKLEKERSEAKME-----------------------------VDDLASTVEQLSK------------------G 1302
Cdd:TIGR02169 578 lplnkmRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfgdtlvVEDIEAARRLMGKyrmvtlegelfeksgamtG 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1303 KATSEKMCRL----YEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKK 1378
Cdd:TIGR02169 658 GSRAPRGGILfsrsEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1379 QLEEenkaknalahalqssrhdcdlLREQYDEEQEAKADLQRALSKANAEVAQwrtkYETDAIQRTEELEEAKKKLvtrl 1458
Cdd:TIGR02169 738 RLEE---------------------LEEDLSSLEQEIENVKSELKELEARIEE----LEEDLHKLEEALNDLEARL---- 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1459 qeAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGL 1538
Cdd:TIGR02169 789 --SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1539 STELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEGTLEHEESK 1618
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108526737 1619 SLRIqLELNQIKADVDRK------------LAEKDEEIDSLRRNHqriLESMQATLDAEAKS 1668
Cdd:TIGR02169 947 PEEE-LSLEDVQAELQRVeeeiralepvnmLAIQEYEEVLKRLDE---LKEKRAKLEEERKA 1004
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1261-1884 |
5.94e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.78 E-value: 5.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1261 VAELSEQIDSLQRVKQKLEKERsEAKMEVDDLASTVEQLSKGKATSEKmcRLYEDQMNEAKAKADELQRQLNETNTQRAR 1340
Cdd:COG1196 195 LGELERQLEPLERQAEKAERYR-ELKEELKELEAELLLLKLRELEAEL--EELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1341 AQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQR 1420
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1421 ALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEETVEtsnakcssLEKTKHRLQTEIEDLVIDLERANAAA 1500
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE--------LAAQLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1501 AVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRE------NKNLQEEIADLS 1574
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEElaeaaaRLLLLLEAEADY 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1575 DQISQGVKTIHELEKmKKGLDMEKSEIQAALEEAEGTLEHEESKSLRiqlelnqikADVDRKLAEKDEEIDSLRRNHQRi 1654
Cdd:COG1196 504 EGFLEGVKAALLLAG-LRGLAGAVAVLIGVEAAYEAALEAALAAALQ---------NIVVEDDEVAAAAIEYLKAAKAG- 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1655 lesmQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAV 1734
Cdd:COG1196 573 ----RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1735 TERRNNLLAAEVEELRALLEQSDRARKLAEHELLEATERvnlLNSQNTGLINQKKKLESDLSMLSNEVDDAVQECRNAEE 1814
Cdd:COG1196 649 VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER---LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1815 KAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEaeqialkggkkqvlkLEARVKELE 1884
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER---------------LEREIEALG 780
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1037-1898 |
1.27e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 99.75 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1037 KNLIEEMAAldetILKLTKEKKallEAHQQ---TLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLR------- 1106
Cdd:TIGR02168 158 RAIFEEAAG----ISKYKERRK---ETERKlerTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRelelall 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1107 -MDLERVRRKLE---GDLKLSLESVMDLENDKQQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQArteeleee 1182
Cdd:TIGR02168 231 vLRLEELREELEelqEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ-------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1183 leadracrakvekqrsdvareleelserleeaggatsaQIEMNKKREADFLKLRRDLEEAMLHHEATtaalRKKHADSVA 1262
Cdd:TIGR02168 303 --------------------------------------QKQILRERLANLERQLEELEAQLEELESK----LDELAEELA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1263 ELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLskgkatsekmcrlyEDQMNEAKAKADELQRQLNETNTQRARAQ 1342
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEEL--------------EEQLETLRSKVAQLELQIASLNNEIERLE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1343 AESGELSRKLEEREAMVSQLQRAKNSfsQNVEDLKKQLEEENKAKNALAHALqssrhdcDLLREQYDEEQEAKADLQRAL 1422
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEEL-------ERLEEALEELREELEEAEQAL 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1423 SKANAEVAQWRTKyeTDAIQRTEELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIED---------LVIDL 1493
Cdd:TIGR02168 478 DAAERELAQLQAR--LDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAalggrlqavVVENL 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1494 ERANAAAAVLDKKQRNFDKVLAEWRQKYEECQS---ELETSQKESRGLSTELFKLKNSYEETLDHL-------ETIKREN 1563
Cdd:TIGR02168 556 NAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGndrEILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvDDLDNAL 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1564 kNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQA---ALEEAEGTLEHEESKSLRIQLELNqikadvdrKLAEK 1640
Cdd:TIGR02168 636 -ELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILErrrEIEELEEKIEELEEKIAELEKALA--------ELRKE 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1641 DEEIDSLRRNHQRILESMQATLDAEaksRNEAVRLRKKMEgdlnEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDE 1720
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISAL---RKDLARLEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1721 TIHQNEELKEQVAVTERRNNLLAAEVEELRALLEQSDRARKLAEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLSN 1800
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1801 EVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAeqialkggKKQVLKLEARV 1880
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL--------REKLAQLELRL 931
|
890
....*....|....*....
gi 2108526737 1881 KELENELESEQKK-SQEYQ 1898
Cdd:TIGR02168 932 EGLEVRIDNLQERlSEEYS 950
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1314-1987 |
1.88e-20 |
|
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: 99.09 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1314 EDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLE-------EREAMVSQLQRAKNSFSQNVEDLKKQLEEENKA 1386
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1387 KNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEeLEEAKKKLVTRLQEAEETVE 1466
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK-LSKERKLLEERISEFTSNLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1467 TSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLK 1546
Cdd:pfam01576 170 EEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1547 NSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEA-EGTLEHEESKSLRIQlE 1625
Cdd:pfam01576 250 ARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTlDTTAAQQELRSKREQ-E 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1626 LNQIKADVDRKLAEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLR 1705
Cdd:pfam01576 329 VTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1706 NLQVQIKDIQLELDETIHQNEELKEQVAVterrnnlLAAEVEELRALLEQSDrarklaehelleatervnllnsqntgli 1785
Cdd:pfam01576 409 KLEGQLQELQARLSESERQRAELAEKLSK-------LQSELESVSSLLNEAE---------------------------- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1786 NQKKKLESDLSMLSNEVDDAvQECRNAEEKAKKAIT--------DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMR 1857
Cdd:pfam01576 454 GKNIKLSKDVSSLESQLQDT-QELLQEETRQKLNLStrlrqledERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1858 LDEaEQIALKGGKKQVLKLEarvKELENELESEQKKSQEYQKGVRKYERRIKELS------YQGEEDKKNLVRLQDLIDK 1931
Cdd:pfam01576 533 LEE-DAGTLEALEEGKKRLQ---RELEALTQQLEEKAAAYDKLEKTKNRLQQELDdllvdlDHQRQLVSNLEKKQKKFDQ 608
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1932 MQAKVKS----YKRQTEEAEEQANTNLSKYRKLQHELDDAEERADMAESQANKLRARTRD 1987
Cdd:pfam01576 609 MLAEEKAisarYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMED 668
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
914-1833 |
2.02e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 98.99 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 914 KEELAKLKEALEKSEvkrkeleerqvSLIQEKNDlslQLQAEQDNLADAEDRCDLLiktKIQLEAKVKEIMERLEDEEEM 993
Cdd:TIGR02169 176 LEELEEVEENIERLD-----------LIIDEKRQ---QLERLRREREKAERYQALL---KEKREYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 994 SANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIE-EMAALDETILKLTKEKKALLEAHQQTLDDLQ 1072
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1073 AEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLrmdlervRRKLEGDLKLSLESVMDLENDKQQLDEKLKKKDFEMNEMS 1152
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKR-------RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1153 TRIEDEQALVNQLQKKIKELQArteeleeeleadracrakvEKQRsdvareleelserleeaggATSAQIEMNKKREadf 1232
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQE-------------------ELQR-------------------LSEELADLNAAIA--- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1233 lklrrDLEEAMLHHEATTAALRKKhadsVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRL 1312
Cdd:TIGR02169 431 -----GIEAKINELEEEKEDKALE----IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARA 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1313 YEDQMNEAKAKADELqrqlnetntqRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVedlkkQLEEENKAKNA--L 1390
Cdd:TIGR02169 502 SEERVRGGRAVEEVL----------KASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNV-----VVEDDAVAKEAieL 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1391 AHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETD---AIQRT---EELEEAKK-----KLVTRlq 1459
Cdd:TIGR02169 567 LKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAfkyVFGDTlvvEDIEAARRlmgkyRMVTL-- 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1460 eAEETVETSNA------KCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQK 1533
Cdd:TIGR02169 645 -EGELFEKSGAmtggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK 723
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1534 ESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKglDMEKSEIQAALEEAEGTLE 1613
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN--DLEARLSHSRIPEIQAELS 801
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1614 HEESKSLRIQLELNQIKADVDRKLAEKdEEIDSLRRNHQRILESMQATLDAEAKsRNEAVRLR--------KKMEGDLNE 1685
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEK-EYLEKEIQELQEQRIDLKEQIKSIEK-EIENLNGKkeeleeelEELEAALRD 879
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1686 MEVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRALLEQSDRARKLAEh 1765
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQA- 958
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526737 1766 ELLEATERVNLLNSQNTGLINQKKKLESDLSMLsnevddavQECRNAEEKAKKAITDAAMMAEELKKE 1833
Cdd:TIGR02169 959 ELQRVEEEIRALEPVNMLAIQEYEEVLKRLDEL--------KEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
900-1597 |
9.18e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 97.06 E-value: 9.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 900 LLRSATTEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKI-QLEA 978
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIaSLER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 979 KVKEIMERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLeitlaKVEKEKhatenkvknLIEEMAALDETILKLTKEKK 1058
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEE-----RKRRDK---------LTEEYAELKEELEDLRAELE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1059 ALLEAHQQTLDDLQAEEDKVNILTKAKAKLEQQVDDLegsLEQEKKLRMDLERVRRKLEgdlklslesvmDLENDKQQLD 1138
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRL---QEELQRLSEELADLNAAIA-----------GIEAKINELE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1139 EKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEELSERLEE----- 1213
Cdd:TIGR02169 441 EEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVlkasi 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1214 -----------------------AGGA------------TSAQIEMNKKRE---ADFLKLRR------------------ 1237
Cdd:TIGR02169 521 qgvhgtvaqlgsvgeryataievAAGNrlnnvvveddavAKEAIELLKRRKagrATFLPLNKmrderrdlsilsedgvig 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1238 ---------------------------DLEEAMLH-------------------------HEATTAALRKKHADSVAELS 1265
Cdd:TIGR02169 601 favdlvefdpkyepafkyvfgdtlvveDIEAARRLmgkyrmvtlegelfeksgamtggsrAPRGGILFSRSEPAELQRLR 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1266 EQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAES 1345
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1346 GELSRKLEEREAMVSQLQRAKN--------SFSQNVEDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKAD 1417
Cdd:TIGR02169 761 KELEARIEELEEDLHKLEEALNdlearlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1418 LQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVT---RLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLE 1494
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDlesRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1495 RANAAAAVLDKKQRNFDKVLAEwRQKYEECQSELETSQKESRGLSTELFKLK-------NSYEETLDHLETIKRENKNLQ 1567
Cdd:TIGR02169 921 ELKAKLEALEEELSEIEDPKGE-DEEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLE 999
|
810 820 830
....*....|....*....|....*....|
gi 2108526737 1568 EEIADLSDqisqgvkTIHELEKMKKGLDME 1597
Cdd:TIGR02169 1000 EERKAILE-------RIEEYEKKKREVFME 1022
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1223-1994 |
1.63e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 96.36 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1223 EMNKKREADFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQrVKQKLEKERSEAKMEVDDLASTVEQLSKG 1302
Cdd:PTZ00121 1031 ELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFD-FDAKEDNRADEATEEAFGKAEEAKKTETG 1109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1303 KATSEKmcrlyedQMNEAKAKADELQRqlneTNTQRARAQAESGELSRKLEEREamvsqlqraKNSFSQNVEDLKKqLEE 1382
Cdd:PTZ00121 1110 KAEEAR-------KAEEAKKKAEDARK----AEEARKAEDARKAEEARKAEDAK---------RVEIARKAEDARK-AEE 1168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1383 ENKAKNAlaHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYE----TDAIQRTEEL----EEAKKKL 1454
Cdd:PTZ00121 1169 ARKAEDA--KKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEdakkAEAVKKAEEAkkdaEEAKKAE 1246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1455 VTRLQEA----EETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELET 1530
Cdd:PTZ00121 1247 EERNNEEirkfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1531 SQKESRglstelfKLKNSYEETLDHLETIKRENKNLQEEiADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEG 1610
Cdd:PTZ00121 1327 AKKKAD-------AAKKKAEEAKKAAEAAKAEAEAAADE-AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKK 1398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1611 TLEHEESKSLRIQ-LELNQIKADVDRKLAEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEavRLRKKMEgdlnemEVQ 1689
Cdd:PTZ00121 1399 KAEEDKKKADELKkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE--EAKKKAE------EAK 1470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1690 LSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEqvaVTERRNNLLAAEVEELRALLE--QSDRARKLAEHEL 1767
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK---ADEAKKAEEAKKADEAKKAEEakKADEAKKAEEKKK 1547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1768 LEATERVN-LLNSQNTGLINQKKKLESDLSMLSNEVDDAVQ-ECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKK 1845
Cdd:PTZ00121 1548 ADELKKAEeLKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1846 NMEQTIKDLQMRLDEAEQI-ALKGGKKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKnlvr 1924
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK---- 1703
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1925 lQDLIDKMQAKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADMAESQANKLRARTRDQGSKLAE 1994
Cdd:PTZ00121 1704 -AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1226-1792 |
3.67e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.00 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1226 KKREADFLKLRRDLEEAMLhheATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKAT 1305
Cdd:COG1196 223 KELEAELLLLKLRELEAEL---EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1306 SEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENK 1385
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1386 AKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKyETDAIQRTEELEEAKKKLVTRLQEAEETV 1465
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA-LAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1466 ETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKyeecqsELETSQKESRGLSTELFKL 1545
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA------LLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1546 KNSYEETLDHLETIKRENKNLQEEiADLSDQIS------QGVKTIHELEKMKKGLDMEKSEIQAALEEA----------- 1608
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDD-EVAAAAIEylkaakAGRATFLPLDKIRARAALAAALARGAIGAAvdlvasdlrea 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1609 ---------------------------EGTLEHEESKSLRIQLELNQIKADVDRKLAEKDEEIDSLRRNHQRILESMQAT 1661
Cdd:COG1196 612 daryyvlgdtllgrtlvaarleaalrrAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1662 LDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRNNL 1741
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2108526737 1742 LAAEVEELRA--LleqsdrarkLAEHELLEATERVNLLNSQNTGLINQKKKLE 1792
Cdd:COG1196 772 LEREIEALGPvnL---------LAIEEYEELEERYDFLSEQREDLEEARETLE 815
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1412-1984 |
7.68e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.85 E-value: 7.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1412 QEAKADLQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVI 1491
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1492 DLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIA 1571
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1572 DLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLELNQIKADVDRKLAEKDEEIDSLRRNH 1651
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1652 QRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQ 1731
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1732 VAVTERrnnlLAAEVEELRALLEQSDRARKLAEHELLEATERVNLLNSQntgLINQKKKLESDLSMLSNEVDDAVQECRN 1811
Cdd:COG1196 536 YEAALE----AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD---KIRARAALAAALARGAIGAAVDLVASDL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1812 AEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVLKLEARVKELENELESEQ 1891
Cdd:COG1196 609 READARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1892 kksQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEAEEQANTNLSkyrKLQHELDDAEERA 1971
Cdd:COG1196 689 ---AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE---EEALEELPEPPDL 762
|
570
....*....|...
gi 2108526737 1972 DMAESQANKLRAR 1984
Cdd:COG1196 763 EELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
914-1592 |
5.27e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.15 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 914 KEE-LAKLKEA---LEKSEVKRKELEeRQVSliqekndlSLQLQAEQ----DNLADAEDRCD--LLIKTKIQLEAKVKEI 983
Cdd:COG1196 174 KEEaERKLEATeenLERLEDILGELE-RQLE--------PLERQAEKaeryRELKEELKELEaeLLLLKLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 984 MERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALLEA 1063
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1064 HQQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQLDEKLKK 1143
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1144 KDFEMNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEADracRAKVEKQRSDVARELEELSERLEEAGGATSAQIE 1223
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA---AEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1224 MNKKREADFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAkmevddLASTVEQLSKGK 1303
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA------LAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1304 ATSEKMCRLYEDQMNEAKAKADELqrqlnetNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLkkqLEEE 1383
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPL-------DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT---LLGR 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1384 NKAKNALAHALQSSRhdcdLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEE 1463
Cdd:COG1196 626 TLVAARLEAALRRAV----TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1464 TVETSNAkcssLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELF 1543
Cdd:COG1196 702 EEEEERE----LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526737 1544 KLKN-------SYEETLDHLETIKRENKNLQEEIADLsdqisqgVKTIHELEKMKK 1592
Cdd:COG1196 778 ALGPvnllaieEYEELEERYDFLSEQREDLEEARETL-------EEAIEEIDRETR 826
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1223-1983 |
5.36e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 91.36 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1223 EMNKKREADFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSE----QIDSLQRVKQKLEKERSEAKMEVDDLASTVEQ 1298
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEarkaEDAKRVEIARKAEDARKAEEARKAEDAKKAEA 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1299 LSKgkatSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRAR--AQAESGELSRKLEEREAMVSQLQRAKNSfsQNVEDL 1376
Cdd:PTZ00121 1181 ARK----AEEVRKAEELRKAEDARKAEAARKAEEERKAEEARkaEDAKKAEAVKKAEEAKKDAEEAKKAEEE--RNNEEI 1254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1377 KKQLEEENKAKNALAHALQSS-RHDCDLLREQydEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLV 1455
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEeARKADELKKA--EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKAD 1332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1456 TRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAaavldKKQRNFDKVLAEWRQKYEECQSELETSQKES 1535
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA-----KKKADAAKKKAEEKKKADEAKKKAEEDKKKA 1407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1536 RGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDmEKSEIQAALEEAEGTLEHE 1615
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE-EAKKADEAKKKAEEAKKAD 1486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1616 ESKSlriQLELNQIKADVDRKLAEKDEEIDSLRRNHQ--------RILESMQATLDAEAKSRNEAVRLRKKMEGDLNEME 1687
Cdd:PTZ00121 1487 EAKK---KAEEAKKKADEAKKAAEAKKKADEAKKAEEakkadeakKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEK 1563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1688 VQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRALLEQSDRARKLAEHEL 1767
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1768 LEATERVNLLNSQNTGLI---NQKKKLESDlsmlsnevDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK 1844
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIkaaEEAKKAEED--------KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1845 KNMEQTIKDLQMRLDEAEQIALKGGKKQVLKLEARVKELENELESEQKKSQEYQKgvrKYERRIKELSYQGEEDKKNLVR 1924
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA---EEIRKEKEAVIEEELDEEDEKR 1792
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2108526737 1925 LQDLidkmQAKVKSYKRQTEEAEEQANTNlSKYRKLQHELDDAE--ERADMAESQANKLRA 1983
Cdd:PTZ00121 1793 RMEV----DKKIKDIFDNFANIIEGGKEG-NLVINDSKEMEDSAikEVADSKNMQLEEADA 1848
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
277-767 |
1.13e-17 |
|
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: 89.80 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 277 IIEANPAMEAFGNAKTLRNDNSSRFGKF--IRIHFGPTG---KLASADIDIYLLEKSRVIFQQ------PGERSYHIYYQ 345
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 346 IMSQ----------KKPELLDMLLVSSNPY----DYH---FCSQGVTTVENMDDGQELMatdHAMDILGFLPDEKYGCYK 408
Cdd:cd14894 329 MVAGvnafpfmrllAKELHLDGIDCSALTYlgrsDHKlagFVSKEDTWKKDVERWQQVI---DGLDELNVSPDEQKTIFK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 409 IVGAIMHFGNMKFKQRQREEQAEADGT---ESADKASYLMGVSSADLIKGLLHPR---VKVGNEYVVKGQNVEQVTYAVG 482
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 483 ALAKATYDRMFKWLVIRINRTLY----------------TSLPRQY-FIGVLDIAGFEIFELNSFEQLCINFTNEKLqqf 545
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATKmsalstdgnkhqmdsnASAPEAVsLLKIVDVFGFEDLTHNSLDQLCINYLSEKL--- 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 546 fnhhmfileqeeYKRE----GIEWTFIDFGLDLQACIDLI---EKPLGIMSILEEECMFPKATDNS----------FKAK 608
Cdd:cd14894 563 ------------YAREeqviAVAYSSRPHLTARDSEKDVLfiyEHPLGVFASLEELTILHQSENMNaqqeekrnklFVRN 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 609 MYDNHIGKSPNFQKPRPDKKRKYEA-----HFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFRKSSNKLLASLY--EN 681
Cdd:cd14894 631 IYDRNSSRLPEPPRVLSNAKRHTPVllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLneSS 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 682 YVG-SDAAFDSKTGSKEKRKKAASfQTVSQVhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDPFMVLHQLRCNGVL 760
Cdd:cd14894 711 QLGwSPNTNRSMLGSAESRLSGTK-SFVGQF-RSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLI 788
|
....*..
gi 2108526737 761 EGIRICR 767
Cdd:cd14894 789 RQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
902-1489 |
2.12e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 89.35 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 902 RSATTEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVK 981
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 982 EIMERLEDEEEMSANVLAKKRKLEDECAELKKD-----IDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKE 1056
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaeLEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1057 ---KKALLEAHQQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERV--------------------- 1112
Cdd:TIGR02168 484 laqLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAAlggrlqavvvenlnaakkaia 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1113 -------------------RRKLEGDLKLSLESV-------MDLE--------------------NDKQQLDEKLKKKDF 1146
Cdd:TIGR02168 564 flkqnelgrvtflpldsikGTEIQGNDREILKNIegflgvaKDLVkfdpklrkalsyllggvlvvDDLDNALELAKKLRP 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1147 EMNE------------MSTRIEDEQALVNQ-LQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEELSERLEE 1213
Cdd:TIGR02168 644 GYRIvtldgdlvrpggVITGGSAKTNSSILeRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1214 AggatsaqiemnkkrEADFLKLRRDLEEAMLHHEATTAALRKKHADsVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLA 1293
Cdd:TIGR02168 724 L--------------SRQISALRKDLARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1294 STVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNV 1373
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1374 EDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKK 1453
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
650 660 670
....*....|....*....|....*....|....*.
gi 2108526737 1454 LVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDL 1489
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
985-1924 |
2.87e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 88.88 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 985 ERLEDEEEMS-ANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKhatenkvknlieemaaldetiLKLTKEKKALLEA 1063
Cdd:pfam02463 154 RRLEIEEEAAgSRLKRKKKEALKKLIEETENLAELIIDLEELKLQE---------------------LKLKEQAKKALEY 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1064 HQQTLDdlqAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQL-DEKLK 1142
Cdd:pfam02463 213 YQLKEK---LELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLqEEELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1143 KKDFEMNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVareleelserleeaggatSAQI 1222
Cdd:pfam02463 290 LLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEL------------------EIKR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1223 EMNKKREADFLKLRRDLEEAmlhheattaalRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLAstveQLSKG 1302
Cdd:pfam02463 352 EAEEEEEEELEKLQEKLEQL-----------EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL----ELARQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1303 KATsekmcrLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEE 1382
Cdd:pfam02463 417 LED------LLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLL 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1383 ENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQ----WRTKYETDAIQRTEELEEAKKKLVTRL 1458
Cdd:pfam02463 491 SRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEnykvAISTAVIVEVSATADEVEERQKLVRAL 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1459 QEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVldkkqRNFDKVLAEWRQKYEECQSELETSQKESRGL 1538
Cdd:pfam02463 571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLE-----ADEDDKRAKVVEGILKDTELTKLKESAKAKE 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1539 STELF-----KLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEGTLE 1613
Cdd:pfam02463 646 SGLRKgvsleEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLAD 725
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1614 HEESKSLRIQLELNQIKADVDRKLAEKDEEIDSLRRNHQRILE-SMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSH 1692
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSElSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRA 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1693 ANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEqvavterrnnllaaevEELRALLEQSDRARKLAEHELLEATE 1772
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELK----------------EEQKLEKLAEEELERLEEEITKEELL 869
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1773 RVNLLNSQNTGLINQKKKLESDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIK 1852
Cdd:pfam02463 870 QELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKE 949
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108526737 1853 DLQMRLDEAEQIALKGGKKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKNLVR 1924
Cdd:pfam02463 950 KEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1060-1751 |
6.26e-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: 87.48 E-value: 6.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1060 LLEAHQQTLDDLQAEEDKVNIL-TKAKAKLEQQVDDLEGSLEQ---EKKLRMDLERVRRKLEGDLKLSLE-SVMDLENDK 1134
Cdd:pfam15921 79 VLEEYSHQVKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLRNQLQnTVHELEAAK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1135 QQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELeaDRACRAKVEKQRSDVARELEELSERLEEA 1214
Cdd:pfam15921 159 CLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEH--DSMSTMHFRSLGSAISKILRELDTEISYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1215 GG---ATSAQIEMNKKREADFLKL-----RRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAK 1286
Cdd:pfam15921 237 KGrifPVEDQLEALKSESQNKIELllqqhQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYM 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1287 MEVDDLASTVEQLskgKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLE-------EREAMV 1359
Cdd:pfam15921 317 RQLSDLESTVSQL---RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQklladlhKREKEL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1360 SqLQRAKNSF--------SQNVEDLKKQLEEENKAKNALAHALQSSRHDCdllREQYDEEQEAKADLQRALSKANAEVAQ 1431
Cdd:pfam15921 394 S-LEKEQNKRlwdrdtgnSITIDHLRRELDDRNMEVQRLEALLKAMKSEC---QGQMERQMAAIQGKNESLEKVSSLTAQ 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1432 WRTKYE---------TDAIQRTEELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVID---LERANAA 1499
Cdd:pfam15921 470 LESTKEmlrkvveelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1500 AAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRenknlqeeIADLSDqisq 1579
Cdd:pfam15921 550 CEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKI--------LKDKKD---- 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1580 gvKTIHELEKMKKGLDMEKSEIQAALEEAEGTLehEESKSLRIQLeLNQIKADVDrKLAEKDEEIDSLRRNHQRILESMQ 1659
Cdd:pfam15921 618 --AKIRELEARVSDLELEKVKLVNAGSERLRAV--KDIKQERDQL-LNEVKTSRN-ELNSLSEDYEVLKRNFRNKSEEME 691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1660 ATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLE---LDETI-----------HQN 1725
Cdd:pfam15921 692 TTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKiqfLEEAMtnankekhflkEEK 771
|
730 740
....*....|....*....|....*.
gi 2108526737 1726 EELKEQVAVTERRNNLLAAEVEELRA 1751
Cdd:pfam15921 772 NKLSQELSTVATEKNKMAGELEVLRS 797
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
902-1572 |
8.76e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.50 E-value: 8.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 902 RSATTEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDlsLQLQAEQDNLAD-AEDRCDLLIKTKIQLEAKV 980
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE--AKKKAEEAKKADeAKKKAEEAKKKADAAKKKA 1338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 981 KEIMERLE--DEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKK 1058
Cdd:PTZ00121 1339 EEAKKAAEaaKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1059 ALLEAHQQTLDDLQAEEdkvnilTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGD-LKLSLESVMDLENDKQQL 1137
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADE------AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAEEAKKADEAKKKA 1492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1138 DEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQarteELEEELEADRACRAKVEKQRSDVARELEELSERLEEagga 1217
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK----KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK---- 1564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1218 tsaQIEMNKKREADFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEakmevDDLASTVE 1297
Cdd:PTZ00121 1565 ---KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-----EEEKKKVE 1636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1298 QLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNEtntqraraQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLK 1377
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE--------DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1378 KQLEEENKAKNALAHALQSSRHDCDLLREQyDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEEL-----EEAKK 1452
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeavieEELDE 1787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1453 KLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKvlaEWRQKYEECQSELETSQ 1532
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEAD---AFEKHKFNKNNENGEDG 1864
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2108526737 1533 KESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIAD 1572
Cdd:PTZ00121 1865 NKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPN 1904
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1265-1968 |
1.45e-16 |
|
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: 86.56 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1265 SEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLnETNTQRARAQAE 1344
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR-EAQEEQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1345 SGELSRKLEEREAMVSQLqraknsfsqnvEDLKKQLEEENKAKNALAHALQSSRHDCDLlREQYDEEQEAKADLQRALSK 1424
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVL-----------EETQERINRARKAAPLAAHIKAVTQIEQQA-QRIHTELQSKMRSRAKLLMK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1425 ANAEVAQWRTKYETDAIQRTEELEEAKKKlvtrlQEAEETVETSNAKCSSLEKTkHRLQTEIEDLVIDLERANAAAAVLD 1504
Cdd:TIGR00618 330 RAAHVKQQSSIEEQRRLLQTLHSQEIHIR-----DAHEVATSIREISCQQHTLT-QHIHTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1505 KKQRNFDKVLAEwRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQgVKTI 1584
Cdd:TIGR00618 404 ILQREQATIDTR-TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQT-KEQI 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1585 HELEKMKKGLDMEKSEIQAALE-EAEGTLEHEESKSLRIQL----------------ELNQIKADVDRKLAEKDEEIDSL 1647
Cdd:TIGR00618 482 HLQETRKKAVVLARLLELQEEPcPLCGSCIHPNPARQDIDNpgpltrrmqrgeqtyaQLETSEEDVYHQLTSERKQRASL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1648 RRNHQRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEE 1727
Cdd:TIGR00618 562 KEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQEL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1728 LKEQVAVTERRNNLLAAEVEElRALLEQSDRARKLAEHELLEATERvnllnsqntgliNQKKKLESDLSMLsNEVDDAVQ 1807
Cdd:TIGR00618 642 ALKLTALHALQLTLTQERVRE-HALSIRVLPKELLASRQLALQKMQ------------SEKEQLTYWKEML-AQCQTLLR 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1808 ECRNAEEKAKKAITD--AAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKggKKQVLKLEARVKELEN 1885
Cdd:TIGR00618 708 ELETHIEEYDREFNEieNASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEE--VTAALQTGAELSHLAA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1886 ELESEQKKSQEYQKGVRKYERRIKE--------LSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEAEE---QANTNL 1954
Cdd:TIGR00618 786 EIQFFNRLREEDTHLLKTLEAEIGQeipsdediLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEEcskQLAQLT 865
|
730
....*....|....
gi 2108526737 1955 SKYRKLQHELDDAE 1968
Cdd:TIGR00618 866 QEQAKIIQLSDKLN 879
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
901-1576 |
1.51e-16 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 86.38 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 901 LRSATTEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADaEDRCDLLIKTKI-QLEAK 979
Cdd:pfam01576 419 ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLrQLEDE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 980 VKEIMERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKA 1059
Cdd:pfam01576 498 RNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1060 LleahQQTLDDLQAEEDK----VNILTKAKAKLEQQVDD----------------------------LEGSLEQEKKLRM 1107
Cdd:pfam01576 578 L----QQELDDLLVDLDHqrqlVSNLEKKQKKFDQMLAEekaisaryaeerdraeaeareketralsLARALEEALEAKE 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1108 DLERVRRKLEGDLKLSLESVMDLENDKQQLDEKLKKKDFEMNEMSTriedeqalvnQLQKKIKELQARTEELEEELEADR 1187
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKT----------QLEELEDELQATEDAKLRLEVNMQ 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1188 ACRAKVEKQrsdvareleelserleeaggaTSAQIEMNKKREADFLKLRRDLeEAMLHHEattaalRKKHADSVAelseq 1267
Cdd:pfam01576 724 ALKAQFERD---------------------LQARDEQGEEKRRQLVKQVREL-EAELEDE------RKQRAQAVA----- 770
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1268 idslqrVKQKLEkerseakMEVDDLASTVEQLSKGKATSEKmcrlyedQMNEAKAKADELQRQLNETNTQRARAQAESGE 1347
Cdd:pfam01576 771 ------AKKKLE-------LDLKELEAQIDAANKGREEAVK-------QLKKLQAQMKDLQRELEEARASRDEILAQSKE 830
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1348 LSRKLEEREAMVSQLQ-------RAKNSFSQNVEDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQR 1420
Cdd:pfam01576 831 SEKKLKNLEAELLQLQedlaaseRARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLND 910
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1421 ALSKANAEVAQWRTKY--ETDAIQRTE----ELEEAKKKLVTRLQEAEETVETS-NAKCSSLEKTKHRLQTEIEdlVIDL 1493
Cdd:pfam01576 911 RLRKSTLQVEQLTTELaaERSTSQKSEsarqQLERQNKELKAKLQEMEGTVKSKfKSSIAALEAKIAQLEEQLE--QESR 988
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1494 ERANAAAAVldkkqRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADL 1573
Cdd:pfam01576 989 ERQAANKLV-----RRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDA 1063
|
...
gi 2108526737 1574 SDQ 1576
Cdd:pfam01576 1064 TES 1066
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
914-1657 |
1.57e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 86.73 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 914 KEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLslQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEIMERLEDEEEM 993
Cdd:PTZ00121 1201 KAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEA--KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR 1278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 994 SANVLAKkrkledecAELKKDIDDLEitlaKVEKEKHATENKVKnlIEEMAALDETILKLTKEKKALLEAHQQTLDDLQA 1073
Cdd:PTZ00121 1279 KADELKK--------AEEKKKADEAK----KAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1074 EEdkvniltKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEgDLKLSLESVMDLENDKQQLDEKLKKKD-FEMNEMS 1152
Cdd:PTZ00121 1345 AE-------AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD-AAKKKAEEKKKADEAKKKAEEDKKKADeLKKAAAA 1416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1153 TRIEDEQALVNQLQKKIKELQARteeleeeleADRACRAKVEKQRSDVARELEELSERLEEAGGATSAQIEMNKKREADF 1232
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKK---------AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1233 LKLRRDlEEAMLHHEATTAALRKKHADSVAELSEQidslqrvKQKLEKERSEAKMEVDDLASTVEqlskgKATSEKMCRL 1312
Cdd:PTZ00121 1488 AKKKAE-EAKKKADEAKKAAEAKKKADEAKKAEEA-------KKADEAKKAEEAKKADEAKKAEE-----KKKADELKKA 1554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1313 YEDQMNEAKAKADELQRQLNETNTQRARAqaesgELSRKLEEREaMVSQLQRAKNSFSQNVEDLKKqlEEENKAKNALAH 1392
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKA-----EEAKKAEEAR-IEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEELK 1626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1393 ALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAiQRTEEL----EEAKKKLVTRLQEAEETVETS 1468
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkkaeEDEKKAAEALKKEAEEAKKAE 1705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1469 NAKCSSLEKTKHRLQTEIEdlvidlERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNS 1548
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKA------EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1549 Y-EETLDHLETIKR-ENKNLQEEIADLSDQISQGVKTIHELEKMKKglDMEKSEIQAALEEAEGTLEhEESKSLRIQLEL 1626
Cdd:PTZ00121 1780 ViEEELDEEDEKRRmEVDKKIKDIFDNFANIIEGGKEGNLVINDSK--EMEDSAIKEVADSKNMQLE-EADAFEKHKFNK 1856
|
730 740 750
....*....|....*....|....*....|.
gi 2108526737 1627 NQIKADVDRKLAEKDEEIDSLRRNHQRILES 1657
Cdd:PTZ00121 1857 NNENGEDGNKEADFNKEKDLKEDDEEEIEEA 1887
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1082-1899 |
2.14e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 86.35 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1082 TKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQLDEKL-----KKKDFEMNEMSTRIE 1156
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRveiarKAEDARKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1157 D----EQALVNQLQKKIKELQ----ARTEELEEELEADR---ACRAKVEKQRSDVARELEELSERLEEAGGAtsaqiemn 1225
Cdd:PTZ00121 1174 DakkaEAARKAEEVRKAEELRkaedARKAEAARKAEEERkaeEARKAEDAKKAEAVKKAEEAKKDAEEAKKA-------- 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1226 kKREADFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQidslQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKAT 1305
Cdd:PTZ00121 1246 -EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA----EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1306 SEKmcrlyedqMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENK 1385
Cdd:PTZ00121 1321 KKK--------AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1386 AKNALAHAlQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAiqrteelEEAKKKlvtrlqeAEETV 1465
Cdd:PTZ00121 1393 ADEAKKKA-EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA-------DEAKKK-------AEEAK 1457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1466 ETSNAKCSSLEKTKhrlqteIEDLVIDLERANAAAAvLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKL 1545
Cdd:PTZ00121 1458 KAEEAKKKAEEAKK------ADEAKKKAEEAKKADE-AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1546 knsyEETLDHLETIKRENKNLQEEIadlsdqisqgvktihelekmKKGLDMEKSEIQAALEEAEgtlEHEESKSLRIQle 1625
Cdd:PTZ00121 1531 ----EEAKKADEAKKAEEKKKADEL--------------------KKAEELKKAEEKKKAEEAK---KAEEDKNMALR-- 1581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1626 lnqiKADVDRKLAEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLR 1705
Cdd:PTZ00121 1582 ----KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE 1657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1706 NLQVQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRALLE-QSDRARKLAEHELLEATERVNLLNSQNTGL 1784
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1785 INQKKKLESDLSMLSNEVDDAVQECRNAEEKAKKAI--TDAAMMAEELKKEQdtsahlERMKKNMEQTIKDLQmrlDEAE 1862
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIrkEKEAVIEEELDEED------EKRRMEVDKKIKDIF---DNFA 1808
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 2108526737 1863 QIaLKGGKKQVLKL-------EARVKELENELESEQKKSQEYQK 1899
Cdd:PTZ00121 1809 NI-IEGGKEGNLVIndskemeDSAIKEVADSKNMQLEEADAFEK 1851
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1480-1988 |
3.78e-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: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1480 HRLQTEIEDLviDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETI 1559
Cdd:COG1196 216 RELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1560 KRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLELNQIKADVDRKLAE 1639
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1640 KDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRKKmEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELD 1719
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1720 ETIHQNEELKEQVAVTERRNNLLAAEVEELRALLeqsdrARKLAEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLS 1799
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEEL-----AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1800 NEVDDAVQECRNAEEKAKKAI--------TDAAMMAEELKKEQD---TSAHLERMKKNMEQTIKDLQMRLDEA-EQIALK 1867
Cdd:COG1196 528 VLIGVEAAYEAALEAALAAALqnivveddEVAAAAIEYLKAAKAgraTFLPLDKIRARAALAAALARGAIGAAvDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1868 GGKKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKEL------------SYQGEEDKKNLVRLQDLIDKMQAK 1935
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLegeggsaggsltGGSRRELLAALLEAEAELEELAER 687
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2108526737 1936 VKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADMAESQANKLRARTRDQ 1988
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1433-1984 |
5.78e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 84.35 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1433 RTKYETDAIQRTEELE----EAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQT------EIEDLVIDLERANAAAAV 1502
Cdd:PRK03918 177 RIERLEKFIKRTENIEelikEKEKELEEVLREINEISSELPELREELEKLEKEVKEleelkeEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1503 LDKKQRNFDKVLAEWRQKYEECQSELETSqKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVK 1582
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1583 TIHELEKMKKgldmEKSEIQAALEEAEGTLEHEEsKSLRIQLELNQIKADVDRKLAEK-DEEIDSLRRNHQRILESMQAT 1661
Cdd:PRK03918 336 KEERLEELKK----KLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEISKI 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1662 LDAEAKSRNEAVRLRKKMEgDLNEMEVQLSHANRQASESQK--FLRNLQVQIKDIQLELDETIHQNEELKeqvavterrn 1739
Cdd:PRK03918 411 TARIGELKKEIKELKKAIE-ELKKAKGKCPVCGRELTEEHRkeLLEEYTAELKRIEKELKEIEEKERKLR---------- 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1740 nllaAEVEELRALLEQSDRARKLaeHELLEatervnllnsqntglinQKKKLESDLSMLS-NEVDDAVQECRNAEEKAKK 1818
Cdd:PRK03918 480 ----KELRELEKVLKKESELIKL--KELAE-----------------QLKELEEKLKKYNlEELEKKAEEYEKLKEKLIK 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1819 AITDAAMMAEELKKEQDtsahLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVLKLEARVKELE------NELESEQK 1892
Cdd:PRK03918 537 LKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEpfyneyLELKDAEK 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1893 KSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQakvKSYKRQTEEAEEQANTNLSK-YRKLQHELDDAEERA 1971
Cdd:PRK03918 613 ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE---KKYSEEEYEELREEYLELSReLAGLRAELEELEKRR 689
|
570
....*....|...
