|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 1480.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVAALGDTPAKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDR 338
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 419 QNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 499 ILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFLKPRPDKKRKY 578
Cdd:cd14927 401 ILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 579 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDSASDPKAGGKEKRKKAASFQTVSQL 658
Cdd:cd14927 481 EAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEDPKSGVKEKRKKAASFQTVSQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 659 HKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPSAI 738
Cdd:cd14927 561 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAI 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 2045330442 739 PDDKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14927 641 PDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-774 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1346.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVAALGdtpakKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASS-----KKKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDR 338
Cdd:cd01377 156 TGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd01377 236 AFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 419 QNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd01377 316 QNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 499 ILEQEEYKREGIEWTFIDFGLDLQACIDLIEKP-LGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFLKPrpdKKRK 577
Cdd:cd01377 396 VLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKP---KPKK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 578 YEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDSasdpkaGGKEKRKKAASFQTVSQ 657
Cdd:cd01377 473 SEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGG------GGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 658 LHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPSA 737
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*..
gi 2045330442 738 IPDDkFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd01377 627 IPKG-FDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 1170.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVAALGDTPAKKGqgpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLG---------ALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKpELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDR 338
Cdd:cd14929 152 RGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd14929 231 AMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 419 QNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14929 311 QNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 499 ILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFLKPRPDKKrKY 578
Cdd:cd14929 391 VLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKK-KF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 579 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDSASDpkaGGKEKRKKAASFQTVSQL 658
Cdd:cd14929 470 EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQ---FGEKKRKKGASFQTVASL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 659 HKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPSAI 738
Cdd:cd14929 547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTF 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 2045330442 739 PDDKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14929 627 PKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-774 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 1147.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 180 SGAGKTVNTKRVIQYFAIVAALGDtPAKKGQgpaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGD-LAKKKD---SKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDRA 339
Cdd:cd14913 158 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 420 NVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14913 318 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 500 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFLKPRPDKKRKyE 579
Cdd:cd14913 398 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRA-E 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDSASDPKAGGKekrKKAASFQTVSQLH 659
Cdd:cd14913 477 AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAK---KKGSSFQTVSALF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 660 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPSAIP 739
Cdd:cd14913 554 RENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIP 633
|
650 660 670
....*....|....*....|....*....|....*
gi 2045330442 740 DDKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14913 634 EGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-774 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 1105.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 180 SGAGKTVNTKRVIQYFAIVAALGDTpAKKGQGPATktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDR-SKKDQTPGK---GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDRA 339
Cdd:cd14917 158 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14917 238 FDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 420 NVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14917 318 NVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 500 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFLKPRpDKKRKYE 579
Cdd:cd14917 398 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPR-NIKGKPE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDSasdPKAGGKEKRKKAASFQTVSQLH 659
Cdd:cd14917 477 AHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADA---PIEKGKGKAKKGSSFQTVSALH 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 660 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPSAIP 739
Cdd:cd14917 554 RENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 633
|
650 660 670
....*....|....*....|....*....|....*
gi 2045330442 740 DDKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14917 634 EGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-774 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 1072.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 180 SGAGKTVNTKRVIQYFAIVAALGDTPAKKGqgpATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKKEN---PNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDRA 339
Cdd:cd14916 159 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 420 NVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 500 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFLKPRpDKKRKYE 579
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPR-NVKGKQE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDSASDPKagGKEKRKKAASFQTVSQLH 659
Cdd:cd14916 478 AHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGK--GKGGKKKGSSFQTVSALH 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 660 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPSAIP 739
Cdd:cd14916 556 RENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 635
|
650 660 670
....*....|....*....|....*....|....*
gi 2045330442 740 DDKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14916 636 EGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-774 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 1046.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 180 SGAGKTVNTKRVIQYFAIVAALGDtpaKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGD---KKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDRA 339
Cdd:cd14923 159 GKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14923 239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 420 NVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 500 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFLKPRPdKKRKYE 579
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKP-AKGKAE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDsASDPKAGGKEKRKKAASFQTVSQLH 659
Cdd:cd14923 478 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAE-AGDSGGSKKGGKKKGSSFQTVSAVF 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 660 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPSAIP 739
Cdd:cd14923 557 RENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIP 636
|
650 660 670
....*....|....*....|....*....|....*
gi 2045330442 740 DDKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14923 637 EGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-774 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1039.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 87 IEDMAMLTHLNEASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 167 RNRENQSMLITGESGAGKTVNTKRVIQYFAIVAalgdtpakkGQGPATKtGGTLEDQIIEANPAMEAFGNAKTLRNDNSS 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVS---------GSGSAGN-VGRLEEQILQSNPILEAFGNAKTVRNNNSS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 247 RFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVsSNPYDYHFCSQ-GVTTVE 325
Cdd:pfam00063 151 RFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TNPKDYHYLSQsGCYTID 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 326 NLDDGQELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLH 405
Cdd:pfam00063 230 GIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 406 PRVKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINF 484
Cdd:pfam00063 310 RRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLdVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 485 TNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNHiGK 563
Cdd:pfam00063 390 VNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 564 SPNFLKPRPdkkrKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENY-VISDSASDPKAGG 642
Cdd:pfam00063 468 HPHFQKPRL----QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYeTAESAAANESGKS 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 643 KEKRKKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRIL 722
Cdd:pfam00063 544 TPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRIT 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2045330442 723 YAEFKQRYRILNPSAIPDDkFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:pfam00063 624 FQEFVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-774 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 1031.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 101 VLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 181 GAGKTVNTKRVIQYFAIVAALGDtpakKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTG 260
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGE----KKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 261 KLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDRAM 340
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 341 DILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQN 420
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 421 VEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMFIL 500
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 501 EQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFLKPRPdKKRKYEA 580
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKV-VKGKAEA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 581 HFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDSASDPKAGGKekrKKAASFQTVSQLHK 660
Cdd:cd14918 478 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAK---KKGSSFQTVSALFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 661 ENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPSAIPD 740
Cdd:cd14918 555 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE 634
|
650 660 670
....*....|....*....|....*....|....
gi 2045330442 741 DKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14918 635 GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-774 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 1029.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 180 SGAGKTVNTKRVIQYFAIVAALGDTpaKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDRA 339
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14910 240 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 420 NVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14910 320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 500 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFLKPRPdKKRKYE 579
Cdd:cd14910 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKVE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYEnyviSDSASDPKAGGKEK--RKKAASFQTVSQ 657
Cdd:cd14910 479 AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFS----GAAAAEAEEGGGKKggKKKGSSFQTVSA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 658 LHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPSA 737
Cdd:cd14910 555 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 634
|
650 660 670
....*....|....*....|....*....|....*..
gi 2045330442 738 IPDDKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14910 635 IPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-774 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 1025.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 180 SGAGKTVNTKRVIQYFAIVAALGDTpaKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDRA 339
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14915 240 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 420 NVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 500 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFLKPRPdKKRKYE 579
Cdd:cd14915 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYEnyviSDSASDPKAGGKEK--RKKAASFQTVSQ 657
Cdd:cd14915 479 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFS----GGQTAEAEGGGGKKggKKKGSSFQTVSA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 658 LHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPSA 737
Cdd:cd14915 555 LFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 634
|
650 660 670
....*....|....*....|....*....|....*..
gi 2045330442 738 IPDDKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14915 635 IPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-774 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 1021.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 180 SGAGKTVNTKRVIQYFAIVAALGDTpaKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDRA 339
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14912 240 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 420 NVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 500 LEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFLKPRPdKKRKYE 579
Cdd:cd14912 400 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKV-VKGKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENyviSDSASDPKAGGKEK---RKKAASFQTVS 656
Cdd:cd14912 479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSG---AQTAEGASAGGGAKkggKKKGSSFQTVS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 657 QLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPS 736
Cdd:cd14912 556 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 635
|
650 660 670
....*....|....*....|....*....|....*...
gi 2045330442 737 AIPDDKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14912 636 AIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 1021.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVAALGDTpAKKGQGpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQ-SSDGKG-------SLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDR 338
Cdd:cd14934 153 TGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd14934 233 AFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 419 QNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14934 313 QNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 499 ILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFLKPRPDKKRKY 578
Cdd:cd14934 393 VLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKGP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 579 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYEnyvisdsaSDPKAGGKEKRKKAASFQTVSQL 658
Cdd:cd14934 473 EAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFK--------EEEAPAGSKKQKRGSSFMTVSNF 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 659 HKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPSAI 738
Cdd:cd14934 545 YREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVI 624
|
650 660 670
....*....|....*....|....*....|....*.
gi 2045330442 739 PDDkFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14934 625 PQG-FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 1008.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVAALGDTPakkgqgPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTD------EAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDR 338
Cdd:cd14909 155 TGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd14909 235 AFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 419 QNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14909 315 RNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 499 ILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFLKPRPDKKRKY 578
Cdd:cd14909 395 VLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 579 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYviSDSASDPKAGGKEKRKKAASFQTVSQL 658
Cdd:cd14909 475 AAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADH--AGQSGGGEQAKGGRGKKGGGFATVSSA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 659 HKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPSAI 738
Cdd:cd14909 553 YKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGI 632
|
650 660 670
....*....|....*....|....*....|....*.
gi 2045330442 739 PDDKfvDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14909 633 QGEE--DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-786 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 1000.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 80 NPPKFDMIEDMAMLTHLNEASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIAD 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 160 NAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAIVAAlgdtpakkgqgpATKTGGTLEDQIIEANPAMEAFGNAKT 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG------------SNTEVGSVEDQILESNPILEAFGNAKT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 240 LRNDNSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQ 319
Cdd:smart00242 149 LRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 320 GVT-TVENLDDGQELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEA-DGTESADKASYLMGVSSA 397
Cdd:smart00242 228 GGClTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTvKDKEELSNAAELLGVDPE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 398 DLIKGLLHPRVKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSF 477
Cdd:smart00242 308 ELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 478 EQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKM 556
Cdd:smart00242 388 EQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 557 YDNHiGKSPNFLKPRpdkkRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYvisdsas 636
Cdd:smart00242 467 NQHH-KKHPHFSKPK----KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 637 dpkAGGKEKRKKaasFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKG 716
Cdd:smart00242 535 ---VSNAGSKKR---FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAG 608
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 717 FPNRILYAEFKQRYRILNPSAIPDDKFvDSRKAAEKLLSSLDIDHNQYRFGHTKVFFKAGLLGHLEEMRD 786
Cdd:smart00242 609 FPYRLPFDEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1123 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 874.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 36 RAWIPDEKEAYIEIEIKELSGDKVIV----ETKDGRSLTVKEGDIQQ--MNPPKFDMIEDMAMLTHLNEASVLYNLRRRY 109
Cdd:COG5022 11 GCWIPDEEKGWIWAEIIKEAFNKGKVteegKKEDGESVSVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPAVLHNLEKRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 110 SAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGESGAGKTVNTK 189
Cdd:COG5022 91 NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 190 RVIQYFAIVaalgdtpakkgQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDI 269
Cdd:COG5022 171 RIMQYLASV-----------TSSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 270 YLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQG-VTTVENLDDGQELMATDRAMDILGFLPD 348
Cdd:COG5022 240 YLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQ-NPKDYIYLSQGgCDKIDGIDDAKEFKITLDALKTIGIDEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 349 EKYGCYKIVGAIMHFGNMKFKqKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVNYAV 428
Cdd:COG5022 319 EQDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 429 GALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKRE 508
Cdd:COG5022 398 DSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 509 GIEWTFIDFgLDLQACIDLIEK--PLGIMSILEEECMFPKATDNSFKAKMYDN-HIGKSPNFlkprpDKKRKYEAHFELV 585
Cdd:COG5022 478 GIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKF-----KKSRFRDNKFVVK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 586 HYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYvisdsasdpkaggkEKRKKAASFQTVSQLHKENLNK 665
Cdd:COG5022 552 HYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE--------------ENIESKGRFPTLGSRFKESLNS 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 666 LMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPSAIPDDKFV- 744
Cdd:COG5022 618 LMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTw 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 745 --DSRKAAEKLLSSLDIDHNQYRFGHTKVFFKAGLLGHLEEMRDERLAKVLTLLQAAARGKIMRTELMKMNERREALMII 822
Cdd:COG5022 698 keDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVI 777
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 823 QWNIRAFNTVKHWPWMKLFFKIKPLLRSAATEKELAALKEELAKLKEALEKsEVKRKELEEKQVSLIQEKNDLALQLQAE 902
Cdd:COG5022 778 QHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKR-EKKLRETEEVEFSLKAEVLIQKFGRSLK 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 903 QDNLADAEDRCDLLIKTKIQLEAKVKELMErLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHAtenK 982
Cdd:COG5022 857 AKKRFSLLKKETIYLQSAQRVELAERQLQE-LKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIA---R 932
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 983 VKNLIEEMAALDETILKLTKEKKalteahqqtLDDLQAEEDKVNTLTKakaKLEQQVDDLEGSLEQEKKVRMDLERVRRK 1062
Cdd:COG5022 933 LKKLLNNIDLEEGPSIEYVKLPE---------LNKLHEVESKLKETSE---EYEDLLKKSTILVREGNKANSELKNFKKE 1000
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1063 LEGDLKLSlesvMDLENDKQQLEEK---------LKKKDFEMNEISSRIEDEQALVNQLHKKIKELQART 1123
Cdd:COG5022 1001 LAELSKQY----GALQESTKQLKELpvevaelqsASKIISSESTELSILKPLQKLKGLLLLENNQLQARY 1066
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-774 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 828.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRR-SEAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 178 GESGAGKTVNTKRVIQYFAIVAalgdtpaKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALS-------GSGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHF----CSQGVTTVENLDDGQEL 333
Cdd:cd00124 154 PTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDDAEEF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 334 MATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREE--QAEADGTESADKASYLMGVSSADLIKGLLHPRVKVG 411
Cdd:cd00124 234 QELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 412 NEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQ--YFIGVLDIAGFEIFDLNSFEQLCINFTNEKL 489
Cdd:cd00124 314 GETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 490 QQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFL 568