gi 2108526737 1972 DMAESQANKLRAR 1984
Cdd:PRK03918 690 EEIKKTLEKLKEE 702
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1033-1732 |
1.55e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 82.76 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1033 ENKVKNLIEEMaaldETILKLTKEKKALLEAHQQTLDDlqAEEDKVNILTKAKaKLEQQVDDLEGSLEQEKKLRMDLERV 1112
Cdd:TIGR04523 32 DTEEKQLEKKL----KTIKNELKNKEKELKNLDKNLNK--DEEKINNSNNKIK-ILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1113 RRKLEGDLKLSLESVMDLENDKQQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAK 1192
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1193 VEKQRSDVARELEELSERLEEaggaTSAQIEMNKKREADFLKLRRDleeamlhheattaalRKKHADSVAELSEQIDSLQ 1272
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLLSN----LKKKIQKNKSLESQISELKKQ---------------NNQLKDNIEKKQQEINEKT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1273 RVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGElsRKL 1352
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQE--KKL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1353 EEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALahalqssrhdcdllreqyDEEQEAKADLQRALSKANAEvaqw 1432
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK------------------QRELEEKQNEIEKLKKENQS---- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1433 rtkyetdAIQRTEELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDK 1512
Cdd:TIGR04523 382 -------YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1513 VLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKK 1592
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1593 GLDMEKSEIQaaleeaegtlehEESKSLRIQLELNQIKADVDrklaEKDEEIDSLRRNhQRILESMQATLDAEAKSR-NE 1671
Cdd:TIGR04523 535 EKESKISDLE------------DELNKDDFELKKENLEKEID----EKNKEIEELKQT-QKSLKKKQEEKQELIDQKeKE 597
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2108526737 1672 AVRLRKKMEgdlnEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQV 1732
Cdd:TIGR04523 598 KKDLIKEIE----EKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
85-129 |
1.60e-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: 1.60e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2108526737 85 DGKKRAWIPDEKEAYIEIEIKELSGDKVIVETKDGKTLTVKDCDI 129
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
901-1588 |
1.86e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 82.86 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 901 LRSATTEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNladAEDRCDLLIKTKIQLEAKV 980
Cdd:pfam15921 250 LKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTV 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 981 KEIMERLEDeeemsanvlaKKRKLEDECAELKKD--IDDLEITLAKVEKEKHATENkvKNLIEEMAALDETILKltKEKK 1058
Cdd:pfam15921 327 SQLRSELRE----------AKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQLQKLLADLHK--REKE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1059 ALLEAHQ-------------------QTLDDLQAEEDKVNILTKA-----KAKLEQQVDDLEG---SLEQEKKLRMDLER 1111
Cdd:pfam15921 393 LSLEKEQnkrlwdrdtgnsitidhlrRELDDRNMEVQRLEALLKAmksecQGQMERQMAAIQGkneSLEKVSSLTAQLES 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1112 VR---RKLEGDL---KLSLES----VMDLENDKQQLDEKLKKKDFEMNEMSTRIEdeqalvnqlqKKIKELQARTEELEE 1181
Cdd:pfam15921 473 TKemlRKVVEELtakKMTLESsertVSDLTASLQEKERAIEATNAEITKLRSRVD----------LKLQELQHLKNEGDH 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1182 ELEADRACRA----------KVEKQRSDVARELEELSERLEEAGG--ATSAQI--EMNKKR-EADFLKLRRDLEEAMLHH 1246
Cdd:pfam15921 543 LRNVQTECEAlklqmaekdkVIEILRQQIENMTQLVGQHGRTAGAmqVEKAQLekEINDRRlELQEFKILKDKKDAKIRE 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1247 -EATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKAD 1325
Cdd:pfam15921 623 lEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLK 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1326 ELQRQLNETNTQRARAQAESG-----------ELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHAL 1394
Cdd:pfam15921 703 SAQSELEQTRNTLKSMEGSDGhamkvamgmqkQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVA 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1395 QSSRH---DCDLLREQYDEEQEAKADLQRALSKANAEVAQWRtkyetDAIQRTEElEEAKKKLVTRL--QEAEETVETSN 1469
Cdd:pfam15921 783 TEKNKmagELEVLRSQERRLKEKVANMEVALDKASLQFAECQ-----DIIQRQEQ-ESVRLKLQHTLdvKELQGPGYTSN 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1470 A-------KCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEEcQSELETSQKESRGLSTEL 1542
Cdd:pfam15921 857 SsmkprllQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINE-EPTVQLSKAEDKGRAPSL 935
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1543 FKLKNSYEETLDHLE----TIKRENKNLQEEIADLSDQISQGVKTIHELE 1588
Cdd:pfam15921 936 GALDDRVRDCIIESSlrsdICHSSSNSLQTEGSKSSETCSREPVLLHAGE 985
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1259-1932 |
5.88e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 81.11 E-value: 5.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1259 DSVAELSEQIDSLQRVKQKLEKERSEAKM--EVDDLASTVEQLSKGKATSEKMCRLYEDQmnEAKAKADELQRQLNETNT 1336
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLW--FAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1337 QRARAQAESGELSRKLEEREAMVSQLQRAKNSFS-QNVEDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAK 1415
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1416 ADLQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQE-----------AEETVETSNAKCSSLEKTKHRL-- 1482
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiaslerrksniPARLLALRDALAEALGLDEAELpf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1483 --------------QTEIE--------DLVIDLERANAAAAVLDK---KQR-NFDKVlaewrqkyEECQSELETSQKESR 1536
Cdd:COG4913 463 vgelievrpeeerwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1537 GLSTELFKLKNSYEETLDHletikrenknlqeEIADLSDQISqgVKTIHELEKMKKGLdmekseIQAALEEAEGTL-EHE 1615
Cdd:COG4913 535 SLAGKLDFKPHPFRAWLEA-------------ELGRRFDYVC--VDSPEELRRHPRAI------TRAGQVKGNGTRhEKD 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1616 ESKSLRiqlELNQIKADVDRKLAEKDEEIDSLRRNH---QRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSH 1692
Cdd:COG4913 594 DRRRIR---SRYVLGFDNRAKLAALEAELAELEEELaeaEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1693 AN-----RQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRALLEQSDRARKLAEHEL 1767
Cdd:COG4913 671 AEleaelERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1768 LEAtERVNLLNSQNTGLInqKKKLESDLSMLSNEVDDAVQECRNAEEKAKK--------------AITDAAMMAEELkKE 1833
Cdd:COG4913 751 LEE-RFAAALGDAVEREL--RENLEERIDALRARLNRAEEELERAMRAFNRewpaetadldadleSLPEYLALLDRL-EE 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1834 QDTSAHLERMK----KNMEQTIKDLQMRLDEAEQIAlkggKKQVLKLEARVKELE-NE-----LESEQKKSQEyqkgVRK 1903
Cdd:COG4913 827 DGLPEYEERFKellnENSIEFVADLLSKLRRAIREI----KERIDPLNDSLKRIPfGPgrylrLEARPRPDPE----VRE 898
|
730 740 750
....*....|....*....|....*....|....
gi 2108526737 1904 YERRIKELS-----YQGEEDKKNLVRLQDLIDKM 1932
Cdd:COG4913 899 FRQELRAVTsgaslFDEELSEARFAALKRLIERL 932
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1306-1965 |
1.22e-14 |
|
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: 79.77 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1306 SEKMCRLYEDQMNEAKakadelqrqlnETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENK 1385
Cdd:pfam05483 73 SEGLSRLYSKLYKEAE-----------KIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1386 AKNALAHALQSSRHDCDLLRE--------------QYDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEELEEAK 1451
Cdd:pfam05483 142 ENKDLIKENNATRHLCNLLKEtcarsaektkkyeyEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1452 KKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELEts 1531
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELE-- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1532 qkesrglstelfKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISqgvKTIHELEKMKKGLDMEKSEIQAALEEAEGT 1611
Cdd:pfam05483 300 ------------DIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKE---AQMEELNKAKAAHSFVVTEFEATTCSLEEL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1612 LEHEESKSLRIQLELNQIKADVDRKLAEKdEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRKKMEgDLNEMEVQLS 1691
Cdd:pfam05483 365 LRTEQQRLEKNEDQLKIITMELQKKSSEL-EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAE-ELKGKEQELI 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1692 HAnRQASEsqKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELraLLEQsdraRKLAEhellEAT 1771
Cdd:pfam05483 443 FL-LQARE--KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL--LLEN----KELTQ----EAS 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1772 ERVNLLNSQNTGLINQKKKLESDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTI 1851
Cdd:pfam05483 510 DMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1852 KDLQMRLDEAeqialkggKKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKnlvRLQDLIDK 1931
Cdd:pfam05483 590 KILENKCNNL--------KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ---KFEEIIDN 658
|
650 660 670
....*....|....*....|....*....|....*..
gi 2108526737 1932 MQAKVKSYKRQTE---EAEEQANTNLSKYRKLQHELD 1965
Cdd:pfam05483 659 YQKEIEDKKISEEkllEEVEKAKAIADEAVKLQKEID 695
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1669-1992 |
1.52e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1669 RNEAVRLRKKMEGDLN-------EMEVQLSHANRQASESQKF------------------LRNLQVQIKDIQLELDETIH 1723
Cdd:COG1196 174 KEEAERKLEATEENLErledilgELERQLEPLERQAEKAERYrelkeelkeleaellllkLRELEAELEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1724 QNEELKEQVAVTERRNNLLAAEVEELRALLEQSDRARKLAEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLSNEVD 1803
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1804 DAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKgGKKQVLKLEARVKEL 1883
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE-LAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1884 ENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEAEEQANTNLSKYRKLQHE 1963
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
330 340
....*....|....*....|....*....
gi 2108526737 1964 LDDAEERADMAESQANKLRARTRDQGSKL 1992
Cdd:COG1196 493 LLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
909-1766 |
2.32e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 79.25 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 909 ELVSLKEELAKLKEALEKseVKRKELEERQVSLIQEKNDLSLQLQAEQdnladAEDRCDLLIKTKIQLEAKVKEIMERLE 988
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKK--LIEETENLAELIIDLEELKLQELKLKEQ-----AKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 989 DEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALLE-AHQQT 1067
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLErRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1068 LDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVR---RKLEGDLKLSLESVMDLENDKQQLDEKLKKK 1144
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEeelEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1145 DFEMNEMSTRIEDEQALVNQLQKKIKELQARTEELEEeleadracrAKVEKQRSDVARELEELSERLEEAGGATSAQIEM 1224
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL---------EILEEEEESIELKQGKLTEEKEELEKQELKLLKD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1225 NKKREADFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKA 1304
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKV 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1305 TSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEEN 1384
Cdd:pfam02463 544 AISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1385 KAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTK-YETDAIQRTEELEEAKKKLVTRLQEAEE 1463
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKElLEIQELQEKAESELAKEEILRRQLEIKK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1464 tvETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQ-SELETSQKESRGLSTEL 1542
Cdd:pfam02463 704 --KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEeEKSELSLKEKELAEERE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1543 FKLKNSYEETLDHLEtiKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDmEKSEIQAALEEAEGTLEHEESKSLRI 1622
Cdd:pfam02463 782 KTEKLKVEEEKEEKL--KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKE-EELEELALELKEEQKLEKLAEEELER 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1623 QLELNQIKADVDRKLAEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQK 1702
Cdd:pfam02463 859 LEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE 938
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108526737 1703 FLRNLQ-VQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEEL--RALLEQSDRARKLAEHE 1766
Cdd:pfam02463 939 ELLLEEaDEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKeeRYNKDELEKERLEEEKK 1005
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1221-1778 |
4.56e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.42 E-value: 4.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1221 QIEMNKKREADFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSE----QIDSLQRVKQKLEKERSEAKMEVDDLASTV 1296
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1297 EQLSKGKATSEKMcrlYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDL 1376
Cdd:COG4913 369 AALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1377 KKqleeenkaknALAHALQSSRHD----CDLL--REQYDEEQEA---------------KADLQRALSKANAEvaQWRTK 1435
Cdd:COG4913 446 RD----------ALAEALGLDEAElpfvGELIevRPEEERWRGAiervlggfaltllvpPEHYAAALRWVNRL--HLRGR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1436 YETDAIQRTEELEEAKK--------KLVTRLQEAEETVETSNA------KCSSLE------------------KTKHRLQ 1483
Cdd:COG4913 514 LVYERVRTGLPDPERPRldpdslagKLDFKPHPFRAWLEAELGrrfdyvCVDSPEelrrhpraitragqvkgnGTRHEKD 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1484 TEI---EDLVIDlERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLStelfKLKNSYEETLDHLEtik 1560
Cdd:COG4913 594 DRRrirSRYVLG-FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ----RLAEYSWDEIDVAS--- 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1561 renknLQEEIADLSDQISQGVKTIHELEKMKKGLDmeksEIQAALEEAEGTLEheeskslriqlELNQIKADVDRKLAEK 1640
Cdd:COG4913 666 -----AEREIAELEAELERLDASSDDLAALEEQLE----ELEAELEELEEELD-----------ELKGEIGRLEKELEQA 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1641 DEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIK----DIQL 1716
Cdd:COG4913 726 EEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNrewpAETA 805
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108526737 1717 ELDETIHQNEELKEQVAVTErRNNLLAAEVEELRALLEQSDR-----ARKLAEhELLEATERVNLLN 1778
Cdd:COG4913 806 DLDADLESLPEYLALLDRLE-EDGLPEYEERFKELLNENSIEfvadlLSKLRR-AIREIKERIDPLN 870
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1060-1686 |
1.13e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.62 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1060 LLEAHQQTLDDLQAE---------EDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGdlklSLESVMDL 1130
Cdd:PRK02224 181 VLSDQRGSLDQLKAQieekeekdlHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEE----RREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1131 ENDKQQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQARTEEleeeleaDRACRAKVEKQRSDVareleelser 1210
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGL-------DDADAEAVEARREEL---------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1211 leeaggatsaqiemnkkrEADFLKLRRDLEEAMLHHEATTAALrKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVD 1290
Cdd:PRK02224 320 ------------------EDRDEELRDRLEECRVAAQAHNEEA-ESLREDADDLEERAEELREEAAELESELEEAREAVE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1291 DLASTVEQLskgkatsekmcrlyEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAmvsQLQRAKNSFS 1370
Cdd:PRK02224 381 DRREEIEEL--------------EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA---TLRTARERVE 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1371 QNvedlkKQLEEENKAKNAlAHALQSSRHDCDLlreqyDEEQEAKADLQRALSKANAEVAQWRTKYET-----DAIQRTE 1445
Cdd:PRK02224 444 EA-----EALLEAGKCPEC-GQPVEGSPHVETI-----EEDRERVEELEAELEDLEEEVEEVEERLERaedlvEAEDRIE 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1446 ELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDlvidlERANAAAAvldkkqrnfdkvlaewRQKYEECQ 1525
Cdd:PRK02224 513 RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEE-----KREAAAEA----------------EEEAEEAR 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1526 SELETSQKESRGLSTELFKLkNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDME-------- 1597
Cdd:PRK02224 572 EEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEfdeariee 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1598 ----KSEIQAALEEAEGTLEHEESKSLRIQLELNQIKADVDRkLAEKDEEIDSLRRNHQRI---------LESMQATLDA 1664
Cdd:PRK02224 651 aredKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE-LEELRERREALENRVEALealydeaeeLESMYGDLRA 729
|
650 660
....*....|....*....|..
gi 2108526737 1665 EAKSRNEAvrlrkKMEGDLNEM 1686
Cdd:PRK02224 730 ELRQRNVE-----TLERMLNET 746
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1550-1910 |
2.14e-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: 76.26 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1550 EETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKkgldmeksEIQAALEEAEGTLEHEESKSLRIQLE--LN 1627
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ--------ALLKEKREYEGYELLKEKEALERQKEaiER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1628 QIkADVDRKLAEKDEEIDSLRRNHQRILESM-QATLDAEAKSRNEAVRLRKKMEgdlnEMEVQLSHANRQASESQKFLRN 1706
Cdd:TIGR02169 245 QL-ASLEEELEKLTEEISELEKRLEEIEQLLeELNKKIKDLGEEEQLRVKEKIG----ELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1707 LQVQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEE-------LRALLEQSDRARKLAEHELLEATERVNLLNS 1779
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAElkeeledLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1780 QNTGLINQKKKLESDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLD 1859
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2108526737 1860 eaeqialkggkkqvlKLEARVKELENEL---ESEQKKSQEYQKGVRKYERRIKE 1910
Cdd:TIGR02169 480 ---------------RVEKELSKLQRELaeaEAQARASEERVRGGRAVEEVLKA 518
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1361-1965 |
5.19e-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: 74.77 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1361 QLQRAKNSFSQNVEDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVaqwrtkyeTDA 1440
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL--------RNQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1441 IQRTEELEEAKKKLvtrlqeAEETVETSNAKCSSLEK---TKHRLQTEIEDLVIDLERANAaaavldKKQRNFDKVlaew 1517
Cdd:pfam15921 147 LQNTVHELEAAKCL------KEDMLEDSNTQIEQLRKmmlSHEGVLQEIRSILVDFEEASG------KKIYEHDSM---- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1518 rqKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKN-----LQEEIADLSDQISQGVKTIHELEKMKK 1592
Cdd:pfam15921 211 --STMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNkiellLQQHQDRIEQLISEHEVEITGLTEKAS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1593 GLDMEKSEIQAALEEAEGTLEHEESKSLR----IQLELNQIKADV---------------------DRKLAEKDEEIDSL 1647
Cdd:pfam15921 289 SARSQANSIQSQLEIIQEQARNQNSMYMRqlsdLESTVSQLRSELreakrmyedkieelekqlvlaNSELTEARTERDQF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1648 RRNHQRILESMQATLdAEAKSRNEAVRLRKKMEGDLNEME----VQLSHANRQASESQKFLRNLQVQIKDIQLELDETIH 1723
Cdd:pfam15921 369 SQESGNLDDQLQKLL-ADLHKREKELSLEKEQNKRLWDRDtgnsITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQME 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1724 Q--------NEELKEQVAVT---ERRNNLLAAEVEELRA---LLEQSDRARKLAEHELLEATERVNLLNSQNTGLINQKK 1789
Cdd:pfam15921 448 RqmaaiqgkNESLEKVSSLTaqlESTKEMLRKVVEELTAkkmTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVD 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1790 KLESDLSMLSNEvDDAVQECRNAEEKAKKAITDAAMMAEELKKEQD-----------TSAHLERMKKNMEQTIKDLQMRL 1858
Cdd:pfam15921 528 LKLQELQHLKNE-GDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgqhgrTAGAMQVEKAQLEKEINDRRLEL 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1859 DEAEQIALKGGKKqVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSyqgEEDKKNLVRLQDLIDKMQAKVKS 1938
Cdd:pfam15921 607 QEFKILKDKKDAK-IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLL---NEVKTSRNELNSLSEDYEVLKRN 682
|
650 660
....*....|....*....|....*..
gi 2108526737 1939 YKRQTEEAEEQANTNLSKYRKLQHELD 1965
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLKSAQSELE 709
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1313-1981 |
6.80e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 73.90 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1313 YEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAH 1392
Cdd:TIGR04523 24 YKNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1393 ALQSSRHDCDLLREQYDEEQEAKADLQRALSKANaevaqwrtKYETDAIQRTEELEEAKKKLVTRLQEAEETVETSNAKC 1472
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENK--------KNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1473 SSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWrQKYEECQSELETSQKEsrgLSTELFKLKNSYEET 1552
Cdd:TIGR04523 176 NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQI-SELKKQNNQLKDNIEK---KQQEINEKTTEISNT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1553 LDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKmkkgldmEKSEIQAALEEAEGTLEHEESKSLRIQLELNQikad 1632
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK-------QLNQLKSEISDLNNQKEQDWNKELKSELKNQE---- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1633 vdrklaEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIK 1712
Cdd:TIGR04523 321 ------KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1713 DIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRALLEQSdrarklaEHELLEATERVNLLNSQNTGLINQKKKLE 1792
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN-------NSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1793 SDLSMLSNEVDDAVQECrnaeEKAKKAITDAAMMAEELKKEqdtsahlermKKNMEQTIKDLQMRLDEAEQiALKGGKKQ 1872
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNL----EQKQKELKSKEKELKKLNEE----------KKELEEKVKDLTKKISSLKE-KIEKLESE 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1873 VLKLEARVKELENELES--EQKKSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEAEEQA 1950
Cdd:TIGR04523 533 KKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612
|
650 660 670
....*....|....*....|....*....|.
gi 2108526737 1951 NTnlskyrkLQHELDDAEERADMAESQANKL 1981
Cdd:TIGR04523 613 SS-------LEKELEKAKKENEKLSSIIKNI 636
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
907-1599 |
7.04e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 73.90 E-value: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 907 EKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIK--TKIQLEAKV-KEI 983
Cdd:TIGR04523 39 EKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSdlSKINSEIKNdKEQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 984 MERLEDE----EEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKA 1059
Cdd:TIGR04523 119 KNKLEVElnklEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1060 LleahQQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESvmdLENDKQQLDE 1139
Cdd:TIGR04523 199 L----ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE---QNKIKKQLSE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1140 KLKkkdfEMNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRAcrAKVEKQRSDvareleelserleeaggaTS 1219
Cdd:TIGR04523 272 KQK----ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSEL--KNQEKKLEE------------------IQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1220 AQIEMNKKR----EADFLKLRRDLEEAMLHHEATTAALRKKHaDSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLAST 1295
Cdd:TIGR04523 328 NQISQNNKIisqlNEQISQLKKELTNSESENSEKQRELEEKQ-NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1296 VEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVED 1375
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1376 LKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDaiqrteELEEAKKKLV 1455
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD------DFELKKENLE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1456 TRLQEAEETVETSNAKCSSLEKTkhrlQTEIEDLVIDLEranaaaavldKKQRNFDKVLAEWRQKYEECQSELETSQKES 1535
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKK----QEEKQELIDQKE----------KEKKDLIKEIEEKEKKISSLEKELEKAKKEN 626
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108526737 1536 RGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKS 1599
Cdd:TIGR04523 627 EKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELS 690
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
981-1586 |
8.79e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.18 E-value: 8.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 981 KEIMERLEDEEEmSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATenKVKNLIEEMAALDETILKLTKEKKAL 1060
Cdd:COG4913 238 ERAHEALEDARE-QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1061 ---LEAHQQTLDDLQAEEDKVNilTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLEsvmDLENDKQQL 1137
Cdd:COG4913 315 earLDALREELDELEAQIRGNG--GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE---EFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1138 DEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQARteeleeeleadracRAKVEKQRSDVARELEELSERLEEAGGA 1217
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAE--------------IASLERRKSNIPARLLALRDALAEALGL 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1218 TSAQ-------IEMnKKREADFlklrRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVK-QKLEKERSEAKMEV 1289
Cdd:COG4913 456 DEAElpfvgelIEV-RPEEERW----RGAIERVLGGFALTLLVPPEHYAAALRWVNRLHLRGRLVyERVRTGLPDPERPR 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1290 DDLASTVEQLS-KGKATSEKMCRLYEDQMNEAK-AKADELQRQ--------LNETNTQRARAQAESGELSR--------- 1350
Cdd:COG4913 531 LDPDSLAGKLDfKPHPFRAWLEAELGRRFDYVCvDSPEELRRHpraitragQVKGNGTRHEKDDRRRIRSRyvlgfdnra 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1351 KLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHALQSSRHDCDLlrEQYDEEQEAKADLQRALSKANAEVa 1430
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV--ASAEREIAELEAELERLDASSDDL- 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1431 qwrtkyetdaiqrtEELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAA---------- 1500
Cdd:COG4913 688 --------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelrallee 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1501 --------AVLDKKQRNFDKVLAEWRQKYEECQSELETSQKE--------SRGLSTELfklkNSYEETLDHLETIKRE-- 1562
Cdd:COG4913 754 rfaaalgdAVERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaeTADLDADL----ESLPEYLALLDRLEEDgl 829
|
650 660 670
....*....|....*....|....*....|....*
gi 2108526737 1563 -----------NKNLQEEIADLSDQISQGVKTIHE 1586
Cdd:COG4913 830 peyeerfkellNENSIEFVADLLSKLRRAIREIKE 864
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
905-1919 |
1.06e-12 |
|
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: 73.93 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 905 TTEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKnDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEIM 984
Cdd:TIGR00606 197 TQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 985 ERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLEitlakvEKEKHATENKVKNLIEEMAALDETILKLTKEKKALLeaH 1064
Cdd:TIGR00606 276 SRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNH------QRTVREKERELVDCQRELEKLNKERRLLNQEKTELL--V 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1065 QQTLDDLQAEEDKVNILTKAKAKLEQQ----VDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQLDEK 1140
Cdd:TIGR00606 348 EQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1141 LKKKDFEMNEMSTRIEDEQAL----VNQLQKKIKELQARTEELEEELEADRACRaKVEKQRSDVARELEELSERleeagg 1216
Cdd:TIGR00606 428 ADEIRDEKKGLGRTIELKKEIlekkQEELKFVIKELQQLEGSSDRILELDQELR-KAERELSKAEKNSLTETLK------ 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1217 atsAQIEMNKKREADFLKLRRDLEEAM--LHHEATTaalrKKHADSVAElsEQIDSLQRVKQKLEKERSEAKMEVDDLAS 1294
Cdd:TIGR00606 501 ---KEVKSLQNEKADLDRKLRKLDQEMeqLNHHTTT----RTQMEMLTK--DKMDKDEQIRKIKSRHSDELTSLLGYFPN 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1295 TvEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLeeREAMVSQlqraknSFSQNVE 1374
Cdd:TIGR00606 572 K-KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL--FDVCGSQ------DEESDLE 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1375 DLKKQLEEENKAKNALAHAlqSSRHDcDLLREQYDEEQEAKADLQRALskanaevaqwrtkyetdaiQRTEELEEAKKKL 1454
Cdd:TIGR00606 643 RLKEEIEKSSKQRAMLAGA--TAVYS-QFITQLTDENQSCCPVCQRVF-------------------QTEAELQEFISDL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1455 VTRLQEAEETVETSNAKCSSLEKTKHRLqteiedlvidLERANAAAAVLDKKQRnfdkvlaewrqkyeecqsELETSQKE 1534
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEM----------LGLAPGRQSIIDLKEK------------------EIPELRNK 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1535 SRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADlsdqisqgVKTIHELEKMKKGLDMEKSEIQAALEEAEGTLEH 1614
Cdd:TIGR00606 753 LQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTD--------VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTV 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1615 EEskslriqleLNQIKADVD---RKLAEKDEEIDSLRRNHQRILESMQATLD---AEAKSRNEAVRLRKKMEGDLNEMEV 1688
Cdd:TIGR00606 825 QQ---------VNQEKQEKQhelDTVVSKIELNRKLIQDQQEQIQHLKSKTNelkSEKLQIGTNLQRRQQFEEQLVELST 895
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1689 QLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEElkeqvavterRNNLLAAEVEELRALLEQSDRARKLAEHELL 1768
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKET----------SNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1769 EATERvnllnsqntglinQKKKLESDLsmlsNEVDDAVQECRNAEEKAKKAIT------DAAMMAEELKKEQDTSAHLER 1842
Cdd:TIGR00606 966 DGKDD-------------YLKQKETEL----NTVNAQLEECEKHQEKINEDMRlmrqdiDTQKIQERWLQDNLTLRKREN 1028
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108526737 1843 MKKNMEQTIKDLqmrLDEAEQIALKGGKKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDK 1919
Cdd:TIGR00606 1029 ELKEVEEELKQH---LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
960-1595 |
1.27e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.17 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 960 ADAEDRCDLLIKTKIQLEAKVKEIMERLEDEEEMSANVLAKKRKLEdecaELKKDIDDLEITLAKVEKEKHATENKVKNL 1039
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1040 IEEMAALDETILKLTKEKKALLEAHQQTLDDLQAEEDKVNILtKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLE-- 1117
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYL-DELREIEKRLSRLEEEINGIEERIKELEEKEERLEel 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1118 -GDLKLSLESVMDLENDKQQLDEKLKKKDfEMNEMSTRIEDEQalVNQLQKKIKELQARTEELEEELEADRACRAKVEKQ 1196
Cdd:PRK03918 344 kKKLKELEKRLEELEERHELYEEAKAKKE-ELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1197 RSDVareleelserleeaggatSAQIEMNKKREADFLKLRRDLEEamlHHEAT-----TAALrKKHADSVAELSEQIDSL 1271
Cdd:PRK03918 421 IKEL------------------KKAIEELKKAKGKCPVCGRELTE---EHRKElleeyTAEL-KRIEKELKEIEEKERKL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1272 QRVKQKLEKERSEAKmEVDDLASTVEQLskgkatsekmcrlyedqmneakakaDELQRQLNETNTQraraqaesgELSRK 1351
Cdd:PRK03918 479 RKELRELEKVLKKES-ELIKLKELAEQL-------------------------KELEEKLKKYNLE---------ELEKK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1352 LEEREamvsQLQRAKNSFSQNVEDLKKQLEEENKAKNALAhalqssrhdcdLLREQYDEEQEAKADLQRALSKANAEVaq 1431
Cdd:PRK03918 524 AEEYE----KLKEKLIKLKGEIKSLKKELEKLEELKKKLA-----------ELEKKLDELEEELAELLKELEELGFES-- 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1432 wrtkyETDAIQRTEELEEAKKKLVtRLQEAEETVEtsnakcsSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKqrnfd 1511
Cdd:PRK03918 587 -----VEELEERLKELEPFYNEYL-ELKDAEKELE-------REEKELKKLEEELDKAFEELAETEKRLEELRKE----- 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1512 kvLAEWRQKYEEcqSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSdqisqgvKTIHELEKMK 1591
Cdd:PRK03918 649 --LEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE-------KAKKELEKLE 717
|
....
gi 2108526737 1592 KGLD 1595
Cdd:PRK03918 718 KALE 721
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
902-1387 |
1.29e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.17 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 902 RSATTEKELVSLKEELAKLKEaLEKSEVKRKELEERQVSLIQEKNDLSL-------QLQAEQDNLADAEDRCDLLIKTKI 974
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKrlsrleeEINGIEERIKELEEKEERLEELKK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 975 QLEaKVKEIMERLEDEEEMSANVLAKKRKLEDECAELK-KDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKL 1053
Cdd:PRK03918 346 KLK-ELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1054 TKEKKALLEAHQQ--TLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSleSVMDLE 1131
Cdd:PRK03918 425 KKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI--KLKELA 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1132 NDKQQLDEKLKKKDFE-MNEMSTRIEDEQALVNQLQKKIKELQARTEeleeeleadracrakvekqrsdvareleelser 1210
Cdd:PRK03918 503 EQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELE--------------------------------- 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1211 leeaggatsaQIEMNKKREADFLKLRRDLEE--AMLHHEattaaLRKKHADSVAELSEQIDSLqrvkQKLEKERSEAKME 1288
Cdd:PRK03918 550 ----------KLEELKKKLAELEKKLDELEEelAELLKE-----LEELGFESVEELEERLKEL----EPFYNEYLELKDA 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1289 VDDLASTVEQLSKGKATSEKMcrlyEDQMNEAKAKADELQRQLNETNT-----QRARAQAESGELSRKLEEREAMVSQLQ 1363
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKA----FEELAETEKRLEELRKELEELEKkyseeEYEELREEYLELSRELAGLRAELEELE 686
|
490 500
....*....|....*....|....
gi 2108526737 1364 RAKNSFSQNVEDLKKQLEEENKAK 1387
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAK 710
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1445-1964 |
1.30e-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: 73.13 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1445 EELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDK---VLAEWRQKY 1521
Cdd:TIGR04523 134 KENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELllsNLKKKIQKN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1522 EECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEI 1601
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1602 QAALEEAEGTLEHEESKSLRIQLELNQikadvdrklaEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRKKMEG 1681
Cdd:TIGR04523 294 KSEISDLNNQKEQDWNKELKSELKNQE----------KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1682 DLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRALLEQSDRARK 1761
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1762 LAEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLSNEVDDAVQECRNAE---EKAKKAITDAAMMAEELKKEQDTSA 1838
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEkelKKLNEEKKELEEKVKDLTKKISSLK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1839 H----LERMKKNMEQTIKDLQMRLDEAEQIALKGG-KKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELsy 1913
Cdd:TIGR04523 524 EkiekLESEKKEKESKISDLEDELNKDDFELKKENlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL-- 601
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2108526737 1914 qgeedKKNLVRLQDLIDKMQAKVKSYKRQTEEAEEQANTNLSKYRKLQHEL 1964
Cdd:TIGR04523 602 -----IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
902-1176 |
1.41e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 902 RSATTEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVK 981
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 982 EIMERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALL 1061
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1062 EAHQQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSL-EQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQLD-- 1138
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpv 987
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2108526737 1139 -----EKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQART 1176
Cdd:TIGR02168 988 nlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
892-1641 |
1.82e-12 |
|
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: 73.16 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 892 KLFFKIKPLLRSATTEKELVSLKEELAKLKEALEKSEVKR--KELEERQVSLIQEKNDLSLQLQAEQDNLADAE------ 963
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhhtttr 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 964 DRCDLLIKTKIQLEAKVKEIMERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKE-------KHATENKV 1036
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKElasleqnKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1037 KNLIEEMAALDETILKLTKEkkallEAHQQTLDDLQAEEDKVN----ILTKAKAKLEQQVDDLEGS-------LEQEKKL 1105
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCGS-----QDEESDLERLKEEIEKSSkqraMLAGATAVYSQFITQLTDEnqsccpvCQRVFQT 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1106 RMDLERVRRKLEGDLKLSlesvmdlENDKQQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQARteeleeelea 1185
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLA-------PDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNK---------- 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1186 DRACRAKVEKQRSDVARELEELserleeagGATSAQIEMNKKREADFLKLRRDLEEamlhheatTAALRKKHADSVAELs 1265
Cdd:TIGR00606 753 LQKVNRDIQRLKNDIEEQETLL--------GTIMPEEESAKVCLTDVTIMERFQME--------LKDVERKIAQQAAKL- 815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1266 eQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLskgkatsEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAES 1345
Cdd:TIGR00606 816 -QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELN-------RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFE 887
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1346 GELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKA 1425
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDG 967
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1426 NAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQteIEDLVIDLERANAAAavldK 1505
Cdd:TIGR00606 968 KDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRK--RENELKEVEEELKQH----L 1041
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1506 KQRNFDKVLaEWRQKYEECQSELETSQKESRGLSTELfklkNSYEETLDHLETIKREN--KNLQEEIADLSDQISQGVKT 1583
Cdd:TIGR00606 1042 KEMGQMQVL-QMKQEHQKLEENIDLIKRNHVLALGRQ----KGYEKEIKHFKKELREPqfRDAEEKYREMMIVMRTTELV 1116
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1584 IHELEKMKKGLDMEKSEIQA-ALEEAEGTLEHEESKSLRIQ-LELNQIKADVDRKLAEKD 1641
Cdd:TIGR00606 1117 NKDLDIYYKTLDQAIMKFHSmKMEEINKIIRDLWRSTYRGQdIEYIEIRSDADENVSASD 1176
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1216-1910 |
3.39e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 72.06 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1216 GATSAQIEMNKKREADFLKLRRDLEEAMLHHEATTAALRKKHaDSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLAST 1295
Cdd:pfam05483 64 GLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKE-NKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1296 VEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNT----------------QRARAQAESGELSRKLEEREAMv 1359
Cdd:pfam05483 143 NKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQvymdlnnniekmilafEELRVQAENARLEMHFKLKEDH- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1360 SQLQRAKNSFSQNVEDLKKQL--------EEENKAKNaLAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQ 1431
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVsllliqitEKENKMKD-LTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1432 WRTKYETD-AIQRT--EELEEAKKKLVTRLQEAEETVETSNAKcssleKTKHRLQ-TEIEDLVIDLERA-NAAAAVLDKK 1506
Cdd:pfam05483 301 IKMSLQRSmSTQKAleEDLQIATKTICQLTEEKEAQMEELNKA-----KAAHSFVvTEFEATTCSLEELlRTEQQRLEKN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1507 QRNFDKVLAEWRQKyeecQSELETSQKESRGLSTELFKLKN---SYEETLDHLETIKRENKNLQEEIADLSDQISQGVKT 1583
Cdd:pfam05483 376 EDQLKIITMELQKK----SSELEEMTKFKNNKEVELEELKKilaEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKE 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1584 IHELEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRI----------QLELNQIKADVDRKLAEKDEEIDSLRRNHQR 1653
Cdd:pfam05483 452 IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELtahcdkllleNKELTQEASDMTLELKKHQEDIINCKKQEER 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1654 ILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHanrqaSESQKFLRNLQVQIKDIQLELDETIHQNeeLKEQVa 1733
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK-----SEENARSIEYEVLKKEKQMKILENKCNN--LKKQI- 603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1734 vtERRNNLLAAEVEELRALLEQSDrarklAEHELLEATE-RVNLLNSQntgLINQKKKLESDLSMLSNEVDD---AVQEC 1809
Cdd:pfam05483 604 --ENKNKNIEELHQENKALKKKGS-----AENKQLNAYEiKVNKLELE---LASAKQKFEEIIDNYQKEIEDkkiSEEKL 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1810 RNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVLK--LEARVKELEN 1885
Cdd:pfam05483 674 LEEVEKAKAIADEAVKLQKEIDKrcQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKaaLEIELSNIKA 753
|
730 740
....*....|....*....|....*
gi 2108526737 1886 ELESEQKKSQEYQKGVRKYERRIKE 1910
Cdd:pfam05483 754 ELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1528-1994 |
3.47e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1528 LETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEE 1607
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1608 AEGtLEHEESKSLRIQLELNQIKADVDRKLAEKDEEIDSLRRNHQRILEsmqatLDAEAKSRNEAVRLRKKMEGDLNEME 1687
Cdd:PRK03918 240 IEE-LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-----LKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1688 VQLSHANRQASESQKFLRNLQ---VQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAA-----------EVEELRALL 1753
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlkkrltglTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1754 EQSDRARKLAEHELLEATERVNLLNSQNTGL---INQKKKLESDLSMLSNEVDD------------AVQECRNAEEKAKK 1818
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELkkaIEELKKAKGKCPVCGRELTEehrkelleeytaELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1819 AITDAAMMAEELKKEQDTSAHLERMKKNMEQtIKDLQMRLDEAEQIALKGGKKQVLKLEARVKELENE---LESEQKKSQ 1895
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEiksLKKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1896 EYQKGVRKYERRIKELsyqgEEDKKNLVR---------LQDLIDKMQAKVKSYKRQTE--EAEEQANTNLSKYRKLQHEL 1964
Cdd:PRK03918 553 ELKKKLAELEKKLDEL----EEELAELLKeleelgfesVEELEERLKELEPFYNEYLElkDAEKELEREEKELKKLEEEL 628
|
490 500 510
....*....|....*....|....*....|
gi 2108526737 1965 DDAEERADMAESQANKLRARTRDQGSKLAE 1994
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKKYSE 658
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
907-1644 |
3.91e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 71.93 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 907 EKELVSLKEELAKLKEALEKSEVKRKELEERQ-VSLIQEKN-------DLSLQLQAEQDNLADAEDRCDLLIKTKIQLEA 978
Cdd:pfam02463 277 EEKEKKLQEEELKLLAKEEEELKSELLKLERRkVDDEEKLKesekekkKAEKELKKEKEEIEELEKELKELEIKREAEEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 979 KVKEIMERLEDEEEMSANVLAKKRKLEDEcaELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKK 1058
Cdd:pfam02463 357 EEEELEKLQEKLEQLEEELLAKKKLESER--LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1059 ALLEahqQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQLD 1138
Cdd:pfam02463 435 EEES---IELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1139 EKLKKKDFEMNEMSTRIEDEQALVNQLQKkiKELQARTEELEEELEADRACRAKVEKQRSDVARELEELSERLEEAGGAT 1218
Cdd:pfam02463 512 LLALIKDGVGGRIISAHGRLGDLGVAVEN--YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKL 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1219 SAQIEMNKKREADFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAK--MEVDDLASTV 1296
Cdd:pfam02463 590 PLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGlaEKSEVKASLS 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1297 EQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDL 1376
Cdd:pfam02463 670 ELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEE 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1377 KKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKlvt 1456
Cdd:pfam02463 750 EEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQ--- 826
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1457 rLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAaaavlDKKQRNFDKVLAEWRQKYEECQSELETSQKESR 1536
Cdd:pfam02463 827 -EEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEE-----LLQELLLKEEELEEQKLKDELESKEEKEKEEKK 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1537 GLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEGTLEHEE 1616
Cdd:pfam02463 901 ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAI 980
|
730 740
....*....|....*....|....*...
gi 2108526737 1617 SKSLRIQLELNQIKADVDRKLAEKDEEI 1644
Cdd:pfam02463 981 EEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1031-1429 |
5.31e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 5.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1031 ATENKVKNLIEEMAALDETILKLTKEKKALLEAhqqtLDDLQAEEDKVNiltKAKAKLEQQVDDLEGSLEQEKKLRMDLE 1110
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKE----LEELEEELEQLR---KELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1111 RVRRKLEGDLKLSLESVMDLENDKQQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACR 1190
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1191 AKVEKQRSDVARELEELserleeaggatSAQIEMNKKREADFLKLRRDLEEAMlhheattaalrkkhadsvAELSEQIDS 1270
Cdd:TIGR02168 827 ESLERRIAATERRLEDL-----------EEQIEELSEDIESLAAEIEELEELI------------------EELESELEA 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1271 LQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQ-RARAQAESGELS 1349
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAE 957
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1350 RKLEEREAMVSQLQRaknsfsqNVEDLKKQLE----------EENKAknalahalQSSRHdcDLLREQYDEEQEAKADLQ 1419
Cdd:TIGR02168 958 ALENKIEDDEEEARR-------RLKRLENKIKelgpvnlaaiEEYEE--------LKERY--DFLTAQKEDLTEAKETLE 1020
|
410
....*....|
gi 2108526737 1420 RALSKANAEV 1429
Cdd:TIGR02168 1021 EAIEEIDREA 1030
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
900-1638 |
1.10e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 70.38 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 900 LLRSATTEKELVSLKEELAKLKEALEKSEVKRKELEerqvsliQEKNDLSLQLQAEQDnlaDAEDRCDLLIKTKIQLEAK 979
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLH-------GKAELLTLRSQLLTL---CTPCMPDTYHERKQVLEKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 980 VKEIMERLEDEEEMSANV------LAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATE--NKVKNLIEEMAALDE--- 1048
Cdd:TIGR00618 228 LKHLREALQQTQQSHAYLtqkreaQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINraRKAAPLAAHIKAVTQieq 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1049 ---TILKLTKEKKALLEAHQQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSle 1125
Cdd:TIGR00618 308 qaqRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQ-- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1126 svMDLENDKQQLDEKLKKKDFEMNEMST---RIEDEQALVNQL--QKKIKELQARTEELEEELEADRACRAKVEKQRSDV 1200
Cdd:TIGR00618 386 --QQKTTLTQKLQSLCKELDILQREQATidtRTSAFRDLQGQLahAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1201 ARELEELSERLEEAGGATSAQIEMNKKREADFL----KLRRDLEEAMLHHEATTAALRKKHADSvAELSEQIDSLQRVKQ 1276
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLlelqEEPCPLCGSCIHPNPARQDIDNPGPLT-RRMQRGEQTYAQLET 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1277 KLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRlyedQMNEAKAKADELQrqlNETNTQRARAQAESGELSRKLEERE 1356
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQ----CDNRSKEDIPNLQ---NITVRLQDLTEKLSEAEDMLACEQH 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1357 AMVSQLQRAKNSFSQNVEDLKKQlEEENKAKNALAHalqssrhdcdLLREQYDEEQEAKADLQRALSKANAEVAQWRTKY 1436
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRLHLQQCS-QELALKLTALHA----------LQLTLTQERVREHALSIRVLPKELLASRQLALQK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1437 ETDAIQRTEELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEdlvidlERANAAAAVLDKKQRNFDKVLAE 1516
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLA------AREDALNQSLKELMHQARTVLKA 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1517 WR-----------------QKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKR-ENKNLQEEIADLSDQIS 1578
Cdd:TIGR00618 759 RTeahfnnneevtaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRLE 838
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1579 QGVKTIHELeKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLELNQIKADVDRKLA 1638
Cdd:TIGR00618 839 EKSATLGEI-THQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFL 897
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1374-1964 |
1.15e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.07 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1374 EDLKKQLEE-ENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRtkyetdaiQRTEELEEAKK 1452
Cdd:PRK02224 190 DQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR--------EELETLEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1453 KLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQ 1532
Cdd:PRK02224 262 DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1533 KESRGLStelfklknsyeETLDHLETikrENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEGTL 1612
Cdd:PRK02224 342 EEAESLR-----------EDADDLEE---RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1613 EHEESKSLRIQLELNQIKADVDRKLAEKDEEIDSLRRNhQRILES------MQATLDAEAKSRNEAVRLRK-KMEGDLNE 1685
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEA-EALLEAgkcpecGQPVEGSPHVETIEEDRERVeELEAELED 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1686 MEVQLSHAN------RQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRallEQSDRA 1759
Cdd:PRK02224 487 LEEEVEEVEerleraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKR---EAAAEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1760 RKLAEhellEATERVNLLNSQNTGLINQKKKLEsDLSMLSNEVDDAVQECRNAEEKAKkaitDAAMMAEELKkeqdtsah 1839
Cdd:PRK02224 564 EEEAE----EAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKRE----ALAELNDERR-------- 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1840 lERMKKNMEQtIKDLQMRLDEAEQIALKGGKKQvlkLEARVKELENELESEQKKSQEYQKGVRKYERRIKELsyqgEEDK 1919
Cdd:PRK02224 627 -ERLAEKRER-KRELEAEFDEARIEEAREDKER---AEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL----EELR 697
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 2108526737 1920 KNLVRLQDLIDKMQAkvksykrQTEEAEEQANTnlskYRKLQHEL 1964
Cdd:PRK02224 698 ERREALENRVEALEA-------LYDEAEELESM----YGDLRAEL 731
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1598-1994 |
1.31e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.07 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1598 KSEIQAALEEAEGTLEHEESKSLRIQL-ELNQIKADVDRKLAEKDEEidslRRNHQRILESMQATLDAEAKSRNEAVRLr 1676
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLnGLESELAELDEEIERYEEQ----REQARETRDEADEVLEEHEERREELETL- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1677 kkmEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNE-ELKEQVAVTERRNNLlAAEVEELRALLEQ 1755
Cdd:PRK02224 257 ---EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlDDADAEAVEARREEL-EDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1756 SDRARKLAEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLSNEVDD---AVQECRNAEEKAKKAITDAAM----MAE 1828
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDAPVdlgnAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1829 ELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIaLKGGK---------------------KQVLKLEARVKELENEL 1887
Cdd:PRK02224 413 FLEELREERDELREREAELEATLRTARERVEEAEAL-LEAGKcpecgqpvegsphvetieedrERVEELEAELEDLEEEV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1888 ESEQKKsQEYQKGVRKYERRIKELsyqgEEDKKNLvrlQDLIDKMQAKVKSYKRQTEEAEEQANtnlskyrKLQHELDDA 1967
Cdd:PRK02224 492 EEVEER-LERAEDLVEAEDRIERL----EERREDL---EELIAERRETIEEKRERAEELRERAA-------ELEAEAEEK 556
|
410 420
....*....|....*....|....*..
gi 2108526737 1968 EERADMAESQANKLRARTRDQGSKLAE 1994
Cdd:PRK02224 557 REAAAEAEEEAEEAREEVAELNSKLAE 583
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1339-1989 |
2.66e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.33 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1339 ARAQAESGELSRKLEEREAMVSQLqraknsfSQNVEDLKKQLEEENKAKnalahalqssrhdcDLLREQYDEEQEAKADL 1418
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEK-------RQQLERLRREREKAERYQ--------------ALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1419 QRALSKANAEVAQWRTKYETDAIQRTEELEEakkkLVTRLQEAEETVETSNAKCSSL-EKTKHRLQTEIEDLVIDLERAn 1497
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISE----LEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASL- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1498 aaaavldkkqrnfdkvlaewRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQI 1577
Cdd:TIGR02169 307 --------------------ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1578 SQGVKTIHELEKMKKGLDMEKSEIQAALEEAegtleheeskslriQLELNQIKADVDRKLAEKDEEIDSLRRNHQRI--L 1655
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKL--------------KREINELKRELDRLQEELQRLSEELADLNAAIagI 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1656 ESMQATLDAEAKSRNEAVrlrKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVT 1735
Cdd:TIGR02169 433 EAKINELEEEKEDKALEI---KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGG 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1736 ERRNNLLAAEVEELRALLEQ----------------SDRARKLAEHELLEATERVNLLNSQNTGL-----INQKKKLESD 1794
Cdd:TIGR02169 510 RAVEEVLKASIQGVHGTVAQlgsvgeryataievaaGNRLNNVVVEDDAVAKEAIELLKRRKAGRatflpLNKMRDERRD 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1795 LSMLSNE--VDDAVQ--ECRNAEEKA-KKAITDAAMMAE-ELKKEQDTSAHL-----ERMKKNMEQTIKDLQMRLDEAEQ 1863
Cdd:TIGR02169 590 LSILSEDgvIGFAVDlvEFDPKYEPAfKYVFGDTLVVEDiEAARRLMGKYRMvtlegELFEKSGAMTGGSRAPRGGILFS 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1864 IALKGgkkQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQT 1943
Cdd:TIGR02169 670 RSEPA---ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2108526737 1944 EEAEEQANTNLSKYRKLQHELDDAEERADMAESQANKLRARTRDQG 1989
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR 792
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
901-1489 |
2.67e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 901 LRSATTEKELVSLKEELAKLKEALEKSEVKRKELEERqvsliqekndlslqlqaeqdnladaedrcdlliktKIQLEAKV 980
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQ-----------------------------------REQARETR 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 981 KEIMERLEDEEEmsanvlakKRkleDECAELKKDIDDLEITLAKVEKEKHAtenkvknLIEEMAALDETILKLTKEKKAL 1060
Cdd:PRK02224 237 DEADEVLEEHEE--------RR---EELETLEAEIEDLRETIAETEREREE-------LAEEVRDLRERLEELEEERDDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1061 LEahQQTLDDLQAEedkvniltkakaKLEQQVDDLEgslEQEKKLRMDLERVR---RKLEGDLKLSLESVMDLENDKQQL 1137
Cdd:PRK02224 299 LA--EAGLDDADAE------------AVEARREELE---DRDEELRDRLEECRvaaQAHNEEAESLREDADDLEERAEEL 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1138 DEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVAreleelserleeagga 1217
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELR---------------- 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1218 tsaqiEMNKKREADFLKLRRDLEEAmlhhEATTAALR----------KKHADSVAELSEQIDslqrvkqKLEKERSEAKM 1287
Cdd:PRK02224 426 -----EREAELEATLRTARERVEEA----EALLEAGKcpecgqpvegSPHVETIEEDRERVE-------ELEAELEDLEE 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1288 EVDDLASTVEQLSKGKATSEKMCRLyEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKN 1367
Cdd:PRK02224 490 EVEEVEERLERAEDLVEAEDRIERL-EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAE 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1368 SFSQNVEDLKKQLEEENKAKNALAH--ALQSSRHDCDLLREQYDEEQEAKADLQRA----LSKANAEVAQWRTKYETDAI 1441
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESLERirTLLAAIADAEDEIERLREKREALAELNDErrerLAEKRERKRELEAEFDEARI 648
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 2108526737 1442 qrtEELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDL 1489
Cdd:PRK02224 649 ---EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL 693
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1228-1977 |
2.77e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.10 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1228 READFLKLRRDLEEAMLHHEATTAALRKKHaDSVAELSEQIDSLQRVkqklEKERSEA---KMEVDDLASTVEQLSKGKA 1304
Cdd:pfam12128 191 KEGKFRDVKSMIVAILEDDGVVPPKSRLNR-QQVEHWIRDIQAIAGI----MKIRPEFtklQQEFNTLESAELRLSHLHF 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1305 TSEKMCRLYEDQMNEAKAKADELQRQL----NETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQ-NVEDLKKQ 1379
Cdd:pfam12128 266 GYKSDETLIASRQEERQETSAELNQLLrtldDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDaDIETAAAD 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1380 LEEENKAKNALAhaLQSSRHDCdLLREQYDEEQEAKADLQRALSKANAEVAqwRTKYETDAIQRTEELEEAKKKLVTRLQ 1459
Cdd:pfam12128 346 QEQLPSWQSELE--NLEERLKA-LTGKHQDVTAKYNRRRSKIKEQNNRDIA--GIKDKLAKIREARDRQLAVAEDDLQAL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1460 EAEETVETSNAKcSSLEKTKHRLQTEIEDLVIDLERANAAAAVLdKKQRNFDKVLaewrqkyEECQSELETSQKESRGLS 1539
Cdd:pfam12128 421 ESELREQLEAGK-LEFNEEEYRLKSRLGELKLRLNQATATPELL-LQLENFDERI-------ERAREEQEAANAEVERLQ 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1540 TELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKmkkgldmekseiqaalEEAEGTLEHEESKS 1619
Cdd:pfam12128 492 SELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLR----------------KEAPDWEQSIGKVI 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1620 LRIQLELNQIKADVDRKLAEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVrlrkkmegdlnEMEVQLSHANRQASE 1699
Cdd:pfam12128 556 SPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKA-----------EEALQSAREKQAAAE 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1700 SQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRNnllaaeveELRALLEQSDRARKLAEHELLEATERVNLLNS 1779
Cdd:pfam12128 625 EQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQS--------EKDKKNKALAERKDSANERLNSLEAQLKQLDK 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1780 QNTGLINQKKKLESDLSMLSNEVDDAVQECRNAEEkakkaitdAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQmrLD 1859
Cdd:pfam12128 697 KHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQL--------ALLKAAIAARRSGAKAELKALETWYKRDLASLG--VD 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1860 EaeqialkggkKQVLKLEARVKELENELESEQKKSQEyqkgVRKYERRIKE--------LSYQGEEDKKNLVRLQDLIDK 1931
Cdd:pfam12128 767 P----------DVIAKLKREIRTLERKIERIAVRRQE----VLRYFDWYQEtwlqrrprLATQLSNIERAISELQQQLAR 832
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 2108526737 1932 MQAKVKSYKRQ-------TEEAEEQANTNLSKYRKLQHELDDAEERADMAESQ 1977
Cdd:pfam12128 833 LIADTKLRRAKlemerkaSEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQ 885
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1074-1965 |
3.35e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 68.92 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1074 EEDKVNILTKAKAkLEQQVDDLEG------SLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQLDEKLKKKDFE 1147
Cdd:TIGR00606 158 QEDSNWPLSEGKA-LKQKFDEIFSatryikALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1148 mNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRacraKVEKQRSDVARELEELSERLEEAGGATSAQIEMNKK 1227
Cdd:TIGR00606 237 -REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALK----SRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1228 REA-----DFLKLRRDL-----EEAMLHHEATTAALRKK----HADSVAELSEQIDSL-QRVKQKLEKERSE----AKME 1288
Cdd:TIGR00606 312 RTVrekerELVDCQRELeklnkERRLLNQEKTELLVEQGrlqlQADRHQEHIRARDSLiQSLATRLELDGFErgpfSERQ 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1289 VDDLASTVEQLSKGKA-TSEKMCRLYEDQMNEAKAKADELQrqlNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKN 1367
Cdd:TIGR00606 392 IKNFHTLVIERQEDEAkTAAQLCADLQSKERLKQEQADEIR---DEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEG 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1368 SfsqnVEDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYdeEQEAKADLQRALSKANAEVAQWRTKYETdaiqRTEEL 1447
Cdd:TIGR00606 469 S----SDRILELDQELRKAERELSKAEKNSLTETLKKEVKS--LQNEKADLDRKLRKLDQEMEQLNHHTTT----RTQME 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1448 EEAKKKLVTRLQEAEETVETSNAKCS---------SLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKvlaewr 1518
Cdd:TIGR00606 539 MLTKDKMDKDEQIRKIKSRHSDELTSllgyfpnkkQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINN------ 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1519 qkyeecqsELETSQKESRGLSTELFKLKNSYEETLDhLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEK 1598
Cdd:TIGR00606 613 --------ELESKEEQLSSYEDKLFDVCGSQDEESD-LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVC 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1599 SEIQAALEEAEGTLEHEESKSLRIQLELNQIKADVdRKLAEKDEEIDSLRRNHQRILESMQATLdAEAKSRNEAV-RLRK 1677
Cdd:TIGR00606 684 QRVFQTEAELQEFISDLQSKLRLAPDKLKSTESEL-KKKEKRRDEMLGLAPGRQSIIDLKEKEI-PELRNKLQKVnRDIQ 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1678 KMEGDLNEMEVQLSHANRQASESQKFL------RNLQVQIKDIQLELDETIHQNE---------ELKEQVAVTERRNNLL 1742
Cdd:TIGR00606 762 RLKNDIEEQETLLGTIMPEEESAKVCLtdvtimERFQMELKDVERKIAQQAAKLQgsdldrtvqQVNQEKQEKQHELDTV 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1743 AAEVEELRALLEQSDRARKLAEHELLE-ATERVNLLNSqntglINQKKKLESDLSMLSNEVDDAVQECRNAEEKA---KK 1818
Cdd:TIGR00606 842 VSKIELNRKLIQDQQEQIQHLKSKTNElKSEKLQIGTN-----LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDsplET 916
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1819 AITDAAMMAEELKKEQDTSAHLERMKKN-MEQTIKDLQMRLDEAEQIALKGGKKQVLKLEARVKELENELESEQKKSQEY 1897
Cdd:TIGR00606 917 FLEKDQQEKEELISSKETSNKKAQDKVNdIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKI 996
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1898 QKGVRKYERRIKELSYQGEEDKKNLVRL--QDLIDKMQAKVKSYKRQTeeAEEQANTNLSKYRKLQHELD 1965
Cdd:TIGR00606 997 NEDMRLMRQDIDTQKIQERWLQDNLTLRkrENELKEVEEELKQHLKEM--GQMQVLQMKQEHQKLEENID 1064
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
907-1728 |
3.55e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 68.92 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 907 EKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQ-------------------LQAEQDNL---ADAED 964
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQadrhqehirardsliqslaTRLELDGFergPFSER 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 965 RCDLLIKTKIQ-LEAKVKEIMERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAK-------VEKEKHATENKV 1036
Cdd:TIGR00606 391 QIKNFHTLVIErQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKkqeelkfVIKELQQLEGSS 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1037 KNLIEEMAALDETILKLTK-EKKALLEAHQQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKL---RMDLERV 1112
Cdd:TIGR00606 471 DRILELDQELRKAERELSKaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLtkdKMDKDEQ 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1113 RRKLEGDLKLSLESVMDLENDKQQLDEKLKKKDFEMNEMSTRIEDeqalvnqLQKKIKELQARTEELEEELEADRACRAK 1192
Cdd:TIGR00606 551 IRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAK-------LNKELASLEQNKNHINNELESKEEQLSS 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1193 VEKQRSDVARELEElserleeaggatsaqiemnkkrEADFLKLRRDLEEAMlHHEATTAALRKKHADSVAELSEQIDSLQ 1272
Cdd:TIGR00606 624 YEDKLFDVCGSQDE----------------------ESDLERLKEEIEKSS-KQRAMLAGATAVYSQFITQLTDENQSCC 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1273 RVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNE----AKAKADELQRQLNETNTQRARAQAESGEl 1348
Cdd:TIGR00606 681 PVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglAPGRQSIIDLKEKEIPELRNKLQKVNRD- 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1349 srkleereamvsqLQRAKNSFSQNVEDLKKQLEEENKAKNALAhalqssrhDCDLLREQYDEEQEAKADLQRALSKANAe 1428
Cdd:TIGR00606 760 -------------IQRLKNDIEEQETLLGTIMPEEESAKVCLT--------DVTIMERFQMELKDVERKIAQQAAKLQG- 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1429 VAQWRTKYETDaiQRTEELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAaaavldkkqr 1508
Cdd:TIGR00606 818 SDLDRTVQQVN--QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQ---------- 885
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1509 nFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETikrENKNLQEEIADLSDQISQGVKTIHELE 1588
Cdd:TIGR00606 886 -FEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKET---SNKKAQDKVNDIKEKVKNIHGYMKDIE 961
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1589 K-MKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLELNQIKADVD---------------RKLAEKDEEIDSLRRNHQ 1652
Cdd:TIGR00606 962 NkIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkiqerwlqdnltlRKRENELKEVEEELKQHL 1041
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1653 RILESMQAT-LDAEAKSRNEAVRLRKKME----GDLNEMEVQLSHANRQASESQkfLRNLQVQIKDIQLELDETIHQNEE 1727
Cdd:TIGR00606 1042 KEMGQMQVLqMKQEHQKLEENIDLIKRNHvlalGRQKGYEKEIKHFKKELREPQ--FRDAEEKYREMMIVMRTTELVNKD 1119
|
.
gi 2108526737 1728 L 1728
Cdd:TIGR00606 1120 L 1120
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1314-1768 |
4.03e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1314 EDQMNEAKAKADE---LQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAknsfsQNVEDLKKQLEEENKAKNAL 1390
Cdd:COG4717 77 EEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY-----QELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1391 AHALQSSRHdcdlLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEETVETSNA 1470
Cdd:COG4717 152 EERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1471 KCSSLEKTKHRLQTE--IEDLVIDLERANAAAAVLDKKQRNFDKV------------LAEWRQKYEECQSELETSQKESR 1536
Cdd:COG4717 228 ELEQLENELEAAALEerLKEARLLLLIAAALLALLGLGGSLLSLIltiagvlflvlgLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1537 GLSTELFKLKNsyEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEGTLEHEE 1616
Cdd:COG4717 308 QALPALEELEE--EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1617 skslriqlELnqikadvdRKLAEKDEEidslRRNHQRILESMQATLDAEAKSRNEAVRlrkkmEGDLNEMEVQLSHANRQ 1696
Cdd:COG4717 386 --------EL--------RAALEQAEE----YQELKEELEELEEQLEELLGELEELLE-----ALDEEELEEELEELEEE 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108526737 1697 ASESQKFLRNLQVQIKDIQLELDETIHQNE--ELKEQVAVTERRNNLLAAEVEELRALLEQSDRARKLAEHELL 1768
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1314-1956 |
6.68e-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: 67.74 E-value: 6.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1314 EDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHA 1393
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1394 L---QSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETdAIQRTEELEEAKKKLVTRLQEAEETVETSNA 1470
Cdd:TIGR04523 203 LsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISN-TQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1471 KCSSLEKTKHRLQTEIEDLVidleranaaaavlDKKQRNFDKVLaewrqkyeecQSELETSQKESRGLSTELFKLKNSYE 1550
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLN-------------NQKEQDWNKEL----------KSELKNQEKKLEEIQNQISQNNKIIS 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1551 ETLDHLETIKRENKNLQEEIADLSDQISQGVKtihELEKMKKGLDMEKSEIQAaLEEAEGTLEHEesksLRIQLELNQik 1630
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEKQN---EIEKLKKENQSYKQEIKN-LESQINDLESK----IQNQEKLNQ-- 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1631 advdrklaEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEavrlrkkmegdlnemevqlshanrqasesqkfLRNLQVQ 1710
Cdd:TIGR04523 409 --------QKDEQIKKLQQEKELLEKEIERLKETIIKNNSE--------------------------------IKDLTNQ 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1711 IKDIQLELDETIHQNEELKEQVAVTERrnnllaaEVEELRALLEQSDRARKLAEHELLEATERVNLLNSQNTGLINQKKK 1790
Cdd:TIGR04523 449 DSVKELIIKNLDNTRESLETQLKVLSR-------SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1791 LESDLSMLSNEVDDAVQECRNAEEKAKKaitdaamMAEELKKEQdtsahLERMKKNMEQTIKDLqmrldeaeqialkggK 1870
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNK-------DDFELKKEN-----LEKEIDEKNKEIEEL---------------K 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1871 KQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEAEEQA 1950
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
....*.
gi 2108526737 1951 NTNLSK 1956
Cdd:TIGR04523 655 KEIRNK 660
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
907-1394 |
6.80e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 67.89 E-value: 6.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 907 EKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQ---EKNDLSLQLQAEQDNlADAEDRcdlliktkiQLEAKVKEI 983
Cdd:pfam01576 572 EKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQmlaEEKAISARYAEERDR-AEAEAR---------EKETRALSL 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 984 MERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALdETILKLTKEKKALLEA 1063
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEEL-EDELQATEDAKLRLEV 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1064 HQQTLD-----DLQAEEDKVNiltKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKlSLESVMDLEND-KQQL 1137
Cdd:pfam01576 721 NMQALKaqferDLQARDEQGE---EKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLK-ELEAQIDAANKgREEA 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1138 DEKLKKKDFEMNEMSTRIEDEQALVNQL-------QKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELeelser 1210
Cdd:pfam01576 797 VKQLKKLQAQMKDLQRELEEARASRDEIlaqskesEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEI------ 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1211 leeAGGATSAQIEMNKKR--EADFLKLRRDLEEAMLHHEATTAALRK--KHADSV-AELSEQIDSLQRV---KQKLEKER 1282
Cdd:pfam01576 871 ---ASGASGKSALQDEKRrlEARIAQLEEELEEEQSNTELLNDRLRKstLQVEQLtTELAAERSTSQKSesaRQQLERQN 947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1283 SEAKMEVDDLASTV----------------------EQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRAR 1340
Cdd:pfam01576 948 KELKAKLQEMEGTVkskfkssiaaleakiaqleeqlEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEK 1027
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2108526737 1341 AQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHAL 1394
Cdd:pfam01576 1028 GNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
895-1309 |
9.79e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 895 FKIKPLLRSATTEKELVSLKEELAKLKEALEKSEVKRKELEE---------RQVSLIQEKNDLSLQLQAEQDNLADAEDR 965
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEElkkklkeleKRLEELEERHELYEEAKAKKEELERLKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 966 cdLLIKTKIQLEAKVKEIMERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLE-----ITLAKVEKEKHATEN------ 1034
Cdd:PRK03918 381 --LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkCPVCGRELTEEHRKElleeyt 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1035 -KVKNLIEEMAALDETILKLTKEKKAL---------LEAHQQTLDDLQAEEDKVNILTkaKAKLEQQVDDLEGSLEQEKK 1104
Cdd:PRK03918 459 aELKRIEKELKEIEEKERKLRKELRELekvlkkeseLIKLKELAEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKLIK 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1105 LRMDLERvrrklegdLKLSLESVMDLENDKQQLDEKLKKKDFEMNEMSTRIEDEQ-ALVNQLQKKIKELQARTEELEEEL 1183
Cdd:PRK03918 537 LKGEIKS--------LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELK 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1184 EADRACRAKVEKQRSdvareleelserleeAGGATSAQIEMNKKREADFLKLRRDLEEA-MLHHEATTAALRKKHadsvA 1262
Cdd:PRK03918 609 DAEKELEREEKELKK---------------LEEELDKAFEELAETEKRLEELRKELEELeKKYSEEEYEELREEY----L 669
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2108526737 1263 ELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKM 1309
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL 716
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
914-1432 |
1.05e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.99 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 914 KEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEIMERLEDEEEM 993
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 994 SANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALLEAHQQTLDDLQA 1073
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGN 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1074 EEDKVNILTKAKAKLEQQVDDLEGSLEQekkLRMDLERVRRKLEG--------DLKLS--LESVMDLENDKQQLDEKLKK 1143
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRT---ARERVEEAEALLEAgkcpecgqPVEGSphVETIEEDRERVEELEAELED 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1144 KDFEMNEMSTRIEDEQALVnQLQKKIKELQARtEELEEELEADRacRAKVEKQRSDVARELEElserleeaggATSAQIE 1223
Cdd:PRK02224 487 LEEEVEEVEERLERAEDLV-EAEDRIERLEER-REDLEELIAER--RETIEEKRERAEELRER----------AAELEAE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1224 MNKKREAdflklRRDLEEAMLHHEATTAALRKKhadsVAELSEQIDSLQRVKQKLEkerseakmEVDDLASTVEQLSKGK 1303
Cdd:PRK02224 553 AEEKREA-----AAEAEEEAEEAREEVAELNSK----LAELKERIESLERIRTLLA--------AIADAEDEIERLREKR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1304 ATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAE---------SGELSRKLEEREAMVSQLQRAKNSFsQNVE 1374
Cdd:PRK02224 616 EALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKEraeeyleqvEEKLDELREERDDLQAEIGAVENEL-EELE 694
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526737 1375 DLKKQLEeenkaknalahALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQW 1432
Cdd:PRK02224 695 ELRERRE-----------ALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLER 741
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1367-1948 |
1.41e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 66.85 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1367 NSFSQNVEDLK---KQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYE--TDAI 1441
Cdd:PRK01156 162 NSLERNYDKLKdviDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1442 QRTEELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQtEIEDLVIDLERANAAAAVLDKKQrnfdkvLAEWRQKY 1521
Cdd:PRK01156 242 NELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHM-KIINDPVYKNRNYINDYFKYKND------IENKKQIL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1522 EECQSELETSQKESRGLStELFKLKNSYEETldhletiKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEI 1601
Cdd:PRK01156 315 SNIDAEINKYHAIIKKLS-VLQKDYNDYIKK-------KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNI 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1602 QAALEEAEGTLEHEESKSLRIQLELNQIKADVDR---KLAEKDEEIDSLRRNHQRILESMqATLDAEAKSRNEAVRLRKK 1678
Cdd:PRK01156 387 ERMSAFISEILKIQEIDPDAIKKELNEINVKLQDissKVSSLNQRIRALRENLDELSRNM-EMLNGQSVCPVCGTTLGEE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1679 MEGDLNEmevqlsHANRQASESQKFLRNLQVQIKDIqlelDETIHQNEELKEQVAVTE-RRNNLLAAEVEELRALLEQ-S 1756
Cdd:PRK01156 466 KSNHIIN------HYNEKKSRLEEKIREIEIEVKDI----DEKIVDLKKRKEYLESEEiNKSINEYNKIESARADLEDiK 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1757 DRARKLAEHElLEATERVNLLNSQNTGLINQKKklESDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKE-QD 1835
Cdd:PRK01156 536 IKINELKDKH-DKYEEIKNRYKSLKLEDLDSKR--TSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGfPD 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1836 TSAHLERMKKNMEQTIKDLQMRLDEAEQIalkggKKQVLKLEARVKELENE---LESEQKKSQEYQKGVRKYERRIKELS 1912
Cdd:PRK01156 613 DKSYIDKSIREIENEANNLNNKYNEIQEN-----KILIEKLRGKIDNYKKQiaeIDSIIPDLKEITSRINDIEDNLKKSR 687
|
570 580 590
....*....|....*....|....*....|....*.
gi 2108526737 1913 YQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEAEE 1948
Cdd:PRK01156 688 KALDDAKANRARLESTIEILRTRINELSDRINDINE 723
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
925-1650 |
1.69e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 66.40 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 925 EKSEVKRKE----LEERQ-VSLIQEKNDLSLQLQAEQDNLADAEDRcdlLIKTKIQLEAKVKEIMERLEDEEEMSANVLA 999
Cdd:pfam12128 214 PKSRLNRQQvehwIRDIQaIAGIMKIRPEFTKLQQEFNTLESAELR---LSHLHFGYKSDETLIASRQEERQETSAELNQ 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1000 KKRKLEDECAELKkdiddleitlAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALLEAHQQTLDDLQAE----E 1075
Cdd:pfam12128 291 LLRTLDDQWKEKR----------DELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSElenlE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1076 DKVNILTKAKAKLEQQVDDLEGSLEQEkkLRMDLERVRRKL----EGDLKLSLESVMDLENDKQQLDEKLKKKDFEMNE- 1150
Cdd:pfam12128 361 ERLKALTGKHQDVTAKYNRRRSKIKEQ--NNRDIAGIKDKLakirEARDRQLAVAEDDLQALESELREQLEAGKLEFNEe 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1151 ---MSTRIEDEQALVNQLQKKIKELQARTEELEEELEADR---ACRAKVEKQRSDVAReleelserleeAGGATSAQIEM 1224
Cdd:pfam12128 439 eyrLKSRLGELKLRLNQATATPELLLQLENFDERIERAREeqeAANAEVERLQSELRQ-----------ARKRRDQASEA 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1225 NKKREADFLKLRRDLEEAMLHHEATTAALrkkHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDlASTVEQLSKGKA 1304
Cdd:pfam12128 508 LRQASRRLEERQSALDELELQLFPQAGTL---LHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWD-GSVGGELNLYGV 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1305 TsekmCRLYEDQMNEAKAKADELQRQLNET----NTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQL 1380
Cdd:pfam12128 584 K----LDLKRIDVPEWAASEEELRERLDKAeealQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLF 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1381 EEENKAKNALAHALQSSRHDCDLLREQYDEEQEAkadLQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQE 1460
Cdd:pfam12128 660 DEKQSEKDKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1461 AEETVETS-NAKCSSLEKTKHR--------------LQTEIEDLVIDLERanaaAAVLDKKQRNFDKVLAE-WRQKYEEC 1524
Cdd:pfam12128 737 AIAARRSGaKAELKALETWYKRdlaslgvdpdviakLKREIRTLERKIER----IAVRRQEVLRYFDWYQEtWLQRRPRL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1525 QSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQ----EEIADLSDQISqGVKTIHELEKMKKgLDMEKSE 1600
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQvrlsENLRGLRCEMS-KLATLKEDANSEQ-AQGSIGE 890
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 2108526737 1601 IQAALEEAEGTLEHEeskSLRIQLELNQIKADVDRKLA-EKDEEIDSLRRN 1650
Cdd:pfam12128 891 RLAQLEDLKLKRDYL---SESVKKYVEHFKNVIADHSGsGLAETWESLREE 938
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1549-1994 |
1.97e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1549 YEETLDHLETIKRENKNLqEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEgtLEHEESKSLRIQLELNQ 1628
Cdd:COG4913 237 LERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1629 IKADVDRKLAEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHA----NRQASESQKFL 1704
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeefAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1705 RNLQVQIKDIQLELDETI-------HQNEELKEQVAVTERRNNLLAAEVEELRALLEQS-----DRARKLAehELLE--- 1769
Cdd:COG4913 394 EALEEELEALEEALAEAEaalrdlrRELRELEAEIASLERRKSNIPARLLALRDALAEAlgldeAELPFVG--ELIEvrp 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1770 -------ATERVnlLNSQNTGL-------------INQKK-----------------------------KLESDLSMLSN 1800
Cdd:COG4913 472 eeerwrgAIERV--LGGFALTLlvppehyaaalrwVNRLHlrgrlvyervrtglpdperprldpdslagKLDFKPHPFRA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1801 EVDDAVQE------CRNAEE--KAKKAITDAAMMAEELKK-EQDTSAHLER---MKKNMEQTIKDLQMRLDEAEQiALKG 1868
Cdd:COG4913 550 WLEAELGRrfdyvcVDSPEElrRHPRAITRAGQVKGNGTRhEKDDRRRIRSryvLGFDNRAKLAALEAELAELEE-ELAE 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1869 GKKQVLKLEARVKELENELESEQK--KSQEYQKGVRKYERRIKELsyqgEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEA 1946
Cdd:COG4913 629 AEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAEL----EAELERLDASSDDLAALEEQLEELEAELEEL 704
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2108526737 1947 EEQANTNLSKYRKLQHELDDAEERADMAESQANKLRARTRDQGSKLAE 1994
Cdd:COG4913 705 EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1312-1863 |
2.07e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1312 LYEDQM---NEAKAKADELQRQLNETNtqRARAQAEsgelsrKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKN 1388
Cdd:COG4913 212 FVREYMleePDTFEAADALVEHFDDLE--RAHEALE------DAREQIELLEPIRELAERYAAARERLAELEYLRAALRL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1389 -ALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEETVET 1467
Cdd:COG4913 284 wFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1468 SNAKCSSLEktkHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLStelfKLKN 1547
Cdd:COG4913 364 LEALLAALG---LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE----RRKS 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1548 SYEEtldHLETIKRE-NKNLQEEIADL---------------------------------SDQISQGVKTIHELEKMKKG 1593
Cdd:COG4913 437 NIPA---RLLALRDAlAEALGLDEAELpfvgelievrpeeerwrgaiervlggfaltllvPPEHYAAALRWVNRLHLRGR 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1594 LDMEKseIQAALEEAEGTLEHEESKSLRIQLELNQIKADVDRKLAEKD-----EEIDSLRRNHQRIlesmqaTLDAEAKS 1668
Cdd:COG4913 514 LVYER--VRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAELGRRFdyvcvDSPEELRRHPRAI------TRAGQVKG 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1669 RNEavRLRKKMEGDLNEMEV-------QLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRNNL 1741
Cdd:COG4913 586 NGT--RHEKDDRRRIRSRYVlgfdnraKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1742 LAAEvEELRALLEQSDRARKlAEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLSNEVDDAVQECRNA----EEKAK 1817
Cdd:COG4913 664 ASAE-REIAELEAELERLDA-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELqdrlEAAED 741
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 2108526737 1818 KAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQ 1863
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
953-1590 |
2.10e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 953 QAEQDNLADAE--DRCDLlIKTKIQLeAKVKEIMERLEDEEEMSANVLAKKRKLEDEcaeLKKDIDDleitlaKVEKEKH 1030
Cdd:PRK02224 137 QGEVNKLINATpsDRQDM-IDDLLQL-GKLEEYRERASDARLGVERVLSDQRGSLDQ---LKAQIEE------KEEKDLH 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1031 ATENKVKnliEEMAALDETILKLTKEK----------KALLEAHQQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLE 1100
Cdd:PRK02224 206 ERLNGLE---SELAELDEEIERYEEQReqaretrdeaDEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVR 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1101 QEKKLRMDLERVRRKLEGDLKLS-------LESVMDLENDKQQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQ 1173
Cdd:PRK02224 283 DLRERLEELEEERDDLLAEAGLDdadaeavEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELR 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1174 ARTEELEEELEAdraCRAKVEKQRSDVARELeelserleeaggatsAQIEMNKKREADFLKLRRDLEEAMLHHEATTAAL 1253
Cdd:PRK02224 363 EEAAELESELEE---AREAVEDRREEIEELE---------------EEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1254 RKKHADSVAELSEQIDSLQRVKQKLEKER-SEAKMEVDDlASTVEQLSKGKATSEKMcrlyEDQMNEAKAKADELQRQLN 1332
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEAGKcPECGQPVEG-SPHVETIEEDRERVEEL----EAELEDLEEEVEEVEERLE 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1333 etntqRARAQAES-GELSRKLEEREAMVSQLQRAKNSfsqnVEDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEE 1411
Cdd:PRK02224 500 -----RAEDLVEAeDRIERLEERREDLEELIAERRET----IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1412 QEAKADLQRALSKANAEVAQWRTKYE-----TDAIQRTEELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHrlQTEI 1486
Cdd:PRK02224 571 REEVAELNSKLAELKERIESLERIRTllaaiADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD--EARI 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1487 EDLVIDLERANAAAAVLDKKqrnfdkvLAEWRQKYEECQSE---LETSQKESRGLSTELFKLknsyEETLDHLETIKREN 1563
Cdd:PRK02224 649 EEAREDKERAEEYLEQVEEK-------LDELREERDDLQAEigaVENELEELEELRERREAL----ENRVEALEALYDEA 717
|
650 660
....*....|....*....|....*..
gi 2108526737 1564 KNLQEEIADLSDQISQgvKTIHELEKM 1590
Cdd:PRK02224 718 EELESMYGDLRAELRQ--RNVETLERM 742
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1258-1474 |
2.54e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.79 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1258 ADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLskgkatsekmcrlyEDQMNEAKAKADELQRQLNETNTQ 1337
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--------------ERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1338 RARAQAESGELSRKLEEREAMVSQLQRA---------------KNSFSQNV----------EDLKKQLEEENKAKNALAH 1392
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRAlyrlgrqpplalllsPEDFLDAVrrlqylkylaPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1393 ALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAiQRTEELEEAKKKLVTRLQEAEETVETSNAKC 1472
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERT 243
|
..