Cdd:cd00124 394 QQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAH-GSHPRFF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 569 KPRPDKKRkyeaHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSAnkllaslyenyvisdsasdpkaggkekrkk 648
Cdd:cd00124 472 SKKRKAKL----EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS------------------------------ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 649 aasfqtvsqLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQ 728
Cdd:cd00124 518 ---------QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLK 588
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2045330442 729 RYRILNPSAiPDDKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd00124 589 RYRILAPGA-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 797.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVAAL----GDTPAKKGQGPATKTGGtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 254
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgSGAVPHPAVNPAVLIGE-LEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 255 HFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS-----QKKPELLDmllvssNPYDYHFCSQGVTTVENLDD 329
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAgatpeQREKFILD------DVKSYAFLSNGSLPVPGVDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 330 GQELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVK 409
Cdd:cd14911 234 YAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 410 VGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEK 488
Cdd:cd14911 314 VGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLdRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 489 LQQFFNHHMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFL 568
Cdd:cd14911 394 LQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFM 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 569 KprpdKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDSA----SDPKAGgke 644
Cdd:cd14911 473 K----TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAqqalTDTQFG--- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 645 KRKKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYA 724
Cdd:cd14911 546 ARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2045330442 725 EFKQRYRILNPSAIPdDKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14911 626 EFRQRYELLTPNVIP-KGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 776.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVAAlgdtpAKKGQGPATkTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVAS-----SHKGRKDHN-IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPEL-LDMLLVSSNpyDYHFCSQGVTTVENLDDGQELMATD 337
Cdd:cd14920 155 TGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 338 RAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVK 417
Cdd:cd14920 233 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 418 GQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLyTSLPRQ--YFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNH 495
Cdd:cd14920 313 AQTKEQADFAVEALAKATYERLFRWLVHRINKAL-DRTKRQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 496 HMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFLKPRp 572
Cdd:cd14920 392 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPR- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 573 dkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENY-----VISDSASDPKAGGKEKRK 647
Cdd:cd14920 470 --QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgLDQVTGMTETAFGSAYKT 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 648 KAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFK 727
Cdd:cd14920 548 KKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2045330442 728 QRYRILNPSAIPdDKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14920 628 QRYEILTPNAIP-KGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 724.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVAAlgDTPAKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVAS--SFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPyDYHFCSQGVTTVENLDDGQELMATDR 338
Cdd:cd14932 159 NGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYS-KYRFLSNGNVTIPGQQDKELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 419 QNVEQVNYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHM 497
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALdKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 498 FILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFLKPrpdK 574
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQ-GNNPKFQKP---K 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 575 KRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENY---VISDSA---SDPKAGGKEKRKk 648
Cdd:cd14932 474 KLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdriVGLDKVagmGESLHGAFKTRK- 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 649 aASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQ 728
Cdd:cd14932 553 -GMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2045330442 729 RYRILNPSAIPDDkFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14932 632 RYEILTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 695.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVAAlgdtpAKKGQGPATKTgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVAS-----SHKGKKDTSIT-GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELL-DMLLVSSNpyDYHFCSQGVTTVENLDDGQELMATD 337
Cdd:cd14921 155 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 338 RAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVK 417
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 418 GQNVEQVNYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHH 496
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKALdKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 497 MFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFLKPrpd 573
Cdd:cd14921 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKP--- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 574 KKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENyVISDSASDPKAGGKEKRKKAAS-- 651
Cdd:cd14921 469 KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKD-VDRIVGLDQMAKMTESSLPSASkt 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 652 ----FQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFK 727
Cdd:cd14921 548 kkgmFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2045330442 728 QRYRILNPSAIPDDkFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14921 628 QRYEILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-774 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 689.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVAALGDTpaKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKT--KKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVsSNPYDYHFCSQGVTTVENLDDGQELMATDR 338
Cdd:cd15896 159 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL-ENYNNYRFLSNGNVTIPGQQDKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 419 QNVEQVNYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHM 497
Cdd:cd15896 318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALdKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 498 FILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFLKPrpdK 574
Cdd:cd15896 398 FILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKP---K 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 575 KRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENyVISDSASDPKAGGKEK----RKKAA 650
Cdd:cd15896 474 KLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKD-VDRIVGLDKVSGMSEMpgafKTRKG 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 651 SFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRY 730
Cdd:cd15896 553 MFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2045330442 731 RILNPSAIPDDkFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd15896 633 EILTPNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 684.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVAAlgDTPAKKGQGpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVAS--SHKSKKDQG-------ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsnPYD-YHFCSQGVTTVENLDDGQELMATD 337
Cdd:cd14919 152 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE--PYNkYRFLSNGHVTIPGQQDKDMFQETM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 338 RAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVK 417
Cdd:cd14919 230 EAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 418 GQNVEQVNYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHH 496
Cdd:cd14919 310 AQTKEQADFAIEALAKATYERMFRWLVLRINKALdKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 497 MFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFLKPrpd 573
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKP--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 574 KKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENyVISDSASDPKAGGKEK------RK 647
Cdd:cd14919 466 KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD-VDRIIGLDQVAGMSETalpgafKT 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 648 KAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFK 727
Cdd:cd14919 545 RKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFR 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2045330442 728 QRYRILNPSAIPDDkFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14919 625 QRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 683.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVAalgdTPAKKGQGPATKtgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVA----SSPKGRKEPGVP--GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYdYHFCSQGVTTvenlDDGQE---LMA 335
Cdd:cd14930 155 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSS----SPGQErelFQE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 336 TDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 415
Cdd:cd14930 230 TLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 416 VKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSlPRQ--YFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFF 493
Cdd:cd14930 310 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRS-PRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 494 NHHMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFLKP 570
Cdd:cd14930 389 NHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 571 RpdkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLY---ENYVISDSASDPKAGGKEKRK 647
Cdd:cd14930 468 R---HLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRP 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 648 KAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFK 727
Cdd:cd14930 545 RRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFR 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2045330442 728 QRYRILNPSAIPDDkFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14930 625 QRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-774 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 682.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 100 SVLYNLRRRYS-AWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVaalgdtpakkgQGPATKTGGTlEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATV-----------GGSSSGETQV-EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQK-KPELLDMLLVSSNpyDYHFCSQG-VTTVENLDDGQELMAT 336
Cdd:cd01380 150 NYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKELHLGSAE--DFFYTNQGgSPVIDGVDDAAEFEET 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 337 DRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVV 416
Cdd:cd01380 228 RKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 417 KGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLP--RQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFN 494
Cdd:cd01380 308 KPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 495 HHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGK-SPNFLKPRPD 573
Cdd:cd01380 388 QHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 574 KKRkyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANkllaslyenyvisdsasdpkaggkekRKKaasfq 653
Cdd:cd01380 467 NTA-----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN--------------------------RKK----- 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 654 TVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRIL 733
Cdd:cd01380 511 TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVL 590
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2045330442 734 NPSAIPDDKfvDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd01380 591 LPSKEWLRD--DKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-774 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 652.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 180 SGAGKTVNTKRVIQYFAIVAalgdtpakkgqGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVS-----------GGSESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDRA 339
Cdd:cd01378 151 GEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADgTESADKASYLMGVSSADLIKGLLHPRVKVGNEY---VV 416
Cdd:cd01378 231 MKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 417 KGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQ-YFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFfnh 495
Cdd:cd01378 310 VPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQI--- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 496 hmFIL-----EQEEYKREGIEWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFP-KATDNSFKAKMydNHIGKSPNFL 568
Cdd:cd01378 387 --FIEltlkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL--NQLFSNHPHF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 569 KPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDSasdpkaggkEKRKK 648
Cdd:cd01378 462 ECPSGHFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDS---------KKRPP 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 649 AASFQTvsqlhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQ 728
Cdd:cd01378 533 TAGTKF-----KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLE 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2045330442 729 RYRILNPSAIPDDKFvDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd01378 608 RYKLLSPKTWPAWDG-TWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-774 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 645.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVAalgdtpakkGQgpatktGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAIS---------GQ------HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVsSNPYDYHFCSQG-VTTVENLDDGQELMATD 337
Cdd:cd01381 146 NGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLEL-GDASDYYYLTQGnCLTCEGRDDAAEFADIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 338 RAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQRE--EQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 415
Cdd:cd01381 225 SAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 416 VKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYF---IGVLDIAGFEIFDLNSFEQLCINFTNEKLQQF 492
Cdd:cd01381 305 VSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 493 FNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLI-EKPLGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFLKPr 571
Cdd:cd01381 385 FVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 572 pdkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVisdsasdpkAGGKEKRKKAas 651
Cdd:cd01381 462 ---KSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDI---------SMGSETRKKS-- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 652 fQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYR 731
Cdd:cd01381 528 -PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYR 606
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2045330442 732 ILNPSAIPDDKfVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd01381 607 VLVPGIPPAHK-TDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-774 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 621.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 180 SGAGKTVNTKRVIQYFAIVaalgdtpakkgqgpaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAV---------------TNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDAS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS--QKKPELLDMLLVSSnPYDYHFCSQ-GVTTVENLDDGQELMAT 336
Cdd:cd14883 147 GHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAgaKHSKELKEKLKLGE-PEDYHYLNQsGCIRIDNINDKKDFDHL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 337 DRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAE-ADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 415
Cdd:cd14883 226 RLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 416 VKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNH 495
Cdd:cd14883 306 EIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 496 HMFILEQEEYKREGIEWTFIDFGlDLQACIDLIEK-PLGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFLKPrpdK 574
Cdd:cd14883 386 YVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKP---D 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 575 KRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASL--YENYVISDSASDPKAGGKEKRKKAASF 652
Cdd:cd14883 461 RRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELftYPDLLALTGLSISLGGDTTSRGTSKGK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 653 QTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRI 732
Cdd:cd14883 541 PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLC 620
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2045330442 733 LNPSAI-PDDKfvDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14883 621 LDPRARsADHK--ETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-774 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 618.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYkGKRRSEaPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY-RQKLLD-SPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 180 SGAGKTVNTKRVIQYfaiVAALGDTpakkgqgpatktGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd01383 80 SGAGKTETAKIAMQY---LAALGGG------------SSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQ-GVTTVENLDDGQELMATDR 338
Cdd:cd01383 145 GKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQsNCLTIDGVDDAKKFHELKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd01383 224 ALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 419 QNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTS-LPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHM 497
Cdd:cd01383 304 LTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGkRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 498 FILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMyDNHigkspnfLKPRPDKKR 576
Cdd:cd01383 384 FKLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQH-------LKSNSCFKG 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 577 KYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDSASDP--KAGGKEKRKkaasfQT 654
Cdd:cd01383 455 ERGGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASRKALPltKASGSDSQK-----QS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 655 VSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILN 734
Cdd:cd01383 530 VATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLL 609
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2045330442 735 PSAIPDDKFVDSRKAAekLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd01383 610 PEDVSASQDPLSTSVA--ILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-774 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 582.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 178 GESGAGKTVNTKRVIQYFAIVAalgdtpakkgqGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG-----------GRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQGVT-TVENLDDGQELMAT 336
Cdd:cd01384 150 DAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLK-DPKQFHYLNQSKCfELDGVDDAEEYRAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 337 DRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKqkqreEQAEADGTESADKASY--------LMGVSSADLIKGLLHPRV 408
Cdd:cd01384 229 RRAMDVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEKSEfhlkaaaeLLMCDEKALEDALCKRVI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 409 KVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEK 488
Cdd:cd01384 304 VTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 489 LQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNhIGKSPNF 567
Cdd:cd01384 384 LQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 568 LKPrpdkKRKYEAhFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYEnyvisdsasdpkAGGKEKRK 647
Cdd:cd01384 462 SKP----KLSRTD-FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFP------------PLPREGTS 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 648 KAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFK 727
Cdd:cd01384 525 SSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2045330442 728 QRYRILNPSAipDDKFVDSRKAAEKLLSSLDIdhNQYRFGHTKVFFK 774
Cdd:cd01384 605 DRFGLLAPEV--LKGSDDEKAACKKILEKAGL--KGYQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-774 |
2.73e-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: 544.92 E-value: 2.73e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 178 GESGAGKTVNTKRVIQYFAivaalgdtpAKKGQGpatktGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLT---------ESWGSG-----AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLvssnpydyhfcsqgvtTVENLDDGQELMATD 337
Cdd:cd01382 147 EKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 338 RAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREE----QAEADGTESADKASYLMGVSSADLIKGLLHpRVKVGNE 413
Cdd:cd01382 211 KAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSgggcNVKPKSEQSLEYAAELLGLDQDELRVSLTT-RVMQTTR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 414 YVVKGQ------NVEQVNYAVGALAKATYDRMFKWLVGRINRtlytSLPRQ---YFIGVLDIAGFEIFDLNSFEQLCINF 484
Cdd:cd01382 290 GGAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQ----CIPFEtssYFIGVLDIAGFEYFEVNSFEQFCINY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 485 TNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNHiGK 563
Cdd:cd01382 366 CNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKH-KN 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 564 SPNFLKPRPDKKRKY------EAhFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDSASD 637
Cdd:cd01382 444 HFRLSIPRKSKLKIHrnlrddEG-FLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDSK 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 638 PKAGgkekrkkAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGF 717
Cdd:cd01382 523 QKAG-------KLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGF 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2045330442 718 PNRILYAEFKQRYRILNPSAIPDdkfVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd01382 596 PSRTSFHDLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-774 |
1.58e-173 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 542.83 E-value: 1.58e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVAalGDTpakkgqgpatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVA--GST-------------NGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnpyDYHFCSQ-GVTTVENLDDGQELMATD 337
Cdd:cd14872 146 RGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA---AYGYLSLsGCIEVEGVDDVADFEEVV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 338 RAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASY---LMGVSSADLIKGLLHPRVKvgney 414
Cdd:cd14872 223 LAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLME----- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 415 vVKGQNV-------EQVNYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTN 486