gi 2108526737 1473 SS 1474
Cdd:COG4942 244 PA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1561-1984 |
5.05e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1561 RENKNLQEEIADLSDQisqgVKTIHELEKMKKGLDMEKSEIQAALEEAEGtlEHEESKSLRIQLELNQIKADVDRKLAEK 1640
Cdd:COG4717 71 KELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELRE--ELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1641 DEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDE 1720
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1721 TIHQNEELKEQVAVTERRNNLLAAEVE-----ELRALLEQSDRARKLAEHELLEATERVNLLNSQNTGLINQKKKLESDL 1795
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLlliaaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1796 SMLsnevdDAVQECRNAEEKAKKAITDAAMMAEELKKEqdtsaHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVLK 1875
Cdd:COG4717 305 EEL-----QALPALEELEEEELEELLAALGLPPDLSPE-----ELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1876 LEARVK-ELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDliDKMQAKVKSYKRQTEEAEEQANTNL 1954
Cdd:COG4717 375 LLAEAGvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELR 452
|
410 420 430
....*....|....*....|....*....|..
gi 2108526737 1955 SKYRKLQHELDDAEE--RADMAESQANKLRAR 1984
Cdd:COG4717 453 EELAELEAELEQLEEdgELAELLQELEELKAE 484
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
965-1733 |
6.65e-10 |
|
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: 64.60 E-value: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 965 RCDLLIKTKIQLEAKVKEIMERLEDEEEMSANVLAKKRKLEDECAELKKDI----DDLEITLAKVEKEKHATENKVKNLI 1040
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1041 EEMAALDETILKLTKEKKALLEAH--QQTLDDLQAEEDKVNILTKAKAKLEQQVDdlegslEQEKKLRMdLERVRRKLEG 1118
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAVLEETQERIN------RARKAAPL-AAHIKAVTQI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1119 DLKlsLESVMDLENDKQQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELqaRTEELEEELEADRACRAKVEKQRS 1198
Cdd:TIGR00618 306 EQQ--AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHI--RDAHEVATSIREISCQQHTLTQHI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1199 dVARELEELSERLEEAGGATSAQIEMNKKREADFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKL 1278
Cdd:TIGR00618 382 -HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1279 EKERSEAKMEVDDLASTVEQLSKGKATSEKmcrLYEDQMNEAKAKADELQRQLNETNtQRARAQAESGELSRKLEEREAM 1358
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKA---VVLARLLELQEEPCPLCGSCIHPN-PARQDIDNPGPLTRRMQRGEQT 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1359 VSQLQRAknsfsqnVEDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYdeeQEAKADLQRaLSKANAEVAQWRTKYET 1438
Cdd:TIGR00618 537 YAQLETS-------EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD---NRSKEDIPN-LQNITVRLQDLTEKLSE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1439 DAIQRTEELEEAKKKLVTRLQEAEETVETSNaKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKqrnfdkvlaewr 1518
Cdd:TIGR00618 606 AEDMLACEQHALLRKLQPEQDLQDVRLHLQQ-CSQELALKLTALHALQLTLTQERVREHALSIRVLPK------------ 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1519 QKYEECQSELETSQKESRGLSTELfklknsyeETLDHLETIKRENKNLQEEIADLSDQISQGVKTihelekmkkgldmEK 1598
Cdd:TIGR00618 673 ELLASRQLALQKMQSEKEQLTYWK--------EMLAQCQTLLRELETHIEEYDREFNEIENASSS-------------LG 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1599 SEIQA---ALEEAEGTLEHEESKSLRIQLELNQIKADVDRKLAEKDEEIDSLRRNHQRILESMQaTLDAEAKSRNEAVRL 1675
Cdd:TIGR00618 732 SDLAAredALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLRE-EDTHLLKTLEAEIGQ 810
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 2108526737 1676 RKKMEGDLNEMEVQLSHANRQASESQ-KFLRNLQVQIKDIQLELDETIHQNEELKEQVA 1733
Cdd:TIGR00618 811 EIPSDEDILNLQCETLVQEEEQFLSRlEEKSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1547-1987 |
1.27e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.50 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1547 NSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLEL 1626
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1627 ---NQIKADVDRKLAEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRK----------KMEGDLNEMEVQLSHA 1693
Cdd:TIGR04523 113 kndKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKqkeelenelnLLEKEKLNIQKNIDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1694 NRQASESQKFLRNLQVQIKD---IQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRALLEQSDRARKLAEHELLEA 1770
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKnksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1771 TERVNLLNSQNTGLINQKKKLESDLSMLSNE---------------VDDAVQECRNAEEKAKKAITDAAMMAEELKKEQD 1835
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwnkelkselknQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1836 TSaHLERMKKNMEQTIKDLQMRLDEAEQialKGGKKQVLKLEARVKELENELESEQKKSQEYQKGVR-------KYERRI 1908
Cdd:TIGR04523 353 NS-ESENSEKQRELEEKQNEIEKLKKEN---QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKklqqekeLLEKEI 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2108526737 1909 KELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADMAESQANKLRARTRD 1987
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1631-1994 |
1.30e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1631 ADVDRKLAEKDEEIDSLRRNHQR---ILESMQATLDAEAKSRNEAVRLrKKMEGDLNEMEVQLSHANRQASESQKflRNL 1707
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAERY-QALLKEKREYEGYELLKEKEALERQK--EAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1708 QVQIKDIQLELDETIHQNEELkeqvavterrnnllAAEVEELRALLEQ-SDRARKLAEHELLEATERVnllnsqntglin 1786
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISEL--------------EKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKI------------ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1787 qkKKLESDLSMLSNEVDDAVQECRNAEEKAKKAItdaammaEELKKEQDTSAHLERmkknmeqTIKDLQMRLDEAEQIal 1866
Cdd:TIGR02169 297 --GELEAEIASLERSIAEKERELEDAEERLAKLE-------AEIDKLLAEIEELER-------EIEEERKRRDKLTEE-- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1867 kggkkqVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEA 1946
Cdd:TIGR02169 359 ------YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2108526737 1947 EEQANTNLSKYRKLQHELDDAEERADMAESQANKLRARTRDQGSKLAE 1994
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1376-1733 |
1.40e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 62.99 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1376 LKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVaqwrtkyETDAIQRTEELEEAKKKLV 1455
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAEL-------KEELRQSREKHEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1456 TRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEE---CQSELETSQ 1532
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAErkqLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1533 KESRGLSTELFKLKNSYEETLDHLETikrenknLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEG-- 1610
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGlg 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1611 -TLEHEESKSLRIQLELNQIK---ADVDRKLAEKD-----------EEIDSLRRN----HQRILESMQATLDAEA---KS 1668
Cdd:pfam07888 258 eELSSMAAQRDRTQAELHQARlqaAQLTLQLADASlalregrarwaQERETLQQSaeadKDRIEKLSAELQRLEErlqEE 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526737 1669 RNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQL---ELDETIHQNEELKEQVA 1733
Cdd:pfam07888 338 RMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAekqELLEYIRQLEQRLETVA 405
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
914-1427 |
1.44e-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: 63.20 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 914 KEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEIMERLEDEE-- 991
Cdd:pfam05483 267 RDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKaa 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 992 ------EMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALLEAHQ 1065
Cdd:pfam05483 347 hsfvvtEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1066 --QTLDDLQAEEDKVNILTKAKaklEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQLDEKLKK 1143
Cdd:pfam05483 427 feKIAEELKGKEQELIFLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1144 KDFEMNEMSTRIEDEQALVN----QLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEELSERLEEAGGATS 1219
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIInckkQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVL 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1220 AQIEMNKKREADFLKLRRDLEEAM-----LHHEatTAALRKKhadSVAElSEQIDSLQRVKQKLEKERSEAKMEVDDLAS 1294
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQIENKNknieeLHQE--NKALKKK---GSAE-NKQLNAYEIKVNKLELELASAKQKFEEIID 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1295 TVEQLSKGKATSEKmcRLYEdQMNEAKAKADELQRQLNETNTQRARAQAEsgelsrkleereaMVSQLQRAKNSFSQNVE 1374
Cdd:pfam05483 658 NYQKEIEDKKISEE--KLLE-EVEKAKAIADEAVKLQKEIDKRCQHKIAE-------------MVALMEKHKHQYDKIIE 721
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1375 DLKKQL-------EEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANA 1427
Cdd:pfam05483 722 ERDSELglyknkeQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTA 781
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
975-1201 |
1.94e-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: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 975 QLEAKVKEIMERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLT 1054
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1055 KEKKALLEAHQQtlddlQAEEDKVNILTKAkakleQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDK 1134
Cdd:COG4942 104 EELAELLRALYR-----LGRQPPLALLLSP-----EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108526737 1135 QQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVA 1201
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
902-1574 |
2.14e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 902 RSATTEKELVSLKEELAKLK--EALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAK 979
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKkeEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK 1432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 980 VKEIMERLedEEEMSANVLAKKRKLEDECAELKKdiddleitlaKVEKEKHATENKVKnlIEEMAALDETILKLTKEKKA 1059
Cdd:PTZ00121 1433 ADEAKKKA--EEAKKADEAKKKAEEAKKAEEAKK----------KAEEAKKADEAKKK--AEEAKKADEAKKKAEEAKKK 1498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1060 LLEAHQQTLDDLQAEEDKvniltkaKAKLEQQVDDLEGSleQEKKLRMDLERVRRKLEGDLKLSLESVMDLEnDKQQLDE 1139
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAK-------KAEEAKKADEAKKA--EEAKKADEAKKAEEKKKADELKKAEELKKAE-EKKKAEE 1568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1140 klKKKDFEMNEMSTRIEDEqalVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDvareleelserleeaggats 1219
Cdd:PTZ00121 1569 --AKKAEEDKNMALRKAEE---AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-------------------- 1623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1220 aqiemnkkreadflKLRRDLEEamlhheattaalRKKHADSVAELSEQIdslqRVKQKLEKERSEAKMEVDDLASTVEQl 1299
Cdd:PTZ00121 1624 --------------ELKKAEEE------------KKKVEQLKKKEAEEK----KKAEELKKAEEENKIKAAEEAKKAEE- 1672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1300 SKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQ 1379
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1380 LEEENK----AKNALAHALQSSRHDCDLLREQYDEEQEAK---ADLQRALSKANAEVAQWRTKYETDAIQRTEELEEAkk 1452
Cdd:PTZ00121 1753 EEEKKKiahlKKEEEKKAEEIRKEKEAVIEEELDEEDEKRrmeVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDS-- 1830
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1453 klvtrlqEAEETVETSNakcSSLEKTKHRLQTEIEDLVIDLERANaaaavldkKQRNFDKvlaEWRQKYEECQSELETSQ 1532
Cdd:PTZ00121 1831 -------AIKEVADSKN---MQLEEADAFEKHKFNKNNENGEDGN--------KEADFNK---EKDLKEDDEEEIEEADE 1889
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2108526737 1533 KE-------SRGLSTELFKLKN--SYEETLDHLETIKRENKNLQEEIADLS 1574
Cdd:PTZ00121 1890 IEkidkddiEREIPNNNMAGKNndIIDDKLDKDEYIKRDAEETREEIIKIS 1940
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1442-1888 |
2.23e-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: 62.40 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1442 QRTEELE-------EAKKKLV---TRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFD 1511
Cdd:pfam05622 14 QRCHELDqqvsllqEEKNSLQqenKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1512 KVLAEWRQKYEEcqseLETSQKESRGLSTELFKLKNS-------------YEETLDHLETIKRENKNLQEEIADLSDQIS 1578
Cdd:pfam05622 94 KEVLELQHRNEE----LTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNAEYMQRTL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1579 QGVKTIHELEKMKKGLDMEKSEIQaaleEAEGTLEHEESKSLRIQLELNQIKADVDRKLAEKD---EEIDSLRRN----- 1650
Cdd:pfam05622 170 QLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKErliIERDTLRETneelr 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1651 ----HQRILESMQATLDAEAKSRNEAVRlrKKMEGDLNEMEVQLSHANRQASESQKflRNLQVQIKDIQLELDETIHQNE 1726
Cdd:pfam05622 246 caqlQQAELSQADALLSPSSDPGDNLAA--EIMPAEIREKLIRLQHENKMLRLGQE--GSYRERLTELQQLLEDANRRKN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1727 ELKEQVAVTERRNNLLAAEVEELRALLEQSDrarklaehelleatervnllnSQNTGLINQKKKLESDLSMLsNEVDDAV 1806
Cdd:pfam05622 322 ELETQNRLANQRILELQQQVEELQKALQEQG---------------------SKAEDSSLLKQKLEEHLEKL-HEAQSEL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1807 QECRNA-EEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQ---TIKDLQMRLDEAEQIALKGGKKQVLKLE 1877
Cdd:pfam05622 380 QKKKEQiEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksVIKTLDPKQNPASPPEIQALKNQLLEKD 459
|
490
....*....|.
gi 2108526737 1878 ARVKELENELE 1888
Cdd:pfam05622 460 KKIEHLERDFE 470
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1502-1994 |
2.35e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1502 VLDKKQRNFDKVLAEWRQKYE----ECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQI 1577
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEEKEEkdlhERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1578 SQGVKTIHELEKMKKGLDMEKSEIQAALEEAEgtlehEESKSLRIQLELNQIKAD-VDRKLAEKDEEIDSLRRnhqrilE 1656
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELE-----EERDDLLAEAGLDDADAEaVEARREELEDRDEELRD------R 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1657 SMQATLDAEAKsRNEAVRLRKKMEgDLNEmevqlshanrQASEsqkflrnLQVQIKDIQLELDETihqneelkeQVAVTE 1736
Cdd:PRK02224 330 LEECRVAAQAH-NEEAESLREDAD-DLEE----------RAEE-------LREEAAELESELEEA---------REAVED 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1737 RRNnllaaEVEELRALLEQSDRARKLAEHELLEATERVNLLNSQNTGLINQKKKLESDLSmlsnEVDDAVQECRNAEEKA 1816
Cdd:PRK02224 382 RRE-----EIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR----TARERVEEAEALLEAG 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1817 KkaitdaammAEELKKEQDTSAHLERMKKNMEQtIKDLQMRLDEAEQialkggkkQVLKLEARVKELEN--ELESEQKKS 1894
Cdd:PRK02224 453 K---------CPECGQPVEGSPHVETIEEDRER-VEELEAELEDLEE--------EVEEVEERLERAEDlvEAEDRIERL 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1895 QEYQKGVrkyERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEER---- 1970
Cdd:PRK02224 515 EERREDL---EELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERiesl 591
|
490 500
....*....|....*....|....
gi 2108526737 1971 ADMAESQAnkLRARTRDQGSKLAE 1994
Cdd:PRK02224 592 ERIRTLLA--AIADAEDEIERLRE 613
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1352-1994 |
2.42e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1352 LEEREAMvSQLQRAKNSFsQNVEDLKKQLEEENKAKNALAHALQssrhdcdlLREQYDEEQEAKADLQRALSKANAEVAQ 1431
Cdd:COG4913 218 LEEPDTF-EAADALVEHF-DDLERAHEALEDAREQIELLEPIRE--------LAERYAAARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1432 wrTKYETdAIQRTEELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTE-IEDLVIDLERANAAAAVLDKKQRNF 1510
Cdd:COG4913 288 --RRLEL-LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1511 DKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDhleTIKRENKNLQEEIADLSDQISqgvktihELEKM 1590
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELRELEAEIA-------SLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1591 KKGLDMEKSEIQAALEEAEGTLEHEesksLRIQLELNQIKAD--------------------VD-RKLAEKDEEIDSLRR 1649
Cdd:COG4913 435 KSNIPARLLALRDALAEALGLDEAE----LPFVGELIEVRPEeerwrgaiervlggfaltllVPpEHYAAALRWVNRLHL 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1650 NHQRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSH-----ANRQASESQKFLRN------LQVQI------- 1711
Cdd:COG4913 511 RGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAelgrrFDYVCVDSPEELRRhpraitRAGQVkgngtrh 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1712 -KDIQLELDE-------TIHQNEELKEQVAVTERRNNLLAAEVEELRALLEQsDRARKLAEHELLEAT-ERVNLLNSQNT 1782
Cdd:COG4913 591 eKDDRRRIRSryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDA-LQERREALQRLAEYSwDEIDVASAERE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1783 --GLINQKKKLESDLSMLSnEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQdtsahlermkKNMEQTIKDLQMRLDE 1860
Cdd:COG4913 670 iaELEAELERLDASSDDLA-ALEEQLEELEAELEELEEELDELKGEIGRLEKEL----------EQAEEELDELQDRLEA 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1861 AEQIALKGgkkQVLKLEARVKELENElESEQKKSQEYQKGVRKYERRIKELSyqgeedkknlvrlQDLIDKMQAkvksYK 1940
Cdd:COG4913 739 AEDLARLE---LRALLEERFAAALGD-AVERELRENLEERIDALRARLNRAE-------------EELERAMRA----FN 797
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2108526737 1941 RQTEEAEEQANTNLSKYRKLQHELDDAEERaDMAESQANKLRARTRDQGSKLAE 1994
Cdd:COG4913 798 REWPAETADLDADLESLPEYLALLDRLEED-GLPEYEERFKELLNENSIEFVAD 850
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
901-1117 |
3.32e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.96 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 901 LRSATTEKELVSLKEELAKLKEALEKSEVKRKELEERQ--VSLIQEKNDLSLQLQAEQDNLADAEDRcdlliktKIQLEA 978
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAE-------LAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 979 KVKEIMERLEDEEEMSANVLAkkrklEDECAELKKDIDDLEITLAkvEKEKHATEN--KVKNLIEEMAALdetilkltke 1056
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL---------- 303
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2108526737 1057 KKALLEAHQQTLDDLQAEedkVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLE 1117
Cdd:COG3206 304 RAQLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1519-1738 |
1.21e-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: 59.39 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1519 QKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEK 1598
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1599 SEIQAALEEAEGTLEHEESKSlRIQLELNQIKA-DVDRKLaekdEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRK 1677
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQP-PLALLLSPEDFlDAVRRL----QYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2108526737 1678 KMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERR 1738
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
902-1334 |
1.82e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 902 RSATTEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVK 981
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 982 EIMERLEDEEEMSAnvlakkrklEDECAELKKDIDDLEI--TLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKA 1059
Cdd:PRK02224 437 TARERVEEAEALLE---------AGKCPECGQPVEGSPHveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1060 llEAHQQTLDDlqAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVR---RKLEGDLKLSLESVMDLENDKQQ 1136
Cdd:PRK02224 508 --EDRIERLEE--RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKReaaAEAEEEAEEAREEVAELNSKLAE 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1137 LDEKLKKKDfemnemstRIEDEQALVNQLQKKIKELQARteeleeeleadRACRAKVEKQRSDvareleelserleeagg 1216
Cdd:PRK02224 584 LKERIESLE--------RIRTLLAAIADAEDEIERLREK-----------REALAELNDERRE----------------- 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1217 atsaqiEMNKKREAdflklRRDLEEAmlHHEATTAALRKKHA----------DSVAELSEQIDSLQR----VKQKLEkER 1282
Cdd:PRK02224 628 ------RLAEKRER-----KRELEAE--FDEARIEEAREDKEraeeyleqveEKLDELREERDDLQAeigaVENELE-EL 693
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2108526737 1283 SEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAK-ADELQRQLNET 1334
Cdd:PRK02224 694 EELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRnVETLERMLNET 746
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1153-1769 |
2.58e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1153 TRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEELSERLEEAgGATSAQIEMNKKREADF 1232
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL-PELREELEKLEKEVKEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1233 LKLRRDLEEAMLHHEATTAALRKKHADsVAELSEQIDSLQRVKQKLEKERSEAKmEVDDLASTVEQLSKGKATSEKMCRL 1312
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEK-IRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1313 YEDQMNEAKAKADELQRQLNETNTQRARAQ---AESGELSRKLEEREAMVSQLQRAKnSFSQNVEDLKKQLEEENKAKna 1389
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEelkKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTPEK-- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1390 lahalqssrhdcdlLREQYDEEQEAKADLQRALSKANAEVAQWRTKyETDAIQRTEELEEAKKKLVTRLQEAEETVEtsn 1469
Cdd:PRK03918 389 --------------LEKELEELEKAKEEIEEEISKITARIGELKKE-IKELKKAIEELKKAKGKCPVCGRELTEEHR--- 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1470 akcsslEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQ--KYEECQSELETSQKESRGLSTELFKLKN 1547
Cdd:PRK03918 451 ------KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEELEKKA 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1548 S-YEETLDHLETIKRENKNLQEEIadlsdqisqgvKTIHELEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRiqlel 1626
Cdd:PRK03918 525 EeYEKLKEKLIKLKGEIKSLKKEL-----------EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVE----- 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1627 nqikadvdrklaEKDEEIDSLRRNHQRILE------SMQATLDAEAKSRNEAVRLRKKM---EGDLNEMEVQLSHANRQA 1697
Cdd:PRK03918 589 ------------ELEERLKELEPFYNEYLElkdaekELEREEKELKKLEEELDKAFEELaetEKRLEELRKELEELEKKY 656
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2108526737 1698 SESQ-KFLRNLQVQIKDIQLELDETIHQNEELKEQVavterrnnllAAEVEELRALLEQSDRARKlaEHELLE 1769
Cdd:PRK03918 657 SEEEyEELREEYLELSRELAGLRAELEELEKRREEI----------KKTLEKLKEELEEREKAKK--ELEKLE 717
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1314-1534 |
3.04e-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: 58.24 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1314 EDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHA 1393
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1394 LQssrhdcDLLREQYDEEQEAKADLqrALSKANAEVAQWRTKYETDAIQ----RTEELEEAKKKLVTRLQEAEETVETsn 1469
Cdd:COG4942 106 LA------ELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAParreQAEELRADLAELAALRAELEAERAE-- 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526737 1470 akcssLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKE 1534
Cdd:COG4942 176 -----LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1636-1894 |
3.10e-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: 58.24 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1636 KLAEKDEEIDSLRRNhqriLESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQ 1715
Cdd:COG4942 21 AAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1716 LELDEtihQNEELKEQVAVTERRNNllaaeVEELRALLEQSDrarklaeheLLEATERVNLLNSQNTGLINQKKKLESDL 1795
Cdd:COG4942 97 AELEA---QKEELAELLRALYRLGR-----QPPLALLLSPED---------FLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1796 smlsnevdDAVQECRNAEEKAKKAITDAAMMAEELKKEqdtsahLERMKKNMEQTIKDLQMRLDEAEQiALKGGKKQVLK 1875
Cdd:COG4942 160 --------AELAALRAELEAERAELEALLAELEEERAA------LEALKAERQKLLARLEKELAELAA-ELAELQQEAEE 224
|
250
....*....|....*....
gi 2108526737 1876 LEARVKELENELESEQKKS 1894
Cdd:COG4942 225 LEALIARLEAEAAAAAERT 243
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
900-1731 |
3.44e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 900 LLRSATT-EKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAE--DRC--DLLiktki 974
Cdd:PRK04863 284 HLEEALElRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEkiERYqaDLE----- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 975 QLEAKVKEIMERLEDEEEMSANVLAKKRKLEDECAELKKDIDDL-------------------------------EITLA 1023
Cdd:PRK04863 359 ELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYqqaldvqqtraiqyqqavqalerakqlcglpDLTAD 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1024 KVEKEKHATENKVKNLIEEMAALdETILKLTKEKKALLE-----------------AHQQTLDDL-QAEEDKvnILTKAK 1085
Cdd:PRK04863 439 NAEDWLEEFQAKEQEATEELLSL-EQKLSVAQAAHSQFEqayqlvrkiagevsrseAWDVARELLrRLREQR--HLAEQL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1086 AKLEQQVDDLEGSLEQEKklrmDLERVRRKLEGDLKLSLESVMDLENDKQQLDEKLKKKDFEMNEMSTRIEDEQALVNQL 1165
Cdd:PRK04863 516 QQLRMRLSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQL 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1166 QKKIKELQARteeleeeLEADRACRAKVEKQRSDVARELeelserleeaggATSAQIEmnkkreadflklrrDLEEAMLH 1245
Cdd:PRK04863 592 QARIQRLAAR-------APAWLAAQDALARLREQSGEEF------------EDSQDVT--------------EYMQQLLE 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1246 HEATTAALRKKHADSVAELSEQIDSLQ--------RVKQKLEKERSEAKME-------------------------VDDL 1292
Cdd:PRK04863 639 RERELTVERDELAARKQALDEEIERLSqpggsedpRLNALAERFGGVLLSEiyddvsledapyfsalygparhaivVPDL 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1293 ASTVEQLSKGKATSEKmcrLY-----EDQMNEAKAKADELQRQLNETNTQRA-------------RA---------QAES 1345
Cdd:PRK04863 719 SDAAEQLAGLEDCPED---LYliegdPDSFDDSVFSVEELEKAVVVKIADRQwrysrfpevplfgRAarekrieqlRAER 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1346 GELSRKLEEREAMVSQLQRAKNSFSQNV---------EDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKA 1416
Cdd:PRK04863 796 EELAERYATLSFDVQKLQRLHQAFSRFIgshlavafeADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLS 875
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1417 DLQRALSKANaevaqwrTKYETDAIQRTEELEEAkkklVTRLQEAEETVETSNAKCSSLEKTkhrlqteiedlvidlera 1496
Cdd:PRK04863 876 ALNRLLPRLN-------LLADETLADRVEEIREQ----LDEAEEAKRFVQQHGNALAQLEPI------------------ 926
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1497 naaAAVLDKKQRNFDKVlaewRQKYEECQSELETSQKESRGLsTELFKLKN--SYEETLDHLetikrenknlqEEIADLS 1574
Cdd:PRK04863 927 ---VSVLQSDPEQFEQL----KQDYQQAQQTQRDAKQQAFAL-TEVVQRRAhfSYEDAAEML-----------AKNSDLN 987
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1575 DQISQgvktihelekmkkgldmekseiqaaleeaegTLEHEESKSLRIQLELNQIKA---DVDRKLAEKDEEIDSLRRNH 1651
Cdd:PRK04863 988 EKLRQ-------------------------------RLEQAEQERTRAREQLRQAQAqlaQYNQVLASLKSSYDAKRQML 1036
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1652 QRILESMQA---TLDAEAKSRneAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKdiqlELDETIHQNEEL 1728
Cdd:PRK04863 1037 QELKQELQDlgvPADSGAEER--ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLR----KLERDYHEMREQ 1110
|
...
gi 2108526737 1729 KEQ 1731
Cdd:PRK04863 1111 VVN 1113
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
975-1360 |
3.87e-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: 58.37 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 975 QLEAKVKEIMERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLT 1054
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1055 KEKKALLEAHQQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDK 1134
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1135 QQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVAreleelserlEEA 1214
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS----------SMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1215 GGATSAQIEMNKKR-EADFLKLR-RDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDL 1292
Cdd:pfam07888 265 AQRDRTQAELHQARlQAAQLTLQlADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKL 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2108526737 1293 ASTVEQlskgkatsEKMCRLYedQMNEAKAKADELQRQLNETNTQRARAQAESGEL---SRKLEEREAMVS 1360
Cdd:pfam07888 345 EVELGR--------EKDCNRV--QLSESRRELQELKASLRVAQKEKEQLQAEKQELleyIRQLEQRLETVA 405
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
907-1174 |
4.63e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 907 EKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEIMER 986
Cdd:PRK03918 492 ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEE 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 987 LedeeemsANVLAKKRKLEDEC-AELKKDIDDLE------ITLAKVEKEKHATENKVKNLIEEmaaLDETILKLTKEKKA 1059
Cdd:PRK03918 572 L-------AELLKELEELGFESvEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEE---LDKAFEELAETEKR 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1060 LLEAHQQtLDDLQAEEDKvniltkakakleqqvDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQLDE 1139
Cdd:PRK03918 642 LEELRKE-LEELEKKYSE---------------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
250 260 270
....*....|....*....|....*....|....*
gi 2108526737 1140 KLKKKdfemnEMSTRIEDEQALVNQLQKKIKELQA 1174
Cdd:PRK03918 706 REKAK-----KELEKLEKALERVEELREKVKKYKA 735
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
896-1078 |
4.76e-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: 56.09 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 896 KIKPLLRSATTEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRcdlliktkiq 975
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 976 lEAKVKEIMERLEDEEEMSAnvlakkrkLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTK 1055
Cdd:COG1579 75 -IKKYEEQLGNVRNNKEYEA--------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
170 180
....*....|....*....|...
gi 2108526737 1056 EKKALLEAHQQTLDDLQAEEDKV 1078
Cdd:COG1579 146 ELDEELAELEAELEELEAEREEL 168
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1291-1795 |
7.05e-08 |
|
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: 57.83 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1291 DLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETntqRARAQAESGELsRKLEEREAMVSQLQRAKnsfS 1370
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRE---SDRNQELQKRI-RLLEKREAEAEEALREQ---A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1371 QNVEDLKKQLEEENKAKNALAHALQSSRhdcDLLREQYDEeqeaKADLQRALSKANAEVAqwRTKYETDAIQRTEELEEA 1450
Cdd:pfam05557 76 ELNRLKKKYLEALNKKLNEKESQLADAR---EVISCLKNE----LSELRRQIQRAELELQ--STNSELEELQERLDLLKA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1451 KkklvtrLQEAEETVETSNAKCSSLEKTKHRLQTEI------EDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQ----- 1519
Cdd:pfam05557 147 K------ASEAEQLRQNLEKQQSSLAEAEQRIKELEfeiqsqEQDSEIVKNSKSELARIPELEKELERLREHNKHlneni 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1520 ------------------KYEECQSELETSQKESRGLSTEL---FKLKNSYEETLDHLETIKRENKNLQEEIADLSDQIS 1578
Cdd:pfam05557 221 enklllkeevedlkrkleREEKYREEAATLELEKEKLEQELqswVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1579 QGVKTIHELEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQlelnqikadvdRKLAEKDEEIDSLRrnhqRILESM 1658
Cdd:pfam05557 301 SLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ-----------RRVLLLTKERDGYR----AILESY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1659 QATLDAEAKSRNEAVRLRK------KMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQ------------LELDE 1720
Cdd:pfam05557 366 DKELTMSNYSPQLLERIEEaedmtqKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRqqesladpsyskEEVDS 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1721 TIHQNEELKEQVAVTERRNNLLAAEVE--ELRALLEQSD-RARKLAEHELLEATER----VNLLNSQNTGLINQKKKLES 1793
Cdd:pfam05557 446 LRRKLETLELERQRLREQKNELEMELErrCLQGDYDPKKtKVLHLSMNPAAEAYQQrknqLEKLQAEIERLKRLLKKLED 525
|
..
gi 2108526737 1794 DL 1795
Cdd:pfam05557 526 DL 527
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1230-1613 |
8.41e-08 |
|
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: 57.65 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1230 ADFLklrRDLEEAMLHHEATtAALRKKHADSVAELSEQIDSLQRVKQKL-EKERSEAKMEvDDLASTVEQLSK---GKAT 1305
Cdd:COG3096 271 ADYM---RHANERRELSERA-LELRRELFGARRQLAEEQYRLVEMARELeELSARESDLE-QDYQAASDHLNLvqtALRQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1306 SEKMCRlYEDQMNEAKAKADELQRQLNETNTQRARAQAEsgeLSRKLEEREAMVSQL---QRAKNS-------FSQNVED 1375
Cdd:COG3096 346 QEKIER-YQEDLEELTERLEEQEEVVEEAAEQLAEAEAR---LEAAEEEVDSLKSQLadyQQALDVqqtraiqYQQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1376 LKK---QLEEEN-KAKNALAHALQssrhdcdlLREQYDEEQEAKADLQRALSKANAEVAQWRTKYE-----TDAIQRTEE 1446
Cdd:COG3096 422 LEKaraLCGLPDlTPENAEDYLAA--------FRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvckiAGEVERSQA 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1447 LEEAKKKLVT--RLQEAEETVETSNAKCSSLEKTKHRLQteiedlviDLERANAAAAVLDKKQRN----FDKVLAEWRQK 1520
Cdd:COG3096 494 WQTARELLRRyrSQQALAQRLQQLRAQLAELEQRLRQQQ--------NAERLLEEFCQRIGQQLDaaeeLEELLAELEAQ 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1521 YEECQSELETSQKESRGLSTELFKLKNSYEEtldhLETIKRENKNLQEEIADLSDQISQGVKTIHEL-EKMKKGLD---- 1595
Cdd:COG3096 566 LEELEEQAAEAVEQRSELRQQLEQLRARIKE----LAARAPAWLAAQDALERLREQSGEALADSQEVtAAMQQLLErere 641
|
410 420
....*....|....*....|
gi 2108526737 1596 --MEKSEIQAALEEAEGTLE 1613
Cdd:COG3096 642 atVERDELAARKQALESQIE 661
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1710-1946 |
9.03e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1710 QIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRALLEQSDRARKLAEHELLEATERVNLLNSQNTGLINQKK 1789
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1790 KLESDLSMLSnevddavqecRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQI--ALK 1867
Cdd:COG4942 101 AQKEELAELL----------RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALraELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2108526737 1868 GGKKQVLKLEARVKELENELESEQkksQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEA 1946
Cdd:COG4942 171 AERAELEALLAELEEERAALEALK---AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
900-1117 |
9.77e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 900 LLRSATTEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAK 979
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 980 VKEIMERLEDEEEMSANVLAK--KRKLEDECAEL--KKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTK 1055
Cdd:COG4942 92 IAELRAELEAQKEELAELLRAlyRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108526737 1056 EKKALLEAHQQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLE 1117
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
642-736 |
1.05e-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: 53.50 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 642 GVVPY---NIIGWLDKNKDPLNETVVACFRKSSNKLLASLYEnyvgSDAAFDSKTGSKEKRKKAASFQTV------SQVH 712
Cdd:cd01363 71 GVIPYlasVAFNGINKGETEGWVYLTEITVTLEDQILQANPI----LEAFGNAKTTRNENSSRFGKFIEIlldiagFEII 146
|
90 100
....*....|....*....|....
gi 2108526737 713 KENLNKLMTNLRSTQPHFVRCIIP 736
Cdd:cd01363 147 NESLNTLMNVLRATRPHFVRCISP 170
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
907-1282 |
1.87e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 907 EKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQekndlSLQLQAEQDNLADAEDRCDlliktkiQLEAKvkeiMER 986
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQR-----LAEYSWDEIDVASAEREIA-------ELEAE----LER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 987 LEDeeemSANVLakkRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALLEAHqq 1066
Cdd:COG4913 680 LDA----SSDDL---AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL-- 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1067 tLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQ-EKKLRMDLERVRRKLEGDLKLSLESVMDLEndkqqldeklkkkD 1145
Cdd:COG4913 751 -LEERFAAALGDAVERELRENLEERIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLP-------------E 816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1146 FEmnEMSTRIEDEqALVnQLQKKIKELQARTEELEEELEAdracrAKVEKQRSDVARELEE--LSERLEEAGGATSAQIE 1223
Cdd:COG4913 817 YL--ALLDRLEED-GLP-EYEERFKELLNENSIEFVADLL-----SKLRRAIREIKERIDPlnDSLKRIPFGPGRYLRLE 887
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2108526737 1224 MNKKREADFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKER 1282
Cdd:COG4913 888 ARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRSEEEESDRRWRAR 946
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1314-1540 |
2.15e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1314 EDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHA 1393
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1394 LQSSRHDCDLL---------------REQYDEEQEAKADLQRALSKANAEVAQwrtkYETDAIQRTEELEEAKKKLVTRL 1458
Cdd:COG3883 95 LYRSGGSVSYLdvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEA----KKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1459 QEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGL 1538
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
..
gi 2108526737 1539 ST 1540
Cdd:COG3883 251 AA 252
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1266-1663 |
2.56e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 56.07 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1266 EQIDSLQRVKQK---LEKERSEAKMEVDDLASTVEQLsKGKATSEKMCRLyedqmneAKAKADELQRQLNETNTQRARAQ 1342
Cdd:PRK11281 70 ALLDKIDRQKEEteqLKQQLAQAPAKLRQAQAELEAL-KDDNDEETRETL-------STLSLRQLESRLAQTLDQLQNAQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1343 AESGELSRKLeerEAMVSQLQRAKNSFSQNVedlkKQLEEENKAKNALAHALQSSRHDcdlLREQYDEEQ---EAKADLQ 1419
Cdd:PRK11281 142 NDLAEYNSQL---VSLQTQPERAQAALYANS----QRLQQIRNLLKGGKVGGKALRPS---QRVLLQAEQallNAQNDLQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1420 RALSKANA---EVAQWRTKYETDAIQRTEELEEAKKKLVT--RLQEAEETVE-------TSNAKCSSLEKTKHRLQTEI- 1486
Cdd:PRK11281 212 RKSLEGNTqlqDLLQKQRDYLTARIQRLEHQLQLLQEAINskRLTLSEKTVQeaqsqdeAARIQANPLVAQELEINLQLs 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1487 EDLVIDLERANA-------AAAVLD---KKQRNFD---KVLaewrqkyeecqseletsqKESRGLSTELFKLKnsyeETL 1553
Cdd:PRK11281 292 QRLLKATEKLNTltqqnlrVKNWLDrltQSERNIKeqiSVL------------------KGSLLLSRILYQQQ----QAL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1554 DHLETIkrenKNLQEEIADL----------SDQISQGVKTIHELEKmkkgldMEKSEIQAALEEAEGTLEHEESKSL-RI 1622
Cdd:PRK11281 350 PSADLI----EGLADRIADLrleqfeinqqRDALFQPDAYIDKLEA------GHKSEVTDEVRDALLQLLDERRELLdQL 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2108526737 1623 QLELNqikadvdrklAEKDEEIdSLRRNHQRIL---ESMQATLD 1663
Cdd:PRK11281 420 NKQLN----------NQLNLAI-NLQLNQQQLLsvsDSLQSTLT 452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1440-1673 |
3.51e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1440 AIQRTEELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQ 1519
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1520 KYEECQSELE----TSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLsdqisqgVKTIHELEKMKKGLD 1595
Cdd:COG4942 98 ELEAQKEELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-------RADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2108526737 1596 MEKSEIQAALEEAEgtlehEESKSL-RIQLELNQIKADVDRKLAEKDEEIDSLRRNHQRiLESMQATLDAEAKSRNEAV 1673
Cdd:COG4942 171 AERAELEALLAELE-----EERAALeALKAERQKLLARLEKELAELAAELAELQQEAEE-LEALIARLEAEAAAAAERT 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
908-1330 |
3.52e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 908 KELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQD--NLADAEDRCDLLIKTKIQLEAKVKEIME 985
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 986 RLEDEEEMSANVLAKKRKLEDECA-----------ELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLT 1054
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEqlslateeelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1055 KEKK-----------ALLEAHQQTLDDLQAEEDKV---------------NILTKAKAKLEQQVDDLEGSLEQEKKLRMD 1108
Cdd:COG4717 241 LEERlkearlllliaAALLALLGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1109 LERVRRKLEGDLKLSLESVMDLENDKQQLDEKLKKKdfemnemstRIEDEQALVNQLQKKIKELQARteeleeeleadra 1188
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREA---------EELEEELQLEELEQEIAALLAE------------- 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1189 crakvekqrsdvareleelserleeAGGATSAQIEMNKKREADFLKLRRDLEEAMLH-HEATTAALRKKHADSVAELSEQ 1267
Cdd:COG4717 379 -------------------------AGVEDEEELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEE 433
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2108526737 1268 IDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKmcrlyEDQMNEAKAKADELQRQ 1330
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEAELEQLEEDGELAEL-----LQELEELKAELRELAEE 491
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
914-1935 |
3.58e-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: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 914 KEELAKLKEALEKSEVKRKELEERQVSLiQEKNDLSLQLQAEQDNLADA----EDRCDLLIKTKIQLEAKVKEImerlED 989
Cdd:TIGR01612 540 KEIEAGLKESYELAKNWKKLIHEIKKEL-EEENEDSIHLEKEIKDLFDKyleiDDEIIYINKLKLELKEKIKNI----SD 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 990 EEEMSANVLAKKRKLEDECAElkkdIDDL-EITLAKVEKEKHATENKVKNLIEEMAALDE-TILKLTKEKKALLEAH--- 1064
Cdd:TIGR01612 615 KNEYIKKAIDLKKIIENNNAY----IDELaKISPYQVPEHLKNKDKIYSTIKSELSKIYEdDIDALYNELSSIVKENaid 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1065 ----QQTLDDLQAEEDKV--NILTKAKAKLEQQVDDLEgslEQEKKLRMDLERVRRKLEGDLKLSLESVM-DLENDKQQL 1137
Cdd:TIGR01612 691 ntedKAKLDDLKSKIDKEydKIQNMETATVELHLSNIE---NKKNELLDIIVEIKKHIHGEINKDLNKILeDFKNKEKEL 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1138 DEKLKKKDFEMNEMstriedeqalvNQLQKKIKELQAR-TEELEEELEADRACRAKVEKQRSDVARELEELSERLEEAGG 1216
Cdd:TIGR01612 768 SNKINDYAKEKDEL-----------NKYKSKISEIKNHyNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINE 836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1217 ATSAQIEMNKKREAdFLKLRRDLEEAM-LHHEATTAALRKKHA----DSVAELSEQIDSLQRVKQKLEKERSEAKMEVDD 1291
Cdd:TIGR01612 837 MKFMKDDFLNKVDK-FINFENNCKEKIdSEHEQFAELTNKIKAeisdDKLNDYEKKFNDSKSLINEINKSIEEEYQNINT 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1292 LASTVEQLSKGKATSEKMCRLYEDQmNEAKAKADELQRQLNETNT-QRARAQAESGELSRKLEE-----REAMVSQLQRA 1365
Cdd:TIGR01612 916 LKKVDEYIKICENTKESIEKFHNKQ-NILKEILNKNIDTIKESNLiEKSYKDKFDNTLIDKINEldkafKDASLNDYEAK 994
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1366 KNSFSQNVEDLKkqleeENKAKNalahalqssrhDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTE 1445
Cdd:TIGR01612 995 NNELIKYFNDLK-----ANLGKN-----------KENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIID 1058
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1446 ELEEAKKKLVTRLQEaeETVETSNAKCSSLEKTKHRLQT-EIEDLVID--LERANAAAAV------LDKKQRNFDKVLAE 1516
Cdd:TIGR01612 1059 EIEKEIGKNIELLNK--EILEEAEINITNFNEIKEKLKHyNFDDFGKEenIKYADEINKIkddiknLDQKIDHHIKALEE 1136
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1517 WRQKYEECQSELETS--------------------QKESRGLSTELFKLKNSYEET---LDHLETIKRENKNLqEEIADL 1573
Cdd:TIGR01612 1137 IKKKSENYIDEIKAQindledvadkaisnddpeeiEKKIENIVTKIDKKKNIYDEIkklLNEIAEIEKDKTSL-EEVKGI 1215
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1574 SDQISQGVKTIHeLEKM----KKGLDMEKS-----EIQAALEEAEGTLEHEESKSLRIQLELN--QIKADVDRKL----A 1638
Cdd:TIGR01612 1216 NLSYGKNLGKLF-LEKIdeekKKSEHMIKAmeayiEDLDEIKEKSPEIENEMGIEMDIKAEMEtfNISHDDDKDHhiisK 1294
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1639 EKDEEIDSLRRNHQRILE--SMQATLDAEAKSRNEAVRLRKKMEGDLNEME---------VQLSHANRQASESQKFLRNL 1707
Cdd:TIGR01612 1295 KHDENISDIREKSLKIIEdfSEESDINDIKKELQKNLLDAQKHNSDINLYLneianiyniLKLNKIKKIIDEVKEYTKEI 1374
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1708 QVQIKDIQLELD------ETIHQNEELKE-----QVAVTERRNNLLAAEVEELRA--LLEQSDRARKLAEHEllEATERV 1774
Cdd:TIGR01612 1375 EENNKNIKDELDksekliKKIKDDINLEEckskiESTLDDKDIDECIKKIKELKNhiLSEESNIDTYFKNAD--ENNENV 1452
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1775 nLLNSQNTGLINQKKK--LESDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEqdtsahlermKKNMEQTIK 1852
Cdd:TIGR01612 1453 -LLLFKNIEMADNKSQhiLKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKN----------KELFEQYKK 1521
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1853 DLQMRLDEAEQIALKGG----KKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDL 1928
Cdd:TIGR01612 1522 DVTELLNKYSALAIKNKfaktKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLS 1601
|
....*..
gi 2108526737 1929 IDKMQAK 1935
Cdd:TIGR01612 1602 LENFENK 1608
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1522-1781 |
4.36e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 55.30 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1522 EECQSELETSQKeSRGLSTELFKLKNSYEETLDHLETIKRENKNL-----------------QEEIADLSDQISQGVKTI 1584
Cdd:PRK11281 39 ADVQAQLDALNK-QKLLEAEDKLVQQDLEQTLALLDKIDRQKEETeqlkqqlaqapaklrqaQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1585 H------ELEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLEL--NQIKAD-VDRKLAEKDEEIDSLRRNHQRIL 1655
Cdd:PRK11281 118 LstlslrQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALyaNSQRLQqIRNLLKGGKVGGKALRPSQRVLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1656 ESMQATLDAEAKSRneavrlRKKMEG-----DLNEMEVQLSHANRQASESQkfLRNLQVQIKDIQLELDE-TIHQNEELK 1729
Cdd:PRK11281 198 QAEQALLNAQNDLQ------RKSLEGntqlqDLLQKQRDYLTARIQRLEHQ--LQLLQEAINSKRLTLSEkTVQEAQSQD 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2108526737 1730 EQVAVTErrNNLLAAEVEELRALleqSDRarklaeheLLEATERVNLLNSQN 1781
Cdd:PRK11281 270 EAARIQA--NPLVAQELEINLQL---SQR--------LLKATEKLNTLTQQN 308
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1724-1906 |
6.27e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1724 QNEELKEQVAVTERRNNLLAAEVEELRALLEQSDRARK--LAEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLSNE 1801
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1802 VDdAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNMEQTIKDLQMRLDEAEQIALKGGKK 1871
Cdd:COG3206 242 LA-ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEA 320
|
170 180 190
....*....|....*....|....*....|....*
gi 2108526737 1872 QVLKLEARVKELENELESEQKKSQEYQKGVRKYER 1906
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1217-1987 |
7.39e-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: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1217 ATSAQIEMNKKREADFLKLRRDLEEAMLhheattaalrkkhaDSVAELSEQIDSLQRVKQKLEKERSEAKME-VDDLAST 1295
Cdd:TIGR00606 234 ESSREIVKSYENELDPLKNRLKEIEHNL--------------SKIMKLDNEIKALKSRKKQMEKDNSELELKmEKVFQGT 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1296 VEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLE--EREAMVSQLQRAKNSFSQNV 1373
Cdd:TIGR00606 300 DEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADrhQEHIRARDSLIQSLATRLEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1374 EDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKK 1453
Cdd:TIGR00606 380 DGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFV 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1454 lVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAavLDKKQRNFDKVLAEWRQKYEEcqseletsqk 1533
Cdd:TIGR00606 460 -IKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKS--LQNEKADLDRKLRKLDQEMEQ---------- 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1534 esrglstelfklKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGV--------------KTIHELEKMKKGLDMEKS 1599
Cdd:TIGR00606 527 ------------LNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELtsllgyfpnkkqleDWLHSKSKEINQTRDRLA 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1600 EIQAALEEAEGTLEHEESKSLRIQLELNQIKADVDRKLAEKDEEIDslrrnhqriLESMQATLDAEAKSRNEAVRLRKKM 1679
Cdd:TIGR00606 595 KLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESD---------LERLKEEIEKSSKQRAMLAGATAVY 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1680 EGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRALLEqsdra 1759
Cdd:TIGR00606 666 SQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIID----- 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1760 rkLAEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLSNEvddavqecrnaEEKAKKAITDAAMMaEELKKEqdtsah 1839
Cdd:TIGR00606 741 --LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE-----------EESAKVCLTDVTIM-ERFQME------ 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1840 LERMKKNMEQTIKDLQ-MRLDEAEQIAlkggKKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEED 1918
Cdd:TIGR00606 801 LKDVERKIAQQAAKLQgSDLDRTVQQV----NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQI 876
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526737 1919 KKNLVRLQDLIDKMQAK---VKSYKRQTEEAEEQANTNLSKYRKLQHE----LDDAEERADMAESQANKLRARTRD 1987
Cdd:TIGR00606 877 GTNLQRRQQFEEQLVELsteVQSLIREIKDAKEQDSPLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKVKN 952
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1532-1987 |
7.66e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 54.44 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1532 QKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQI-SQGVKTIHELEKMKKGLDMekSEIQAALEEAEG 1610
Cdd:pfam10174 122 QSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLqSKGLPKKSGEEDWERTRRI--AEAEMQLGHLEV 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1611 TLEHEESKSLRIQLEL---NQIKADVDRKLA------EKDEEIDSLRRNHQRILESMQATldaeaksRNEAVRLRKKMEG 1681
Cdd:pfam10174 200 LLDQKEKENIHLREELhrrNQLQPDPAKTKAlqtvieMKDTKISSLERNIRDLEDEVQML-------KTNGLLHTEDREE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1682 DLNEMEVQLSHANRQASESQKFLRNLQ---VQIKDIQLELDETIHQN-------EELKEQVAVTERRNNLLAAEVEELRA 1751
Cdd:pfam10174 273 EIKQMEVYKSHSKFMKNKIDQLKQELSkkeSELLALQTKLETLTNQNsdckqhiEVLKESLTAKEQRAAILQTEVDALRL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1752 LLEQSDRARKLAEHELLEATERVNLLNSQNTGL----------INQ-KKKLESdlsmLSNEVDDAVQECRNAEEKAKKAI 1820
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLkdmldvkerkINVlQKKIEN----LQEQLRDKDKQLAGLKERVKSLQ 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1821 TDAAMMAEELKKEQDTSAHLERMKKNM-EQTIKDLQMRLDEAEQI--ALKGGKKQVLKLEARVKELENELESEQKKSQEY 1897
Cdd:pfam10174 429 TDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESLkkENKDLKEKVSALQPELTEKESSLIDLKEHASSL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1898 QKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQakvksykrQTEEAEEQANTNLSKYRKLQHELDDAEERADMAESQ 1977
Cdd:pfam10174 509 ASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAE 580
|
490
....*....|
gi 2108526737 1978 ANKLRARTRD 1987
Cdd:pfam10174 581 VERLLGILRE 590
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1217-1427 |
8.12e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1217 ATSAQIEMNKKREADFLKLRRDLEEAMlhheATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTV 1296
Cdd:COG4942 38 ELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1297 EQL-----------SKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRA 1365
Cdd:COG4942 114 YRLgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108526737 1366 KnsfsQNVEDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANA 1427
Cdd:COG4942 194 K----AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1261-1439 |
9.33e-07 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 53.05 E-value: 9.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1261 VAELSEQIdslqrvkqKLEKERSEakmevdDLASTVEQLSKGKATSEkmcrlyedqmneakAKADELQRQLNETNTQRAR 1340
Cdd:PRK09039 62 IAELADLL--------SLERQGNQ------DLQDSVANLRASLSAAE--------------AERSRLQALLAELAGAGAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1341 AQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLeeenkakNALAHALQSSrhdcdllrEQYDEEQEAK-ADLQ 1419
Cdd:PRK09039 114 AEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQL-------AALEAALDAS--------EKRDRESQAKiADLG 178
|
170 180
....*....|....*....|
gi 2108526737 1420 RALSKANAEVAQWRTKYETD 1439
Cdd:PRK09039 179 RRLNVALAQRVQELNRYRSE 198
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
901-1573 |
1.07e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 901 LRSATTEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQL-QAEQDNLADAEdrcdlliktkiqleak 979
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLE---------------- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 980 vKEImERLEDEeemsanvlakKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIE----EMAALDETILKLTK 1055
Cdd:COG4913 345 -REI-ERLERE----------LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEaleeELEALEEALAEAEA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1056 EKKALLEAHQQTLDDLQA-EEDKVNI---LTKAKAKLEQQVDDLEGSL----------EQEKKLRMDLERV----RRKL- 1116
Cdd:COG4913 413 ALRDLRRELRELEAEIASlERRKSNIparLLALRDALAEALGLDEAELpfvgelievrPEEERWRGAIERVlggfALTLl 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1117 --EGDLKLSLESVmDLENDKQQLD-EKLKKKDFEMNEMSTrieDEQALVNQLQKKIKELQARteelEEELEADRACRAKV 1193
Cdd:COG4913 493 vpPEHYAAALRWV-NRLHLRGRLVyERVRTGLPDPERPRL---DPDSLAGKLDFKPHPFRAW----LEAELGRRFDYVCV 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1194 EkqrsdvareleelserleeaggatsaqiemnkkREADFLKLRRDL-EEAMLHHEATtaalRKKHADSVAELS------- 1265
Cdd:COG4913 565 D---------------------------------SPEELRRHPRAItRAGQVKGNGT----RHEKDDRRRIRSryvlgfd 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1266 --EQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMcrlyeDQMNEAKAKADELQRQLNETNTQRARAQA 1343
Cdd:COG4913 608 nrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRL-----AEYSWDEIDVASAEREIAELEAELERLDA 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1344 ESGELsRKLEEreamvsQLQRAKnsfsQNVEDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRals 1423
Cdd:COG4913 683 SSDDL-AALEE------QLEELE----AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--- 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1424 kanAEVAQWRTKYETDAIQRT--EELEEAKKKLVTRLQEAEETVEtsnakcSSLEKTKHRLQTEIEDLVIDLERANAAAA 1501
Cdd:COG4913 749 ---ALLEERFAAALGDAVERElrENLEERIDALRARLNRAEEELE------RAMRAFNREWPAETADLDADLESLPEYLA 819
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108526737 1502 VLDKKQRNfdkVLAEWRQKYEEcqseletsqkesrglstelFKLKNSYEETLDHLETIKRENKNLQEEIADL 1573
Cdd:COG4913 820 LLDRLEED---GLPEYEERFKE-------------------LLNENSIEFVADLLSKLRRAIREIKERIDPL 869
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1410-1977 |
1.13e-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: 53.96 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1410 EEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEELEEaKKKLVTRLQEAEETVETSNakcsslEKTKHRLQTEIEDL 1489
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQE-NRKIIEAQRKAIQELQFEN------EKVSLKLEEEIQEN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1490 VIDLERANAA----------AAVLDKKQRNFDKVLAEWRQKYEECQSELETS---------QKESRGLSTElFKLKNSYE 1550
Cdd:pfam05483 144 KDLIKENNATrhlcnllketCARSAEKTKKYEYEREETRQVYMDLNNNIEKMilafeelrvQAENARLEMH-FKLKEDHE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1551 EtLDHLEtikrenKNLQEEIADLSDQISQGVKTIHELEKMKKGLD--MEKSEIQAALEEAEGTLEHEESKSL-----RIQ 1623
Cdd:pfam05483 223 K-IQHLE------EEYKKEINDKEKQVSLLLIQITEKENKMKDLTflLEESRDKANQLEEKTKLQDENLKELiekkdHLT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1624 LELNQIKADVDRKLAEK---DEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLShanrqasES 1700
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQkalEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR-------TE 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1701 QKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRALLEQSDRARKLAEHelLEATERvnllnsQ 1780
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEE--LKGKEQ------E 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1781 NTGLINQKKKLESDLSMlsnevddAVQECRNAEEKAKKAITDaamMAEELKKEQ----DTSAHLERM---KKNMEQTIKD 1853
Cdd:pfam05483 441 LIFLLQAREKEIHDLEI-------QLTAIKTSEEHYLKEVED---LKTELEKEKlkniELTAHCDKLlleNKELTQEASD 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1854 LQMRLDEAEQIALKGGKKQvlklEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQ 1933
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQE----ERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE 586
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2108526737 1934 AKVKSYKRQTEEAEEQANtNLSKYRKLQHELDDAEERADMAESQ 1977
Cdd:pfam05483 587 KQMKILENKCNNLKKQIE-NKNKNIEELHQENKALKKKGSAENK 629
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
979-1594 |
1.15e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 979 KVKEIMERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETIlkltKEKK 1058
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSAL----NELS 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1059 ALLEAHQQTLDDLQAEEDKvniltkaKAKLEQQVDDLEGSLEQEKKLRMDLERVRRklegdlklslESVMDLENDKQQLD 1138
Cdd:PRK01156 246 SLEDMKNRYESEIKTAESD-------LSMELEKNNYYKELEERHMKIINDPVYKNR----------NYINDYFKYKNDIE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1139 EKlkkkdfemNEMSTRIEDEQALVNQLQKKIKELQArteeleeeleaDRACRAKVEKQRSDVARELEELSERLEEAGGAT 1218
Cdd:PRK01156 309 NK--------KQILSNIDAEINKYHAIIKKLSVLQK-----------DYNDYIKKKSRYDDLNNQILELEGYEMDYNSYL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1219 SAQIEMNKKREADFLKLRR---DLEEAMLHHEATTAALRKKHAD---SVAELSEQIDSLQRVKQKLEkersEAKMEVDDL 1292
Cdd:PRK01156 370 KSIESLKKKIEEYSKNIERmsaFISEILKIQEIDPDAIKKELNEinvKLQDISSKVSSLNQRIRALR----ENLDELSRN 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1293 ASTVEQLSK--------GKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGEL-SRKLEEREAMVSQLQ 1363
Cdd:PRK01156 446 MEMLNGQSVcpvcgttlGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLeSEEINKSINEYNKIE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1364 RAKNSFSQNVEDLKKQLEEENKAKNALAhalQSSRHDCDLLREQYDEEQEAKADlqralskanaevaqwRTKYETDAIQ- 1442
Cdd:PRK01156 526 SARADLEDIKIKINELKDKHDKYEEIKN---RYKSLKLEDLDSKRTSWLNALAV---------------ISLIDIETNRs 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1443 RTEELEEAKKKLVTRLQEAEETVETSNakcSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYE 1522
Cdd:PRK01156 588 RSNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDS 664
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108526737 1523 ECQSELETSQKESRgLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGL 1594
Cdd:PRK01156 665 IIPDLKEITSRIND-IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
905-1513 |
1.17e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.97 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 905 TTEKELVSLKEELAKLKEALEKSEVKRKEL------EER-------QVSLIQEKNDLSLQ----LQAEQDNLADAEDRCD 967
Cdd:pfam15921 472 STKEMLRKVVEELTAKKMTLESSERTVSDLtaslqeKERaieatnaEITKLRSRVDLKLQelqhLKNEGDHLRNVQTECE 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 968 LLiktKIQLEAKVKEIMERLEDEEEMSANVLAKKRK---LEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMA 1044
Cdd:pfam15921 552 AL---KLQMAEKDKVIEILRQQIENMTQLVGQHGRTagaMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVS 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1045 ALDETILKLTKEKKALLEAhqqtLDDLQAEEDKV-NILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKlS 1123
Cdd:pfam15921 629 DLELEKVKLVNAGSERLRA----VKDIKQERDQLlNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLK-S 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1124 LESvmDLENDKQQLDEKLKKKDFEMN---EMSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDV 1200
Cdd:pfam15921 704 AQS--ELEQTRNTLKSMEGSDGHAMKvamGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTV 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1201 ARELEELSERLEEAGGATSAQIEMNKKREADFLKLRRDLEEA---MLHHEATTAALRKKHADSVAELS-EQIDSLQRVKQ 1276
Cdd:pfam15921 782 ATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECqdiIQRQEQESVRLKLQHTLDVKELQgPGYTSNSSMKP 861
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1277 KLEKERSEAKMEvDDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNT-QRARAQAES-----GELSR 1350
Cdd:pfam15921 862 RLLQPASFTRTH-SNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTvQLSKAEDKGrapslGALDD 940
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1351 KLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHALQ-SSRHDCDLLREQYDEEQEAKADLQRALSKANAEV 1429
Cdd:pfam15921 941 RVRDCIIESSLRSDICHSSSNSLQTEGSKSSETCSREPVLLHAGElEDPSSCFTFPSTASPSVKNSASRSFHSSPKKSPV 1020
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1430 AQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEET--VETSNAKCSSLEKTKHRLQTEIEDLVIdleRANAAAAVLDKKQ 1507
Cdd:pfam15921 1021 HSLLTSSAEGSIGSSSQYRSAKTIHSPDSVKDSQSlpIETTGKTCRKLQNRLESLQTLVEDLQL---KNQAMSSMIRNQE 1097
|
....*.
gi 2108526737 1508 RNFDKV 1513
Cdd:pfam15921 1098 KRIQKV 1103
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1341-1579 |
1.20e-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: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1341 AQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHALQSsrhdcdlLREQYDEEQEAKADLQR 1420
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA-------LEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1421 ALSKANAEVAQWRTKYET--DAIQRTEELEEAkkKLVTRLQEAEETVETSNAkcssLEKTKHRLQTEIEDLVIDLERANA 1498
Cdd:COG4942 91 EIAELRAELEAQKEELAEllRALYRLGRQPPL--ALLLSPEDFLDAVRRLQY----LKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1499 AAAVLDKKQRNFDKVLAEWRQKyeecQSELETSQKESRGLSTELFKLKNSYEETLDHLetiKRENKNLQEEIADLSDQIS 1578
Cdd:COG4942 165 LRAELEAERAELEALLAELEEE----RAALEALKAERQKLLARLEKELAELAAELAEL---QQEAEELEALIARLEAEAA 237
|
.
gi 2108526737 1579 Q 1579
Cdd:COG4942 238 A 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1412-1643 |
1.84e-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: 52.46 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1412 QEAKADLQRALSKANAEVAQwrtkyetdAIQRTEELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVI 1491
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAE--------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1492 DLERANAAaavLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIA 1571
Cdd:COG4942 91 EIAELRAE---LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108526737 1572 DLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLELNQIKADVDRKLAEKDEE 1643
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1541-1890 |
2.17e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 52.38 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1541 ELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAAL-------EEAEGTL- 1612
Cdd:pfam19220 49 RLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELrdktaqaEALERQLa 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1613 -EHEESKSLRIQLELNQIKADV-DRKLAEKDEEIDSLRRNHQRilesmqatldAEAKSRneavRLRKKMEgdlnEMEVQL 1690
Cdd:pfam19220 129 aETEQNRALEEENKALREEAQAaEKALQRAEGELATARERLAL----------LEQENR----RLQALSE----EQAAEL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1691 SHANRQASESQKFLRNLQVQIKDIQLELDETIHQNE----ELKEQVAVTERRNNLLAAEVEELRALLEQSDRARKLAEHE 1766
Cdd:pfam19220 191 AELTRRLAELETQLDATRARLRALEGQLAAEQAEREraeaQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1767 LLEATERVNLLNSQNTGLINQKKKLESDLSMLSNEVDDAVQEcRNAEEKAKKAITD-AAMMAEELKkeqDTSAHLERMkk 1845
Cdd:pfam19220 271 LRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQ-FQEMQRARAELEErAEMLTKALA---AKDAALERA-- 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2108526737 1846 nmEQTIKDLQMRLDEAEQIALKggkkQVLKLEARVKELENELESE 1890
Cdd:pfam19220 345 --EERIASLSDRIAELTKRFEV----ERAALEQANRRLKEELQRE 383
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1154-1763 |
2.43e-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: 52.83 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1154 RIEDEQALVNQ--LQKKIKeLQARTEELEEELEADRACRAKVEKQRSDVAreleelserleeaggatSAQIEMNKKREAD 1231
Cdd:pfam07111 77 RLEEEVRLLREtsLQQKMR-LEAQAMELDALAVAEKAGQAEAEGLRAALA-----------------GAEMVRKNLEEGS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1232 flklRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERS-----------EAKMEVDDLASTVEQLS 1300
Cdd:pfam07111 139 ----QRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAgeakqlaeaqkEAELLRKQLSKTQEELE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1301 KGKATSEKMCRLYEDQM-NEAKAKADELQRQ-----LNETNTQRARAQA------------------ESGELSRKLEERE 1356
Cdd:pfam07111 215 AQVTLVESLRKYVGEQVpPEVHSQTWELERQelldtMQHLQEDRADLQAtvellqvrvqslthmlalQEEELTRKIQPSD 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1357 AMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNaLAH--ALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRT 1434
Cdd:pfam07111 295 SLEPEFPKKCRSLLNRWREKVFALMVQLKAQD-LEHrdSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERM 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1435 KYETDAIQrTEELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVL 1514
Cdd:pfam07111 374 SAKGLQME-LSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLM 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1515 AewrQKYEECQSELETSQKESRG------LSTELFKLKNSYEETLDHLE----TIKRENKNLQEEIADLSDQISQGVKTI 1584
Cdd:pfam07111 453 A---RKVALAQLRQESCPPPPPAppvdadLSLELEQLREERNRLDAELQlsahLIQQEVGRAREQGEAERQQLSEVAQQL 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1585 -HELEKMKKGLDMEKSEIQAALE-EAEGTlehEESKSLRiqLELNQIKADVDRKLAEKDEEIDSlrrnhqRILESMQATl 1662
Cdd:pfam07111 530 eQELQRAQESLASVGQQLEVARQgQQEST---EEAASLR--QELTQQQEIYGQALQEKVAEVET------RLREQLSDT- 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1663 daeAKSRNEAVRLRKKMEGDLNemevQLSHANRQASESQKFLRNLQVQIKDiqleldetiHQNEELKEQVAVTERRNNLL 1742
Cdd:pfam07111 598 ---KRRLNEARREQAKAVVSLR----QIQHRATQEKERNQELRRLQDEARK---------EEGQRLARRVQELERDKNLM 661
|
650 660
....*....|....*....|.
gi 2108526737 1743 AAEVEElRALLEQSDRARKLA 1763
Cdd:pfam07111 662 LATLQQ-EGLLSRYKQQRLLA 681
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1511-1702 |
3.36e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1511 DKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKT------- 1583
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1584 -----------------------IHELEKMKKGLDMEKSEI------QAALEEAEGTLEHEESKSLRIQLELNQIKADVD 1634
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsdfLDRLSALSKIADADADLLeelkadKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526737 1635 RKLAEKDEEIDSLRRNhQRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQK 1702
Cdd:COG3883 175 AQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1554-1764 |
3.43e-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: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1554 DHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLELNQIKADv 1633
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1634 drkLAEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVR--------------LRKKMEGDLNEMEVQLSHANRQASE 1699
Cdd:COG4942 99 ---LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRrlqylkylaparreQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526737 1700 SQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRALLEQSDRARKLAE 1764
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1588-1966 |
4.53e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.83 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1588 EKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLELNQIKA----DVDRKLAEKDEEIDSLRRNHQRILESMQATLD 1663
Cdd:PLN02939 48 KKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTssddDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1664 AEAKSRNEAVRLRKKMEGDLNEMEVQ-LSHANRQASESQKflrnLQVQIKDIQLELDETIHQNEELKEQVAVTErrnnLL 1742
Cdd:PLN02939 128 FQLEDLVGMIQNAEKNILLLNQARLQaLEDLEKILTEKEA----LQGKINILEMRLSETDARIKLAAQEKIHVE----IL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1743 AAEVEELRALLEQSDRARKLAEHELleaTERVNLLNSQNTGLINqkkklesDLSMLSNEVDdavqecrnaeekakkaitd 1822
Cdd:PLN02939 200 EEQLEKLRNELLIRGATEGLCVHSL---SKELDVLKEENMLLKD-------DIQFLKAELI------------------- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1823 aammaeELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVLKLEARVKELENELESEQKKSQEYQ---K 1899
Cdd:PLN02939 251 ------EVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAAlvlD 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526737 1900 GVRKYERRIKELSYQGEEdkKNLVRLQ-DLIDKMQAKVKSYKRQTEEAEEQANTNLSKYRKLQHELDD 1966
Cdd:PLN02939 325 QNQDLRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQD 390
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1810-1951 |
4.56e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.70 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1810 RNAEEKAKKAITDAAMMAEELKKEQDTSA---------HLERMKKNMEQTIKDLQMRLDEAEQIaLKGGKKQVLKLEARV 1880
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAkeeihklrnEFEKELRERRNELQKLEKRLLQKEEN-LDRKLELLEKREEEL 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108526737 1881 KELENELESEQ----KKSQEYQKGVRKYERRIKELS-YQGEEDKKNLvrLQDLIDKMQAKVKSYKRQTE-EAEEQAN 1951
Cdd:PRK12704 113 EKKEKELEQKQqeleKKEEELEELIEEQLQELERISgLTAEEAKEIL--LEKVEEEARHEAAVLIKEIEeEAKEEAD 187
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1320-1551 |
4.90e-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: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1320 AKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHALQSsrh 1399
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1400 dcdlLREQYDEEQEAKADLQRAL---SKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEETVETsnakcssLE 1476
Cdd:COG4942 95 ----LRAELEAQKEELAELLRALyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526737 1477 KTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEE 1551
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1117-1383 |
5.72e-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: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1117 EGDLKLSLESVMDLENDKQQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQARteeleeeleADRAcRAKVEKQ 1196
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---------IAEA-EAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1197 RSDVAREleelserleeaggATSAQIEMNKKREADFLKLRRDLEEAMlhheaTTAALRKKHADSVAELseqIDSLQRVKQ 1276
Cdd:COG3883 85 REELGER-------------ARALYRSGGSVSYLDVLLGSESFSDFL-----DRLSALSKIADADADL---LEELKADKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1277 KLEKERSEAKMEVDDLASTVEQLskgkatsekmcrlyEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEERE 1356
Cdd:COG3883 144 ELEAKKAELEAKLAELEALKAEL--------------EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
250 260
....*....|....*....|....*..
gi 2108526737 1357 AMVSQLQRAKNSFSQNVEDLKKQLEEE 1383
Cdd:COG3883 210 AAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1318-1680 |
5.82e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1318 NEAKAKAD---ELQRQLNETNTQRARAQAESGELSRKLEE---REAMVSQ--------LQRAKNSFSQN---------VE 1374
Cdd:COG3096 278 NERRELSEralELRRELFGARRQLAEEQYRLVEMARELEElsaRESDLEQdyqaasdhLNLVQTALRQQekieryqedLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1375 DLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALskanaEVAQWRTKYETDAIQRteeLEEAKkkl 1454
Cdd:COG3096 358 ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQAL-----DVQQTRAIQYQQAVQA---LEKAR--- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1455 vTRLQEAEETVEtsNAKcSSLEKTKHRLQtEIEDLVIDLER--ANAAAAVldkkqRNFDKVLaewrQKYEECQSELETSQ 1532
Cdd:COG3096 427 -ALCGLPDLTPE--NAE-DYLAAFRAKEQ-QATEEVLELEQklSVADAAR-----RQFEKAY----ELVCKIAGEVERSQ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1533 KESRGlsTELFKLKNSYEETLDHLETIKRE----------NKNLQEEIADLSDQISQGVKTIHELEkmkkgldMEKSEIQ 1602
Cdd:COG3096 493 AWQTA--RELLRRYRSQQALAQRLQQLRAQlaeleqrlrqQQNAERLLEEFCQRIGQQLDAAEELE-------ELLAELE 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1603 AALEEAEGTLEHEESKSLRIQLELNQIKADVDR-------------KLAEKDEEIDSLRRNHQRILESMQATLDAEAK-- 1667
Cdd:COG3096 564 AQLEELEEQAAEAVEQRSELRQQLEQLRARIKElaarapawlaaqdALERLREQSGEALADSQEVTAAMQQLLEREREat 643
|
410
....*....|....
gi 2108526737 1668 -SRNEAVRLRKKME 1680
Cdd:COG3096 644 vERDELAARKQALE 657
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
960-1221 |
7.23e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 960 ADAEDRCDLLIKTKIQLEAKVKEIMERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNL 1039
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1040 IEEMAALDETILKLTkekkALLEAhqQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKlrmdlervrrklegd 1119
Cdd:COG3883 92 ARALYRSGGSVSYLD----VLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA--------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1120 lklslesvmDLENDKQQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSD 1199
Cdd:COG3883 151 ---------ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
250 260
....*....|....*....|..
gi 2108526737 1200 VARELEELSERLEEAGGATSAQ 1221
Cdd:COG3883 222 AAAAAAAAAAAAAAAAAAAAAA 243
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
905-1172 |
7.50e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 905 TTEKELVSLKEELAKLKEALEKsevKRKELEERQVSLIQEKNDLS--------LQLQAEQDNLADAEDRCDLLIKTKIQL 976
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIKKQLSE---KQKELEQNNKKIKELEKQLNqlkseisdLNNQKEQDWNKELKSELKNQEKKLEEI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 977 EAKVKEIMERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKE 1056
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1057 KKALLEAHQQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQ 1136
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486
|
250 260 270
....*....|....*....|....*....|....*.
gi 2108526737 1137 LDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKEL 1172
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1468-1977 |
8.07e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.89 E-value: 8.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1468 SNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESrglsTELFKLKN 1547
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQ----AELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1548 SYEETLDHLEtikRENKNLQEEIADLSDQISQgvktihELEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQlELN 1627
Cdd:pfam05557 83 KYLEALNKKL---NEKESQLADAREVISCLKN------ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAS-EAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1628 QIKADVDRK---LAEKDEEIDSLRRNHQrilesMQATLDAEAKSRNEAVRLRKKMEGDLNemevQLSHANRQASESQKFL 1704
Cdd:pfam05557 153 QLRQNLEKQqssLAEAEQRIKELEFEIQ-----SQEQDSEIVKNSKSELARIPELEKELE----RLREHNKHLNENIENK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1705 RNLQVQIKDIQLELDetihQNEELKEQVAVTERRNNLLAAEVEELRALLEqsDRARKLAEHELLeaTERVNLLNSQNTGL 1784
Cdd:pfam05557 224 LLLKEEVEDLKRKLE----REEKYREEAATLELEKEKLEQELQSWVKLAQ--DTGLNLRSPEDL--SRRIEQLQQREIVL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1785 INQKKKLESDLSMLSNEVDDAVQECRNAEEKakkaitdaammAEELKKEqdtsahlermKKNMEQTIKDLQMRLDEAEQi 1864
Cdd:pfam05557 296 KEENSSLTSSARQLEKARRELEQELAQYLKK-----------IEDLNKK----------LKRHKALVRRLQRRVLLLTK- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1865 aLKGGKKQVlkLEARVKELENELESEQK--KSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQ 1942
Cdd:pfam05557 354 -ERDGYRAI--LESYDKELTMSNYSPQLleRIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQ 430
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2108526737 1943 TEEAEEQANTNL--SKYRKLQH---ELDDAEERADMAESQ 1977
Cdd:pfam05557 431 ESLADPSYSKEEvdSLRRKLETlelERQRLREQKNELEME 470
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1125-1380 |
8.62e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1125 ESVMDLENDKQQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSdvarel 1204
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1205 eelserleeaggATSAQIEMNKKREADFLKL-----RRDLEEAMLHHEATTAALRKKH--ADSVAELSEQIDSLQRVKQK 1277
Cdd:COG4942 94 ------------ELRAELEAQKEELAELLRAlyrlgRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1278 LEKERSEAKMEVDDLASTVEQLSKGKATsekmcrlYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREA 1357
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAA-------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
250 260
....*....|....*....|...
gi 2108526737 1358 MVSqlQRAKNSFSQNVEDLKKQL 1380
Cdd:COG4942 235 EAA--AAAERTPAAGFAALKGKL 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1030-1286 |
9.25e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1030 HATENKVKNLIEEMAALDETILKLTKEKKALLEAHQQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSL----EQEKKL 1105
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1106 RMDLERVRRKLEGDLKlslesVMDLENDKQQLDEKLKKKDFemNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEA 1185
Cdd:COG4942 96 RAELEAQKEELAELLR-----ALYRLGRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1186 DRACRAKVEKQRSDVAreleelserleeaggatsaqiemnkkreadflKLRRDLEEAMLHHEATTAALRKK---HADSVA 1262
Cdd:COG4942 169 LEAERAELEALLAELE--------------------------------EERAALEALKAERQKLLARLEKElaeLAAELA 216
|
250 260
....*....|....*....|....
gi 2108526737 1263 ELSEQIDSLQRVKQKLEKERSEAK 1286
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAA 240
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1515-1971 |
9.25e-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: 51.12 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1515 AEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLEtikRENKNLQEEIADLsdQISQGVKTiHELEKMKKGL 1594
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLE---KELKHLREALQQT--QQSHAYLT-QKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1595 DMEKSEIQAALEEAEGTLEHEESKSLRIQLELNQIKAdvdrKLAEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVR 1674
Cdd:TIGR00618 257 KKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA----PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1675 LRK-KMEGDLNEMEVQLSHA----NRQASESQKFLRnlqvQIKDIQLELDETIHQneeLKEQVAVTERRNNLLAAEVEEL 1749
Cdd:TIGR00618 333 HVKqQSSIEEQRRLLQTLHSqeihIRDAHEVATSIR----EISCQQHTLTQHIHT---LQQQKTTLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1750 RALL------------EQSDRARKLAEHELLEATERVNLLNSQNTGLI-NQKKKLESDLSMLSNEVDDAVQECRNAEEKA 1816
Cdd:TIGR00618 406 QREQatidtrtsafrdLQGQLAHAKKQQELQQRYAELCAAAITCTAQCeKLEKIHLQESAQSLKEREQQLQTKEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1817 KKAITDAAMMAEELKKEQdtsahLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVLKLEARVKELENELESEQKKSQE 1896
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEP-----CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRAS 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1897 Y-------QKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEE 1969
Cdd:TIGR00618 561 LkeqmqeiQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQE 640
|
..