Cdd:cd14872 298 -IKGCDPtripltpAQATDACDALAKAAYSRLFDWLVKKINESMrPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 487 EKLQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIEK-PLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSp 565
Cdd:cd14872 377 EKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 566 NFLkprPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYenyvisdsasdPKAGGKEK 645
Cdd:cd14872 455 TFV---YAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF-----------PPSEGDQK 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 646 RKKAasfqTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAE 725
Cdd:cd14872 521 TSKV----TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHER 596
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2045330442 726 FKQRYRILnPSAIPDDKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14872 597 FLKRYRFL-VKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-774 |
1.05e-165 |
|
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: 522.03 E-value: 1.05e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLR----NRENQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 174 MLITGESGAGKTVNTKRVIQYFAIVAAlGDTPAKKGQGPAT-----KTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITS-GFAQGASGEGEAAseaieQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 249 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQGVTTVENLD 328
Cdd:cd14890 160 GKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQ-TPVEYFYLRGECSSIPSCD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 329 DGQELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGT-ESADKASYLMGVSSADLIKGLLHPR 407
Cdd:cd14890 239 DAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 408 VKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNE 487
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 488 KLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPLGIMSIL------------EEECMFPKATDNSFKA 554
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFitlddcwrfkgeEANKKFVSQLHASFGR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 555 KMYDNHIGKS----PNFLKPRPDKKRkyeaHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLlaslyenyv 630
Cdd:cd14890 478 KSGSGGTRRGssqhPHFVHPKFDADK----QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI--------- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 631 isdsasdpkaggkekRKKAASFQTVSQLHKenlnkLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGI 710
Cdd:cd14890 545 ---------------REVSVGAQFRTQLQE-----LMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAI 604
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2045330442 711 RICRKGFPNRILYAEFKQRYRILNPSAipddkfvDSRKAAEKLLSS-LDIDHNQYRFGHTKVFFK 774
Cdd:cd14890 605 QIRQQGFALREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKmLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-774 |
7.91e-165 |
|
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: 519.72 E-value: 7.91e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 178 GESGAGKTVNTKRVIQYFAIVAA-LGDTPAKKgqgpatktggtledqIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 256
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGgLNDSTIKK---------------IIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 257 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDmLLVSSNPYDYHFcSQGVTTVENLDDGQELMAT 336
Cdd:cd14903 146 DKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERL-FLDSANECAYTG-ANKTIKIEGMSDRKHFART 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 337 DRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAE--ADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEY 414
Cdd:cd14903 224 KEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 415 VVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFN 494
Cdd:cd14903 304 YTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 495 HHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFLKPRPDK 574
Cdd:cd14903 384 QDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 575 krkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDSASDPKAGGKEKRK--KAASF 652
Cdd:cd14903 463 -----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRrgGALTT 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 653 QTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRI 732
Cdd:cd14903 538 TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2045330442 733 LNPSAipDDKFVDSRKAAEKLLSSLDIDH-NQYRFGHTKVFFK 774
Cdd:cd14903 618 FLPEG--RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-774 |
1.13e-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: 1.13e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 180 SGAGKTVNTKRVIQYfaiVAALGDTPAKkgqgpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd01379 82 SGAGKTESANLLVQQ---LTVLGKANNR-----------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIM----SQKKpeLLDMLLVSSNPYDY-HFCSQGVTTVENLDDGQE-L 333
Cdd:cd01379 148 GAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYaglaEDKK--LAKYKLPENKPPRYlQNDGLTVQDIVNNSGNREkF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 334 MATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQ----AEADGTESADKASYLMGVSSADLIKGLLHPRVK 409
Cdd:cd01379 226 EEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 410 VGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLY---TSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTN 486
Cdd:cd01379 306 TRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKpdrSASDEPLSIGILDIFGFENFQKNSFEQLCINIAN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 487 EKLQQFFNHHMFILEQEEYKREGIEWTFIDFG-----LDLqacidLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHi 561
Cdd:cd01379 386 EQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 562 gKSPNFLKPRPDkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLAslyenyvisdsasdpkag 641
Cdd:cd01379 460 -KSKYYWRPKSN-----ALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 642 gkekrkkaasfQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRI 721
Cdd:cd01379 516 -----------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRI 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 2045330442 722 LYAEFKQRYRILNPSAipDDKFVDSRKAAEKLLSSLDIDHnqYRFGHTKVFFK 774
Cdd:cd01379 585 LFADFLKRYYFLAFKW--NEEVVANRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-774 |
3.88e-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: 518.09 E-value: 3.88e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSeAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSIS-KSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 178 GESGAGKTVNTKRVIQYFAIVAAlgdtpakkgqgPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF- 256
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGS-----------EDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFs 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 257 --------GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS-----------------------QKKPELLDML 305
Cdd:cd14888 149 klkskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 306 LVSS-NPYDYHFCSqGVTTVENLDDGQELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQA---EADG 381
Cdd:cd14888 229 SFEPhLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASC 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 382 TESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYF 460
Cdd:cd14888 308 TDDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIgYSKDNSLLF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 461 IGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLI-EKPLGIMSILE 539
Cdd:cd14888 388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 540 EECMFPKATDNSFKAKMYDNHIGKSpnflkpRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSAN 619
Cdd:cd14888 467 EECFVPGGKDQGLCNKLCQKHKGHK------RFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKN 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 620 KLLASLYENYVisdsaSDPKAGGKEKRKkaasFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLH 699
Cdd:cd14888 541 PFISNLFSAYL-----RRGTDGNTKKKK----FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNE 611
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2045330442 700 QLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPsaipddkfvdsrKAAEKLLSSldidhnqYRFGHTKVFFK 774
Cdd:cd14888 612 QLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN------------GEGKKQLSI-------WAVGKTLCFFK 667
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-772 |
1.02e-160 |
|
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: 508.17 E-value: 1.02e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAY------KGKRRSEAPPHIYSIADNAYNDMLRNRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 171 --NQSMLITGESGAGKTVNTKRVIQYFAIVAAlgdtpaKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS------ATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 249 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKP-ELLDMLLVSSNPYDYHFCSQGVTTVENL 327
Cdd:cd14901 155 GKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSdELHALGLTHVEEYKYLNSSQCYDRRDGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 328 DDGQELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTES-ADKASYLMGVSSADLIKGLLHP 406
Cdd:cd14901 235 DDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLAnVRAACDLLGLDMDVLEKTLCTR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 407 RVKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQY-FIGVLDIAGFEIFDLNSFEQLCINF 484
Cdd:cd14901 315 EIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaYSESTGASrFIGIVDIFGFEIFATNSLEQLCINF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 485 TNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNhIGK 563
Cdd:cd14901 395 ANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 564 SPNFlkpRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASlyenyvisdsasdpkaggk 643
Cdd:cd14901 473 HASF---SVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 644 ekrkkaasfqTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILY 723
Cdd:cd14901 531 ----------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPH 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 2045330442 724 AEFKQRYRILNPSAIPDDKFVdsRKAAEKLLSSLDI------DHNQYRFGHTKVF 772
Cdd:cd14901 601 DAFVHTYSCLAPDGASDTWKV--NELAERLMSQLQHselnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-774 |
4.73e-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: 506.60 E-value: 4.73e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVAalgdtpaKKGQGPATktggtleDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN-------QRRNNLVT-------EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-E 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS------QKKPELLDmllvssnPYDYHFCSQGVTT-VENLDDGQ 331
Cdd:cd01387 146 GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAglpaqlRQKYGLQE-------AEKYFYLNQGGNCeIAGKSDAD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 332 ELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQRE---EQAEADGTESADKASYLMGVSSADLIKGLLHPRV 408
Cdd:cd01387 219 DFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 409 KVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEK 488
Cdd:cd01387 299 ETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANEN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 489 LQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLI-EKPLGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNF 567
Cdd:cd01387 379 LQYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELY 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 568 LKPRPDkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDSASDPKAGGKEKRK 647
Cdd:cd01387 457 SKPRMP-----LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGKGRFVT 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 648 KAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFK 727
Cdd:cd01387 532 MKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFI 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2045330442 728 QRYRILNPSAIPDDKFVDSRkaaEKLLSSLD--IDHNQYRFGHTKVFFK 774
Cdd:cd01387 612 DRYRCLVALKLPRPAPGDMC---VSLLSRLCtvTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-774 |
1.85e-159 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 506.14 E-value: 1.85e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYfaiVAALgdtpAKKGQGPATktggtlEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01385 81 ESGSGKTESTNFLLHH---LTAL----SQKGYGSGV------EQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSqKKPELLDMLLVSSNPYDYHFCSQGVT-TVENLDDGQELMATD 337
Cdd:cd01385 148 NGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLA-GASEEERKELHLKQPEDYHYLNQSDCyTLEGEDEKYEFERLK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 338 RAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQK--QREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 415
Cdd:cd01385 227 QAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 416 VKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTL----YTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQ 491
Cdd:cd01385 307 ILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 492 FFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKmYDNHIGKSPNFLKP 570
Cdd:cd01385 387 YFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 571 rpdkkRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASL--------------------YENYV 630
Cdd:cd01385 465 -----QVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrwavlraffraMAAFR 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 631 ISDSASDPKAGGKEK------------RKKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVL 698
Cdd:cd01385 540 EAGRRRAQRTAGHSLtlhdrttksllhLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVL 619
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2045330442 699 HQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPSAIpdDKFVDSRKaaeKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd01385 620 RQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGL--ISSKEDIK---DFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
854-1931 |
1.90e-159 |
|
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: 519.35 E-value: 1.90e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 854 EKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELMER 933
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 934 LEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALTEAHQQ 1013
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1014 TLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQLEEKLKKKDF 1093
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1094 EMNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQRGDVARELEELSERLEEAGGATSAQIEINK 1173
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1174 KRETDFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATS 1253
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1254 EKMCRLYEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKA 1333
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1334 KSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSKANAEVAQWRTKYETDAiQRTEELEEAKKKLVTRLQEAEESVE 1413
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1414 ASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQKESRGLSTELFKLK 1493
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1494 NSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQLEL 1573
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1574 NQIKADVDRKLAEKDEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLRKKMECDLNEMEVQLNHANRQASESQKLLRN 1653
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1654 LQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTGLIN 1733
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1734 QKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLERMKKNMEQTVKDLQMRLDEAEQIAL 1813
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1814 KGGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEA 1893
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 2045330442 1894 EEQANSNLTKYRKLQHELDDAEERADMAETQVNKLRVR 1931
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-774 |
5.71e-155 |
|
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: 492.39 E-value: 5.71e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 178 GESGAGKTVNTKRVIQYfaiVAALGDTPAKKGQGPATKTggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14873 81 GESGAGKTESTKLILKF---LSVISQQSLELSLKEKTSC---VEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNIC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQ-GVTTVENLDDGQELMAT 336
Cdd:cd14873 155 QKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST-PENYHYLNQsGCVEDKTISDQESFREV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 337 DRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFkqkqreeqAEADGTESADK-----ASYLMGVSSADLIKGLLHPRVKVG 411
Cdd:cd14873 234 ITAMEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 412 NEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSlPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQ 491
Cdd:cd14873 306 GEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGK-EDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 492 FFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFLKPR 571
Cdd:cd14873 385 YFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 572 PDkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDSASDPKAGGKEKRKkaas 651
Cdd:cd14873 463 VA-----VNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRP---- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 652 fqTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYR 731
Cdd:cd14873 534 --TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYK 611
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2045330442 732 ILNPSAIPDDkfvDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14873 612 VLMRNLALPE---DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-774 |
3.93e-153 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 487.73 E-value: 3.93e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKG--KRRSEAPPHIYSIADNAYNDMLRNR----EN 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 172 QSMLITGESGAGKTVNTKRVIQYFAIVAALGDTPAKKGQgpATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKF 251
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKG--AANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 252 IRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKpELLDMLLVSSNPYDYHFCSQG-VTTVENLDDG 330
Cdd:cd14892 159 IQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGnCVEVDGVDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 331 QELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQ--KQREEQAEADGTESADKASYLMGVSSADLIKGLLhPRV 408
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLV-TQT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 409 KV---GNEYVVKGQNVEQVNyAVGALAKATYDRMFKWLVGRINR----------TLYTSLPRQYFIGVLDIAGFEIFDLN 475
Cdd:cd14892 317 TStarGSVLEIKLTAREAKN-ALDALCKYLYGELFDWLISRINAchkqqtsgvtGGAASPTFSPFIGILDIFGFEIMPTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 476 SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIEK-PLGIMSILEEECMFP-KATDNSFK 553
Cdd:cd14892 396 SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 554 AKMYDNHIGKSPNFLKPRPDKKrkyeaHFELVHYAGVVPYNIIGWLDKNKDPLnetvvacfqksANKLLASLyenyvisd 633
Cdd:cd14892 475 TIYHQTHLDKHPHYAKPRFECD-----EFVLRHYAGDVTYDVHGFLAKNNDNL-----------HDDLRDLL-------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 634 sasdpkaggkEKRKKaasFQTvsqlhkeNLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRIC 713
Cdd:cd14892 531 ----------RSSSK---FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIR 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 714 RKGFPNRILYAEFKQRYRIL-------NPSAIPDDKFVDSRKAAEKLLSSLdiDHNQYRFGHTKVFFK 774
Cdd:cd14892 591 REGFPIRRQFEEFYEKFWPLarnkagvAASPDACDATTARKKCEEIVARAL--ERENFQLGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-774 |
4.48e-145 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 464.55 E-value: 4.48e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKR-RSEAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 178 GESGAGKTVNTKRVIQYFAIVAALGDTpakkgqgpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDS--------------DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQGVTTVENLDDGQEL---- 333
Cdd:cd14897 147 ENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLE-DPDCHRILRDDNRNRPVFNDSEELeyyr 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 334 -MATD--RAMDILGFLPDEKYGCYKIVGAIMHFGNMKFkqkqrEEQAEADGTESADK-----ASYLMGVSSADLIKGLLH 405
Cdd:cd14897 226 qMFHDltNIMKLIGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALIS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 406 PRVKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYF-----IGVLDIAGFEIFDLNSFEQL 480
Cdd:cd14897 301 NVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 481 CINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLI-EKPLGIMSILEEECMFPKATDNSFKAKMyDN 559
Cdd:cd14897 381 CINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 560 HIGKSPNFLKPRPDKkrkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVisdsasdpk 639
Cdd:cd14897 459 YCGESPRYVASPGNR-----VAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSYF--------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 640 aggkekrkkaasfqtvsqlhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPN 719
Cdd:cd14897 525 --------------------KRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPI 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 2045330442 720 RILYAEFKQRYRILNPSaiPDDKFVDSRKAAEKLLSSLDIDhnQYRFGHTKVFFK 774
Cdd:cd14897 585 RIKYEDFVKRYKEICDF--SNKVRSDDLGKCQKILKTAGIK--GYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-733 |
1.32e-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: 452.07 E-value: 1.32e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP------------VYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLR 167
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPglyssdtmakylLSFEARSSSTRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 168 NR----ENQSMLITGESGAGKTVNTKRVIQYFAIVaalGDTPAKKGQGpATKTGGTLEDQIIEANPAMEAFGNAKTLRND 243
Cdd:cd14900 82 GLngvmSDQSILVSGESGSGKTESTKFLMEYLAQA---GDNNLAASVS-MGKSTSGIAAKVLQTNILLESFGNARTLRND 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 244 NSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLdmllvSSNPYdyhfcsqgvtt 323
Cdd:cd14900 158 NSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAAR-----KRDMY----------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 324 venlddgQELMatdRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTE-------SADKASYLMGVSS 396
Cdd:cd14900 222 -------RRVM---DAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDlapssiwSRDAAATLLSVDA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 397 ADLIKGLLHPRVKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTL-----YTSLPRQYFIGVLDIAGFEI 471
Cdd:cd14900 292 TKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 472 FDLNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLI-EKPLGIMSILEEECMFPKATDN 550
Cdd:cd14900 372 FPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECVMPKGSDT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 551 SFKAKMYdNHIGKSPNFLKPRPDKKRkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKsankllaslyenyv 630
Cdd:cd14900 451 TLASKLY-RACGSHPRFSASRIQRAR---GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVY-------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 631 isdsasdpkaGGKekrkkaasfqtvsqlHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGI 710
Cdd:cd14900 513 ----------GLQ---------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAV 567
|
650 660
....*....|....*....|...
gi 2045330442 711 RICRKGFPNRILYAEFKQRYRIL 733
Cdd:cd14900 568 RVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-774 |
5.16e-140 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 451.79 E-value: 5.16e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGK--------RRSEAPPHIYSIADNAYNDMLRNR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 170 ENQSMLITGESGAGKTVNTKRVIQYFAIVAALGDTPAKKGQGP-----ATKTGGTLEDQIIEANPAMEAFGNAKTLRNDN 244
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 245 SSRFGKFIRIHFG-PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYD-YHFCSQGV 321
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDrYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 322 T-TVENLDDGQELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQ--REEQAEADGTESADKASYLMGVSSAD 398
Cdd:cd14907 241 CyEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 399 LIKGLLHPRVKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTL--YTSLPRQYF------IGVLDIAGFE 470
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpKDEKDQQLFqnkylsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 471 IFDLNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTF--IDFgLDLQACIDLIEK-PLGIMSILEEECMFPKA 547
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 548 TDNSFKAKMYDNHiGKSPNFLKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYe 627
Cdd:cd14907 480 TDEKLLNKIKKQH-KNNSKLIFPNKINKDT----FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 628 nYVISDSASDPKAGGKEKRKKAasfQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVL 707
Cdd:cd14907 554 -SGEDGSQQQNQSKQKKSQKKD---KFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVL 629
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2045330442 708 EGIRICRKGFPNRILYAEFKQRYRILNpsaipddkfvdsrkaaekllssldidhNQYRFGHTKVFFK 774
Cdd:cd14907 630 ESIRVRKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-774 |
9.62e-140 |
|
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: 450.26 E-value: 9.62e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNL--RRRYSAWMIYTYSGLFCVTVNPYKWLPvytAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRE---NQS 173
Cdd:cd14891 1 AGILHNLeeRSKLDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 174 MLITGESGAGKTVNTKRVIQYFAIVAALGDTPAKKGQGPATKT----GGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFG 249
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKrklsVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 250 KFIRIHFGPTG-KLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQ-GVTTVENL 327
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLS-PEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 328 DDGQELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKA----SYLMGVSSADLIKGL 403
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEAlataAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 404 LHPRVKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTL---YTSLPrqyFIGVLDIAGFEIFDL-NSFEQ 479
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLghdPDPLP---YIGVLDIFGFESFETkNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 480 LCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLI-EKPLGIMSILEEECMFPKATDNSFKAKMYD 558
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 559 NHiGKSPNFLKPRPDKKRKyeaHFELVHYAGVVPYNIIGWLDKNKDPLNETvVACFQKSANKLLASLYEnyvisdsasdp 638
Cdd:cd14891 473 TH-KRHPCFPRPHPKDMRE---MFIVKHYAGTVSYTIGSFIDKNNDIIPED-FEDLLASSAKFSDQMQE----------- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 639 kaggkekrkkaasfqtvsqlhkenlnkLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFP 718
Cdd:cd14891 537 ---------------------------LVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLP 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2045330442 719 NRILYAEFKQRYRILNPSAI------PDDKFVdsrkaaEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14891 590 TRVTYAELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-774 |
3.66e-137 |
|
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: 443.58 E-value: 3.66e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 101 VLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDML----RNRENQSMLI 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 177 TGESGAGKTVNTKRVIQYFAIVAalgdtpakkgqgpatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC---------------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 257 gPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI---MSQKKPELLDMLlvssNPYDYHFCSQGVTTVENLDD-GQE 332
Cdd:cd14889 148 -RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLL----DPGKYRYLNNGAGCKREVQYwKKK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 333 LMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREE-QAEADGTESADKASYLMGVSSADLIKGLLHPRVKVG 411
Cdd:cd14889 223 YDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 412 NEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLytsLPRQYF------IGVLDIAGFEIFDLNSFEQLCINFT 485
Cdd:cd14889 303 GEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQACINLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 486 NEKLQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDL-IEKPLGIMSILEEECMFPKATDNSFKAKMyDNHIGKS 564
Cdd:cd14889 380 NEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 565 PNFlkprpDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDSASDPKAG--- 641
Cdd:cd14889 458 SYY-----GKSRSKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKlpq 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 642 -----GKEKRKkaasfQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKG 716
Cdd:cd14889 533 agsdnFNSTRK-----QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREG 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 2045330442 717 FPNRILYAEFKQRYRIL-NPSAIPDDKfvdsrKAAEKLLSSLDIdhNQYRFGHTKVFFK 774
Cdd:cd14889 608 FSWRPSFAEFAERYKILlCEPALPGTK-----QSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-736 |
1.04e-135 |
|
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: 441.64 E-value: 1.04e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYK--------GKRRSEAPPHIYSIADNAYNDMLRN- 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 169 RENQSMLITGESGAGKTVNTKRVIQYFAIVAAlgDTPAKKGQGPATKTGGTledQIIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGR--DQSSTEQEGSDAVEIGK---RILQTNPILESFGNAQTIRNDNSSRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 249 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYDYH---FCSQGVTTV 324
Cdd:cd14902 156 GKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLgLQKGGKYELLnsyGPSFARKRA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 325 ENLDDGQELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESA---DKASYLMGVSSADLIK 401
Cdd:cd14902 236 VADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLET 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 402 GLLHPRVKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTL-------YTSLPRQYF--IGVLDIAGFEIF 472
Cdd:cd14902 316 LLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEInyfdsavSISDEDEELatIGILDIFGFESL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 473 DLNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFPKATDNS 551
Cdd:cd14902 396 NRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGSNQA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 552 FKAKMYDNHIGkspnflkprpdkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVI 631
Cdd:cd14902 475 LSTKFYRYHGG----------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENR 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 632 SDSASDPKAGGKeKRKKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIR 711
Cdd:cd14902 539 DSPGADNGAAGR-RRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVR 617
|
650 660
....*....|....*....|....*
gi 2045330442 712 ICRKGFPNRILYAEFKQRYRILNPS 736
Cdd:cd14902 618 IARHGYSVRLAHASFIELFSGFKCF 642
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-774 |
6.14e-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: 434.37 E-value: 6.14e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 178 GESGAGKTVNTKRVIQYFAIVAAlgdtpakkgqGPATKTggtlEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG----------GRKDKT----IAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNpYDYHFCSQGV--TTVENLDDGQELMA 335
Cdd:cd14904 147 GRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPN-CQYQYLGDSLaqMQIPGLDDAKLFAS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 336 TDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGtESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 415
Cdd:cd14904 226 TQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNG-SQLSQVAKMLGLPTTRIEEALCNRSVVTRNESV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 416 VKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQY-FIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFN 494
Cdd:cd14904 305 TVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 495 HHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSPNFLKPRPDK 574
Cdd:cd14904 385 TDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTKKDNESIDFPKV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 575 KRkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYEnyviSDSASDPKAGGKEKRKKAASFQT 654
Cdd:cd14904 464 KR---TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFG----SSEAPSETKEGKSGKGTKAPKSL 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 655 VSQLhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILN 734
Cdd:cd14904 537 GSQF-KTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMF 615
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2045330442 735 PSAIPDDkfvDSRKAAEKLLSSLDIDHN-QYRFGHTKVFFK 774
Cdd:cd14904 616 PPSMHSK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
61-827 |
3.32e-130 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 429.45 E-value: 3.32e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 61 VETKDGRSLTVKEGDI----QQMNPPKFDmieDMAMLTHLNEASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTA 136
Cdd:PTZ00014 71 IDPPTNSTFEVKPEHAfnanSQIDPMTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 137 PVVAAYKGKRRSEA-PPHIYSIADNAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAivaalgdtPAKKGQgpatk 215
Cdd:PTZ00014 148 DWIRRYRDAKDSDKlPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA--------SSKSGN----- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 216 TGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS 295
Cdd:PTZ00014 215 MDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 296 QKKPELLDML-LVSSNpyDYHFCSQGVTTVENLDDGQELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQRE 374
Cdd:PTZ00014 295 GANDEMKEKYkLKSLE--EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEG 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 375 EQAEA-----DGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINR 449
Cdd:PTZ00014 373 GLTDAaaisdESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 450 TLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGI-----EWTfidfglDLQAC 524
Cdd:PTZ00014 453 TIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGIsteelEYT------SNESV 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 525 IDLI-EKPLGIMSILEEECMFPKATDNSFKAKMYdNHIGKSPNFLKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNK 603
Cdd:PTZ00014 527 IDLLcGKGKSVLSILEDQCLAPGGTDEKFVSSCN-TNLKNNPKYKPAKVDSNKN----FVIKHTIGDIQYCASGFLFKNK 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 604 DPLNETVVACFQKSANKLLASLYENYVISDsasdpkagGKEKRKKAASFQTVSQlhkenLNKLMTNLRSTQPHFVRCIIP 683
Cdd:PTZ00014 602 DVLRPELVEVVKASPNPLVRDLFEGVEVEK--------GKLAKGQLIGSQFLNQ-----LDSLMSLINSTEPHFIRCIKP 668
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 684 NETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNpSAIPDDKFVDSRKAAEKLLSSLDIDHNQ 763
Cdd:PTZ00014 669 NENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD-LAVSNDSSLDPKEKAEKLLERSGLPKDS 747
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2045330442 764 YRFGHTKVFFKAGLLGHLEEMRDERLAK---VLTLLQAAARGKIMRTELMKmneRREALMIIQWNIR 827
Cdd:PTZ00014 748 YAIGKTMVFLKKDAAKELTQIQREKLAAwepLVSVLEALILKIKKKRKVRK---NIKSLVRIQAHLR 811
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
105-774 |
9.05e-124 |
|
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: 407.42 E-value: 9.05e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 105 LRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTapvVAAYKGKRR--SEAPPHIYSIADNAYNDMLR-------NRENQSM 174
Cdd:cd14895 7 LAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEMPgwTALPPHVFSIAEGAYRSLRRrlhepgaSKKNQTI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 175 LITGESGAGKTVNTKRVIQYFAIVAAlgDTPAKKGQGPATKTGGtleDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 254
Cdd:cd14895 84 LVSGESGAGKTETTKFIMNYLAESSK--HTTATSSSKRRRAISG---SELLSANPILESFGNARTLRNDNSSRFGKFVRM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 255 HFGP-----TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYDYHFCSQGVTTV--EN 326
Cdd:cd14895 159 FFEGheldtSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELqLELLSAQEFQYISGGQCYQrnDG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 327 LDDGQELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESA------------------DKA 388
Cdd:cd14895 239 VRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqhlDIV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 389 SYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRIN----RTLYTSLPRQY----- 459
Cdd:cd14895 319 SKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNsaspQRQFALNPNKAankdt 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 460 --FIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGLDlQACIDLIE-KPLGIMS 536
Cdd:cd14895 399 tpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEqRPSGIFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 537 ILEEECMFPKATDNSFKAKMYDNHIGKSpNFLKPRPDKKrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQK 616
Cdd:cd14895 478 LLDEECVVPKGSDAGFARKLYQRLQEHS-NFSASRTDQA---DVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGK 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 617 SANKLLASLYENYVISDSASDPKAGGKEKRKKA--ASFQTVSQLhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDP 694
Cdd:cd14895 554 TSDAHLRELFEFFKASESAELSLGQPKLRRRSSvlSSVGIGSQF-KQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDM 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 695 FMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPSAIPDDkfvdsrKAAEKLLSSLDIDHNQyrFGHTKVFFK 774
Cdd:cd14895 633 AKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASD------ATASALIETLKVDHAE--LGKTRVFLR 704
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-774 |
2.02e-123 |
|
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: 405.83 E-value: 2.02e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYK--GKRRS---EAP----PHIYSIADNAYNDMLRN- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 169 RENQSMLITGESGAGKTVNTKRVIQYFAIVAALGDTPAKKGQgpaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGE---ELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 249 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIM------SQKKPELLDMLLVSSN-PYDYHFCSQG- 320
Cdd:cd14908 158 GKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggdeeEHEKYEFHDGITGGLQlPNEFHYTGQGg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 321 VTTVENLDDGQELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASY---LMGVSSA 397
Cdd:cd14908 238 APDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 398 DLIKGLLHPRVKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQY--FIGVLDIAGFEIFDLN 475
Cdd:cd14908 318 KLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrsSVGVLDIFGFECFAHN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 476 SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFP-KATDNSFK 553
Cdd:cd14908 398 SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 554 AKMYDNHIgksPNFLKPRPDKKR-------KYEAHFELVHYAGVVPYNI-IGWLDKNKDPLnetvvacfQKSANKLLASl 625
Cdd:cd14908 477 SRLYETYL---PEKNQTHSENTRfeatsiqKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEI--------PLTADSLFES- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 626 yenyvisdsasdpkaggkekrkkaasfqtvSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNG 705
Cdd:cd14908 545 ------------------------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGG 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 706 VLEGIRICRKGFPNRILYAEFKQRYRILNPSaIPDD----------------KFVDSRKAAEKLLSSLDIDHN----QYR 765
Cdd:cd14908 595 VLEAVRVARSGYPVRLPHKDFFKRYRMLLPL-IPEVvlswsmerldpqklcvKKMCKDLVKGVLSPAMVSMKNipedTMQ 673
|
....*....
gi 2045330442 766 FGHTKVFFK 774
Cdd:cd14908 674 LGKSKVFMR 682
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-774 |
4.14e-122 |
|
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: 400.70 E-value: 4.14e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVaalgdtpakkGQGPATKTGGTLEDQIieanPAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL----------YQDQTEDRLRQPEDVL----PILESFGHAKTILNANASRFGQVLRLHL-Q 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQG-VTTVENLDDGQELMATD 337
Cdd:cd14896 146 HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQG-PETYYYLNQGgACRLQGKEDAQDFEGLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 338 RAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESAD--KASYLMGVsSADLIKGLLHPRVKVGN-EY 414
Cdd:cd14896 225 KALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQV-PPERLEGAVTHRVTETPyGR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 415 VVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLytSLPRQY----FIGVLDIAGFEIFDLNSFEQLCINFTNEKLQ 490
Cdd:cd14896 304 VSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWL--APPGEAesdaTIGVVDAYGFEALRVNGLEQLCINLASERLQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 491 QFFNHHMFILEQEEYKREGIEWTFIDfGLDLQACIDLI-EKPLGIMSILEEECMFPKATDNSFKAKMYDNHiGKSPNFLK 569
Cdd:cd14896 382 LFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 570 PR---PdkkrkyeaHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENyvisdsaSDPKAGGKEKR 646
Cdd:cd14896 460 PQlplP--------VFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE-------AEPQYGLGQGK 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 647 KKAAS-FQtvsqlhkENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAE 725
Cdd:cd14896 525 PTLASrFQ-------QSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQA 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2045330442 726 FKQRYRILNPSAIPDdkFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14896 598 FLARFGALGSERQEA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-731 |
1.11e-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: 390.61 E-value: 1.11e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYK-------GKRRSEA---PPHIYSIADNAYNDMLR 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 168 NRENQSMLITGESGAGKTVNTKRVIQYFAIVAALGDTPAK---KGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDN 244
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTnseSISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 245 SSRFGKFIRIHF-GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQK----KPELLDMLLVSSNPYDYHFCSQ 319
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 320 GVTTV--ENLDDGQELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQ--KQREEQAEADGTESA---------- 385
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 386 DKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQY------ 459
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 460 ---------FIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE- 529
Cdd:cd14899 401 vddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEh 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 530 KPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKS--PNFlkpRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLN 607
Cdd:cd14899 480 RPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNshPHF---RSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFC 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 608 ETVVACFQKSANKLLASLYENYVISDSASDPKAGGKEKR-----KKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCII 682
Cdd:cd14899 557 ESAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRtrrraKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIK 636
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2045330442 683 PNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYR 731
Cdd:cd14899 637 PNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-774 |
5.23e-117 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 386.27 E-value: 5.23e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKG-KRRSEAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 178 GESGAGKTVNTKRVIQYFAivaalgdtPAKKGQgpatkTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA--------SAKSGN-----MDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS------QKKPELLDMllvssnpYDYHFCSQGVTTVENLDDGQ 331
Cdd:cd14876 148 SEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKgadsemKSKYHLLGL-------KEYKFLNPKCLDVPGIDDVA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 332 ELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADK-----ASYLMGVSSADLIKGLLHP 406
Cdd:cd14876 221 DFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVDDAAAISNESLevfkeACSLLFLDPEALKRELTVK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 407 RVKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTN 486
Cdd:cd14876 301 VTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 487 EKLQQFFNHHMFILEQEEYKREGI-----EWTfidfglDLQACID-LIEKPLGIMSILEEECMFPKATDNSFKAKMYDNh 560
Cdd:cd14876 381 EMLQKNFIDIVFERESKLYKDEGIptaelEYT------SNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 561 IGKSPNFLKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVIsdsasdpka 640
Cdd:cd14876 454 LKSNGKFKPAKVDSNIN----FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVV--------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 641 ggkEKRKKAASFQTVSQLHKeNLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNR 720
Cdd:cd14876 521 ---EKGKIAKGSLIGSQFLK-QLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYR 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 2045330442 721 ILYAEFKQRYRILNPsAIPDDKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14876 597 RPFEEFLYQFKFLDL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-772 |