gi 2108526737 1970 RA 1971
Cdd:TIGR00618 641 LA 642
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1223-1966 |
1.04e-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: 50.82 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1223 EMNKKREADFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDS-----LQRVKQKLEKERSEAKMEVDDLASTVE 1297
Cdd:TIGR01612 700 DLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGeinkdLNKILEDFKNKEKELSNKINDYAKEKD 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1298 QLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAM-------VSQLQRAKNSFS 1370
Cdd:TIGR01612 780 ELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMkddflnkVDKFINFENNCK 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1371 QNVEDLKKQLEE-ENKAKNALA----HALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETdaiqrTE 1445
Cdd:TIGR01612 860 EKIDSEHEQFAElTNKIKAEISddklNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKICENTKES-----IE 934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1446 ELEEAKKKLVTRLQEAEETVETSNakcsSLEKT-KHRLQTEIEDLVIDLERANAAAAVLDKKQRNfdkvlAEWRQKYEEC 1524
Cdd:TIGR01612 935 KFHNKQNILKEILNKNIDTIKESN----LIEKSyKDKFDNTLIDKINELDKAFKDASLNDYEAKN-----NELIKYFNDL 1005
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1525 QSELETSQKESrglstelfkLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTI-HELEK-MKKGLDMEKSEIq 1602
Cdd:TIGR01612 1006 KANLGKNKENM---------LYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIiDEIEKeIGKNIELLNKEI- 1075
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1603 aaLEEAEGTLEHeeSKSLRIQLELNQIKADVDRKLAEKDEEIDSLRRNhqriLESMQATLDaeaKSRNEAVRLRKKMEGD 1682
Cdd:TIGR01612 1076 --LEEAEINITN--FNEIKEKLKHYNFDDFGKEENIKYADEINKIKDD----IKNLDQKID---HHIKALEEIKKKSENY 1144
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1683 LNEMEVQLSH---------ANRQASESQKFLRNLQVQI---KDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELR 1750
Cdd:TIGR01612 1145 IDEIKAQINDledvadkaiSNDDPEEIEKKIENIVTKIdkkKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLG 1224
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1751 AL-LEQSDRARKLAEHelleatervnllnsqntgLINQKKKLESDLsmlsNEVDDAVQECRNaeEKAKKAITDAAMMAEE 1829
Cdd:TIGR01612 1225 KLfLEKIDEEKKKSEH------------------MIKAMEAYIEDL----DEIKEKSPEIEN--EMGIEMDIKAEMETFN 1280
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1830 LKKEQDTSAHLerMKKNMEQTIKDLQMRldeaeqiALKggKKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIK 1909
Cdd:TIGR01612 1281 ISHDDDKDHHI--ISKKHDENISDIREK-------SLK--IIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIA 1349
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 2108526737 1910 ELSyqgeedkkNLVRLQDlIDKMQAKVKSYKRQTEEAEEQANTNLSKYRKLQHELDD 1966
Cdd:TIGR01612 1350 NIY--------NILKLNK-IKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD 1397
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1692-1917 |
1.16e-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: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1692 HANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRALLEQsdrarklAEHELLEAT 1771
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-------AEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1772 ERVN------------------LLNSQNTG-LINQkkklESDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKK 1832
Cdd:COG3883 86 EELGeraralyrsggsvsyldvLLGSESFSdFLDR----LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1833 EQDTsahLERMKKNMEQTIKDLQMRLDEAEQialkggkkQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELS 1912
Cdd:COG3883 162 LKAE---LEAAKAELEAQQAEQEALLAQLSA--------EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
....*
gi 2108526737 1913 YQGEE 1917
Cdd:COG3883 231 AAAAA 235
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1231-1892 |
1.17e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.59 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1231 DFLKLRRDLEEaMLHHEATTAALRKKHADSVAELSEQ-IDSLQRVKQKLEKERSEAKMEVDDLASTVE-QLSKGKATSEK 1308
Cdd:pfam10174 81 DELRAQRDLNQ-LLQQDFTTSPVDGEDKFSTPELTEEnFRRLQSEHERQAKELFLLRKTLEEMELRIEtQKQTLGARDES 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1309 MCRLYEdqMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKK--QLEEENKA 1386
Cdd:pfam10174 160 IKKLLE--MLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKtkALQTVIEM 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1387 KNALAHALQSSrhdcdlLREQYDEEQEAKADL-----QRALSKANAEVAQWRTKYETDAI-QRTEELEEAKKKLVTrLQE 1460
Cdd:pfam10174 238 KDTKISSLERN------IRDLEDEVQMLKTNGllhteDREEEIKQMEVYKSHSKFMKNKIdQLKQELSKKESELLA-LQT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1461 AEETVETSNAKC--------SSLEKTKHR---LQTEIEDLVIDLERAnaaAAVLDKKQRnfdkvlaewrqkyeecqsELE 1529
Cdd:pfam10174 311 KLETLTNQNSDCkqhievlkESLTAKEQRaaiLQTEVDALRLRLEEK---ESFLNKKTK------------------QLQ 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1530 TSQKESRGLSTELFKLKnsyeetlDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALeeae 1609
Cdd:pfam10174 370 DLTEEKSTLAGEIRDLK-------DMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL---- 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1610 GTLEHEESKSLRIqleLNQIKADVDRKLAEKDEEIDSLRRNHQ-----------RILESMQATLDAEAKSRNEAVRLRKK 1678
Cdd:pfam10174 439 TTLEEALSEKERI---IERLKEQREREDRERLEELESLKKENKdlkekvsalqpELTEKESSLIDLKEHASSLASSGLKK 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1679 mEGDLNEMEVQLSHANRQASEsqkflrnLQVQIKDIQlELDETIHQNEELKEQVAVTERRNNLLA-------AEVEELRA 1751
Cdd:pfam10174 516 -DSKLKSLEIAVEQKKEECSK-------LENQLKKAH-NAEEAVRTNPEINDRIRLLEQEVARYKeesgkaqAEVERLLG 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1752 LL-----EQSDRARKLAEHELLEATErvnlLNSQNTGLINQKKKLESDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMM 1826
Cdd:pfam10174 587 ILrevenEKNDKDKKIAELESLTLRQ----MKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMG 662
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108526737 1827 AeelkkeqdtsahLERMKKNMEQTikdlQMRLDEAEQ-IALKGGKKQVLKLEARvKELENELESEQK 1892
Cdd:pfam10174 663 A------------LEKTRQELDAT----KARLSSTQQsLAEKDGHLTNLRAERR-KQLEEILEMKQE 712
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1498-1921 |
1.50e-05 |
|
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: 50.06 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1498 AAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETiKRENKNLQEEIADLSDQI 1577
Cdd:pfam13166 82 KPIFTLGEESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDECWKKIK-RKKNSALSEALNGFKYEA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1578 SQGVKTIHELEK--MKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLELNQIKADV--DRKLAEKDEEIDSLRRNH-- 1651
Cdd:pfam13166 161 NFKSRLLREIEKdnFNAGVLLSDEDRKAALATVFSDNKPEIAPLTFNVIDFDALEKAEilIQKVIGKSSAIEELIKNPdl 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1652 ----QRILESMQATLDAEAKSRNEAVRLRKKmegdlnEMEvqlSHANRqasESQKFLRNLQVQIKDIQL----------E 1717
Cdd:pfam13166 241 adwvEQGLELHKAHLDTCPFCGQPLPAERKA------ALE---AHFDD---EFTEFQNRLQKLIEKVESaissllaqlpA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1718 LDETIHQNEELKEQVAVTERRNNLLAAEVEELRALLEQSdRARKLAEHELLEATERvnllnsqntglINQKKKLESDLSM 1797
Cdd:pfam13166 309 VSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAK-RKDPFKSIELDSVDAK-----------IESINDLVASINE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1798 LSNEVDDAVQECRNAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQMRLDEAEqialkggkKQVLKLE 1877
Cdd:pfam13166 377 LIAKHNEITDNFEEEKNKAKKKL--RLHLVEEFKSEIDE---YKDKYAGLEKAINSLEKEIKNLE--------AEIKKLR 443
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2108526737 1878 ARVKELENELESEQKKSQEYQKGVRKYERRIKELSYqgEEDKKN 1921
Cdd:pfam13166 444 EEIKELEAQLRDHKPGADEINKLLKAFGFGELELSF--NEEGKG 485
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1814-1994 |
1.52e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1814 EKAKKAITdaamMAEELKKEQDTSAHLERmkKNMEQTIKDLQMRLDEAEQiALKGGKKQVLKLEARVKELENELESEQKK 1893
Cdd:COG1196 210 EKAERYRE----LKEELKELEAELLLLKL--RELEAELEELEAELEELEA-ELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1894 SQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADM 1973
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180
....*....|....*....|.
gi 2108526737 1974 AESQANKLRARTRDQGSKLAE 1994
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEE 383
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1710-1980 |
1.60e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1710 QIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRALL-EQSDRARKLAEhELLEATERVNLLNSQNTGLINQK 1788
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRdELNAQVKELRE-EAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1789 KKLESDLSMLSNEVDDAVQEcRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIalkg 1868
Cdd:COG1340 81 DELNEKLNELREELDELRKE-LAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKA---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1869 gkkqvLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEAEE 1948
Cdd:COG1340 156 -----LEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHE 230
|
250 260 270
....*....|....*....|....*....|..
gi 2108526737 1949 QANTNLSKYRKLQHELDDAEERADMAESQANK 1980
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1404-1681 |
1.73e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.15 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1404 LREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTeELEEAKKKLVTRLQEAEETVETSNAKCSSLE------K 1477
Cdd:pfam00038 59 LRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRT-SAENDLVGLRKDLDEATLARVDLEAKIESLKeelaflK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1478 TKHrlQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEEcQSELETSQKEsrglstelfklknsyeetldhlE 1557
Cdd:pfam00038 138 KNH--EEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEE-IAAKNREEAE----------------------E 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1558 TIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEGTLEHEESkslRIQLELNQIKadvdRKL 1637
Cdd:pfam00038 193 WYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEE---RYELQLADYQ----ELI 265
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2108526737 1638 AEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRKKMEG 1681
Cdd:pfam00038 266 SELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEG 309
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1518-1894 |
1.89e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.08 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1518 RQKYEECQSELETSQKESRGLS------TELFKLKNSYEETLDHLETIKRENKNLQEE---IADLSDQISQGVKTIHELE 1588
Cdd:COG5022 833 RETEEVEFSLKAEVLIQKFGRSlkakkrFSLLKKETIYLQSAQRVELAERQLQELKIDvksISSLKLVNLELESEIIELK 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1589 KMKKGLDMEKSEIQaaLEEAEGTLEHEESKSLRIQLELNQIKADVDRKLAEKDEEIDSLRRNHQRILESMQATLDAEAKS 1668
Cdd:COG5022 913 KSLSSDLIENLEFK--TELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKA 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1669 RNEAVRLRKKmegdLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQL--ELDETIHQNEELKEQVAVTERRNNLLAAEV 1746
Cdd:COG5022 991 NSELKNFKKE----LAELSKQYGALQESTKQLKELPVEVAELQSASKIisSESTELSILKPLQKLKGLLLLENNQLQARY 1066
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1747 EELraLLEQSDRARKLAEHELLEATErvNLLNSQNTGLINQKKKLESDLSMLSNEVDDAV---QECRNAEEKAKKAITDA 1823
Cdd:COG5022 1067 KAL--KLRRENSLLDDKQLYQLESTE--NLLKTINVKDLEVTNRNLVKPANVLQFIVAQMiklNLLQEISKFLSQLVNTL 1142
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2108526737 1824 AMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVLKLEARVKELENELESEQKKS 1894
Cdd:COG5022 1143 EPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKI 1213
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1298-1553 |
2.51e-05 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 49.47 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1298 QLSKGKAtsekMCRLYED------QMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQ 1371
Cdd:pfam09726 390 QLSKPDA----LVRLEQDikklkaELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1372 NVEDLKKQLEEENKAKNALAHALQSSRhdcdllreQYDEEQEAKADLQRALSKANaevaqwrTKYETDAI-QRTEELEEA 1450
Cdd:pfam09726 466 TVQQLEKRLKAEQEARASAEKQLAEEK--------KRKKEEEATAARAVALAAAS-------RGECTESLkQRKRELESE 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1451 KKKLVTRLQEAEETVETSNAKCSSLEKTKHRlQTEIEDLVidleraNAAAAVLDKKQRNFDKVLAEWRQKYE------EC 1524
Cdd:pfam09726 531 IKKLTHDIKLKEEQIRELEIKVQELRKYKES-EKDTEVLM------SALSAMQDKNQHLENSLSAETRIKLDlfsalgDA 603
|
250 260
....*....|....*....|....*....
gi 2108526737 1525 QSELETSQKESRGLSTELFKLKNSYEETL 1553
Cdd:pfam09726 604 KRQLEIAQGQIYQKDQEIKDLKQKIAEVM 632
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1234-1656 |
2.62e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1234 KLRRDLEEAMLHHEATTAALRK-KHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKgkatsekmcrl 1312
Cdd:COG4717 99 ELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEE----------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1313 YEDQMNEAKAKADELQRQLNETNTQR-ARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENK----AK 1387
Cdd:COG4717 168 LEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeerlKE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1388 NALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKlvTRLQEAEetvet 1467
Cdd:COG4717 248 ARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL--EELEEEE----- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1468 snakcsslektkhrLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQkyEECQSELETSQKESRGLsteLFKLKN 1547
Cdd:COG4717 321 --------------LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE--LEEELQLEELEQEIAAL---LAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1548 SYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKM--KKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLE 1625
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAELEAE 461
|
410 420 430
....*....|....*....|....*....|.
gi 2108526737 1626 LNQIKAdvDRKLAEKDEEIDSLRRNHQRILE 1656
Cdd:COG4717 462 LEQLEE--DGELAELLQELEELKAELRELAE 490
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1699-1909 |
3.54e-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: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1699 ESQKFLRNLQvqikDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRALLEQSDRARKLAEHELLEATERVnlln 1778
Cdd:COG1579 4 EDLRALLDLQ----ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1779 sqntglinqkKKLESDLSMLSN--EVDDAVQEcrnaEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQM 1856
Cdd:COG1579 76 ----------KKYEEQLGNVRNnkEYEALQKE----IESLKRRISDLEDEILELMERIEE---LEEELAELEAELAELEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526737 1857 RLDEAEQialkggkkqvlKLEARVKELENELESEQKKSQEYQKGV-----RKYERRIK 1909
Cdd:COG1579 139 ELEEKKA-----------ELDEELAELEAELEELEAEREELAAKIppellALYERIRK 185
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1497-1983 |
4.07e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1497 NAAAAVLDKKQRNFDKVLAEWRQKYEECQsELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDq 1576
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1577 isqgVKTIHELEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLELNQIKADVDRKLAEKDEEIDSLRRNHQRILE 1656
Cdd:COG4717 131 ----YQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1657 SMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQlshanrQASESQKFLRNLQVQIkDIQLELDETIHQNEELKEQVAvte 1736
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAA------ALEERLKEARLLLLIA-AALLALLGLGGSLLSLILTIA--- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1737 rrnNLLAAEVEELRALLEQSDRARKLAEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLSNEVDDAVQECRNAEEKA 1816
Cdd:COG4717 277 ---GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1817 KKaitdaammAEELKKEQDTSAHLERMKKNMEQTIKDlqmrlDEAEQIALKGGKKQVLKLEARVKELENELESEQKKSQE 1896
Cdd:COG4717 354 RE--------AEELEEELQLEELEQEIAALLAEAGVE-----DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1897 YQKGVRKYERRIKELSYQGEEDkknlvRLQDLIDKMQAKVKSYKRQTEEAEEQAntnlsKYRKLQHELDDAEERADMAES 1976
Cdd:COG4717 421 LLEALDEEELEEELEELEEELE-----ELEEELEELREELAELEAELEQLEEDG-----ELAELLQELEELKAELRELAE 490
|
....*..
gi 2108526737 1977 QANKLRA 1983
Cdd:COG4717 491 EWAALKL 497
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1453-1631 |
4.40e-05 |
|
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: 47.70 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1453 KLVTRLQEAEETVETsnaKCSSLEKTKHRLQTEIEDLVIDLEranaaaaVLDKKQRNFDKVLAEWRQKYEECQSELETSQ 1532
Cdd:smart00787 123 KTFARLEAKKMWYEW---RMKLLEGLKEGLDENLEGLKEDYK-------LLMKELELLNSIKPKLRDRKDALEEELRQLK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1533 KESRGL----STELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKmkkgldmEKSEIQAALEEA 1608
Cdd:smart00787 193 QLEDELedcdPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT-------EIAEAEKKLEQC 265
|
170 180
....*....|....*....|...
gi 2108526737 1609 EGTLEHEESKslrIQLELNQIKA 1631
Cdd:smart00787 266 RGFTFKEIEK---LKEQLKLLQS 285
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1006-1221 |
4.54e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1006 DECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKAL---LEAHQQTLDDLQAEEDKVNI-L 1081
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALeqeLAALEAELAELEKEIAELRAeL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1082 TKAKAKLEQQVDDLEGSLEQEKKLRM-------DLERVRRKLEGDLKLSLESVMDLENDKQQLDEKLKKKDFEMNEMSTR 1154
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLlspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108526737 1155 IEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEELSERLEEAGGATSAQ 1221
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1605-1994 |
4.70e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1605 LEEAEGTLEHEESKSLRIQLELNQIKAD-VDRKLAEKDEEIDSLRRNHQRILESmqaTLDAEAKSR-NEAVRLRKKMEGD 1682
Cdd:PTZ00121 1026 IEKIEELTEYGNNDDVLKEKDIIDEDIDgNHEGKAEAKAHVGQDEGLKPSYKDF---DFDAKEDNRaDEATEEAFGKAEE 1102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1683 LNEMEVQLSHANRQASESQKFLRNLQvqiKDIQLELDETIHQNEELKEqvaVTERRNNLLAAEVEELRALLE--QSDRAR 1760
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEEAKKKAEDAR---KAEEARKAEDARKAEEARK---AEDAKRVEIARKAEDARKAEEarKAEDAK 1176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1761 KLAEHELLEATERVN-LLNSQNTGLINQKKKLESDLSmlsnevddaVQECRNAEEkAKKAitDAAMMAEELKKEQDTSAH 1839
Cdd:PTZ00121 1177 KAEAARKAEEVRKAEeLRKAEDARKAEAARKAEEERK---------AEEARKAED-AKKA--EAVKKAEEAKKDAEEAKK 1244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1840 LERMKKNMEqtikdlqMRLDEAEQIALKGGKKQVLKLEARVKELENELESEQKKSQEYQKGVRKyeRRIKELSYQGEEDK 1919
Cdd:PTZ00121 1245 AEEERNNEE-------IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEK--KKADEAKKKAEEAK 1315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526737 1920 KnLVRLQDLIDKMQAKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADMAESQANKLRARTrDQGSKLAE 1994
Cdd:PTZ00121 1316 K-ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA-DAAKKKAE 1388
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1511-1662 |
4.74e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1511 DKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQgVKTIHELEKM 1590
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-VRNNKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1591 KKGLDMEKSEIQAA----------LEEAEGTLEHEESKSLRIQLELNQIKADVDRKLAEKDEEIDSLRRNHQRILESMQA 1660
Cdd:COG1579 95 QKEIESLKRRISDLedeilelmerIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
..
gi 2108526737 1661 TL 1662
Cdd:COG1579 175 EL 176
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
1562-1780 |
5.24e-05 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 47.33 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1562 ENKNLQEEIADLSDQISQGVktiHELEKMKKGL-----DMEKSEIQAALEEAEGTLEHEESKSLRIQLELNQikadvdRK 1636
Cdd:pfam04849 102 RNEALEEQLGSAREEILQLR---HELSKKDDLLqiysnDAEESETESSCSTPLRRNESFSSLHGCVQLDALQ------EK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1637 LAEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQL 1716
Cdd:pfam04849 173 LRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKMEENLRQQEEITSLLAQIVDLQH 252
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526737 1717 ELDETIHQNEELKEQVAVTERRNNLLAAEVEELRAlleqsdrarKLAEHE--LLEATERVNLLNSQ 1780
Cdd:pfam04849 253 KCKELGIENEELQQHLQASKEAQRQLTSELQELQD---------RYAECLgmLHEAQEELKELRKK 309
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1247-1490 |
5.52e-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: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1247 EATTAALRKKHADSVAELSEQIDSLQRVKQKLEkersEAKMEVDDLASTVEQLSkgkatsekmcrLYEDqmNEAKAKADE 1326
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLD----QLKEQLQLLNKLLPQAN-----------LLAD--ETLADRLEE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1327 LQRQLNETNtqraRAQAESGELSRKLEEREAMVSQLQRAKNSF---SQNVEDLKKQLEEENKAKNALAHALQSSRH---- 1399
Cdd:COG3096 898 LREELDAAQ----EAQAFIQQHGKALAQLEPLVAVLQSDPEQFeqlQADYLQAKEQQRRLKQQIFALSEVVQRRPHfsye 973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1400 --------DCDL---LREQYDEEQEAKADLQRALSKANAEVAQW-----------RTKYET--DAIQRTEELE-----EA 1450
Cdd:COG3096 974 davgllgeNSDLnekLRARLEQAEEARREAREQLRQAQAQYSQYnqvlaslkssrDAKQQTlqELEQELEELGvqadaEA 1053
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2108526737 1451 KKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLV 1490
Cdd:COG3096 1054 EERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQ 1093
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1563-1964 |
5.57e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.93 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1563 NKNLQEEIADLSDQIsQGVKTIHELEKMKKGLDMEKS-EIQAALEEAEGTLEHEESKSL-RIQLELNQIKADVDR----- 1635
Cdd:pfam06160 5 RKKIYKEIDELEERK-NELMNLPVQEELSKVKKLNLTgETQEKFEEWRKKWDDIVTKSLpDIEELLFEAEELNDKyrfkk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1636 ---KLAEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRKK---------------------MEGDLNEMEVQLS 1691
Cdd:pfam06160 84 akkALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKyrelrktllanrfsygpaideLEKQLAEIEEEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1692 HANrQASESQKFlrnlqVQIKDIQLELDETIHQNEELKEQV-AVTERRNNLLAAEVEELRALLEQSDRAR-KLAEHELLE 1769
Cdd:pfam06160 164 QFE-ELTESGDY-----LEAREVLEKLEEETDALEELMEDIpPLYEELKTELPDQLEELKEGYREMEEEGyALEHLNVDK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1770 ATERVNLLNSQNTGLINQK--KKLESDLSMLSNEVDdAVQECRNAEEKAKKaitdaammaeELKKEQDT-SAHLERMKKN 1846
Cdd:pfam06160 238 EIQQLEEQLEENLALLENLelDEAEEALEEIEERID-QLYDLLEKEVDAKK----------YVEKNLPEiEDYLEHAEEQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1847 MEQTIKDLQM-----RLDEAEQIALKGGKKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKElsyqgeedkkn 1921
Cdd:pfam06160 307 NKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEE----------- 375
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2108526737 1922 lvrlqdlIDKMQAKVKSYKRQTEEAEEQANTNLSKYRKLQHEL 1964
Cdd:pfam06160 376 -------IEEEQEEFKESLQSLRKDELEAREKLDEFKLELREI 411
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1038-1240 |
6.23e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1038 NLIEEMAALDETILKLTKEKKAL---LEAHQQTLDDLQAEEDKVNILTKAKAkLEQQVDDLEGSLEQEKKLRMDLERVRR 1114
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELrkeLEEAEAALEEFRQKNGLVDLSEEAKL-LLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1115 KLEGDLKLSLESVMDLENDK--QQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAK 1192
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELE 323
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2108526737 1193 VEKQRSDVARELEElserleeaggATSAQIEMNKKREADFLKLRRDLE 1240
Cdd:COG3206 324 ALQAREASLQAQLA----------QLEARLAELPELEAELRRLEREVE 361
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
834-1158 |
6.63e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 834 LEELRDERLAKVLTLLQAAARGKIMRMELLKLMERREALMIIQwnirafnavkhwpwmKLFFKIkplLRSATTEKELVSL 913
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA---------------EYSWDE---IDVASAEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 914 KEE----------LAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRcdLLIKTKIQLEAKVKEI 983
Cdd:COG4913 674 EAElerldassddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR--LEAAEDLARLELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 984 MERLEdEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKE-KHATENKVKNLIEEMAALDETILKLTKEKKALLE 1062
Cdd:COG4913 752 EERFA-AALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALLDRLEEDGLP 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1063 AHQQTLDDL---QAEEDKVNILTKAKAKLE---QQVDDLEGSLEQ-----EKKLRMDLERVRRKlegDLKLSLESVMDLE 1131
Cdd:COG4913 831 EYEERFKELlneNSIEFVADLLSKLRRAIReikERIDPLNDSLKRipfgpGRYLRLEARPRPDP---EVREFRQELRAVT 907
|
330 340
....*....|....*....|....*...
gi 2108526737 1132 NDKQQLDEKLKKKDFE-MNEMSTRIEDE 1158
Cdd:COG4913 908 SGASLFDEELSEARFAaLKRLIERLRSE 935
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1314-1558 |
7.98e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 46.18 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1314 EDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHa 1393
Cdd:pfam00261 7 KEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLEN- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1394 lqssrhdcdllREQYDEEqeaKADLQRALSKANAEVAQwrtkyetDAIQRTEELEEAKKKLVTRLQEAEETVETSNAKCS 1473
Cdd:pfam00261 86 -----------RALKDEE---KMEILEAQLKEAKEIAE-------EADRKYEEVARKLVVVEGDLERAEERAELAESKIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1474 SLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETL 1553
Cdd:pfam00261 145 ELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAIS 224
|
....*
gi 2108526737 1554 DHLET 1558
Cdd:pfam00261 225 EELDQ 229
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1512-1722 |
8.53e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 8.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1512 KVLAEWRQKYEECQSEL--ETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKnlqeeIADLSDQISQGVKTIHELEK 1589
Cdd:COG3206 152 AVANALAEAYLEQNLELrrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1590 MKKGLDMEKSEIQAALEEAEGTLE------HEESKSLRIQLELNQIkADVDRKLAEK--------------DEEIDSLRR 1649
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGsgpdalPELLQSPVIQQLRAQL-AELEAELAELsarytpnhpdvialRAQIAALRA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1650 NHQRILESMQATLDAEAKS--------RNEAVRLRKKMEgDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDET 1721
Cdd:COG3206 306 QLQQEAQRILASLEAELEAlqareaslQAQLAQLEARLA-ELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
.
gi 2108526737 1722 I 1722
Cdd:COG3206 385 V 385
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1102-1521 |
8.68e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1102 EKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQLDEKLKkkdfEMNEMSTRIEDEQALVNQLQKKIKELQARTEELEE 1181
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1182 ELEADRACRAKVEKQRSDVARELEELSERLEEAggATSAQIEMNKKREADFLKLRRDLEEAMLHHEATTAALRKKHADSV 1261
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLE--ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1262 AELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRL----------------------------- 1312
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLliaaallallglggsllsliltiagvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1313 -------YEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKL--------EEREAMVSQLQRAKNSFSQnVEDLK 1377
Cdd:COG4717 282 vlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlspEELLELLDRIEELQELLRE-AEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1378 KQL---EEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKA---DLQRALSKANAEVAQWRTKYETDAI-QRTEELEEA 1450
Cdd:COG4717 361 EELqleELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEeleELEEQLEELLGELEELLEALDEEELeEELEELEEE 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2108526737 1451 KKKLVTRLQEAEETVETSNAKCSSLEK--TKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKY 1521
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
904-1063 |
8.82e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 904 ATTEKELVSLKEELAKLKEALEKSEvkrKELEERQVSLIQEKNDLSLQLQAEQ---------------DNLADAEDRCDL 968
Cdd:COG3883 47 EELNEEYNELQAELEALQAEIDKLQ---AEIAEAEAEIEERREELGERARALYrsggsvsyldvllgsESFSDFLDRLSA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 969 LiktkIQLEAKVKEIMERLEDEEEMSANvlaKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDE 1048
Cdd:COG3883 124 L----SKIADADADLLEELKADKAELEA---KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196
|
170
....*....|....*
gi 2108526737 1049 TILKLTKEKKALLEA 1063
Cdd:COG3883 197 QLAELEAELAAAEAA 211
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
899-1063 |
9.33e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 899 PLLRSATTEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEA 978
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 979 KVKEIMERLEDEEEMSANVLAKKRKLEDECAELKKDIDDL-------EITLAKVEKEKHATENKVKNLIEEMAALDETIL 1051
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaIEEYEELEERYDFLSEQREDLEEARETLEEAIE 819
|
170
....*....|..
gi 2108526737 1052 KLTKEKKALLEA 1063
Cdd:COG1196 820 EIDRETRERFLE 831
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1152-1389 |
9.50e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1152 STRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEELSERLEeaggATSAQIEMNKKREAd 1231
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAELAELEKEIA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1232 flKLRRDLEEAMLHHEATTAALRKKHADSVAEL---SEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEK 1308
Cdd:COG4942 94 --ELRAELEAQKEELAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1309 mcrlyedQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKN 1388
Cdd:COG4942 172 -------ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
.
gi 2108526737 1389 A 1389
Cdd:COG4942 245 A 245
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1271-1577 |
1.14e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1271 LQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSR 1350
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1351 KLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVA 1430
Cdd:COG4372 88 QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1431 QWRTKYETDAIQrteELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNF 1510
Cdd:COG4372 168 ALEQELQALSEA---EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2108526737 1511 --DKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQI 1577
Cdd:COG4372 245 eeDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGAL 313
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1781-1978 |
1.39e-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: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1781 NTGLINQKKKLESDLSMLSNEVDDAvqecrnaeEKAKKAITDAAMMAEEL-KKEQDTSAHLERMKKNMEQTIKDLQMRLD 1859
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENAHKIQI--------EILEKELSSLAQETEELqKKATQTLAKAQQVNAESERTLGHAKELAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1860 EAEQIALKggKKQVLKLEARVKELENELESE--QKKSQEYQKGVRkyERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVK 1937
Cdd:pfam06008 90 AIKNLIDN--IKEINEKVATLGENDFALPSSdlSRMLAEAQRMLG--EIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2108526737 1938 SYKRQTEEAEEQANTNLSKYrklQHELDDAEERADMAESQA 1978
Cdd:pfam06008 166 SPQEENKALANALRDSLAEY---EAKLSDLRELLREAAAKT 203
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1595-1978 |
1.58e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.87 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1595 DMEkseiqAALEEAEGTLEH-EESKSLR------IQLELNQIKADVDRKLAEKDEEIDS---LRRNH---QRILESMQAT 1661
Cdd:COG3096 233 DME-----AALRENRMTLEAiRVTQSDRdlfkhlITEATNYVAADYMRHANERRELSERaleLRRELfgaRRQLAEEQYR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1662 LDAEAKSRNEAVRLRKKMEGDLNEMEvqlSHANR--QASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRN 1739
Cdd:COG3096 308 LVEMARELEELSARESDLEQDYQAAS---DHLNLvqTALRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1740 NLLAAEVEEL--------RALLEQSDRArkLAEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLSNEVDDAV--QEC 1809
Cdd:COG3096 385 EAAEEEVDSLksqladyqQALDVQQTRA--IQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVleLEQ 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1810 RNAEEKAKKAITDAAMMA-EELKKEQDTSAHLERMKKNMEQTiKDLQMRLDEAEQialkggkkqvlkLEARVKELENELE 1888
Cdd:COG3096 463 KLSVADAARRQFEKAYELvCKIAGEVERSQAWQTARELLRRY-RSQQALAQRLQQ------------LRAQLAELEQRLR 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1889 SEQKKsqeyqkgvrkyERRIKELSYQGEEDKKNLVRLQDLIDKMQAkvksykrQTEEAEEQANTNLSKYRKLQHELDDAE 1968
Cdd:COG3096 530 QQQNA-----------ERLLEEFCQRIGQQLDAAEELEELLAELEA-------QLEELEEQAAEAVEQRSELRQQLEQLR 591
|
410
....*....|
gi 2108526737 1969 ERADMAESQA 1978
Cdd:COG3096 592 ARIKELAARA 601
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1569-1993 |
1.62e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1569 EIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEGTLEHEESK--SLRIQL-----ELNQIKADVDRKLAEKD 1641
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLlrTLDDQWkekrdELNGELSAADAAVAKDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1642 EEIDSLRRNHQRI---------------------LESMQATLDA---------------------------------EAK 1667
Cdd:pfam12128 322 SELEALEDQHGAFldadietaaadqeqlpswqseLENLEERLKAltgkhqdvtakynrrrskikeqnnrdiagikdkLAK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1668 SRNEAVRLRKKMEGDLNEMEVQLSH----ANRQASESQKFLR----NLQVQIKDIQL--ELDETIHQNEEL--KEQVAVT 1735
Cdd:pfam12128 402 IREARDRQLAVAEDDLQALESELREqleaGKLEFNEEEYRLKsrlgELKLRLNQATAtpELLLQLENFDERieRAREEQE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1736 ERRNNLLAAEVEE--LRALLEQSDRARKLAEHELLEATERVNLLNSQntgLINQKKKLesdLSMLSNEVDDavqecrnAE 1813
Cdd:pfam12128 482 AANAEVERLQSELrqARKRRDQASEALRQASRRLEERQSALDELELQ---LFPQAGTL---LHFLRKEAPD-------WE 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1814 EKAKKAITDAAMMAEELKKEQDTSAHLErmkknmEQTIKDLQMRLDeaeQIALKGGKKQVLKLEARVKELENELESEQKK 1893
Cdd:pfam12128 549 QSIGKVISPELLHRTDLDPEVWDGSVGG------ELNLYGVKLDLK---RIDVPEWAASEEELRERLDKAEEALQSAREK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1894 SQEYQKGVRKYERRIKELSyQGEED-----KKNLVRLQDLIDKMQAKVKSYKRQTEEAEEQANTNLSKYRKlQHELDDAE 1968
Cdd:pfam12128 620 QAAAEEQLVQANGELEKAS-REETFartalKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEA-QLKQLDKK 697
|
490 500
....*....|....*....|....*
gi 2108526737 1969 ERADMAESQANKLRARTRDQGSKLA 1993
Cdd:pfam12128 698 HQAWLEEQKEQKREARTEKQAYWQV 722
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1649-1824 |
1.74e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1649 RNHQRILESMQAtLDAEAksrNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEEL 1728
Cdd:COG1579 3 PEDLRALLDLQE-LDSEL---DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1729 KEQVAvtERRNNllaaevEELRAL---LEQSDRARKLAEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLSNEVDDA 1805
Cdd:COG1579 79 EEQLG--NVRNN------KEYEALqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170
....*....|....*....
gi 2108526737 1806 VQECRNAEEKAKKAITDAA 1824
Cdd:COG1579 151 LAELEAELEELEAEREELA 169
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1236-1838 |
1.76e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.74 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1236 RRDLEEAMLHHEATTAALRKKhADSVAElseqiDSLQRVKQKLEKERSEAKmevddlastvEQLSKGKATSEKMCRLYED 1315
Cdd:NF041483 166 RRLLDESRAEAEQALAAARAE-AERLAE-----EARQRLGSEAESARAEAE----------AILRRARKDAERLLNAAST 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1316 QMNEAKAKADELqRQLNETNTQRARAQAesGELSRKLEER-----EAMVSQLQRAKNSFSQNVEDLKKQL---EEENKAK 1387
Cdd:NF041483 230 QAQEATDHAEQL-RSSTAAESDQARRQA--AELSRAAEQRmqeaeEALREARAEAEKVVAEAKEAAAKQLasaESANEQR 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1388 NALAHAlQSSRhdcdLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAiqRTEELEEAKKKLVTRLQEAEETV-- 1465
Cdd:NF041483 307 TRTAKE-EIAR----LVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKA--RTVAAEDTAAQLAKAARTAEEVLtk 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1466 ------ETSNAKCSSLEKTKHRLQTEIEDLvidleRANAAAAVLDKKQRNFDKVlAEWRQKYEECQseletsqKESRGLS 1539
Cdd:NF041483 380 asedakATTRAAAEEAERIRREAEAEADRL-----RGEAADQAEQLKGAAKDDT-KEYRAKTVELQ-------EEARRLR 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1540 TELFKLKnsyEETLDHLETIK----RENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAA------LEEAE 1609
Cdd:NF041483 447 GEAEQLR---AEAVAEGERIRgearREAVQQIEEAARTAEELLTKAKADADELRSTATAESERVRTEAIerattlRRQAE 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1610 GTLEH-------------EESKSLRIQLE--LNQIKADVDRKL-AEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAV 1673
Cdd:NF041483 524 ETLERtraeaerlraeaeEQAEEVRAAAEraARELREETERAIaARQAEAAEELTRLHTEAEERLTAAEEALADARAEAE 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1674 RLRKKMEgdlnemevqlSHANRQASESQKFLRNLQVQIKD----IQLELDETIHQNEELKEQVAVTERRNnlLAAEVEEL 1749
Cdd:NF041483 604 RIRREAA----------EETERLRTEAAERIRTLQAQAEQeaerLRTEAAADASAARAEGENVAVRLRSE--AAAEAERL 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1750 RALLEQS-DRARKlaehELLEATERV-----NLLNSQNTGLINQKKKLESDLSMLSNEVDDAVQECRNAEEK----AKKA 1819
Cdd:NF041483 672 KSEAQESaDRVRA----EAAAAAERVgteaaEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEEllasARKR 747
|
650
....*....|....*....
gi 2108526737 1820 ITDAAMMAEELKKEQDTSA 1838
Cdd:NF041483 748 VEEAQAEAQRLVEEADRRA 766
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
831-1316 |
2.18e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 831 LGHLEELRDERLAKVLTLLQAAARGKIMRMELLKLMERREALMIiqwnirafnAVKHWPWMKLFFKIKPLLrsATTEKEL 910
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK---------LLQLLPLYQELEALEAEL--AELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 911 VSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRcdlliktkiqLEAKVKEIMERLEde 990
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE----------LQQRLAELEEELE-- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 991 eemsanvlakkrKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIE----EMAALDETILKLTKEKKALLEAHQQ 1066
Cdd:COG4717 217 ------------EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAaallALLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1067 TLDDLqaeedkVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQLDEKLKKKdf 1146
Cdd:COG4717 285 LLALL------FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA-- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1147 emnemstRIEDEQALVNQLQKKIKELQARTEELEEELEADRAcrAKVEKQRSDVARELEELSERLEEAGGATSAQIEMNK 1226
Cdd:COG4717 357 -------EELEEELQLEELEQEIAALLAEAGVEDEEELRAAL--EQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1227 KR-EADFLKLRRDLEEAmlhheattAALRKKHADSVAELSEQIDSLQRVK--QKLEKERSEAKMEVDDLASTVEQLSKGK 1303
Cdd:COG4717 428 EElEEELEELEEELEEL--------EEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEEWAALKLAL 499
|
490
....*....|...
gi 2108526737 1304 ATSEKMCRLYEDQ 1316
Cdd:COG4717 500 ELLEEAREEYREE 512
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
907-1076 |
2.32e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 907 EKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKvkeiMER 986
Cdd:pfam07888 79 ESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE----LER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 987 LEDEEEMSanvLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEkkaLLEAHQQ 1066
Cdd:pfam07888 155 MKERAKKA---GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK---LTTAHRK 228
|
170
....*....|
gi 2108526737 1067 TLDDLQAEED 1076
Cdd:pfam07888 229 EAENEALLEE 238
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1372-1612 |
2.50e-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: 45.10 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1372 NVEDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVaqwrtkyeTDAIQRTEELEEAK 1451
Cdd:pfam06008 20 NLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAES--------ERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1452 KKLVTRLQEAEETVETSNAKCSSL-EKTKHRLQTEIEDLVIDLERANaaaavLDKKQRNFDKVLAEWRQKYEECQSELET 1530
Cdd:pfam06008 92 KNLIDNIKEINEKVATLGENDFALpSSDLSRMLAEAQRMLGEIRSRD-----FGTQLQNAEAELKAAQDLLSRIQTWFQS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1531 SQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSdqiSQGVKTIHELEKMKKGLDMEKSEIQAALEEAEG 1610
Cdd:pfam06008 167 PQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLN---LANQANLREFQRKKEEVSEQKNQLEETLKTARD 243
|
..
gi 2108526737 1611 TL 1612
Cdd:pfam06008 244 SL 245
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1229-1391 |
2.58e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1229 EADFLKLRRDLEEAMLHHEATTAALRKKHADsVAELSEQIDSLQrvkQKLEKERSEAKMEV------------------- 1289
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAEIAEAE---AEIEERREELGERAralyrsggsvsyldvllgs 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1290 ---DDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAK 1366
Cdd:COG3883 112 esfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
170 180
....*....|....*....|....*
gi 2108526737 1367 NSFSQNVEDLKKQLEEENKAKNALA 1391
Cdd:COG3883 192 AAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
900-1174 |
2.63e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 900 LLRSATTEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLslqLQAEQDNLADAEDrcdlLIKTKIQLEAK 979
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL---VNAGSERLRAVKD----IKQERDQLLNE 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 980 VKEIMERLEDeeeMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNlieeMAALDETILKLTKEKKA 1059
Cdd:pfam15921 662 VKTSRNELNS---LSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS----MEGSDGHAMKVAMGMQK 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1060 LLEAHQQTLDDLQAeedKVNILTKAKAKLEQQVDDLEgslEQEKKLRMDLERV---RRKLEGDLKLslesvmdLENDKQQ 1136
Cdd:pfam15921 735 QITAKRGQIDALQS---KIQFLEEAMTNANKEKHFLK---EEKNKLSQELSTVateKNKMAGELEV-------LRSQERR 801
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2108526737 1137 LDEKLKKKDFEMNEMSTRIEDEQALVNQLQKK-----------IKELQA 1174
Cdd:pfam15921 802 LKEKVANMEVALDKASLQFAECQDIIQRQEQEsvrlklqhtldVKELQG 850
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
902-1059 |
2.96e-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: 45.53 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 902 RSATTEKELVSLKEELAKLKEALEKsevKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDL------------- 968
Cdd:COG4942 77 ELAALEAELAELEKEIAELRAELEA---QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYlkylaparreqae 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 969 -LIKTKIQLEAKVKEIMERLEDEEEMSANVLAKKRKLEdecaelkKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALD 1047
Cdd:COG4942 154 eLRADLAELAALRAELEAERAELEALLAELEEERAALE-------ALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
170
....*....|..
gi 2108526737 1048 ETILKLTKEKKA 1059
Cdd:COG4942 227 ALIARLEAEAAA 238
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1485-1790 |
3.15e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1485 EIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENK 1564
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1565 NLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLELNQIkadvdrKLAEKDEEI 1644
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL------SEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1645 DSLRRNHQRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDEtihq 1724
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE---- 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526737 1725 nEELKEQVAVTERRNNLLAAEVEELRALLEQSDRARKLAEHELLEATERVNLLNSQNTGLINQKKK 1790
Cdd:COG4372 262 -ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1741-1978 |
3.77e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1741 LLAAEVEELRALLEQSDRARKLAEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLSNEVDDAVQECRNAEEKAKKAI 1820
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1821 TDAAMMAEELKKEQDTSAHLER-MKKNMEQTIKDLQMRLDEAEQIAlkggkKQVLKLEARVKELENELESEQKKSQEYQK 1899
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRaLYRLGRQPPLALLLSPEDFLDAV-----RRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2108526737 1900 GVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADMAESQA 1978
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
906-1144 |
3.95e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 906 TEKELVSLKEE---LAKLKEALEKSEVKRKELEERQVSliqeknDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKE 982
Cdd:PRK01156 488 IEIEVKDIDEKivdLKKRKEYLESEEINKSINEYNKIE------SARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLE 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 983 IME--RLEDEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKE----KHATENKVKNLIEEMAALDETIlKLTKE 1056
Cdd:PRK01156 562 DLDskRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGfpddKSYIDKSIREIENEANNLNNKY-NEIQE 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1057 KKALLEAHQQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQ 1136
Cdd:PRK01156 641 NKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
....*...
gi 2108526737 1137 LDEKLKKK 1144
Cdd:PRK01156 721 INETLESM 728
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1255-1761 |
4.19e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1255 KKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEV----DDLASTVEQLSKGKATSEKMCRlYEDQMNEAKAKADELQRQ 1330
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYnnamDDYNNLKSALNELSSLEDMKNR-YESEIKTAESDLSMELEK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1331 LNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAhALQSSRHDCDLLREQYDE 1410
Cdd:PRK01156 272 NNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS-VLQKDYNDYIKKKSRYDD 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1411 EQEAKADLQRALSKANAEV------AQWRTKYETDAIQRTEELEEAKKK-------LVTRLQEAEETVETSNAKCSSLEK 1477
Cdd:PRK01156 351 LNNQILELEGYEMDYNSYLksieslKKKIEEYSKNIERMSAFISEILKIqeidpdaIKKELNEINVKLQDISSKVSSLNQ 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1478 TKHRLQTEIEDLVIDLERANA-------AAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLK---- 1546
Cdd:PRK01156 431 RIRALRENLDELSRNMEMLNGqsvcpvcGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKeyle 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1547 ----NSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKKG-LDMEKSE---------------IQAALE 1606
Cdd:PRK01156 511 seeiNKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEdLDSKRTSwlnalavislidietNRSRSN 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1607 EAEGTLEHEESKSLRIQLELNQIKADVDRKLAEKDEEIDSLRrNHQRILESMQATLDaeaKSRNEAVRLRKKMEGdLNEM 1686
Cdd:PRK01156 591 EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLN-NKYNEIQENKILIE---KLRGKIDNYKKQIAE-IDSI 665
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526737 1687 EVQLSHANRQASESQKFLRNLQVQIKDIQLELdetihqnEELKEQVAVTERRNNLLAAEVEELRALLEQSDRARK 1761
Cdd:PRK01156 666 IPDLKEITSRINDIEDNLKKSRKALDDAKANR-------ARLESTIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1409-1529 |
4.43e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1409 DEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKklvtRLQEAEETVETsnaKCSSLEKTKHRLQTEIED 1488
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEK----RLLQKEENLDR---KLELLEKREEELEKKEKE 118
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2108526737 1489 lvidleranaaaavLDKKQRNFDKVLAEWRQKYEECQSELE 1529
Cdd:PRK12704 119 --------------LEQKQQELEKKEEELEELIEEQLQELE 145
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1597-1987 |
5.30e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 45.05 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1597 EKSEIQAALEEAEGTLEHEESKSlrIQLELNQIKADVDRKLAEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLR 1676
Cdd:pfam13166 90 ESIEIQEKIAKLKKEIKDHEEKL--DAAEANLQKLDKEKEKLEADFLDECWKKIKRKKNSALSEALNGFKYEANFKSRLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1677 KKMEGDLNEMEVQLSHANRQASESQKFLRNLQ----VQIKDIQLEldeTIHQNEELKEQVAVTE------RRNNLLAAEV 1746
Cdd:pfam13166 168 REIEKDNFNAGVLLSDEDRKAALATVFSDNKPeiapLTFNVIDFD---ALEKAEILIQKVIGKSsaieelIKNPDLADWV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1747 EELRALLEQ-------------SDRARKLAEHELLEATERVNLLNSQntglinqKKKLESDLSMLSNEVDDAVQecrnae 1813
Cdd:pfam13166 245 EQGLELHKAhldtcpfcgqplpAERKAALEAHFDDEFTEFQNRLQKL-------IEKVESAISSLLAQLPAVSD------ 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1814 ekakkaiTDAAMMAEELKKEQdtsahLERMKKNMEQTIKDLQMRLDEaeqialkggKKQVLKLEARVKELENELESEQKK 1893
Cdd:pfam13166 312 -------LASLLSAFELDVED-----IESEAEVLNSQLDGLRRALEA---------KRKDPFKSIELDSVDAKIESINDL 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1894 SQEYQKGVRKYERRIKELsyqgeEDKKNlvrlqdlidkmQAKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADM 1973
Cdd:pfam13166 371 VASINELIAKHNEITDNF-----EEEKN-----------KAKKKLRLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKN 434
|
410
....*....|....
gi 2108526737 1974 AESQANKLRARTRD 1987
Cdd:pfam13166 435 LEAEIKKLREEIKE 448
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1469-1796 |
5.39e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 45.23 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1469 NAKCSSLEKTKHR-LQTEIEDLVIDLERANAAAAVLDkkqrnfDKVLAEWRQKYEEcQSELETSQK-ESRGLSTELFKLK 1546
Cdd:PLN03229 420 NMKKREAVKTPVReLEGEVEKLKEQILKAKESSSKPS------ELALNEMIEKLKK-EIDLEYTEAvIAMGLQERLENLR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1547 NSYEETLDHLETIkreNKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKseiqaALEEAEGTLEHeESKSLRIQLEL 1626
Cdd:PLN03229 493 EEFSKANSQDQLM---HPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDMLN-----EFSRAKALSEK-KSKAEKLKAEI 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1627 NQ-IKADVDRklAEKDEEIDSLRRNHQRILESMQATLDAEAKSrnEAVRLRKKMEGDLNE------MEVQLSHANRQASE 1699
Cdd:PLN03229 564 NKkFKEVMDR--PEIKEKMEALKAEVASSGASSGDELDDDLKE--KVEKMKKEIELELAGvlksmgLEVIGVTKKNKDTA 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1700 SQKFLRNLQVQIKDIQLELdetihqNEELKEQVAVTERRNnllaaEVEELRALLEQSDRARKLAEHELLEATE---RVNL 1776
Cdd:PLN03229 640 EQTPPPNLQEKIESLNEEI------NKKIERVIRSSDLKS-----KIELLKLEVAKASKTPDVTEKEKIEALEqqiKQKI 708
|
330 340
....*....|....*....|.
gi 2108526737 1777 LNSQNTGLINQK-KKLESDLS 1796
Cdd:PLN03229 709 AEALNSSELKEKfEELEAELA 729
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
909-1172 |
5.44e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 909 ELVSLKEELAKLKEALEKSEVKrkELEERQVSLIQEKndlslqlqaeqdnladaedrcdllIKTKIQLEAKVKEIMERLE 988
Cdd:PRK05771 10 LIVTLKSYKDEVLEALHELGVV--HIEDLKEELSNER------------------------LRKLRSLLTKLSEALDKLR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 989 DEeeMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEkhatenkVKNLIEEMAALDETILKLTKEKKAL--LEAhqq 1066
Cdd:PRK05771 64 SY--LPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERLepWGN--- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1067 tLD-DLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKklrmdLERVRRKLEGDLKLslesVMDLENDKQQLDEKLKKKD 1145
Cdd:PRK05771 132 -FDlDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVEN-----VEYISTDKGYVYVV----VVVLKELSDEVEEELKKLG 201
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2108526737 1146 FE-------------MNEMSTRIEDEQALVNQLQKKIKEL 1172
Cdd:PRK05771 202 FErleleeegtpselIREIKEELEEIEKERESLLEELKEL 241
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1847-1986 |
5.89e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 43.28 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1847 MEQTIKDLQMRLDEAEQialkggkkQVLKLEARVKELENELEseqkksqEYQKGVRKYERRIKELSYQGEED--KKNLVR 1924
Cdd:COG1842 28 LDQAIRDMEEDLVEARQ--------ALAQVIANQKRLERQLE-------ELEAEAEKWEEKARLALEKGREDlaREALER 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108526737 1925 LQDLidkmQAKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADMAESQANKLRARTR 1986
Cdd:COG1842 93 KAEL----EAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEK 150
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1251-1391 |
5.93e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1251 AALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSK---------GKATSEKMCRLYEDQMNEAK 1321
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikkyeeqlGNVRNNKEYEALQKEIESLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1322 AKADELQRQLNETNTQRARAQAESGELSRKLEEREAmvsQLQRAKNSFSQNVEDLKKQLEEENKAKNALA 1391
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1724-1994 |
6.72e-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: 44.78 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1724 QNEELK---EQVAVTERRNNLLAAEVEELRALLEQSDRARKLAEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLSN 1800
Cdd:pfam01576 3 QEEEMQakeEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1801 EVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVLkLEARV 1880
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKL-LEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1881 KELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEAEEQANTNLSKYRKL 1960
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270
....*....|....*....|....*....|....
gi 2108526737 1961 QHELDDAEERADMAESQANKLRARTRDQGSKLAE 1994
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISE 275
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1569-1775 |
6.81e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 44.63 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1569 EIADLSDQISQGVKTIHELEKM-----KKGLDMEKSEIQAALEEAEGTLEHEESKSLRiQLELNQIKA---DVDRKLAEK 1640
Cdd:pfam05667 276 DLAELLSSFSGSSTTDTGLTKGsrfthTEKLQFTNEAPAATSSPPTKVETEEELQQQR-EEELEELQEqleDLESSIQEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1641 DEEIDSLRRNHQRILESMQaTLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELde 1720
Cdd:pfam05667 355 EKEIKKLESSIKQVEEELE-ELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPL-- 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526737 1721 tIHQNEELKEQVAVTERRNNLLAAEVEELRALLEQ-SDRARKLAE--HELLEATERVN 1775
Cdd:pfam05667 432 -IEEYRALKEAKSNKEDESQRKLEEIKELREKIKEvAEEAKQKEElyKQLVAEYERLP 488
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1264-1464 |
6.83e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1264 LSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEkmcrlYEDQMNEAKAKADELQRQLNETNTQRARAQA 1343
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1344 ESGELSRKLEEREAMVSQLQRaknsfSQNVEDLKKQLEEenkaknalahaLQSSRhdcDLLREQYDEE----QEAKADLQ 1419
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAE-----------LEAEL---AELSARYTPNhpdvIALRAQIA 301
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2108526737 1420 RALSKANAEVAQWRTKYETD---AIQRTEELEEAKKKLVTRLQEAEET 1464
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAEleaLQAREASLQAQLAQLEARLAELPEL 349
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
904-1169 |
7.04e-04 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 44.76 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 904 ATTEKELVSLKEELAKLKEALEKSEVKR----KELEERQVSLIQEKNDLSLQLQAEQDnladaEDRCDLLIKTKIQLEAK 979
Cdd:pfam18971 599 AVAEAKSTGNYDEVKKAQKDLEKSLRKRehleKEVEKKLESKSGNKNKMEAKAQANSQ-----KDEIFALINKEANRDAR 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 980 VKEIMERLEdeeemsanvlAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKnliEEMAALDETI--LKLTKEK 1057
Cdd:pfam18971 674 AIAYTQNLK----------GIKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAE---ETLKALKGSVkdLGINPEW 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1058 KALLEAHQQTLDDLQAEEDK-VNILTKAKAKLEQQVDDLEGSLEQEKKL-RMDLERVRRKLEGDLKLSLESVMDLEN-DK 1134
Cdd:pfam18971 741 ISKVENLNAALNEFKNGKNKdFSKVTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKNfSK 820
|
250 260 270
....*....|....*....|....*....|....*.
gi 2108526737 1135 QQLDEKLKK-KDFEMNEMStriEDEQALVNQLQKKI 1169
Cdd:pfam18971 821 EQLAQQAQKnEDFNTGKNS---ELYQSVKNSVNKTL 853
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
826-1171 |
7.10e-04 |
|
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: 44.94 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 826 FKAGLLGHLEELRDERLAKVLTLLQAaarGKIMrMELLKLMERREALM-----IIQWNIRAFNAVKHWPWMKLFF----K 896
Cdd:pfam15818 5 FKTSLLEALEELRMRREAETQYEEQI---GKII-VETQELKWQKETLQnqketLAKQHKEAMAVFKKQLQMKMCAleeeK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 897 IKPLLRSATTEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQL 976
Cdd:pfam15818 81 GKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLHLLAKEDHHKQLNEIEKYYATITGQFGLVKENHGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 977 EAKVKEIMerledeeEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVE---KEKHATEN--------KVKNLIEEMAA 1045
Cdd:pfam15818 161 EQNVQEAI-------QLNKRLSALNKKQESEICSLKKELKKVTSDLIKSKvtcQYKMGEENinltikeqKFQELQERLNM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1046 LDETILKLTKEKKALLEAHQQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEgslEQEKKLRMDLERVRRKlegdLKLSLE 1125
Cdd:pfam15818 234 ELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALK---ENNQTLERDNELQREK----VKENEE 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2108526737 1126 SVMDLENDKQQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKE 1171
Cdd:pfam15818 307 KFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQE 352
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
894-1175 |
7.16e-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: 44.46 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 894 FFKIKPLLRSAT-----TEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEkndlslqLQAEQDNLADAEDrcdl 968
Cdd:pfam06160 81 FKKAKKALDEIEellddIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKT-------LLANRFSYGPAID---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 969 liktkiQLEAKVKEIMERLEDEEEMSAN---VLAKK--RKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEM 1043
Cdd:pfam06160 150 ------ELEKQLAEIEEEFSQFEELTESgdyLEAREvlEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREM 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1044 A----ALDEtiLKLTKEKKALLEAHQQTLDDL-QAEEDKVNiltKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEG 1118
Cdd:pfam06160 224 EeegyALEH--LNVDKEIQQLEEQLEENLALLeNLELDEAE---EALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIED 298
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2108526737 1119 DLKlslesvmDLENDKQQLDEKLK--KKDFEMNemstriEDEQALVNQLQKKIKELQAR 1175
Cdd:pfam06160 299 YLE-------HAEEQNKELKEELErvQQSYTLN------ENELERVRGLEKQLEELEKR 344
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
900-1173 |
7.44e-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: 44.78 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 900 LLRSATTEKELVSLKEELAKLKEALEKSEVKRKELEerqvsliQEKNDLslqlqaeQDNLADAEDRCDLLIKTKIQLEAK 979
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQ-------QERDEL-------ADEIASGASGKSALQDEKRRLEAR 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 980 VKEIMERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETIlkLTKEKKA 1059
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTV--KSKFKSS 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1060 LleahqqtlddlqaeedkvniltkakAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQLDE 1139
Cdd:pfam01576 969 I-------------------------AALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKD 1023
|
250 260 270
....*....|....*....|....*....|....
gi 2108526737 1140 KLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQ 1173
Cdd:pfam01576 1024 QAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQ 1057
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1226-1503 |
7.48e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 44.29 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1226 KKREADFLKLRRDLEEAMLHHEATTAALrKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEvddLASTVEQLSKGKAT 1305
Cdd:pfam19220 100 REAEAAKEELRIELRDKTAQAEALERQL-AAETEQNRALEEENKALREEAQAAEKALQRAEGE---LATARERLALLEQE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1306 SEKMCRLYEDQMNEA---KAKADELQRQLNetnTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEE 1382
Cdd:pfam19220 176 NRRLQALSEEQAAELaelTRRLAELETQLD---ATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1383 ENKAKNALAHALQSSRHdcdLLREQYDEEQEAKA---DLQRALSKANAEVAQWRTKYEtDAIQRTEELEEAKKKLVTR-- 1457
Cdd:pfam19220 253 LTARAAATEQLLAEARN---QLRDRDEAIRAAERrlkEASIERDTLERRLAGLEADLE-RRTQQFQEMQRARAELEERae 328
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108526737 1458 ------------LQEAEETVETSNAKCSSL----EKTKHRLQTEIEDLVIDLERANAAAAVL 1503
Cdd:pfam19220 329 mltkalaakdaaLERAEERIASLSDRIAELtkrfEVERAALEQANRRLKEELQRERAERALA 390
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1347-1618 |
8.08e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1347 ELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKAN 1426
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1427 AEVAQWRTKYETDAIQRTEeleeaKKKLVTRLQEAEETVETSNakcSSLEKTKhRLQTEIEDLVIDLERANAAAAVLDKK 1506
Cdd:COG1340 92 EELDELRKELAELNKAGGS-----IDKLRKEIERLEWRQQTEV---LSPEEEK-ELVEKIKELEKELEKAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1507 QRNFDKvLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHE 1586
Cdd:COG1340 163 KELRAE-LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE 241
|
250 260 270
....*....|....*....|....*....|..
gi 2108526737 1587 LEKMKKGLDMEKSEIQAALEEAEGTLEHEESK 1618
Cdd:COG1340 242 LRKELKKLRKKQRALKREKEKEELEEKAEEIF 273
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1635-1975 |
8.10e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1635 RKLAEKDEEIDSLRRNHQRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDI 1714
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1715 QLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRAlleqsdrARKLAEHELLEATERVNLLNSQNTGLINQKKKLESD 1794
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK-------ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1795 LSMLSNEVDDAVQECRNAEEKAKKAItdaammAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVL 1874
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQA------LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1875 KLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEEAEEQANTNL 1954
Cdd:COG4372 233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
|
330 340
....*....|....*....|.
gi 2108526737 1955 SKYRKLQHELDDAEERADMAE 1975
Cdd:COG4372 313 LEDALLAALLELAKKLELALA 333
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1257-1474 |
8.91e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1257 HADS-VAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKmcrlyedQMNEAKAKADELQRQLNETN 1335
Cdd:COG3883 13 FADPqIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA-------EIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1336 TQ---RARAQAESGE-----------------------LSRKLEEREAMVSQLQRAKNSFSQ---NVEDLKKQLEEENKA 1386
Cdd:COG3883 86 EElgeRARALYRSGGsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAkkaELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1387 KNALAHALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEETVE 1466
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
....*...
gi 2108526737 1467 TSNAKCSS 1474
Cdd:COG3883 246 AAGAGAAG 253
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
913-1167 |
9.10e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.43 E-value: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 913 LKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLiktkiqlEAKVKEIMERLEDEEE 992
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL-------QTEVDALRLRLEEKES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 993 MSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALLEAHQQ------ 1066
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNtdtalt 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1067 TLDDLQAEEDKV-NILTKAKAKLEQQVDDlegSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQLDEKLKKKD 1145
Cdd:pfam10174 440 TLEEALSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKD 516
|
250 260
....*....|....*....|....*.
gi 2108526737 1146 FEMN----EMSTRIEDEQALVNQLQK 1167
Cdd:pfam10174 517 SKLKsleiAVEQKKEECSKLENQLKK 542
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
907-1409 |
9.92e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 907 EKELVSLKEELAKLKEALEKSEVKRKELEerqvsliQEKNDLSLQLQA---EQDNLADAEDRCDLLIKTKIQLEAKVKEI 983
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKSHSITL-------KEIERLSIEYNNamdDYNNLKSALNELSSLEDMKNRYESEIKTA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 984 MERLEDEE--------------EMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIE-------- 1041
Cdd:PRK01156 262 ESDLSMELeknnyykeleerhmKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVlqkdyndy 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1042 -----EMAALDETILKLT-------------KEKKALLEAHQQTLDDLQAEEDKV--------NILTKAKAKLEQQVDDL 1095
Cdd:PRK01156 342 ikkksRYDDLNNQILELEgyemdynsylksiESLKKKIEEYSKNIERMSAFISEIlkiqeidpDAIKKELNEINVKLQDI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1096 E---GSLEQEKK-LRMDLERVRRKLE---------------GDLKlSLESVMDLENDKQQLDEKLKKKDFEMNEMSTRIE 1156
Cdd:PRK01156 422 SskvSSLNQRIRaLRENLDELSRNMEmlngqsvcpvcgttlGEEK-SNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIV 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1157 DEQALVNQLQ-KKIKELQARTEELEEEleadracRAKVEKQRSDVARELEELSERLEEAGGATSAQIEMNKKREADFLKL 1235
Cdd:PRK01156 501 DLKKRKEYLEsEEINKSINEYNKIESA-------RADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1236 RRDLEEAMLHH-EATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMcRLYE 1314
Cdd:PRK01156 574 LAVISLIDIETnRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKL-RGKI 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1315 DQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLE-------EREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAK 1387
Cdd:PRK01156 653 DNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDdakanraRLESTIEILRTRINELSDRINDINETLESMKKIK 732
|
570 580
....*....|....*....|..
gi 2108526737 1388 NALAhalqssrhDCDLLREQYD 1409
Cdd:PRK01156 733 KAIG--------DLKRLREAFD 746
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
892-1301 |
1.01e-03 |
|
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: 43.98 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 892 KLFFKIKPLLRSA-----TTEKELVSLKEELAKLK-EALEKSEVKRKELEErqvsliQEKNDLSLQLQAEQDNLADAE-D 964
Cdd:pfam09731 34 DFFEEYIPYGEEVvlyalGEDPPLAPKPKTFRPLQpSVVSAVTGESKEPKE------EKKQVKIPRQSGVSSEVAEEEkE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 965 RCDLLIKTKIQLEAKVKEIMERLEdeeEMSANVLAKKRKLEDECAELKKDiddleitlakvekEKHATENKVKNLIEEMA 1044
Cdd:pfam09731 108 ATKDAAEAKAQLPKSEQEKEKALE---EVLKEAISKAESATAVAKEAKDD-------------AIQAVKAHTDSLKEASD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1045 ALDETILKLTKEKKALLEAHQQTLDDLQAEEDKVNIlTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSL 1124
Cdd:pfam09731 172 TAEISREKATDSALQKAEALAEKLKEVINLAKQSEE-EAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1125 ESVMDLENDKQQLDEKL--------KKKDFEMNEMSTRIEDEQALVNQLQKKIKELQARteeleeeleADRACRAKVEKQ 1196
Cdd:pfam09731 251 LVASERIVFQQELVSIFpdiipvlkEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKR---------EEKHIERALEKQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1197 RSDVARELEELSERLEEAGGATSAQIEmnKKREADFLKLRRDLEEAM---LHHEATTAALRKKHADSVAELSEQIDSLQR 1273
Cdd:pfam09731 322 KEELDKLAEELSARLEEVRAADEAQLR--LEFEREREEIRESYEEKLrteLERQAEAHEEHLKDVLVEQEIELQREFLQD 399
|
410 420
....*....|....*....|....*...
gi 2108526737 1274 VKQKLEKERSEAKMEVDDLASTVEQLSK 1301
Cdd:pfam09731 400 IKEKVEEERAGRLLKLNELLANLKGLEK 427
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1853-1994 |
1.01e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1853 DLQMRLDEAEQiALKGGKKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKNL--VRLQDLID 1930
Cdd:COG1579 14 ELDSELDRLEH-RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNKEYE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108526737 1931 KMQAKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADMAESQANKLRARTRDQGSKLAE 1994
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1525-1912 |
1.03e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1525 QSELETSQKESRGLSTELFKLKNSYEETLDHLETIK----RENKNLQEEIADLSDQISQGVKTIHELEKMKKGLDMEKSE 1600
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDReqweRQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1601 IQaalEEAEGTLEHEESKSLRIqLELNQIKADVDRKLAEKDEEIDSLRRNHQRILesmqatldaeaKSRNEAVRLRKKME 1680
Cdd:pfam07888 113 LS---EEKDALLAQRAAHEARI-RELEEDIKTLTQRVLERETELERMKERAKKAG-----------AQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1681 GDLNEMEVQLSHANrqaSESQKfLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEVEELRALLEQSDRAR 1760
Cdd:pfam07888 178 AKLQQTEEELRSLS---KEFQE-LRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1761 KLAEHELLEatervnlLNSQNTGLINQKKKLESDLSMLSNEVDDAVQECRnaEEKAKKAiTDAAMMAEELKKEQDTSAHL 1840
Cdd:pfam07888 254 EGLGEELSS-------MAAQRDRTQAELHQARLQAAQLTLQLADASLALR--EGRARWA-QERETLQQSAEADKDRIEKL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1841 ERMKKNMEQTIKDLQMRLDEAE----------QIALKGGKKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKE 1910
Cdd:pfam07888 324 SAELQRLEERLQEERMEREKLEvelgrekdcnRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLET 403
|
..
gi 2108526737 1911 LS 1912
Cdd:pfam07888 404 VA 405
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1517-1957 |
1.04e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.27 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1517 WRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQIsqgvktihelEKMKKGLDM 1596
Cdd:TIGR01612 556 WKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDKN----------EYIKKAIDL 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1597 EK--SEIQAALEEAEGTLEHEESKSLR--------IQLELNQI-KADVDRKLAE-----KDEEIDSLRRNHQriLESMQA 1660
Cdd:TIGR01612 626 KKiiENNNAYIDELAKISPYQVPEHLKnkdkiystIKSELSKIyEDDIDALYNElssivKENAIDNTEDKAK--LDDLKS 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1661 TLDAE-AKSRN---EAVRLR-KKMEGDLNEMEVQLSHANRQA-SESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAV 1734
Cdd:TIGR01612 704 KIDKEyDKIQNmetATVELHlSNIENKKNELLDIIVEIKKHIhGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNK 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1735 TERRNNLLAAEVEELRALLEQSDRARKLAEHELLEATERVNLLNSQNTGLINQKKKLESDlsmLSNEVDDAVQECRNAEE 1814
Cdd:TIGR01612 784 YKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDD---FLNKVDKFINFENNCKE 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1815 KAKKAITDAAMMAEELKKE--QDTSAHLERMKKNMEQTIKDLQMRLDEAEQialkgGKKQVLKLEARVKELENELESEQK 1892
Cdd:TIGR01612 861 KIDSEHEQFAELTNKIKAEisDDKLNDYEKKFNDSKSLINEINKSIEEEYQ-----NINTLKKVDEYIKICENTKESIEK 935
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526737 1893 KSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQD-LIDKMQAKVKSYKRQTEEAEEQANTNLSKY 1957
Cdd:TIGR01612 936 FHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNtLIDKINELDKAFKDASLNDYEAKNNELIKY 1001
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1401-1619 |
1.05e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1401 CDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEETVETSNAKCSSLEKTKH 1480
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1481 RLQTEIEDLV------IDLERA----NAAAAVLDKKQRNFDKVLAEWRQKYEECQSELE--------TSQKESRGLSTEL 1542
Cdd:PRK05771 118 ELEQEIERLEpwgnfdLDLSLLlgfkYVSVFVGTVPEDKLEELKLESDVENVEYISTDKgyvyvvvvVLKELSDEVEEEL 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526737 1543 fkLKNSYEE-TLDHLETIKRENKNLQEEIADLSDQISqgvKTIHELEKMKKGLDmekSEIQAALEEAEGTLEHEESKS 1619
Cdd:PRK05771 198 --KKLGFERlELEEEGTPSELIREIKEELEEIEKERE---SLLEELKELAKKYL---EELLALYEYLEIELERAEALS 267
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
864-987 |
1.16e-03 |
|
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).
Pssm-ID: 409646 [Multi-domain] Cd Length: 149 Bit Score: 41.34 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 864 KLMERREALMIIQWNIRAFNAVK-HWPwmklffKIKPLLRSATTEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLI 942
Cdd:cd21759 40 KILYRREALIKIQKTVRGYLARKkHRP------RIKGLRKIRALEKQLKEMEEIASQLKKDKDKWTKQVKELKKEIDALI 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2108526737 943 QE-KNDlslqlqaEQDNLADAEDRCDlliktkiQLEAKVKEIMERL 987
Cdd:cd21759 114 KKiKTN-------DMITRKEIDKLYN-------ALVKKVDKQLAEL 145
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1705-1942 |
1.42e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1705 RNLQVQIKDIQLELDetiHQNEELKEQVAVTERRNNLLAAEVEELRALLEQSDRARKLAEHELLEATERVNLLNSQNTGL 1784
Cdd:PHA02562 177 RELNQQIQTLDMKID---HIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1785 INQKKKLESDLSMLSNEVDDAvqecrNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQI 1864
Cdd:PHA02562 254 SAALNKLNTAAAKIKSKIEQF-----QKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEI 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526737 1865 alkggKKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKRQ 1942
Cdd:PHA02562 329 -----MDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
920-1152 |
1.46e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.77 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 920 LKEALEKSEVKRKELEERQVSLIQE---KNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEIM-ERLEDEEEMSA 995
Cdd:PLN03188 1045 PEKKLEQERLRWTEAESKWISLAEElrtELDASRALAEKQKHELDTEKRCAEELKEAMQMAMEGHARMlEQYADLEEKHI 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 996 NVLAKKRKLEDECAELKKD-------------IDDL--EITLAKVEKEKHAT----ENK-----VKNLIEEMAALDETIL 1051
Cdd:PLN03188 1125 QLLARHRRIQEGIDDVKKAaaragvrgaeskfINALaaEISALKVEREKERRylrdENKslqaqLRDTAEAVQAAGELLV 1204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1052 KLTKEKKALLEAHQQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEgslEQEKKLRMDLERVRRKLEGDLKLSLESVMDLE 1131
Cdd:PLN03188 1205 RLKEAEEALTVAQKRAMDAEQEAAEAYKQIDKLKRKHENEISTLN---QLVAESRLPKEAIRPACNDDCMAKYDAGEPLS 1281
|
250 260
....*....|....*....|....*
gi 2108526737 1132 NDKQQLDEKL----KKKDFEMNEMS 1152
Cdd:PLN03188 1282 EGDQQWREEFepfyKKEDGELSKLA 1306
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
1516-1589 |
1.46e-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: 1.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108526737 1516 EWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEK 1589
Cdd:COG4026 132 ELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLK 205
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1837-1971 |
1.61e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1837 SAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVLKL----EARVKELENELESEQKKSQEYQKGVRKYERRIKELS 1912
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLrnefEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526737 1913 YQGEEDKKNLVRLQDLIDKMQAKVksykrqtEEAEEQANTNLSKYRKLQHE------LDDAEERA 1971
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEEL-------EELIEEQLQELERISGLTAEeakeilLEKVEEEA 167
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1810-1973 |
1.78e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1810 RNAEEKAKKAITDAAMMAEELKKEqdtsahLERMKKNMEQTIKDLQMRL-DEAEQiALKGGKKQVLKLEARVKE----LE 1884
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKE------AEAIKKEALLEAKEEIHKLrNEFEK-ELRERRNELQKLEKRLLQkeenLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1885 NELESEQKKSQEYQKGVRKYERRIKELSYQGEEdkknlvrLQDLIDKMQAKVKSY---------KRQTEEAEEQANTNLS 1955
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEE-------LEELIEEQLQELERIsgltaeeakEILLEKVEEEARHEAA 172
|
170
....*....|....*...
gi 2108526737 1956 KYRKLQHEldDAEERADM 1973
Cdd:PRK12704 173 VLIKEIEE--EAKEEADK 188
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1334-1537 |
2.08e-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: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1334 TNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQE 1413
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1414 AKADLQRALSKANAEVAQWRTKYE----TDAIQRTEELE---EAKKKLVTRLQEAEETVETSNAKCSS----LEKTKHRL 1482
Cdd:COG3883 87 ELGERARALYRSGGSVSYLDVLLGsesfSDFLDRLSALSkiaDADADLLEELKADKAELEAKKAELEAklaeLEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2108526737 1483 QTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRG 1537
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1849-1986 |
2.36e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1849 QTIKDLQMRLDEAEQiALKGGKKQVLKLEA----RVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKNLVR 1924
Cdd:PHA02562 181 QQIQTLDMKIDHIQQ-QIKTYNKNIEEQRKkngeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNK 259
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526737 1925 LQDLIDKMQAKVKSYKR----------------QTEEAEEQANTNLSKYRKLQHELDDAEERADMAESQANKLRARTR 1986
Cdd:PHA02562 260 LNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSK 337
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1247-1992 |
2.63e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1247 EATT--AALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKmcrlyedqmnEAKAKA 1324
Cdd:PRK04863 265 ESTNyvAADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQ----------DYQAAS 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1325 DELQRQLNETNTQRA--RAQAESGELSRKLEEREAMVS----QLQRAKNSFSQN---VEDLKKQLEEENKA-----KNAL 1390
Cdd:PRK04863 335 DHLNLVQTALRQQEKieRYQADLEELEERLEEQNEVVEeadeQQEENEARAEAAeeeVDELKSQLADYQQAldvqqTRAI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1391 A-----HALQSSRHDCDL--------------LREQYDEEQEAKADLQRALSKANAEVAQWRTKYE-----TDAIQRTEE 1446
Cdd:PRK04863 415 QyqqavQALERAKQLCGLpdltadnaedwleeFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQlvrkiAGEVSRSEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1447 LEEAKkklvtrlqEAEETVETSNAKCSSLEKTKHRLQteiedlviDLERAnaaaavlDKKQRNFDKVLAEWRQKY---EE 1523
Cdd:PRK04863 495 WDVAR--------ELLRRLREQRHLAEQLQQLRMRLS--------ELEQR-------LRQQQRAERLLAEFCKRLgknLD 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1524 CQSELETSQKEsrgLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKMKK--GLDMEKSE- 1600
Cdd:PRK04863 552 DEDELEQLQEE---LEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREqsGEEFEDSQd 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1601 ----IQAALE-EAEGTLEHEESKSLRIQLE----------------LNQIKADVDRKL-AE--KDEEID----------- 1645
Cdd:PRK04863 629 vteyMQQLLErERELTVERDELAARKQALDeeierlsqpggsedprLNALAERFGGVLlSEiyDDVSLEdapyfsalygp 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1646 ----------SLRRNHQRILES-------MQATLDAEAKSRNEAVRLRKKMEGDLNEMEVQLSHA------NRQASESqk 1702
Cdd:PRK04863 709 arhaivvpdlSDAAEQLAGLEDcpedlylIEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFpevplfGRAAREK-- 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1703 flrnlqvQIKDIQLELDETIHQNEELKEQVAVTERRNNLLAAEV-------------EELRALLEQ-SDRARKLAEHELL 1768
Cdd:PRK04863 787 -------RIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIgshlavafeadpeAELRQLNRRrVELERALADHESQ 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1769 EATERVNLLNSQNtgLINQKKKLESDLSMLSNE-VDDAVQECR---NAEEKAKKAITDAAMMAEELKKE----QDTSAHL 1840
Cdd:PRK04863 860 EQQQRSQLEQAKE--GLSALNRLLPRLNLLADEtLADRVEEIReqlDEAEEAKRFVQQHGNALAQLEPIvsvlQSDPEQF 937
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1841 ERMKKNMEQ---TIKDLQMRLD---------------EAEQIaLKGGKKQVLKLEARVKELENELESEQKKSQEYQKGVR 1902
Cdd:PRK04863 938 EQLKQDYQQaqqTQRDAKQQAFaltevvqrrahfsyeDAAEM-LAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLA 1016
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1903 KYERRIKEL--SYQGEEDKknlvrLQDLIDKMQAKVKSYkrqTEEAEEQANtnlSKYRKLQHELDDAEERADMAESQANK 1980
Cdd:PRK04863 1017 QYNQVLASLksSYDAKRQM-----LQELKQELQDLGVPA---DSGAEERAR---ARRDELHARLSANRSRRNQLEKQLTF 1085
|
890
....*....|..
gi 2108526737 1981 LRARTRDQGSKL 1992
Cdd:PRK04863 1086 CEAEMDNLTKKL 1097
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
921-1598 |
2.79e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 921 KEALEKSEvKRKELEERQVSLIQEKNDLSLQLQAEQDN---LADAEDRCDLLIKTKIQLEAKVKEIMERLEDEEEMSANV 997
Cdd:PRK04863 499 RELLRRLR-EQRHLAEQLQQLRMRLSELEQRLRQQQRAerlLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEA 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 998 LAKKRKLEDECAELKKDIDdleiTLAKVEKEKHATENKVKNLIEEMAALDETilkltkeKKALLEAHQQTLDDLQAEEDK 1077
Cdd:PRK04863 578 RERRMALRQQLEQLQARIQ----RLAARAPAWLAAQDALARLREQSGEEFED-------SQDVTEYMQQLLERERELTVE 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1078 VNILTKAKAKLEQQVDDLE----GSLEQEKKLR------------------------------------MDLERVRRKLE 1117
Cdd:PRK04863 647 RDELAARKQALDEEIERLSqpggSEDPRLNALAerfggvllseiyddvsledapyfsalygparhaivvPDLSDAAEQLA 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1118 GdLKLSLESVMDLENDKQQLDEKLkkkdFEMNEMstriedEQALVNQLqkkikelqarteeleeeleADRACRakvekqr 1197
Cdd:PRK04863 727 G-LEDCPEDLYLIEGDPDSFDDSV----FSVEEL------EKAVVVKI-------------------ADRQWR------- 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1198 sdvareleelserleeaggatsaqiemnkkreadflkLRRDLEEAMLHHEAttaalRKKHAdsvAELSEQIDSLQRvkqk 1277
Cdd:PRK04863 770 -------------------------------------YSRFPEVPLFGRAA-----REKRI---EQLRAEREELAE---- 800
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1278 lekERSEAKMEVDDLASTVEQLSKGKATSEKMCRLY--EDQMNEAKAKADELQRQLN--ETNTQRARAQAesgelsRKLE 1353
Cdd:PRK04863 801 ---RYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEAdpEAELRQLNRRRVELERALAdhESQEQQQRSQL------EQAK 871
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1354 EREAMVSQLQR-----AKNSFSQNVEDLKKQLEEENKAKNALAH-------------ALQSSRHDCDLLREQYdeeQEAK 1415
Cdd:PRK04863 872 EGLSALNRLLPrlnllADETLADRVEEIREQLDEAEEAKRFVQQhgnalaqlepivsVLQSDPEQFEQLKQDY---QQAQ 948
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1416 ADLQRALSKANA--EVAQWRT--KYEtDAIQRTEELEEAKKKLVTRLQEAEETVETSNAKcssLEKTKHRLqTEIEDLVI 1491
Cdd:PRK04863 949 QTQRDAKQQAFAltEVVQRRAhfSYE-DAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQ---LRQAQAQL-AQYNQVLA 1023
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1492 DLE-RANAAAAVLDKKQRNFDKVLAEWRQKYEEC----QSELETSQKESRGLSTELFKLKNSYEETLDHLEtikRENKNL 1566
Cdd:PRK04863 1024 SLKsSYDAKRQMLQELKQELQDLGVPADSGAEERararRDELHARLSANRSRRNQLEKQLTFCEAEMDNLT---KKLRKL 1100
|
730 740 750
....*....|....*....|....*....|..
gi 2108526737 1567 QEEIADLSDQISQGVKTIHELEKMKKGLDMEK 1598
Cdd:PRK04863 1101 ERDYHEMREQVVNAKAGWCAVLRLVKDNGVER 1132
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1313-1468 |
2.86e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.03 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1313 YEDQMNEAKAKADELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNaLAH 1392
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV-LAP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1393 ALQSSRHDCDLLREQYDEEQEAKADLQRALSKANAEVAQWRTKY----ETDAIQRTEELEEAKKKLVTRLQEAEETVETS 1468
Cdd:pfam00529 135 IGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENqaevRSELSGAQLQIAEAEAELKLAKLDLERTEIRA 214
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1011-1172 |
2.87e-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: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1011 LKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKalleahqqtlddlQAEEDKVnILTKAKAKLEQ 1090
Cdd:pfam13851 31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLE-------------NYEKDKQ-SLKNLKARLKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1091 QVDDLEgSLEQEKK-LRMDLERVRRKLEGDLKLSLESVMD-----------LENDKQQLDEKLKKKDFEMNEMSTRIEDE 1158
Cdd:pfam13851 97 LEKELK-DLKWEHEvLEQRFEKVERERDELYDKFEAAIQDvqqktglknllLEKKLQALGETLEKKEAQLNEVLAAANLD 175
|
170
....*....|....
gi 2108526737 1159 QALVNQLQKKIKEL 1172
Cdd:pfam13851 176 PDALQAVTEKLEDV 189
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
904-1059 |
2.88e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 904 ATTEKELVSLKEELAKLKEALEK-SEVKRKELEERQVSLIQEKNDLslqlqaeqdnladaEDRCDLLIKTKIQLEAKVKE 982
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEKeLRERRNELQKLEKRLLQKEENL--------------DRKLELLEKREEELEKKEKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 983 IMERLEDEEEMSANVLAKKRKLEDE---CAELKKDiDDLEITLAKVEKE-KHATENKVKNlIEEMAaldetilKLTKEKK 1058
Cdd:PRK12704 119 LEQKQQELEKKEEELEELIEEQLQElerISGLTAE-EAKEILLEKVEEEaRHEAAVLIKE-IEEEA-------KEEADKK 189
|
.