5.26e-110 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 366.48 E-value: 5.26e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEA-PPHIYSIADNAYNDMLRNRE--NQSM 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 175 LITGESGAGKTVNTKRVIQYFAIVAALGDTPAKKgqgpatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESH------KIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 255 HFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS-QKKPELLDMLLVSSNPYDYhfcsqgVTTVENLDDGQEL 333
Cdd:cd14880 155 QLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKgASADERLQWHLPEGAAFSW------LPNPERNLEEDCF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 334 MATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQA---EADGTESADKASYLMGVSSADLIKGLLHPRVKV 410
Cdd:cd14880 229 EVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 411 GNEYVV--KGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPR-QYFIGVLDIAGFEIFDLNSFEQLCINFTNE 487
Cdd:cd14880 309 GKQQQVfkKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 488 KLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKSP- 565
Cdd:cd14880 389 KLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPc 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 566 ---NFLKPRPDkkrkyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYenyvisdsASDPKAGG 642
Cdd:cd14880 468 lghNKLSREPS--------FIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLF--------PANPEEKT 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 643 KEK---RKKAASFQTVSQLhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPN 719
Cdd:cd14880 532 QEEpsgQSRAPVLTVVSKF-KASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPI 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 2045330442 720 RILYAEFKQRYRILNPSAIPDDKFVDSRKAAEKLLSSLDIdhnqyrfGHTKVF 772
Cdd:cd14880 611 RVSHQNFVERYKLLRRLRPHTSSGPHSPYPAKGLSEPVHC-------GRTKVF 656
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-774 |
2.04e-107 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 358.82 E-value: 2.04e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRS-----EAPPHIYSIADNAYNDMLRNRENQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 173 SMLITGESGAGKTVNTKRVIQYFAIVAALGDTPAKKgqgpatktggtledQIIEANPAMEAFGNAKTLRNDNSSRFGKFI 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSSTDVQS--------------LILGSNPLLESFGNAKTLRNNNSSRFGKFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 253 RIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYdYHFCSQG-VTTVENLDDGQ 331
Cdd:cd14886 147 KLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASkCYDAPGIDDQK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 332 ELMATDRAMDILgFLPDEKYGCYKIVGAIMHFGNMKFKQKQR---EEQAEADGTESADKASYLMGVSSADLIKGLLHPRV 408
Cdd:cd14886 226 EFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 409 KVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEK 488
Cdd:cd14886 305 VINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANER 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 489 LQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIEKP-LGIMSILEEECMFPKATDNSFKAKMyDNHIgKSPNF 567
Cdd:cd14886 385 LQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 568 LkprPDKKRkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLlaslyenyvISDSASD-PKAGGKEKR 646
Cdd:cd14886 462 I---PGKGS--QCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPI---------VNKAFSDiPNEDGNMKG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 647 KKAASfqtvsqLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEF 726
Cdd:cd14886 528 KFLGS------TFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEF 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2045330442 727 KQRYRILNP-SAIPDDKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14886 602 FHRNKILIShNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-774 |
2.93e-107 |
|
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: 358.74 E-value: 2.93e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMI-YTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEA-PPHIYSIADNAYNDM-LRNRENQSML 175
Cdd:cd14875 1 ATLLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 176 ITGESGAGKTVNTKRVIQYfaivaaLGDTPAKKGQGPATKTggtLEDQIIE----ANPAMEAFGNAKTLRNDNSSRFGKF 251
Cdd:cd14875 81 ISGESGSGKTENAKMLIAY------LGQLSYMHSSNTSQRS---IADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 252 IRIHFGPT-GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTV------ 324
Cdd:cd14875 152 IKLYFDPTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 325 ENLDDGQELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESAdKASYLMGVSSADLIKGLL 404
Cdd:cd14875 232 KTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLRECFL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 405 hprVKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLY--TSLPRQYFIGVLDIAGFEIFDLNSFEQLCI 482
Cdd:cd14875 311 ---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpqGDCSGCKYIGLLDIFGFENFTRNSFEQLCI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 483 NFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNHI 561
Cdd:cd14875 388 NYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 562 GKSPNFLKPrpdkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDsasdpkag 641
Cdd:cd14875 467 NKSPYFVLP----KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLA-------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 642 gkeKRKkaasfQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRI 721
Cdd:cd14875 535 ---RRK-----QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRR 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 722 LYAEF-KQRYRILNPSAIPDDKFVDSRKAAEKLLSSLDIDHN----QYRFGHTKVFFK 774
Cdd:cd14875 607 PIEQFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYYQRLYGwakpNYAVGKTKVFLR 664
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-736 |
9.55e-106 |
|
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: 356.21 E-value: 9.55e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRR-SEAPPHIYSIADNAYNDMLRNRENQSMLI 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 177 TGESGAGKTVNTKRVIQYfaivaaLGDTPAKKGQGPAT--KTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 254
Cdd:cd14906 81 SGESGSGKTEASKTILQY------LINTSSSNQQQNNNnnNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 255 HFGPT-GKLASADIDIYLLEKSRvIFQQPGER--SYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVE------ 325
Cdd:cd14906 155 EFRSSdGKIDGASIETYLLEKSR-ISHRPDNInlSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISsfksqs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 326 ---------NLDDGQELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQ---REEQAEADGTESADKASYLMG 393
Cdd:cd14906 234 snknsnhnnKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 394 VSSADLIKGLLHPRVKVGNEYVV--KGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTL-----------YTSLPRQYF 460
Cdd:cd14906 314 YIESVFKQALLNRNLKAGGRGSVycRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFnqntqsndlagGSNKKNNLF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 461 IGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLIE-KPLGIMSILE 539
Cdd:cd14906 394 IGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 540 EECMFPKATDNSFKAK---MYDNhigkspnflKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQK 616
Cdd:cd14906 473 DECIMPKGSEQSLLEKynkQYHN---------TNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLA 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 617 SANKLLASLYENYVISDSASDpkaggkekrKKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFM 696
Cdd:cd14906 544 SSNFLKKSLFQQQITSTTNTT---------KKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVH 614
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2045330442 697 VLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPS 736
Cdd:cd14906 615 VLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-774 |
1.78e-105 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 354.31 E-value: 1.78e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAIVAALGDTPAKKgqgpatktggtleDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSV-------------EKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML----LVSSNpydyhfcSQGVTTVENLDDGQ--- 331
Cdd:cd01386 148 AGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELhlnqLAESN-------SFGIVPLQKPEDKQkaa 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 332 -ELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGN---MKFKQKQREEQAEadgTESADKASYLMGVSSADLIKGLLHPR 407
Cdd:cd01386 221 aAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFAR---PEWAQRAAYLLGCTLEELSSAIFKHH 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 408 VKVGNEYVVKGQNVEQVNY------------AVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEifdlN 475
Cdd:cd01386 298 LSGGPQQSTTSSGQESPARsssggpkltgveALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQ----N 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 476 ----------SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPL------------- 532
Cdd:cd01386 374 pahsgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPqqalvrsdlrded 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 533 --GIMSILEEECMFPKATDNSFKAKMYdNHIGKSPNFLKPRPDKKRKYEAHFELVHYAGV--VPYNIIGWLDKNK-DPLN 607
Cdd:cd01386 454 rrGLLWLLDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSA 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 608 ETVVACFQKSANKLLASlyenyvisdsasdpkaggkekRKKAASFQTvsqlhKENLNKLMTNLRSTQPHFVRCIIPN--- 684
Cdd:cd01386 533 QNATQLLQESQKETAAV---------------------KRKSPCLQI-----KFQVDALIDTLRRTGLHFVHCLLPQhna 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 685 ---ETKTPGIIDPFMVLH------QLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPS----AIPDDKFVDSRKAAE 751
Cdd:cd01386 587 gkdERSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPltkkLGLNSEVADERKAVE 666
|
730 740
....*....|....*....|...
gi 2045330442 752 KLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd01386 667 ELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-774 |
1.48e-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: 318.11 E-value: 1.48e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYtapvVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFAivaalgdtpakkgqgPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL---------------SGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPyDYHFCSQGVTTVENLDDGQE---LMA 335
Cdd:cd14937 142 YQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDfgnLMI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 336 TDRAMDilgfLPDEKYGCYKIVGAIMHFGNMKFKQ-----KQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKV 410
Cdd:cd14937 221 SFDKMN----MHDMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 411 GNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQ 490
Cdd:cd14937 297 ANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIH 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 491 QFFNHHMFILEQEEYKREGIEWTFIDFGLDlQACIDLIEKPLGIMSILEEECMFPKATDNSFkAKMYDNHIGKSPNFlkp 570
Cdd:cd14937 377 SIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKY--- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 571 rPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDSASdpkaggkekRKKAA 650
Cdd:cd14937 452 -ASTKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLG---------RKNLI 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 651 SFQtvsqlHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRIcRKGFPNRILYAEFKQRY 730
Cdd:cd14937 522 TFK-----YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2045330442 731 RILNPSAIPDDKFVDSRKAAEKLLSSLDIDhnQYRFGHTKVFFK 774
Cdd:cd14937 596 EYLDYSTSKDSSLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-774 |
1.65e-92 |
|
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: 315.60 E-value: 1.65e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAY---KGKRRSEAPPHIYSIADNAYNDMLRNRENQSML 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 176 ITGESGAGKTVNTKRVIQYFAivaalgdtpakkgqGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 255
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLT--------------CRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 256 FGPTGK-LASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQG----VTTVENLDDG 330
Cdd:cd14878 147 FCERKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQTmredVSTAERSLNR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 331 QELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKV 410
Cdd:cd14878 226 EKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 411 GNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTL-----YTSLPrQYFIGVLDIAGFEIFDLNSFEQLCINFT 485
Cdd:cd14878 306 KGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdeQKSMQ-TLDIGILDIFGFEEFQKNEFEQLCVNMT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 486 NEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGLDLQACID-LIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGKS 564
Cdd:cd14878 385 NEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESSN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 565 PNFL-KPRPDKK-----RKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISdsasdp 638
Cdd:cd14878 465 TNAVySPMKDGNgnvalKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLVT------ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 639 kaggkekrkkaasfqTVSQLHKeNLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFP 718
Cdd:cd14878 539 ---------------IASQLRK-SLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYP 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2045330442 719 NRILYAEFKQRYRILNPSAIPDDKfvdSRKAAEKL-LSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14878 603 VRLSFSDFLSRYKPLADTLLGEKK---KQSAEERCrLVLQQCKLQGWQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-737 |
6.51e-92 |
|
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: 311.45 E-value: 6.51e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKwlPVYTAPVVAAYKgKRRSEAPPHIYSIADNAYNDMLRNrENQSMLITGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 180 SGAGKTVNTKRVIQYFAivaalgdtpakkgqgPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgpT 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLV---------------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKpelldmLLVSSNPYDYHFCSQGVTTVENLDdgQELMATDRA 339
Cdd:cd14898 141 GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESIVQLS--EKYKMTCSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 340 MDILGFLPDEKYGcyKIVGAIMHFGNMKFKQkqrEEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14898 213 MKSLGIANFKSIE--DCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 420 NVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQyfIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14898 288 TLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 500 LEQEEYKREGIEWTFIDFgLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKM--YDNHigkspnFLKPRPDKKRK 577
Cdd:cd14898 366 AKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNG------FINTKARDKIK 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 578 yeahfeLVHYAGVVPYNIIGWLDKNKDPLNetvvacfqksankllASLYENYVISDSASdpkaggkeKRKKAASFqtvsq 657
Cdd:cd14898 439 ------VSHYAGDVEYDLRDFLDKNREKGQ---------------LLIFKNLLINDEGS--------KEDLVKYF----- 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 658 lhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPSA 737
Cdd:cd14898 485 --KDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-774 |
2.56e-87 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 302.72 E-value: 2.56e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSA--------WMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 171 NQSMLITGESGAGKTVNTKRVIQYFAIVAALgdtpaKKGQgpatkTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGK 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDR-----RHGA-----DSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 251 FIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI-MSQKKPELLDMLLVSSNPYDYhfcsqgvttvenldd 329
Cdd:cd14887 151 MLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALcNAAVAAATQKSSAGEGDPEST--------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 330 gqELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGT--------ESADKASYLMGVSS----- 396
Cdd:cd14887 216 --DLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvgceETAADRSHSSEVKClssgl 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 397 ---ADLIKGLLHPRVKVGNEYVVKGQN-------------------VEQVNYAVGALAKATYDRMFKWLVGRINRTLYTS 454
Cdd:cd14887 294 kvtEASRKHLKTVARLLGLPPGVEGEEmlrlalvsrsvretrsffdLDGAAAARDAACKNLYSRAFDAVVARINAGLQRS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 455 LPRQY--------------FIGVLDIAGFEIF---DLNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREG--IEWTFI 515
Cdd:cd14887 374 AKPSEsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQDCS 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 516 DFGLDLQACIDLIEKP------------------------LGIMSILEEE-CMFPKATDNSFKA----KMYDNHIGKSPN 566
Cdd:cd14887 454 AFPFSFPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSdlfyEKLNKNIINSAK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 567 FLKPRPDKKRKyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVvacfqksaNKLLASLyeNYVISDSASDPKAGgkeKR 646
Cdd:cd14887 534 YKNITPALSRE-NLEFTVSHFACDVTYDARDFCRANREATSDEL--------ERLFLAC--STYTRLVGSKKNSG---VR 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 647 KKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEF 726
Cdd:cd14887 600 AISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVEL 679
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 2045330442 727 KQRYRILNPSAIpdDKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14887 680 WRRYETKLPMAL--REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-773 |
4.67e-74 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 261.33 E-value: 4.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 96 LNEASVLYNLRRRYSAWMIYTY---SGLfcVTVNPYKWLPVYTAPVVAAYK-------GKRRSEAPPHIYSIADNAYNDM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 166 LRNRENQSMLITGESGAGKTVNTKRVIQyfaivaALGD--TPAKKGqgpaTKtggtLEDQIIEANPAMEAFGNAKTLRND 243
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLR------QLLRlsSHSKKG----TK----LSSQISAAEFVLDSFGNAKTLTNP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 244 NSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYDYHFCSQGVT 322
Cdd:cd14879 145 NASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLgLDDPSDYALLASYGCHP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 323 TVENL--DDG---QELMAtdrAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQ--REEQAEADGTESADKASYLMGVS 395
Cdd:cd14879 225 LPLGPgsDDAegfQELKT---ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 396 SADLiKGLLHPRVKvgneYVVKgqnvEQVNY---AVGA------LAKATYDRMFKWLVGRINRTLytSLPRQY---FIGV 463
Cdd:cd14879 302 PEDL-ETSLTYKTK----LVRK----ELCTVfldPEGAaaqrdeLARTLYSLLFAWVVETINQKL--CAPEDDfatFISL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 464 LDIAGFEIFD---LNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFgLDLQACIDLI-EKPLGIMSILE 539
Cdd:cd14879 371 LDFPGFQNRSstgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 540 EEC-MFPKATDNSFKAKMYDNHIGKSPnFLKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAcfqksa 618
Cdd:cd14879 450 DQTrRMPKKTDEQMLEALRKRFGNHSS-FIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVN------ 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 619 nkLLASlyenyvisdsasdpkaggkekrkkaasfqtVSQLhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVL 698
Cdd:cd14879 523 --LLRG------------------------------ATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVK 569
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2045330442 699 HQLRCNGVLEGIRICRKGFPNRILYAEFKQRYrilnpsaIPDDKFVDSRKAAEKLLSSLDIDHNQYRFGHTKVFF 773
Cdd:cd14879 570 AQIRSLGLPELAARLRVEYVVSLEHAEFCERY-------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-725 |
4.54e-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: 250.59 E-value: 4.54e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEA-------PPHIYSIADNAYNDMLRNRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 171 NQSMLITGESGAGKTVNTKRVIQYFAIVaalgdtpakkgQGPATKTggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGK 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI-----------QTDSQMT--ERIDKLIYINNILESMSNATTIKNNNSSRCGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 251 FIRIHF---------GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGV 321
Cdd:cd14884 148 INLLIFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 322 ------------TTVENLDDGQELMATDRA--MDILGFLPDEKYGCYKI------VGAIMHFGNMKFKQkqreeqaeadg 381
Cdd:cd14884 228 shqkrsvkgtlrLGSDSLDPSEEEKAKDEKnfVALLHGLHYIKYDERQIneffdiIAGILHLGNRAYKA----------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 382 tesadkASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQ--- 458
Cdd:cd14884 297 ------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDesd 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 459 ---------YFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDF--GLDLQACIDL 527
Cdd:cd14884 371 nediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVApsYSDTLIFIAK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 528 IEKPLGIMSILeEECMFPKATDNSFK-----AKMY----DNHIGKSPNFLKPRPDKKRKYEAH-FELVHYAGVVPYNIIG 597
Cdd:cd14884 451 IFRRLDDITKL-KNQGQKKTDDHFFRyllnnERQQqlegKVSYGFVLNHDADGTAKKQNIKKNiFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 598 WLDKNKDPLNETVVACFQKSANKLLAslyENYVisdsasdpkaggkekRKKAASFQTVSQLHKENLNKLMTNLRSTQPHF 677
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLR---EANN---------------GGNKGNFLSVSKKYIKELDNLFTQLQSTDMYY 591
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2045330442 678 VRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAE 725
Cdd:cd14884 592 IRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-773 |
6.43e-70 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 248.49 E-value: 6.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAaykgkRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVGNPLTLTST-----RSSPLAPQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 180 SGAGKTVNTKRVI-QYFAIVaalgdtpakkGQGPATKTGGTLEdqiiEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 258
Cdd:cd14881 77 SGSGKTYASMLLLrQLFDVA----------GGGPETDAFKHLA----AAFTVLRSLGSAKTATNSESSRIGHFIEVQV-T 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYDYHFCSQGVTTVENLDDGQELMATD 337
Cdd:cd14881 142 DGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLhLDGYSPANLRYLSHGDTRQNEAEDAARFQAWK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 338 RAMDILG--FLpdekyGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASyLMGVSSADLIKGLlHPRVKVGNEYV 415
Cdd:cd14881 222 ACLGILGipFL-----DVVRVLAAVLLLGNVQFIDGGGLEVDVKGETELKSVAA-LLGVSGAALFRGL-TTRTHNARGQL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 416 VKGQN-VEQVNYAVGALAKATYDRMFKWLVGRINrtlytSLPRQY----------FIGVLDIAGFEIFDLNSFEQLCINF 484
Cdd:cd14881 295 VKSVCdANMSNMTRDALAKALYCRTVATIVRRAN-----SLKRLGstlgthatdgFIGILDMFGFEDPKPSQLEHLCINL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 485 TNEKLQQFFNHHMFILEQEEYKREGIEwTFIDFG-LDLQACIDLIEK-PLGIMSILEEECMfPKATDNSFKAKMYDNHIG 562
Cdd:cd14881 370 CAETMQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQ 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 563 kSPNFLKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLlaslyenyvisdsasdpkagg 642
Cdd:cd14881 448 -NPRLFEAKPQDDRM----FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF--------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 643 kekrkkaaSFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRIL 722
Cdd:cd14881 502 --------GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMR 573
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 2045330442 723 YAEFKQRYRILNPSAIP---DDKFVDSRKAAEKLLSSLDIDHN-----QYRFGHTKVFF 773
Cdd:cd14881 574 FKAFNARYRLLAPFRLLrrvEEKALEDCALILQFLEAQPPSKLssvstSWALGKRHIFL 632
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-738 |
2.95e-66 |
|
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: 237.85 E-value: 2.95e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 99 ASVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYkgkrrseappHIYSIADNAYNDMLRNRENQSMLI-T 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNAESIVfG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 178 GESGAGKTVNTKRVIQYfaivaaLGDTPAKKgqgPATKTGGTLEDQIieanpamEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKY------LTSQPKSK---VTTKHSSAIESVF-------KSFGCAKTLKNDEATRFGCSIDLLYK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNpYDYHFCSQGVTTVENLDDGQELMATD 337
Cdd:cd14874 135 RNVLTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL-QKFFYINQGNSTENIQSDVNHFKHLE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 338 RAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQR---EEQAEADGTESADK-ASYLMGVSSADLIKGLLhPRVKVGNE 413
Cdd:cd14874 214 DALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnvEQDVVEIGNMSEVKwVAFLLEVDFDQLVNFLL-PKSEDGTT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 414 YvvkgqnveQVNYAVG---ALAKATYDRMFKWLVGRINRTLYTSLpRQYFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQ 490
Cdd:cd14874 293 I--------DLNAALDnrdSFAMLIYEELFKWVLNRIGLHLKCPL-HTGVISILDHYGFEKYNNNGVEEFLINSVNERIE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 491 QFFNHHMFILEQEEYKREGIEwtfIDFglDLQACID-------LIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHIGK 563
Cdd:cd14874 364 NLFVKHSFHDQLVDYAKDGIS---VDY--KVPNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDR 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 564 SpNFLKPRpdKKRKYEahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYviSDSASDpkaggk 643
Cdd:cd14874 439 S-SYGKAR--NKERLE--FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY--SSNTSD------ 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 644 ekrkkaaSFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILY 723
Cdd:cd14874 506 -------MIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISK 578
|
650
....*....|....*
gi 2045330442 724 AEFKQRYRILNPSAI 738
Cdd:cd14874 579 TTFARQYRCLLPGDI 593
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-774 |
5.85e-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: 231.17 E-value: 5.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 180 SGAGKTVNTKRVIQYFAIVaalgdtpakkGQGPATKTGgtledQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYL----------GDGNRGATG-----RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGST 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS--QKKPELLDMLLVSSNPYDYHFCSQGVTTV----------ENL 327
Cdd:cd14882 147 GKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEVPPSklkyrrddpeGNV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 328 DDGQELMATDRAMDilgFLPDEKYGCYKIVGAIMHFGNMKFKQKQREeqAEADGTESADKASYLMGVSSADLIKGLLHPR 407
Cdd:cd14882 227 ERYKEFEEILKDLD---FNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 408 VKVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLytSLPR-----QYFIGVLDIAGFEIFDLNSFEQLCI 482
Cdd:cd14882 302 LIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKM--SFPRavfgdKYSISIHDMFGFECFHRNRLEQLMV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 483 NFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPLGIMSILEE---ECMFPKATDNSFKAKmydn 559
Cdd:cd14882 380 NTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDasrSCQDQNYIMDRIKEK---- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 560 higKSPnFLKPrpdkkrkYEAH-FELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVIsdsasdp 638
Cdd:cd14882 456 ---HSQ-FVKK-------HSAHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQV------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 639 kaggKEKRKKAASFQTVSQlhkENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFP 718
Cdd:cd14882 518 ----RNMRTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFS 590
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 2045330442 719 NRILYAEFKQRYRILnpsAIPDDKFVDSRKAAEKLLsSLDIDHNQYRFGHTKVFFK 774
Cdd:cd14882 591 YRIPFQEFLRRYQFL---AFDFDETVEMTKDNCRLL-LIRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-773 |
1.34e-63 |
|
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: 232.55 E-value: 1.34e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 102 LYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRR----------SEAPPHIYSIADNAYNDMLRNREN 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 172 QSMLITGESGAGKTVNTKRVIQYFAIVAAlGDTPAKKGQGpATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKF 251
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGD-ETEPRPDSEG-ASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 252 IRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS--QKKPELLDMLLVSSNPYDYHFCSQGVTTVENLD- 328
Cdd:cd14893 162 ISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAgvQHDPTLRDSLEMNKCVNEFVMLKQADPLATNFAl 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 329 ---DGQELMATDRAMDIlgfLPDEKYGCYKIVGAIMHFGNMKF--KQKQREEQAEADGTESADKAS-YLMGVSSADLIKG 402
Cdd:cd14893 242 darDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFvpDPEGGKSVGGANSTTVSDAQScALKDPAQILLAAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 403 LL--HPRV------------KVGNEYV--VKGQNVEQVNYAVGALAKATYDRMFKWLVGRINRTLYTSLPR--------- 457
Cdd:cd14893 319 LLevEPVVldnyfrtrqffsKDGNKTVssLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksnivin 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 458 QYFIGVLDIAGFEIFD--LNSFEQLCINFTNEKLQQFFNHHMF-----ILEQEEYKREG--IEWTFIDFGLDLQACIDLI 528
Cdd:cd14893 399 SQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLainfsFLEDESQQVENrlTVNSNVDITSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 529 E-KPLGIMSILEEECMFPKATDNSFKAKMY--DNHIG--KSPN----FLKPRPDKKRKYEAHFELVHYAGVVPYNIIGWL 599
Cdd:cd14893 479 EdKPFGIFDLLTENCKVRLPNDEDFVNKLFsgNEAVGglSRPNmgadTTNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 600 DKNKDPLNETVVACFQKSANKLLASLYENYVISDSASDPKAGGKEKRKKAASFQTVSQLHKENLN--------------K 665
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 666 LMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRilnpsaipddKFVD 745
Cdd:cd14893 639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK----------NVCG 708
|
730 740 750
....*....|....*....|....*....|..
gi 2045330442 746 SRKAAEKLLSSLD----IDHNQYRFGHTKVFF 773
Cdd:cd14893 709 HRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
105-726 |
1.54e-59 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 218.81 E-value: 1.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 105 LRRRYSAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRrsEAPPHIYSIADNAYNDMLRNRENQSMLITGESGAG 183
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 184 KTVNTKRVIQYFAIVaalgDTPAKKgqgpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLA 263
Cdd:cd14905 85 KSENTKIIIQYLLTT----DLSRSK----------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 264 SADIDIYLLEKSRVIFQQPGERSYHIYYQIM---SQKKPELLDMLLVSSnpydYHFCSQGVT-TVENLDDGQELmatDR- 338
Cdd:cd14905 151 GAKLYSYFLDENRVTYQNKGERNFHIFYQFLkgiTDEEKAAYQLGDINS----YHYLNQGGSiSVESIDDNRVF---DRl 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 339 AMDILGF-LPDEKYG-CYKIVGAIMHFGNMKFKQKQreEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVv 416
Cdd:cd14905 224 KMSFVFFdFPSEKIDlIFKTLSFIIILGNVTFFQKN--GKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAV- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 417 kgQNVEqvnyavgALAKATYDRMFKWLVGRINRTLYtslPRQY--FIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFN 494
Cdd:cd14905 301 --ENRD-------SLARSLYSALFHWIIDFLNSKLK---PTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 495 HHMFILEQEEYKREGIEW-TFIDFGlDLQACIDLIEKplgIMSILEEECMFPKATDNSFKAKMyDNHIGKSPNFLKpRPD 573
Cdd:cd14905 369 QTVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL-QNFLSRHHLFGK-KPN 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 574 KkrkyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSANKLLASLYENYVISDSASDPK----AGGKEKRKKA 649
Cdd:cd14905 443 K-------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSRDGVFNINATVAELNqmfdAKNTAKKSPL 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 650 ASFQTVSQLHKENLNKL--------------------------MTNLRSTQP---------HFVRCIIPNETKTPGIIDP 694
Cdd:cd14905 516 SIVKVLLSCGSNNPNNVnnpnnnsgggggggnsgggsgsggstYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDV 595
|
650 660 670
....*....|....*....|....*....|....*.
gi 2045330442 695 FMVLHQLRCNGVLEGIRICRKGFP----NRILYAEF 726
Cdd:cd14905 596 KSVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-254 |
5.72e-55 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 189.48 E-value: 5.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 121 FCVTVNPYKWLPVYTAPVV-AAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAIVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2045330442 200 ALGDTPAK-KGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 254
Cdd:cd01363 81 FNGINKGEtEGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-772 |
6.70e-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: 160.00 E-value: 6.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 100 SVLYNLRRRYSAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSE-APPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 179 ESGAGKTVNTKRVIQYFA---------IVAALGDTPAKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFG 249
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAyqvkgsrrlPTNLNDQEEDNIHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 250 KFIRIHFgPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQGVTTVENLDD 329
Cdd:cd14938 162 KFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLK-NIENYSMLNNEKGFEKFSDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 330 GQELMATDRAMDILGFLPDEKYGCYKIVGAIMHFGN-------------MKFKQKQRE----------EQAEADGTESAD 386
Cdd:cd14938 240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDENV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 387 K----ASYLMGVSSADLIKGLLHPRVkVGNEYVVKGQNVEQVNYAVGALAKATYDRMFKWLVGRINrTLYTSLPR----Q 458
Cdd:cd14938 320 KnlllACKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKIN-EKCTQLQNininT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 459 YFIGVLDIAGFEIFDLNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWTFIDFGLDLQACIDLIEKPL--GIMS 536
Cdd:cd14938 398 NYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 537 ILEEECMfPKATDNSFKAKMYDNHIGKSPNFLKPRPDKKRKyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQK 616
Cdd:cd14938 478 LLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNK--KTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 617 SANKLLASLYENYVISDSA---------SDPKAGGKEKRKKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETK 687
Cdd:cd14938 555 SENEYMRQFCMFYNYDNSGniveekrrySIQSALKLFKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 688 TP-GIIDPFMVLHQLRCNGVLEGIRICRKGFPNRILYAEFKQRYRILNPsaipddkfvDSRKAAEKLLSSLDIDHNQYRF 766
Cdd:cd14938 635 RElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMI 705
|
....*.
gi 2045330442 767 GHTKVF 772
Cdd:cd14938 706 GNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1169-1916 |
2.58e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 128.25 E-value: 2.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1169 IEINKKRETDFLKLRRDLEEAmlhhEATTAALRKKhadsvaELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSK 1248
Cdd:TIGR02168 205 LERQAEKAERYKELKAELREL----ELALLVLRLE------ELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1249 GKATSEKMCRLYEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLE 1328
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1329 EENKAKSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSKANAEVAQWRTKYEtDAIQRTEELEEAKKKLVTRLQEA 1408
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE-RLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1409 EesVEASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQKESRGLST- 1487
Cdd:TIGR02168 434 E--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAl 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1488 ---------------ELFKLKNSYEETLD-----HLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMK-KGLDMEKS 1546
Cdd:TIGR02168 512 lknqsglsgilgvlsELISVDEGYEAAIEaalggRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKgTEIQGNDR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1547 DIQAALEEVEGTLEHEESKTLRIQLELNQIKADV-----------DRKLAEKDEEI-----DNLRRSHQRSMESMQTTLD 1610
Cdd:TIGR02168 592 EILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvddldnaleLAKKLRPGYRIvtldgDLVRPGGVITGGSAKTNSS 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1611 AEAKSRN--EAVRLRKKMECDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNL 1688
Cdd:TIGR02168 672 ILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1689 LSSEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDD---AVQECRNAEEKAKK 1765
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneEAANLRERLESLER 831
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1766 AITDAAMMAEELKKE-QDTSSHLERMKKNMEqtvkDLQMRLDEAEqIALKGGKKQVQKLEARVKELENELESEQRKSQEY 1844
Cdd:TIGR02168 832 RIAATERRLEDLEEQiEELSEDIESLAAEIE----ELEELIEELE-SELEALLNERASLEEALALLRSELEELSEELREL 906
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2045330442 1845 QKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKS-YKRQAEEAEEQANSNLTKYRKLQHELDDAEE 1916
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1180-1929 |
1.69e-27 |
|
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: 122.09 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1180 LKLRRDLEEAMLHHEATTAALrKKHADSVAELSEQIDSLQRVKQKLEKERseakmevdDLASTVEQLSKgkatsekmcRL 1259
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERYK--------ELKAELRELEL---------AL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1260 YEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELkkqleeeNKAKSALAH 1339
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL-------ANEISRLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1340 SLQSSRHDCDLLREQYDEEQEAKAELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKK------LVTRLQEAEESVE 1413
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELeaeleeLESRLEELEEQLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1414 ASNAKCSSLEKTKHRLQTEIEDLVIDLERanaaaaaLDKKQRNFDKVLAEWKQKYEEcqSELESSQKESRGLSTELFKLK 1493
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLER-------LEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1494 NSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMK----------KGLDMEKSDI--------------- 1548
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQenlegfsegvKALLKNQSGLsgilgvlselisvde 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1549 --QAALEEV-EGTLEHEESKTLRIQLELNQIKADVDRKLA-------EKDEEIDNLRRSHQRSMESMQTTLDAEAKSrne 1618
Cdd:TIGR02168 534 gyEAAIEAAlGGRLQAVVVENLNAAKKAIAFLKQNELGRVtflpldsIKGTEIQGNDREILKNIEGFLGVAKDLVKF--- 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1619 AVRLRKKMECDLNEMEV--QLNHANRQASESQKLLRNLqvqIKDIQLELDDTVHQNEELKEQMALTERRNNL--LSSEVE 1694
Cdd:TIGR02168 611 DPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGYRIV---TLDGDLVRPGGVITGGSAKTNSSILERRREIeeLEEKIE 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1695 ELRALLEQNDRARKLAEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMA 1774
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1775 EELKKEQDTSSHLERMKKNMEQTVKDLQmrldeaeqialkggkKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERR 1854
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLK---------------EELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2045330442 1855 IKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQVNKLR 1929
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1268-1929 |
2.01e-25 |
|
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: 115.54 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1268 KAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNsltqnveelkKQLEEENKAKSALAHSLQSSRHD 1347
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE----------LKAELRELELALLVLRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1348 CDLLREQYDEEQEAKAELQRALSKANAEVaqwrtkyetdaiqrtEELEEAKKKLVTRLQEAEESVEASNAKCSSLEKTKH 1427
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKL---------------EELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1428 RLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIK 1507
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1508 RENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQLE--------LNQIKAD 1579
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelqeelerLEEALEE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1580 VDRKLAEKDEEIDNLRRSHQR------SMESMQTTLDAEAKSRNEAV-----------RLRKKMECD------------- 1629
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQlqarldSLERLQENLEGFSEGVKALLknqsglsgilgVLSELISVDegyeaaieaalgg 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1630 -LNEMEVQLNHANRQASESQK----------------------LLRNLQVQIKDIQLELDDTVHQNEEL----------- 1675
Cdd:TIGR02168 546 rLQAVVVENLNAAKKAIAFLKqnelgrvtflpldsikgteiqgNDREILKNIEGFLGVAKDLVKFDPKLrkalsyllggv 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1676 -----------------------------------------KEQMALTERRNNL--LSSEVEELRALLEQNDRARKLAEH 1712
Cdd:TIGR02168 626 lvvddldnalelakklrpgyrivtldgdlvrpggvitggsaKTNSSILERRREIeeLEEKIEELEEKIAELEKALAELRK 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1713 ELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLERMKK 1792
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1793 NMEQTVKDLQMRLDEAEQiALKGGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARL 1872
Cdd:TIGR02168 786 ELEAQIEQLKEELKALRE-ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 2045330442 1873 QDLIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQVNKLR 1929
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
925-1769 |
1.16e-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: 112.84 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 925 AKVKELMERLED---EEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHatENKVKNLIEEMAALDETILKLT 1001
Cdd:TIGR02168 182 ERTRENLDRLEDilnELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEEL--REELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1002 KEKKALTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKlslesvmDLENDK 1081
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE-------ELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1082 QQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARTeeleeeleadRASRAKVEKQRGDVARELEELSerleea 1161
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL----------EELEEQLETLRSKVAQLELQIA------ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1162 ggATSAQIEINKKRETDfLKLRRDLEeamlhHEATTAALRKKHADSVAELSEQIDslqrvkqKLEKERSEAKMEVDDLAS 1241
Cdd:TIGR02168 397 --SLNNEIERLEARLER-LEDRRERL-----QQEIEELLKKLEEAELKELQAELE-------ELEEELEELQEELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1242 TVEQLSKGKATSEKMCRLYEDQMNEAKAKVDELQRQLN--ETNTQRARAQAESGE--------VGRKLEERE-------- 1303
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlEGFSEGVKALLKNQSglsgilgvLSELISVDEgyeaaiea 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1304 --------AMVSQLQRAK---NSLTQN----VEELKKQLEEENKAKSALAHSLQSSRHDCDLLREQYDEEQEAKA----- 1363
Cdd:TIGR02168 542 alggrlqaVVVENLNAAKkaiAFLKQNelgrVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyl 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1364 --------ELQRALSKANAEVAQWR-------------------TKYETDAIQRTEELEEAKKKLvtrlQEAEESVEASN 1416
Cdd:TIGR02168 622 lggvlvvdDLDNALELAKKLRPGYRivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKI----EELEEKIAELE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1417 AKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQKESRGLSTELfklknsy 1496
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL------- 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1497 EETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKmkkgldmEKSDIQAALEEVEGTLEHEESKTLRIQLELNqi 1576
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA-------ELTLLNEEAANLRERLESLERRIAATERRLE-- 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1577 kaDVDRKLAEKDEEIDNLRRSH---QRSMESMQTTLDAEAKSRNEAVRLRKKMECDLNEMEVQLNHANRQASESQKLLRN 1653
Cdd:TIGR02168 842 --DLEEQIEELSEDIESLAAEIeelEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1654 LQVQIKDIQLELddtvhqnEELKEQMA-LTERRNNLLSSEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTGLI 1732
Cdd:TIGR02168 920 LREKLAQLELRL-------EGLEVRIDnLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAI 992
|
890 900 910
....*....|....*....|....*....|....*..