gi 2108526737 1059 A 1059
Cdd:PRK12704 190 A 190
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1786-1994 |
3.14e-03 |
|
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: 42.06 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1786 NQKKKLESDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQia 1865
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1866 lkggkkqvlKLEARVKELENELESEQKKSQEY-------QKGVRKYERRIKELSY-------QGEEDKKNLVRLQDLIDK 1931
Cdd:COG4942 98 ---------ELEAQKEELAELLRALYRLGRQPplalllsPEDFLDAVRRLQYLKYlaparreQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2108526737 1932 MQAKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADMAESQANKLRARTRDQGSKLAE 1994
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1637-1984 |
3.18e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1637 LAEKDEEIDSLRRNHQRILESMQatLDAEA-------------KSRNEAVRLRKKMEGDLNEMEvQLSHANRQASESQKF 1703
Cdd:PRK02224 101 LETPEGTIDGARDVREEVTELLR--MDAEAfvncayvrqgevnKLINATPSDRQDMIDDLLQLG-KLEEYRERASDARLG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1704 LRNLQVQIKDIQLELDETIHQNEE--LKEQVAVTERRNNLLAAEVEELRALLEQSDRARKLAEHELLEATERVNLLNSqn 1781
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEkdLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET-- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1782 tglinqkkkLESDLSmlsnEVDDAVQECRNAEEKAKKAITDAAMMAEELKKE-QDTSAHLErmkknmeqtikdlqmrLDE 1860
Cdd:PRK02224 256 ---------LEAEIE----DLRETIAETEREREELAEEVRDLRERLEELEEErDDLLAEAG----------------LDD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1861 AEQIALKggkKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYK 1940
Cdd:PRK02224 307 ADAEAVE---ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRR 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2108526737 1941 RQTEEAEEQANTNLSKYRKLQHELDDAEERADMAESQANKLRAR 1984
Cdd:PRK02224 384 EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1226-1390 |
3.20e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 42.74 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1226 KKREADFLKLRRDLEEAMLhhEATTAALRKKHADsvAELSEQIDSLQRVKQKLEKERSEAKMevddlastveqlskgKAT 1305
Cdd:pfam05911 20 EKAEAEALALKQQLESVTL--QKLTAEERAAHLD--GALKECMQQLRNVKEEQEQKIHDVVL---------------KKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1306 SekmcrlyedQMNEAKAkadELQRQLNETNTQRARAQAESGELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENK 1385
Cdd:pfam05911 81 K---------EWEKIKA---ELEAKLVETEQELLRAAAENDALSRSLQERENLLMKLSEEKSQAEAEIEALKSRLESCEK 148
|
....*
gi 2108526737 1386 AKNAL 1390
Cdd:pfam05911 149 EINSL 153
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1536-1649 |
3.31e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1536 RGLSTE--LFKLKNsyEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELEKmkkgldmEKSEIQAALEEAEGTLE 1613
Cdd:COG2433 374 RGLSIEeaLEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA-------EVEELEAELEEKDERIE 444
|
90 100 110
....*....|....*....|....*....|....*.
gi 2108526737 1614 HEESKSLRIQLELNQiKADVDRKLAEKDEEIDSLRR 1649
Cdd:COG2433 445 RLERELSEARSEERR-EIRKDREISRLDREIERLER 479
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
869-1835 |
3.39e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.73 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 869 REALMIIQWNIRAFNAVKHwpwmklffKIKPLLRSATTEKELVSLKEELAKLKEAL----EKSEVKRKELEErqvslIQE 944
Cdd:TIGR01612 1073 KEILEEAEINITNFNEIKE--------KLKHYNFDDFGKEENIKYADEINKIKDDIknldQKIDHHIKALEE-----IKK 1139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 945 KNDLSLQLQAEQdnLADAEDRCDLLIKTK--IQLEAKVKEIMERLEDEEEMSANVlakkRKLEDECAELKKDIDDLE--- 1019
Cdd:TIGR01612 1140 KSENYIDEIKAQ--INDLEDVADKAISNDdpEEIEKKIENIVTKIDKKKNIYDEI----KKLLNEIAEIEKDKTSLEevk 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1020 ------------ITLAKVEKEKHATENKVKNLIEEMAALDETilkltKEKKALLEAHQQTLDDLQAEEDKVNI------- 1080
Cdd:TIGR01612 1214 ginlsygknlgkLFLEKIDEEKKKSEHMIKAMEAYIEDLDEI-----KEKSPEIENEMGIEMDIKAEMETFNIshdddkd 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1081 -LTKAKAKLEQQVDDLEGSLE--QEKKLRMDLERVRRKLE----------GDLKLSLESVMDLEN-----DKQQLDEKLK 1142
Cdd:TIGR01612 1289 hHIISKKHDENISDIREKSLKiiEDFSEESDINDIKKELQknlldaqkhnSDINLYLNEIANIYNilklnKIKKIIDEVK 1368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1143 KKDFEMNEMSTRIEDEQALVNQLQKKIKE-LQARTEELEEELEAD----RACRAKVEKQRSDVARELEELSERLEEAGGA 1217
Cdd:TIGR01612 1369 EYTKEIEENNKNIKDELDKSEKLIKKIKDdINLEECKSKIESTLDdkdiDECIKKIKELKNHILSEESNIDTYFKNADEN 1448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1218 TS------AQIEMNKKREADFLKLRRD---------LEEAMLHHEA-----TTAALRKKHADSVAELSEQ---------- 1267
Cdd:TIGR01612 1449 NEnvlllfKNIEMADNKSQHILKIKKDnatndhdfnINELKEHIDKskgckDEADKNAKAIEKNKELFEQykkdvtelln 1528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1268 ----------IDSLQRVKQKLEKERSEAKMEVDDLASTVEQlsKGKATSEKMCRLYEDQMNEAKA--------------- 1322
Cdd:TIGR01612 1529 kysalaiknkFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQ--KIKEIKKEKFRIEDDAAKNDKSnkaaidiqlslenfe 1606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1323 ----KADELQRQLNETNTQRARAQAESGELS-----RKLEEREAMVSQLQraknSFSQNVEDLKKQLEEENKAKNALAHA 1393
Cdd:TIGR01612 1607 nkflKISDIKKKINDCLKETESIEKKISSFSidsqdTELKENGDNLNSLQ----EFLESLKDQKKNIEDKKKELDELDSE 1682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1394 LQSSRHDCDllreQYdeeqeakadlqralsKANAEVAQWRTKYETdAIQRTEELEEAKKKLVTRLQEAEETVETSNAKCS 1473
Cdd:TIGR01612 1683 IEKIEIDVD----QH---------------KKNYEIGIIEKIKEI-AIANKEEIESIKELIEPTIENLISSFNTNDLEGI 1742
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1474 SLEKTKHRLQTEIEDLVID-LERANAAAAVLD---KKQRNFDKVLAEWRQKYEECQSELETSQKESRGL----STELFKL 1545
Cdd:TIGR01612 1743 DPNEKLEEYNTEIGDIYEEfIELYNIIAGCLEtvsKEPITYDEIKNTRINAQNEFLKIIEIEKKSKSYLddieAKEFDRI 1822
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1546 KNSYEETLDHL-ETIKRENKNLQEEIADLSDQIsQGVKTIHELEKMKKGLDMEKSEIQAALEEAEGTLEHEESK------ 1618
Cdd:TIGR01612 1823 INHFKKKLDHVnDKFTKEYSKINEGFDDISKSI-ENVKNSTDENLLFDILNKTKDAYAGIIGKKYYSYKDEAEKifinis 1901
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1619 ----SLRIQLE-------LNQIKADVDRKLAEKDEeiDSLR---------RNHQRILESMQATLDAEAKSRNeavrLRKK 1678
Cdd:TIGR01612 1902 klanSINIQIQnnsgidlFDNINIAILSSLDSEKE--DTLKfipspekepEIYTKIRDSYDTLLDIFKKSQD----LHKK 1975
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1679 MEGDLNEM--EVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVTERRNNLLaaEVEELRALLEQS 1756
Cdd:TIGR01612 1976 EQDTLNIIfeNQQLYEKIQASNELKDTLSDLKYKKEKILNDVKLLLHKFDELNKLSCDSQNYDTIL--ELSKQDKIKEKI 2053
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2108526737 1757 DRARKlaEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQD 1835
Cdd:TIGR01612 2054 DNYEK--EKEKFGIDFDVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTEIKIIED 2130
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1236-1577 |
3.69e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.20 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1236 RRDLEEAMLHHEATTAalRKKHADSVAELSEQIDSLQRVKQKLEKERSEAkmeVDDLASTVEQLSKGKATSEKMCRLYED 1315
Cdd:pfam15964 382 KRAQEKEALRKEMKKE--REELGATMLALSQNVAQLEAQVEKVTREKNSL---VSQLEEAQKQLASQEMDVTKVCGEMRY 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1316 QMNEAKAKADELQRQLNETNTQraraqaesgeLSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHALQ 1395
Cdd:pfam15964 457 QLNQTKMKKDEAEKEHREYRTK----------TGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLG 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1396 SSRHDCDLLREQYDEEQEAKADlqraLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEETVETSNAK---- 1471
Cdd:pfam15964 527 ESEHQLHLTRLEKESIQQSFSN----EAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEecct 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1472 -CSSLEKTKHRLQTEIEDLVIDLERANAAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYE 1550
Cdd:pfam15964 603 lAKKLEEITQKSRSEVEQLSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQLDKHCQATAQQLVQLLSKQN 682
|
330 340
....*....|....*....|....*..
gi 2108526737 1551 ETLdhletikRENKNLQEEIADLSDQI 1577
Cdd:pfam15964 683 QLF-------KERQNLTEEVQSLRSQV 702
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1840-1958 |
3.70e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1840 LERMKK-NMEQTIKDLQMRLDEAE------QIALKGGKKQVLKLEARVKELENELESEQKKSQEYQkgvrkyeRRIKELS 1912
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEaersrlQALLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2108526737 1913 YQGEEDKKNLVRLQDLIDKMQAKVKSYKRQTEE-------AEEQANTNLSKYR 1958
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADlgrrlnvALAQRVQELNRYR 196
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
933-1278 |
4.18e-03 |
|
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: 42.12 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 933 ELEERQVSLIQEK-NDLSLQLQAEQDNLADAEDR----------CDLLIKTKIQLEAKVKEIMERLEDEEEMSanvlakK 1001
Cdd:pfam10174 390 DVKERKINVLQKKiENLQEQLRDKDKQLAGLKERvkslqtdssnTDTALTTLEEALSEKERIIERLKEQRERE------D 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1002 RKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALLEAHQQTLDD---LQAEEDKV 1078
Cdd:pfam10174 464 RERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEEcskLENQLKKA 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1079 NILTKAKAKLEQQVDDLEgSLEQEKKLRMDLErvrRKLEGDLKLSLESVMDLENDKQQLDEKL----KKKDFEMNEMSTR 1154
Cdd:pfam10174 544 HNAEEAVRTNPEINDRIR-LLEQEVARYKEES---GKAQAEVERLLGILREVENEKNDKDKKIaeleSLTLRQMKEQNKK 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1155 IEDEQALVNQLQKKIKELqarteELEEELEADRACRAKVEKQRSDVARELEELSERLEEAGGATSAQIEMNKKREADFLK 1234
Cdd:pfam10174 620 VANIKHGQQEMKKKGAQL-----LEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTN 694
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526737 1235 L----RRDLEEAM-LHHEATTAALRKKHAD-SVAELS--------EQIDSLQRVKQKL 1278
Cdd:pfam10174 695 LraerRKQLEEILeMKQEALLAAISEKDANiALLELSsskkkktqEEVMALKREKDRL 752
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1274-1732 |
4.39e-03 |
|
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: 41.87 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1274 VKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLY-------EDQMNEAKAKADELQRQLNETNTQRARAQAESG 1346
Cdd:COG5185 108 KLPNYEWSADILISLLYLYKSEIVALKDELIKVEKLDEIAdieasygEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1347 ELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHALQSsrhdcdllREQYDEEQEAKADLQRALSKAN 1426
Cdd:COG5185 188 LLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKG--------FQDPESELEDLAQTSDKLEKLV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1427 AEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAE----ETVETSNAKCSSLEKTKHRLQTEIEDLVIDLERA-----N 1497
Cdd:COG5185 260 EQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKekiaEYTKSIDIKKATESLEEQLAAAEAEQELEESKREtetgiQ 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1498 AAAAVLDKKQRNFDKVLAEWRQKYEECQSELETSQKESrglstELFKLKNSYEETLDHLETIKRENKNLQEEIADlsdqi 1577
Cdd:COG5185 340 NLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSE-----ELDSFKDTIESTKESLDEIPQNQRGYAQEILA----- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1578 sqgvktihELEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLELNQIKADVDrklAEKDEEIDSLRRNHQRILES 1657
Cdd:COG5185 410 --------TLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREAD---EESQSRLEEAYDEINRSVRS 478
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526737 1658 MQATLDAEAKSRNEAVR-LRKKMEGDLNEMEVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQV 1732
Cdd:COG5185 479 KKEDLNEELTQIESRVStLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQAS 554
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1689-1964 |
4.63e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.75 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1689 QLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKEQVAVT-----ERRNNLLA---------AEVEE-LRALL 1753
Cdd:PRK04778 99 RFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLkdlyrELRKSLLAnrfsfgpalDELEKqLENLE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1754 EQSDRARKLAEH-ELLEATERVNLLNSQNTGLINQKKKLESDLSMLSNEVDDAVQECRNAEEKAKKA---ITDAAMMAE- 1828
Cdd:PRK04778 179 EEFSQFVELTESgDYVEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEgyhLDHLDIEKEi 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1829 -ELKKE-QDTSAHLERMK-KNMEQTIKDLQMRLD------EAEQIA-------LKGGKKQVLKLEARVKELENELESEQK 1892
Cdd:PRK04778 259 qDLKEQiDENLALLEELDlDEAEEKNEEIQERIDqlydilEREVKArkyveknSDTLPDFLEHAKEQNKELKEEIDRVKQ 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1893 K---SQEYQKGVRKYERRIKELSYQGEEDKKNLV-----------RLQDL------IDKMQAKVKSYKRQTEEAEEQANT 1952
Cdd:PRK04778 339 SytlNESELESVRQLEKQLESLEKQYDEITERIAeqeiayselqeELEEIlkqleeIEKEQEKLSEMLQGLRKDELEARE 418
|
330
....*....|..
gi 2108526737 1953 NLSKYRKLQHEL 1964
Cdd:PRK04778 419 KLERYRNKLHEI 430
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
910-1061 |
4.80e-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: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 910 LVSLKEELAKLKeaLEKSEVKRKELEerqvsLIQEKNDLSLQLQAEQDNLADAEdrcdlLIKTKI-QLEAKVKEIMERLE 988
Cdd:pfam10186 21 LYELRVDLARLL--SEKDSLKKKVEE-----ALEGKEEGEQLEDNIGNKKLKLR-----LLKSEVaISNERLNEIKDKLD 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108526737 989 -DEEEMSAnvlaKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALL 1061
Cdd:pfam10186 89 qLRREIAE----KKKKIEKLRSSLKQRRSDLESASYQLEERRASQLAKLQNSIKRIKQKWTALHSKTAESRSFL 158
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1298-1945 |
5.61e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.71 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1298 QLSKGKATSEKMCRLYEDQMneaKAKADELQRQLNETNTQRARAQAESGELSRkLEEREAMVSQLQRAKNSfsqnvedLK 1377
Cdd:PRK10246 199 ELEKLQAQASGVALLTPEQV---QSLTASLQVLTDEEKQLLTAQQQQQQSLNW-LTRLDELQQEASRRQQA-------LQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1378 KQLEEENKAKNALAhALQSSrHDCDLLREQYDEEQEAKADL---QRALSKANA---EVAQWRTKYETDAIQRTEELEEAK 1451
Cdd:PRK10246 268 QALAAEEKAQPQLA-ALSLA-QPARQLRPHWERIQEQSAALahtRQQIEEVNTrlqSTMALRARIRHHAAKQSAELQAQQ 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1452 KKLVTRLQEAEETVETSN------AKCSSLEKTKHRLQTEIEDLVIDLE-RANAAAAVLDKKQRNFDKVLAEW------R 1518
Cdd:PRK10246 346 QSLNTWLAEHDRFRQWNNelagwrAQFSQQTSDREQLRQWQQQLTHAEQkLNALPAITLTLTADEVAAALAQHaeqrplR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1519 QKYEECQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADlsdqisqgVKTIHELEKMKKGLDMEK 1598
Cdd:PRK10246 426 QRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLAD--------VKTICEQEARIKDLEAQR 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1599 SEIQAALE------------EAEGTLEHEESKSLRIQLE-------------LNQIKAdVDRKLAEKDEEIDSLRRNHQR 1653
Cdd:PRK10246 498 AQLQAGQPcplcgstshpavEAYQALEPGVNQSRLDALEkevkklgeegaalRGQLDA-LTKQLQRDESEAQSLRQEEQA 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1654 ILESMQATLDAEAKSRNEAVRLRKKMEGDlNEMEVQLSHANR------QASESQKFLRNLQVQIKDIQLELDE-----TI 1722
Cdd:PRK10246 577 LTQQWQAVCASLNITLQPQDDIQPWLDAQ-EEHERQLRLLSQrhelqgQIAAHNQQIIQYQQQIEQRQQQLLTalagyAL 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1723 HQNEELKEQVAVTERRN--NLLAAEVEELRALLEQSDRARKL-----AEHELLEATERVNLLNSQNtgLINQKKKLESDL 1795
Cdd:PRK10246 656 TLPQEDEEASWLATRQQeaQSWQQRQNELTALQNRIQQLTPLletlpQSDDLPHSEETVALDNWRQ--VHEQCLSLHSQL 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1796 SMLSNEVDDAVQECRNAEEKAKKAITD------AAMMAEELKKEqdTSAHLERMKKNMEQTIKDLQMRLDEAEQialkgg 1869
Cdd:PRK10246 734 QTLQQQDVLEAQRLQKAQAQFDTALQAsvfddqQAFLAALLDEE--TLTQLEQLKQNLENQRQQAQTLVTQTAQ------ 805
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108526737 1870 kKQVLKLEARVKELENELESEQKKSQEYQ--KGVRKYERRIKELSYQGEEDKKNLVRLQDLIdkmqAKVKSYKRQTEE 1945
Cdd:PRK10246 806 -ALAQHQQHRPDGLDLTVTVEQIQQELAQlaQQLRENTTRQGEIRQQLKQDADNRQQQQALM----QQIAQATQQVED 878
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1623-1992 |
5.75e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1623 QLELNQIKADVDRKLAEKDEEIDSLRRNHQRILESMQATLDAEAKSR-----NEAVRLRKKMEGDLNEmEVQLSHANRQA 1697
Cdd:NF041483 82 QIQADQLRADAERELRDARAQTQRILQEHAEHQARLQAELHTEAVQRrqqldQELAERRQTVESHVNE-NVAWAEQLRAR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1698 SESQKflRNLqvqIKDIQLELDETIHQNEELKEQVAVTERRNnlLAAEVEELRALLEQS-DRARKLAEHEL-------LE 1769
Cdd:NF041483 161 TESQA--RRL---LDESRAEAEQALAAARAEAERLAEEARQR--LGSEAESARAEAEAIlRRARKDAERLLnaastqaQE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1770 ATERVNLLNSQNTGLINQKKKLESDLSMLS----NEVDDAVQECRNAEEKAKKAITDAA---MMAEELKKEQDTSAHLER 1842
Cdd:NF041483 234 ATDHAEQLRSSTAAESDQARRQAAELSRAAeqrmQEAEEALREARAEAEKVVAEAKEAAakqLASAESANEQRTRTAKEE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1843 MKKNMEQTIKDLQMRLDEAEQiALKGGKKQVLKLEARVKELENELESEQKKSQeyqkgVRKYERRIKELSYQGEEDKKNL 1922
Cdd:NF041483 314 IARLVGEATKEAEALKAEAEQ-ALADARAEAEKLVAEAAEKARTVAAEDTAAQ-----LAKAARTAEEVLTKASEDAKAT 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1923 VRlqdlidkmqAKVKSYKRQTEEAEEQANTNLSKYRKLQHEL-----DDAEE-RADMAESQ---------ANKLRARTRD 1987
Cdd:NF041483 388 TR---------AAAEEAERIRREAEAEADRLRGEAADQAEQLkgaakDDTKEyRAKTVELQeearrlrgeAEQLRAEAVA 458
|
....*
gi 2108526737 1988 QGSKL 1992
Cdd:NF041483 459 EGERI 463
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1220-1896 |
5.75e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1220 AQIEMNKKREADFLKLRRDLEEAM----LHHEATTAALRKKHA--DSVAELSEQ-------IDSLQR-------VKQKLE 1279
Cdd:PRK04863 345 RQQEKIERYQADLEELEERLEEQNevveEADEQQEENEARAEAaeEEVDELKSQladyqqaLDVQQTraiqyqqAVQALE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1280 KERS---EAKMEVDDLASTVEQL-SKGKATSEKMCRLyEDQMNEAKA------KADELQRQLNEtNTQRARAQAESGELS 1349
Cdd:PRK04863 425 RAKQlcgLPDLTADNAEDWLEEFqAKEQEATEELLSL-EQKLSVAQAahsqfeQAYQLVRKIAG-EVSRSEAWDVARELL 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1350 RKLEEREAMVSQLQRAKNSFSqnveDLKKQLEEENKAKNALAHALQSSRHDCDL--LREQYDEEQEAkadlqrALSKANA 1427
Cdd:PRK04863 503 RRLREQRHLAEQLQQLRMRLS----ELEQRLRQQQRAERLLAEFCKRLGKNLDDedELEQLQEELEA------RLESLSE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1428 EVAQwrtkyetdAIQRTEELEEAKKKLVTRLQEAEETVETSNAKCSSLEktkhRLQTEIEDLVIDLERANAAAAVLDKKQ 1507
Cdd:PRK04863 573 SVSE--------ARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALA----RLREQSGEEFEDSQDVTEYMQQLLERE 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1508 RNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNS---------YEE-TLDH-------------------LET 1558
Cdd:PRK04863 641 RELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERfggvllseiYDDvSLEDapyfsalygparhaivvpdLSD 720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1559 IKRENKNLQEEIADL------SDQISQGVktiHELEKMKKGLDMEKSEIQ--------------AALEEaegTLEheesk 1618
Cdd:PRK04863 721 AAEQLAGLEDCPEDLyliegdPDSFDDSV---FSVEELEKAVVVKIADRQwrysrfpevplfgrAAREK---RIE----- 789
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1619 SLRIQLELnqikadVDRKLAEKDEEIDSLRRNHQR----ILESMQATLDAE-----AKSRNEAVRLRKKMEgDLNEMEVQ 1689
Cdd:PRK04863 790 QLRAEREE------LAERYATLSFDVQKLQRLHQAfsrfIGSHLAVAFEADpeaelRQLNRRRVELERALA-DHESQEQQ 862
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1690 LSHANRQASESQKFLRNLQVQIKdiqLELDETIHQN-EELKEQVAVTE------RRNNLLAAEVEELRALL--EQSDRAR 1760
Cdd:PRK04863 863 QRSQLEQAKEGLSALNRLLPRLN---LLADETLADRvEEIREQLDEAEeakrfvQQHGNALAQLEPIVSVLqsDPEQFEQ 939
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1761 KLAEHELLEAT---------------ERVNLLNSQNT-GLINQkkklESDLS-MLSNEVDDAVQECRNAEEKAKKA---I 1820
Cdd:PRK04863 940 LKQDYQQAQQTqrdakqqafaltevvQRRAHFSYEDAaEMLAK----NSDLNeKLRQRLEQAEQERTRAREQLRQAqaqL 1015
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1821 TDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQMRLDEAEQIALKGGK------------------KQVLKLEARVKE 1882
Cdd:PRK04863 1016 AQYNQVLASLKSSYDA---KRQMLQELKQELQDLGVPADSGAEERARARRdelharlsanrsrrnqleKQLTFCEAEMDN 1092
|
810
....*....|....
gi 2108526737 1883 LENELESEQKKSQE 1896
Cdd:PRK04863 1093 LTKKLRKLERDYHE 1106
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1398-1702 |
5.78e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 41.63 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1398 RHDCDLlREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAIQRTEEL-------EEAKKKLV---TRLQEAEETVET 1467
Cdd:pfam03528 1 QPDEDL-QQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLkrqnavlQEAQVELDalqNQLALARAEMEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1468 SNAKCSSLEKTKHRLQTEIEDLVidLERANAAAAVLDKKQRNF--------DKVLAEWRQKYEECQSEL-ETSQKESRGL 1538
Cdd:pfam03528 80 IKAVATVSENTKQEAIDEVKSQW--QEEVASLQAIMKETVREYevqfhrrlEQERAQWNQYRESAEREIaDLRRRLSEGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1539 STElfKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGVKTIHELE--KMKK---GLDMEKS-----EIQAALEEA 1608
Cdd:pfam03528 158 EEE--NLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEasKMKElnhYLEAEKScrtdlEMYVAVLNT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1609 EGTLEHEESKSLRIQLElnqikaDVDRKLAEKdeeidslRRNHQRILESMQATLDAEAKSRNEAVRLRKKMEGDLNEMEV 1688
Cdd:pfam03528 236 QKSVLQEDAEKLRKELH------EVCHLLEQE-------RQQHNQLKHTWQKANDQFLESQRLLMRDMQRMESVLTSEQL 302
|
330
....*....|....
gi 2108526737 1689 qlshanRQASESQK 1702
Cdd:pfam03528 303 ------RQVEEIKK 310
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
896-1028 |
5.87e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 40.84 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 896 KIKPLLRSATTE---KELVSLKEELAKLKEaleksevKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKT 972
Cdd:pfam15294 118 KLEPLNEGGGSAllhMEIERLKEENEKLKE-------RLKTLESQATQALDEKSKLEKALKDLQKEQGAKKDVKSNLKEI 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2108526737 973 KiQLEAKVKEIMERLEDEEEMSANVLAkkrKLEDECAELKKDIDDLEITLAKVEKE 1028
Cdd:pfam15294 191 S-DLEEKMAALKSDLEKTLNASTALQK---SLEEDLASTKHELLKVQEQLEMAEKE 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1770-1994 |
5.92e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1770 ATERVNLLNSQNTGLINQKKKLESDLSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNMEQ 1849
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1850 TIKDLQMRLDEAEQIALKGGKKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELsyqgeedKKNLVRLQDLI 1929
Cdd:COG3883 91 RARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAEL-------EAKLAELEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526737 1930 DKMQAKVKSYKRQTEEAEEQANTNLSKYRKLQHELDDAEERADMAESQANKLRARTRDQGSKLAE 1994
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
894-1175 |
6.46e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 894 FFKIKPLLRSA-----TTEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEkndlslqLQAEQDNLADAEDrcdl 968
Cdd:PRK04778 100 FRKAKHEINEIeslldLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKS-------LLANRFSFGPALD---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 969 liktkiQLEAKVKEIMERLE--DEEEMSANVLAKKR---KLEDECAELKKDIDDLEITLAKVEKEKHATENKVKN----L 1039
Cdd:PRK04778 169 ------ELEKQLENLEEEFSqfVELTESGDYVEAREildQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1040 IEEMAALDEtiLKLTKEKKALLEAHQQTLDDLQAEEdkvniLTKAKAKLEQ---QVDDLEGSLEQEKKLRMDLERVRRKL 1116
Cdd:PRK04778 243 VEEGYHLDH--LDIEKEIQDLKEQIDENLALLEELD-----LDEAEEKNEEiqeRIDQLYDILEREVKARKYVEKNSDTL 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2108526737 1117 EGDLKLSLESVMDLENDKQQLDEKlkkkdFEMNEmstrieDEQALVNQLQKKIKELQAR 1175
Cdd:PRK04778 316 PDFLEHAKEQNKELKEEIDRVKQS-----YTLNE------SELESVRQLEKQLESLEKQ 363
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1261-1398 |
6.49e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1261 VAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKADELQRQLNETNTQR-- 1338
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKey 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108526737 1339 ------------ARAQAES--GELSRKLEEREAMVSQLQRAKNSFSQNVEDLKKQLEEENKAKNALAHALQSSR 1398
Cdd:COG1579 92 ealqkeieslkrRISDLEDeiLELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1747-1967 |
6.63e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.40 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1747 EELRALLEQSDRAR---KLAEHELLEATERVNLLNSQNTGLINQKKKLESDLSMLSNEVDDAVQECRNAEEKAKKAITDA 1823
Cdd:pfam00261 1 KKMQQIKEELDEAEerlKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1824 AMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAE------QIALKGGKKQVLKLEARVKELENELE--------- 1888
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVArklvvvEGDLERAEERAELAESKIVELEEELKvvgnnlksl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1889 --SEQKKSQ---EYQKGVRKYERRIKELSYQGEEDKKNLVRLQDLIDKMQAKVKSYKrqteeaeeqantnlSKYRKLQHE 1963
Cdd:pfam00261 161 eaSEEKASEredKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEK--------------EKYKAISEE 226
|
....
gi 2108526737 1964 LDDA 1967
Cdd:pfam00261 227 LDQT 230
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1575-1801 |
6.87e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.58 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1575 DQISQgvktihELEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQL------ELNQIKADVDRKLAEKDEEIDSLR 1648
Cdd:PRK10929 26 KQITQ------ELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQyqqvidNFPKLSAELRQQLNNERDEPRSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1649 RN------HQRILESMQATLDAEAKSRNEAVRLRkKMEGDLNEMEVQLSHANRQASESQKFLRNL--------QVQIKDI 1714
Cdd:PRK10929 100 PNmstdalEQEILQVSSQLLEKSRQAQQEQDRAR-EISDSLSQLPQQQTEARRQLNEIERRLQTLgtpntplaQAQLTAL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1715 Q------------LELDETIHQN-EEL-KEQVAVTERRNNLLAAEVEELRALLeQSDRARKlAEhellEATERVNLLNSQ 1780
Cdd:PRK10929 179 QaesaalkalvdeLELAQLSANNrQELaRLRSELAKKRSQQLDAYLQALRNQL-NSQRQRE-AE----RALESTELLAEQ 252
|
250 260
....*....|....*....|....
gi 2108526737 1781 NTGL---INQKKKLESDLSMLSNE 1801
Cdd:PRK10929 253 SGDLpksIVAQFKINRELSQALNQ 276
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1221-1992 |
7.04e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1221 QIEMNKKREADFL-KLRRDLEEAMLHHEATTAALRKKHADSVAELSEQID-SLQRVKQKLEKERSEAKMEVDDLASTVEQ 1298
Cdd:NF041483 474 QIEEAARTAEELLtKAKADADELRSTATAESERVRTEAIERATTLRRQAEeTLERTRAEAERLRAEAEEQAEEVRAAAER 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1299 lsKGKATSEKMCRLYEDQMNEAkakADELQRQLNETNTQRARAQAESGELSRKLE--EREAmVSQLQRAKNSFSQNVEDL 1376
Cdd:NF041483 554 --AARELREETERAIAARQAEA---AEELTRLHTEAEERLTAAEEALADARAEAEriRREA-AEETERLRTEAAERIRTL 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1377 KKQLEEENKAKNALAHALQS-SRHDCD-----LLREQYDEEQEAKADLQRALSKANAEVAQWRTKYETDAiqrTEELEEA 1450
Cdd:NF041483 628 QAQAEQEAERLRTEAAADASaARAEGEnvavrLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEA---AEALAAA 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1451 KKKLVTRLQEAEETVETSNAKCSSlEKTKHRLQTEiedlvidleranaaaavldkkqrnfdKVLAEWRQKYEECQSELET 1530
Cdd:NF041483 705 QEEAARRRREAEETLGSARAEADQ-ERERAREQSE--------------------------ELLASARKRVEEAQAEAQR 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1531 SQKESRGLSTELFklkNSYEETLDHL-ETIKRENKNLQEEIADLSDQISqgvktiHELEKMKKGLDMEKSEIQA-ALEEA 1608
Cdd:NF041483 758 LVEEADRRATELV---SAAEQTAQQVrDSVAGLQEQAEEEIAGLRSAAE------HAAERTRTEAQEEADRVRSdAYAER 828
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1609 EGTLEHEESKSLRIQLELNQIKADVDRKLAEKDEEIDSLRRNHQRILESMQATL-DAEAKSRNEAVRLRKKMEGDLNEME 1687
Cdd:NF041483 829 ERASEDANRLRREAQEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEAsDTLASAEQDAARTRADAREDANRIR 908
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1688 VQL-SHANRQASESQKFLRNLQVQIK-DIQLELDETIHQNEELK-EQVAVTERRNNLLAAEVEELRA-LLEQSDRARKLA 1763
Cdd:NF041483 909 SDAaAQADRLIGEATSEAERLTAEARaEAERLRDEARAEAERVRaDAAAQAEQLIAEATGEAERLRAeAAETVGSAQQHA 988
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1764 EHELLEAtERVNLLNSQNTGLINQKKKLESDlSMLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAhLERM 1843
Cdd:NF041483 989 ERIRTEA-ERVKAEAAAEAERLRTEAREEAD-RTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEA-LRTT 1065
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1844 KKNMEQTIKDLQMRLDEAEQIALkggkkqvlklEARVkELENELESEQKKSQEYQKGVRKYERRIKElsyqgeedkknlv 1923
Cdd:NF041483 1066 TEAEAQADTMVGAARKEAERIVA----------EATV-EGNSLVEKARTDADELLVGARRDATAIRE------------- 1121
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1924 RLQDLIDKMQAKVKS-YKRQTEEAEEQANTNLSKYRKLqheLDDAEERADMAESQANKLRARTRDQGSKL 1992
Cdd:NF041483 1122 RAEELRDRITGEIEElHERARRESAEQMKSAGERCDAL---VKAAEEQLAEAEAKAKELVSDANSEASKV 1188
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1419-1970 |
7.20e-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: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1419 QRALSKANAEVAQWRtkyetdaiQRTEELEEAKkklvtrLQEAEEtvetsnakcssLEKTKHrlqtEIEDLVIDLERANA 1498
Cdd:pfam05701 41 ELELEKVQEEIPEYK--------KQSEAAEAAK------AQVLEE-----------LESTKR----LIEELKLNLERAQT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1499 AAAvldkkQRNFDKVLAEWRQKyeecQSELETSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQIS 1578
Cdd:pfam05701 92 EEA-----QAKQDSELAKLRVE----EMEQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1579 QGVKTIH-------ELEKMKKGLDMEKSEIQAALEEAEGTLEHEESKSLRIQLELNQIKADVDRKLAEKDEEIdslrrnh 1651
Cdd:pfam05701 163 IAIKRAEeavsaskEIEKTVEELTIELIATKESLESAHAAHLEAEEHRIGAALAREQDKLNWEKELKQAEEEL------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1652 QRILESMQATLDAEAKSrNEAVRLRKKMEGDLNE-MEVQLSHANRQASESQKFLRNLQVQIKDIQLELDETIHQNEELKE 1730
Cdd:pfam05701 236 QRLNQQLLSAKDLKSKL-ETASALLLDLKAELAAyMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1731 QVavterrnNLLAAEVEELRALLEQsdrarklaEHELLEATERVNLLNSqntglinqkkkleSDLSMLSNEVDDAVQECR 1810
Cdd:pfam05701 315 EV-------NCLRVAAASLRSELEK--------EKAELASLRQREGMAS-------------IAVSSLEAELNRTKSEIA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1811 NAEEKAKKAitdAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQiALKGGKKQVLKLEARVKELENELESE 1890
Cdd:pfam05701 367 LVQAKEKEA---REKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQ-AKAAASTVESRLEAVLKEIEAAKASE 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1891 Q------KKSQEYQKGVRKyerrikelsyQGEEDKKNLVRLqdlidkmqaKVKSY---KRQTEEAEEQANTNLSKYRKLQ 1961
Cdd:pfam05701 443 KlalaaiKALQESESSAES----------TNQEDSPRGVTL---------SLEEYyelSKRAHEAEELANKRVAEAVSQI 503
|
....*....
gi 2108526737 1962 HELDDAEER 1970
Cdd:pfam05701 504 EEAKESELR 512
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
977-1104 |
7.43e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 977 EAKvKEIMERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEmaaLDETILKLTKE 1056
Cdd:PRK00409 506 EAK-KLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE---AEKEAQQAIKE 581
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2108526737 1057 KKALLEAHQQTLDDLQAEED---KVNILTKAKAKLEQQVDDLEGSLEQEKK 1104
Cdd:PRK00409 582 AKKEADEIIKELRQLQKGGYasvKAHELIEARKRLNKANEKKEKKKKKQKE 632
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1442-1625 |
7.60e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.51 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1442 QRTEELEEAKKKLVTRLQEA--EETVETSNAKCSSLEKTKHR----------LQTEIEDLVIDL----ERANAAAAVLDK 1505
Cdd:pfam09787 14 QKAARILQSKEKLIASLKEGsgVEGLDSSTALTLELEELRQErdllreeiqkLRGQIQQLRTELqeleAQQQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1506 KQRNFDKVLAEWRQKYEECQSELETSQKESRGLSTELFKLKNSYEETLdhletikrenKNLQEEIADLSDQI---SQGVK 1582
Cdd:pfam09787 94 QLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRI----------KDREAEIEKLRNQLtskSQSSS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2108526737 1583 TIHELEKMKKGLDMEKSEIQAALEEaegtLEHEESkSLRIQLE 1625
Cdd:pfam09787 164 SQSELENRLHQLTETLIQKQTMLEA----LSTEKN-SLVLQLE 201
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1840-1994 |
7.68e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1840 LERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVLKLEARVKELENELESEQKKSQEYQKGVRKYERRIKELSYQGEEDk 1919
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERRE- 460
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108526737 1920 knlVRLQDLIDKMQAKVKSYKRQTEEAEEQANTNLSKYRKLQhELDDAEERADMAesQANKLRARTRDQGSKLAE 1994
Cdd:COG2433 461 ---IRKDREISRLDREIERLERELEEERERIEELKRKLERLK-ELWKLEHSGELV--PVKVVEKFTKEAIRRLEE 529
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
941-1101 |
7.80e-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: 40.43 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 941 LIQEKNDLSLQLQAEQdNLADAEDRCDLLIKTKIQLEAKVKEIMERLedeeemsanvlakkRKLEDECAELKKDIDDLEI 1020
Cdd:cd22656 99 LIDDLADATDDEELEE-AKKTIKALLDDLLKEAKKYQDKAAKVVDKL--------------TDFENQTEKDQTALETLEK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1021 TL-AKVEKEKHATENK-VKNLIEEMAALDETILKLTKEKkalLEAHQQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEGS 1098
Cdd:cd22656 164 ALkDLLTDEGGAIARKeIKDLQKELEKLNEEYAAKLKAK---IDELKALIADDEAKLAAALRLIADLTAADTDLDNLLAL 240
|
...
gi 2108526737 1099 LEQ 1101
Cdd:cd22656 241 IGP 243
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1044-1174 |
7.81e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1044 AALDETILKLTKEKKALLEAHQQTLD-DLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERvrrklegdlkl 1122
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHEErELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLER----------- 448
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2108526737 1123 SLESVMDLENDKQQLDEKLKKKDFEMNEMSTRIEDEQALVNQLQKKIKELQA 1174
Cdd:COG2433 449 ELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
904-1253 |
9.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 904 ATTEKELVSLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEI 983
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 984 MERLEDEEEMSANVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKallea 1063
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA----- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1064 hQQTLDDLQAEEDKVNILTKAKAKLEQQVDDLEGSLEQEKKLRMDLERVRRKLEGDLKLSLESVMDLENDKQQLDEKLKK 1143
Cdd:COG4372 182 -EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108526737 1144 KDFEMNEMSTRIEDEQALVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRSDVARELEELSERLEEAGGATSAQIE 1223
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
330 340 350
....*....|....*....|....*....|
gi 2108526737 1224 MNKKREADFLKLRRDLEEAMLHHEATTAAL 1253
Cdd:COG4372 341 DLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| |