gi 2045330442 1733 NQKKKLESDLSTLSNEVDDAVQecrnAEEKAKKAITD 1769
Cdd:TIGR02168 993 EEYEELKERYDFLTAQKEDLTE----AKETLEEAIEE 1025
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
851-1597 |
1.97e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.52 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 851 AATEKELAALKEELAKLKEALEKSEVKRKELEEKQV-------SLIQEKNDLALQLQAEQDNLADAEDRCDLLIKTKIQL 923
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 924 EAKVKELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKE 1003
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1004 KKALTEAHQQTLDDLQAEEDKvntltkakaKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQ 1083
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKK---------LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1084 LEEKLKKKDFE---MNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQRGdvARELEELSERLEE 1160
Cdd:TIGR02168 480 AERELAQLQARldsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALG--GRLQAVVVENLNA 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1161 AGGATSAQIEINKKRETdFLKLRRDLEEAMlhhEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMeVDDLA 1240
Cdd:TIGR02168 558 AKKAIAFLKQNELGRVT-FLPLDSIKGTEI---QGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLV-VDDLD 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1241 STVEQLSK----------------------GKATSEKMCRLYEDQ-MNEAKAKVDELQRQLNETNTQRARAQAEsgevgr 1297
Cdd:TIGR02168 633 NALELAKKlrpgyrivtldgdlvrpggvitGGSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKE------ 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1298 kLEEREAMVSQLQRAKNSLTQnveelkkqleeenkaksalahslQSSRHDCDLLREQydEEQEAKAELQRALSKANAEVA 1377
Cdd:TIGR02168 707 -LEELEEELEQLRKELEELSR-----------------------QISALRKDLARLE--AEVEQLEERIAQLSKELTELE 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1378 QWRTKYETDAIQRTEELEEAKKKLVT---RLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQ 1454
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEEleaQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1455 RNFDKVLAEWKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHEL 1534
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2045330442 1535 EKMKKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQLELnqiKADVDRKLAEKDEEIDNLRRS 1597
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAL---ENKIEDDEEEARRRLKRLENK 980
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
847-1436 |
3.37e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.63 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 847 LLRSAATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLIKTKIQLEAK 926
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 927 VKELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKA 1006
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1007 LTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQLEE 1086
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1087 KLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQR--GDVARELEELSERLEEAGGA 1164
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlaGAVAVLIGVEAAYEAALEAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1165 TSAQIEINKKRETDFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVE 1244
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1245 QLSKGKATSEKMCRLyedqMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELK 1324
Cdd:COG1196 624 GRTLVAARLEAALRR----AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1325 KQLEEENKAKSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLvTR 1404
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI-EA 778
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2045330442 1405 L-----------QEAEESVEASNAKCSSLEKTKHRLQTEIEDL 1436
Cdd:COG1196 779 LgpvnllaieeyEELEERYDFLSEQREDLEEARETLEEAIEEI 821
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1168-1917 |
3.75e-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: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1168 QIEINKKREtdFLKLRRDLEEAmlhhEATTAALRKKHAD-SVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQL 1246
Cdd:TIGR02169 204 RREREKAER--YQALLKEKREY----EGYELLKEKEALErQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1247 SKgkatseKMCRLYEDQMNEAKAKVDELQrqlnetnTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQ 1326
Cdd:TIGR02169 278 NK------KIKDLGEEEQLRVKEKIGELE-------AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1327 LEEENKAKSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRalskanaEVAQWRTKYEtDAIQRTEELEEAKKKLVTRLQ 1406
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-------ELKDYREKLE-KLKREINELKRELDRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1407 EAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQKEsrgLS 1486
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE---LA 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1487 TELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGL---------DMEKSDIQAALEEVEG 1557
Cdd:TIGR02169 494 EAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRlnnvvveddAVAKEAIELLKRRKAG 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1558 TLE-------HEESKTLRIQLELNQIKADVDrkLAEKDEEIDNLRRSHQRS---MESMQT-----------TLDAE---- 1612
Cdd:TIGR02169 574 RATflplnkmRDERRDLSILSEDGVIGFAVD--LVEFDPKYEPAFKYVFGDtlvVEDIEAarrlmgkyrmvTLEGElfek 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1613 ------------------AKSRNEAVRLR---KKMECDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQ 1671
Cdd:TIGR02169 652 sgamtggsraprggilfsRSEPAELQRLRerlEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1672 NEELKEQMALTERRNNLLSSEVEELRALLEQN-----DRARKLAEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLS 1746
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSELKELearieELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIE 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1747 NEVDDavqecrnAEEKAKKAITDAAMMAEELKKEQDTSSHLERMKKNMEQTVKDLQMRLDEAEQialkggkkQVQKLEAR 1826
Cdd:TIGR02169 812 ARLRE-------IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE--------ELEELEAA 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1827 VKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEAEEQAnSNLTKYRK 1906
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP-EEELSLED 955
|
810
....*....|.
gi 2045330442 1907 LQHELDDAEER 1917
Cdd:TIGR02169 956 VQAELQRVEEE 966
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
847-1597 |
2.06e-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: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 847 LLRSAATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLIKTKI-QLEA 925
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIaSLER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 926 KVKELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVE---KEKHATENKVKNLIEEMAA-LDETILKLT 1001
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTeeyAELKEELEDLRAELEEVDKeFAETRDELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1002 KEKKALtEAHQQTLDDLQAEEDKvntLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDK 1081
Cdd:TIGR02169 389 DYREKL-EKLKREINELKRELDR---LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1082 QQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQRGDVARELEELSERLEEA 1161
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVA 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1162 GGATSAQI----EINKKRETDFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEA---KM 1234
Cdd:TIGR02169 545 AGNRLNNVvvedDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVfgdTL 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1235 EVDDLASTVEQLSK------------------GKATSEKMCRL----YEDQMNEAKAKVDELQRQLNETNTQRARAQAES 1292
Cdd:TIGR02169 625 VVEDIEAARRLMGKyrmvtlegelfeksgamtGGSRAPRGGILfsrsEPAELQRLRERLEGLKRELSSLQSELRRIENRL 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1293 GEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKAKSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSKA 1372
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1373 NAEVAQWRTKYETDAIqrtEELEEAKKKLVTRLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDK 1452
Cdd:TIGR02169 785 EARLSHSRIPEIQAEL---SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1453 KQRNFDKVLAEWKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIH 1532
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 1533 ELEKMkKGLDMEKSDIQAALEEVEGTL------------EHEESKTLRIQLELNQIKADVDRK-LAEKDEEIDNLRRS 1597
Cdd:TIGR02169 942 EDEEI-PEEELSLEDVQAELQRVEEEIralepvnmlaiqEYEEVLKRLDELKEKRAKLEEERKaILERIEEYEKKKRE 1018
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1197-1931 |
3.47e-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: 98.22 E-value: 3.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1197 TAALRKKHADSVAELSEQIDSLQRVKQKLEK-ERSEAKME--VDDLASTVEQLSKGKATSEK----MCRLYEDQMNEAKA 1269
Cdd:TIGR02169 151 SPVERRKIIDEIAGVAEFDRKKEKALEELEEvEENIERLDliIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1270 KVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKAKsalAHSLQSSRHDC- 1348
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK---IGELEAEIASLe 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1349 DLLREQYDEEQEAKAELQRA---LSKANAEVAQWRTKYETDAIQR---TEELEEAKKK---LVTRLQEAEESVEASNAKC 1419
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLeaeIDKLLAEIEELEREIEEERKRRdklTEEYAELKEEledLRAELEEVDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1420 SSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQKESRGLSTELfklknsyEET 1499
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL-------EQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1500 LDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGL-----------DMEKSDIQAALEEVEGTLEHEESKTLR 1568
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASeervrggraveEVLKASIQGVHGTVAQLGSVGERYATA 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1569 IQL----ELNQIKADVDRKLAE-----KDEEIDNLRRSHQRSMESMQttLDAEAKSRNEAVrlrkKMECDLNEMEVQLNH 1639
Cdd:TIGR02169 541 IEVaagnRLNNVVVEDDAVAKEaiellKRRKAGRATFLPLNKMRDER--RDLSILSEDGVI----GFAVDLVEFDPKYEP 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1640 ANRQA------SESQKLLRNLQVQIKDIQLELD--------------------DTVHQNEE---LKEQMALTERRNNLLS 1690
Cdd:TIGR02169 615 AFKYVfgdtlvVEDIEAARRLMGKYRMVTLEGElfeksgamtggsraprggilFSRSEPAElqrLRERLEGLKRELSSLQ 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1691 SEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSnevddavQECRNAEEKAKKAITDA 1770
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE-------QEIENVKSELKELEARI 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1771 AMMAEELKKEQDTSSHLERMKKnmEQTVKDLQMRLDEAEqialkggkKQVQKLEARVKELENEL-------ESEQRKSQE 1843
Cdd:TIGR02169 768 EELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLE--------EEVSRIEARLREIEQKLnrltlekEYLEKEIQE 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1844 YQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAEERADMAET 1923
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
....*...
gi 2045330442 1924 QVNKLRVR 1931
Cdd:TIGR02169 918 RLSELKAK 925
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
856-1780 |
1.33e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 96.29 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 856 ELAALKEELAKLKEALEKSEVKRKELEEKQvSLIQEKNDlalQLQAEQDNLADAEdRCDLLIKTKIQLEAKVKelmerle 935
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEELEEVEENIERLD-LIIDEKRQ---QLERLRREREKAE-RYQALLKEKREYEGYEL------- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 936 deeemsanvLAKKRKLEDECSELKKDIDDLEITLAKVEKEkhatenkVKNLIEEMAALDETILKLTKEKKALTEAHQQTL 1015
Cdd:TIGR02169 229 ---------LKEKEALERQKEAIERQLASLEEELEKLTEE-------ISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1016 ddlqaeedkvntltkaKAKLEqqvdDLEGSLEQekkvrmdlervrrkLEGDLKLSLESVMDLENDKQQLEEKLKKKDFEM 1095
Cdd:TIGR02169 293 ----------------KEKIG----ELEAEIAS--------------LERSIAEKERELEDAEERLAKLEAEIDKLLAEI 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1096 NEISSRIEDEQALVNQLHKKIKELQARTEELEEELEA-DRASRAKVEKQRgDVARELEELSERLEEAGGATSAQIEINKK 1174
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvDKEFAETRDELK-DYREKLEKLKREINELKRELDRLQEELQR 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1175 RETDFLKLRRDLEEAMLHHEATTAALRKKhADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSE 1254
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDK-ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1255 KMCRLYEDQMNEAKAKVDELqrqlnetntqRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLeeenkAK 1334
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEVL----------KASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAV-----AK 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1335 SA--LAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSKANAEVAQWRTKYETD---AIQRT---EELEEAKK-----KL 1401
Cdd:TIGR02169 562 EAieLLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAfkyVFGDTlvvEDIEAARRlmgkyRM 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1402 VTRlqeAEESVEASNA------KCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSEL 1475
Cdd:TIGR02169 642 VTL---EGELFEKSGAmtggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI 718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1476 ESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKglDMEKSDIQAALEEV 1555
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN--DLEARLSHSRIPEI 796
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1556 EGTLEHEESKTLRIQLELNQIKADVDRKLAEKD------EEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLRKKMECD 1629
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEylekeiQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1630 LNEMEVQLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQNDRARKL 1709
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV 956
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2045330442 1710 AEhELLEATERVNLLHSQNTGLINQKKKLESDLSTLsnevddavQECRNAEEKAKKAITDAAMMAEELKKE 1780
Cdd:TIGR02169 957 QA-ELQRVEEEIRALEPVNMLAIQEYEEVLKRLDEL--------KEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
984-1916 |
1.69e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 95.89 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 984 KNLIEEMAAldetILKLTKEKKaltEAHQQ---TLDDLQAEEDKVNTLTKAKAKLEQQVDdlegSLEQEKKVRMDLERVR 1060
Cdd:TIGR02168 158 RAIFEEAAG----ISKYKERRK---ETERKlerTRENLDRLEDILNELERQLKSLERQAE----KAERYKELKAELRELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1061 RKLEGDLKLSLESVMD-LENDKQQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARteeleEELEADRASRAK 1139
Cdd:TIGR02168 227 LALLVLRLEELREELEeLQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE-----LYALANEISRLE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1140 VEKQRGDVARELEELSERleeaggATSAQIEINKKR----ETDFLKLRRDLEEAMLHHEATTAALRKKHADsVAELSEQI 1215
Cdd:TIGR02168 302 QQKQILRERLANLERQLE------ELEAQLEELESKldelAEELAELEEKLEELKEELESLEAELEELEAE-LEELESRL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1216 DSLQRVKQKLEKERSEAKMEVDDLASTVEQLskgkatsekmcrlyEDQMNEAKAKVDELQRQLNETNTQRARAQAEsgEV 1295
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERL--------------EARLERLEDRRERLQQEIEELLKKLEEAELK--EL 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1296 GRKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKAKSALAHSLQSSRHDCDLL---REQYDEEQEAKAELQRALSKA 1372
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLerlQENLEGFSEGVKALLKNQSGL 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1373 NAEVAQWRTKYETDaiqrtEELEEAKKK---------LVTRLQEAEESVEA----SNAKCSSLEKTKHR---LQTEIEDL 1436
Cdd:TIGR02168 519 SGILGVLSELISVD-----EGYEAAIEAalggrlqavVVENLNAAKKAIAFlkqnELGRVTFLPLDSIKgteIQGNDREI 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1437 VIDLERANAAAAALDKKQRNFDKVLAEWKQKY---EECQSELESSQKESRG-----LSTELFK-----LKNSYEETLDHL 1503
Cdd:TIGR02168 594 LKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvDDLDNALELAKKLRPGyrivtLDGDLVRpggviTGGSAKTNSSIL 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1504 ETiKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQLELNQIKadvdrk 1583
Cdd:TIGR02168 674 ER-RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE------ 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1584 laekdEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLRKKMEcdlnEMEVQLNHANRQASESQKLLRNLQVQIKDIQL 1663
Cdd:TIGR02168 747 -----ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE----ELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1664 ELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQndrarklAEHELLEATERVNLLHSQNTGLINQKKKLESDLS 1743
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-------LAAEIEELEELIEELESELEALLNERASLEEALA 890
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1744 TLSNEVDDAVQECRNAEEKakkaitdaammaeelkkeqdtsshlermkknmeqtVKDLQMRLDEAeqialkggKKQVQKL 1823
Cdd:TIGR02168 891 LLRSELEELSEELRELESK-----------------------------------RSELRRELEEL--------REKLAQL 927
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1824 EARVKELENELESEQrksqeyQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEAEEQANSNLTK 1903
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQ------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKER 1001
|
970
....*....|...
gi 2045330442 1904 YRKLQHELDDAEE 1916
Cdd:TIGR02168 1002 YDFLTAQKEDLTE 1014
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1170-1927 |
2.87e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 95.59 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1170 EINKKRETDFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSE----QIDSLQRVKQKLEKERSEAKMEVDDLASTVEQ 1245
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEarkaEDAKRVEIARKAEDARKAEEARKAEDAKKAEA 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1246 LSKgkatSEKMCRLYEDQMNEAKAKVDELQRQLNETNTQRAR--AQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEEL 1323
Cdd:PTZ00121 1181 ARK----AEEVRKAEELRKAEDARKAEAARKAEEERKAEEARkaEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRK 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1324 KKQLEEENKAKSALAHSLQSSRHDCDLLREqydEEQEAKAELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVT 1403
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKA---EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1404 RLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLERANAaaaalDKKQRNFDKVLAEWKQKYEECQSELESSQKESR 1483
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE-----AKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1484 GLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDmEKSDIQAALEEVEGTLEHEE 1563
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE-EAKKADEAKKKAEEAKKADE 1487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1564 SKTlriQLELNQIKADVDRKLAEKDEEIDNLRRSHQ--------RSMESMQTTLDAEAKSRNEAVRLRKKMECDLNEMEV 1635
Cdd:PTZ00121 1488 AKK---KAEEAKKKADEAKKAAEAKKKADEAKKAEEakkadeakKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK 1564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1636 QLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQNDRARKLAEHELL 1715
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1716 EATERVNLLHSQNTGLI---NQKKKLESDlstlsnevDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLERMKK 1792
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIkaaEEAKKAEED--------KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1793 NMEQTVKDLQMRLDEAEQIALKGGKKQVQKLEARVKELENELESEQRKSQEYQKvvrKYERRIKELSYQAEEDKKNLARL 1872
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA---EEIRKEKEAVIEEELDEEDEKRR 1793
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 2045330442 1873 QDlidkLQAKVKSYKRQAEEAEEQANSNlTKYRKLQHELDDAE--ERADMAETQVNK 1927
Cdd:PTZ00121 1794 ME----VDKKIKDIFDNFANIIEGGKEG-NLVINDSKEMEDSAikEVADSKNMQLEE 1845
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1331-1919 |
1.21e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.08 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1331 NKAKSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSKANAEVAQWRTKYEtdaiQRTEELEEAKKKLvtrlQEAEE 1410
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELA----ELEAELEELRLEL----EELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1411 SVEASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQKESRGLSTELF 1490
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1491 KLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQ 1570
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1571 LELNQIKadvdRKLAEKDEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLRKKMEcDLNEMEVQLNHANRQASESQKL 1650
Cdd:COG1196 442 EALEEAA----EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL-LLLEAEADYEGFLEGVKAALLL 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1651 LRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQNDRAR-------KLAEHELLEATERVNL 1723
Cdd:COG1196 517 AGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRatflpldKIRARAALAAALARGA 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1724 LHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAIT----------------DAAMMAEELKKEQDTSshL 1787
Cdd:COG1196 597 IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTlagrlrevtlegeggsAGGSLTGGSRRELLAA--L 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1788 ERMKKNMEQTVKDLQMRLDEAEQIALKGGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKK 1867
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1868 NLARLQDlIDKLQAKVKSYKRQAEE-------AEEQANSNLTKYRKLQHELDD-AEERAD 1919
Cdd:COG1196 755 ELPEPPD-LEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDlEEARET 813
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1170-1924 |
7.03e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.97 E-value: 7.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1170 EINKKRETDFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQrVKQKLEKERSEAKMEVDDLASTVEQLSKG 1249
Cdd:PTZ00121 1031 ELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFD-FDAKEDNRADEATEEAFGKAEEAKKTETG 1109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1250 KATSEKMCRLYEDQMNEAKaKVDELQRQLNETNTQRAR--AQAESGEVGRKLEE--REAMVSQLQRAKNSLTQNVEELKK 1325
Cdd:PTZ00121 1110 KAEEARKAEEAKKKAEDAR-KAEEARKAEDARKAEEARkaEDAKRVEIARKAEDarKAEEARKAEDAKKAEAARKAEEVR 1188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1326 QLEEENKAKSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRL 1405
Cdd:PTZ00121 1189 KAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARR 1268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1406 QEAEESVEASNA----KCSSLEKTKHRLQTEIEDLVIDLERANAAAAALD---KKQRNFDKVLAEWKQKYEECQSELESS 1478
Cdd:PTZ00121 1269 QAAIKAEEARKAdelkKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADeakKKAEEAKKKADAAKKKAEEAKKAAEAA 1348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1479 QKESRGLSTELFKLKNSYEETldhlETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEGT 1558
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAA----EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1559 LEHEESKtlriqlelnqiKADVDRKLAEKDEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLRKKMECDLNEMEVQLN 1638
Cdd:PTZ00121 1425 KKAEEKK-----------KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE 1493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1639 HANRQASESQKllrnlqvqikdiQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALlEQNDRARKLAEHELLEAT 1718
Cdd:PTZ00121 1494 EAKKKADEAKK------------AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA-EEKKKADELKKAEELKKA 1560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1719 ERVNLlhsqntglINQKKKLESDLSTLSNEVDDAVQ-ECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLERMKKNMEQT 1797
Cdd:PTZ00121 1561 EEKKK--------AEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1798 VKDLQMRLDEAEQI-ALKGGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKnlarlqdlI 1876
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK--------A 1704
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 2045330442 1877 DKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQ 1924
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1210-1937 |
1.77e-17 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 89.46 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1210 ELSEQIDSLQRVKQKLEKerseAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNEAK-------AKVDELQRQLNETN 1282
Cdd:pfam01576 6 EMQAKEEELQKVKERQQK----AESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEemrarlaARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1283 TqraraqaesgevgrKLEEREAMVSQLQRAKNSLTQNVEElkkqleeenkaksalahslqssrhdcdlLREQYDEEQEAK 1362
Cdd:pfam01576 82 S--------------RLEEEEERSQQLQNEKKKMQQHIQD----------------------------LEEQLDEEEAAR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1363 AELQRALSKANAEVAQWRTKYETDAIQRTEeLEEAKKKLVTRLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLER 1442
Cdd:pfam01576 120 QKLQLEKVTTEAKIKKLEEDILLLEDQNSK-LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKK 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1443 ANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSD 1522
Cdd:pfam01576 199 EEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1523 QISQGSKTIHELEKMKKGLDMEKSDIQAALEE-VEGTLEHEESKTLRIQlELNQIKADVDRKLAEKDEEIDNLRRSHQRS 1601
Cdd:pfam01576 279 DLESERAARNKAEKQRRDLGEELEALKTELEDtLDTTAAQQELRSKREQ-EVTELKKALEEETRSHEAQLQEMRQKHTQA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1602 MESMQTTLDAEAKSRNEAVRLRKKMECDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMAL 1681
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1682 terrnnlLSSEVEELRALLEQNDrarklaehelleatervnllhsqntgliNQKKKLESDLSTLSNEVDDAvQECRNAEE 1761
Cdd:pfam01576 438 -------LQSELESVSSLLNEAE----------------------------GKNIKLSKDVSSLESQLQDT-QELLQEET 481
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1762 KAKKAIT--------DAAMMAEELKKEQDTSSHLERMKKNMEQTVKDLQMRLDEAEQI--ALKGGKKQVQKlearvkELE 1831
Cdd:pfam01576 482 RQKLNLStrlrqledERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTleALEEGKKRLQR------ELE 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1832 NELESEQRKSQEYQKVVRKYERRIKELS------YQAEEDKKNLARLQDLIDKLQAKVKS----YKRQAEEAEEQANSNL 1901
Cdd:pfam01576 556 ALTQQLEEKAAAYDKLEKTKNRLQQELDdllvdlDHQRQLVSNLEKKQKKFDQMLAEEKAisarYAEERDRAEAEAREKE 635
|
730 740 750
....*....|....*....|....*....|....*.
gi 2045330442 1902 TKYRKLQHELDDAEERADMAETQVNKLRVRTRDQVS 1937
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQLRAEMEDLVS 671
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1183-1739 |
2.51e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1183 RRDLEEAMLHHEATTAALRKKHADsVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQ-------LSKGKATSEK 1255
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELELELEEaqaeeyeLLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1256 MCRLYEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKAKS 1335
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1336 ALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSKANAEVAQWRTKyETDAIQRTEELEEAKKKLVTRLQEAEESVEAS 1415
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA-LAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1416 NAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKyeecqsELESSQKESRGLSTELFKLKNS 1495
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA------LLLAGLRGLAGAVAVLIGVEAA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1496 YEETLDHLETIKRENKNLQEEiADLSDQIS------QGSKTIHELEKMKKGLDMEKSDIQAALEE----VEGTLEHEESK 1565
Cdd:COG1196 536 YEAALEAALAAALQNIVVEDD-EVAAAAIEylkaakAGRATFLPLDKIRARAALAAALARGAIGAavdlVASDLREADAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1566 TLRIQLELNQIKADVDRKLAEKD--EEIDNLRRSHQRSMESMQTTLDAEAKSRNE-------AVRLRKKMECDLNEMEVQ 1636
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALRraVTLAGRLREVTLEGEGGSAGGSLTGGSRREllaalleAEAELEELAERLAEEELE 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1637 LNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSE-----------VEELRALLEQNDR 1705
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEealeelpeppdLEELERELERLER 774
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2045330442 1706 ARK-------LAEHELLEATERVNLLHSQNTGLINQKKKLE 1739
Cdd:COG1196 775 EIEalgpvnlLAIEEYEELEERYDFLSEQREDLEEARETLE 815
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
224-714 |
4.51e-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: 87.88 E-value: 4.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 224 IIEANPAMEAFGNAKTLRNDNSSRFGKF--IRIHFGPTG---KLASADIDIYLLEKSRVIFQQ------PGERSYHIYYQ 292
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 293 IMSQ----------KKPELLDMLLVSSNPY----DYH---FCSQGVTTVENLDDGQELMatdRAMDILGFLPDEKYGCYK 355
Cdd:cd14894 329 MVAGvnafpfmrllAKELHLDGIDCSALTYlgrsDHKlagFVSKEDTWKKDVERWQQVI---DGLDELNVSPDEQKTIFK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 356 IVGAIMHFGNMKFKQKQREEQAEADGT---ESADKASYLMGVSSADLIKGLLHPR---VKVGNEYVVKGQNVEQVNYAVG 429
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 430 ALAKATYDRMFKWLVGRINRTLY----------------TSLPRQY-FIGVLDIAGFEIFDLNSFEQLCINFTNEKLqqf 492
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATKmsalstdgnkhqmdsnASAPEAVsLLKIVDVFGFEDLTHNSLDQLCINYLSEKL--- 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 493 fnhhmfileqeeYKRE----GIEWTFIDFGLDLQACIDLI---EKPLGIMSILEEECMFPKATDNS----------FKAK 555
Cdd:cd14894 563 ------------YAREeqviAVAYSSRPHLTARDSEKDVLfiyEHPLGVFASLEELTILHQSENMNaqqeekrnklFVRN 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 556 MYDNHIGKSPNFLKPRPDKKRKYEA-----HFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKS-ANKLLASLYENY 629
Cdd:cd14894 631 IYDRNSSRLPEPPRVLSNAKRHTPVllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSnSSHFCRMLNESS 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 630 VISDSASDPKAGGKEKRKKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIIDPFMVLHQLRCNGVLEG 709
Cdd:cd14894 711 QLGWSPNTNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQ 790
|
....*
gi 2045330442 710 IRICR 714
Cdd:cd14894 791 MEICR 795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1389-1895 |
2.20e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 85.50 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1389 QRTEELEEAKKKLVTRLQEAEESVEASNAKCSSLEKTKhrlqTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKY 1468
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1469 EECQSELESSqKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKgldmEKSDI 1548
Cdd:PRK03918 276 EELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK----KLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1549 QAALEEVEGTLEHEEsKTLRIQLELNQIKADVDRKLAEK-DEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLRKKME 1627
Cdd:PRK03918 351 EKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1628 cDLNEMEVQLNHANRQASESQK--LLRNLQVQIKDIQLELDDTVHQNEELK------EQMALTERRNNLLSSEVEELRAL 1699
Cdd:PRK03918 430 -ELKKAKGKCPVCGRELTEEHRkeLLEEYTAELKRIEKELKEIEEKERKLRkelrelEKVLKKESELIKLKELAEQLKEL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1700 LEQ----NDRARKLAEHELLEATERVNLLHSQNTGL---INQKKKLESDLSTLSNEVDDAVQECRN----AEEKAKKAIT 1768
Cdd:PRK03918 509 EEKlkkyNLEELEKKAEEYEKLKEKLIKLKGEIKSLkkeLEKLEELKKKLAELEKKLDELEEELAEllkeLEELGFESVE 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1769 DAAMMAEELKKEQDTSSHLERMKKNMEQTVKDLQMRLDEAEQIalkggKKQVQKLEARVKELENELESEQRK--SQEYQK 1846
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKA-----FEELAETEKRLEELRKELEELEKKysEEEYEE 663
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2045330442 1847 VVRKYERRIKELSYQAEEdkknLARLQDLIDKLQAKVKSYKRQAEEAEE 1895
Cdd:PRK03918 664 LREEYLELSRELAGLRAE----LEELEKRREEIKKTLEKLKEELEEREK 708
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
848-1523 |
2.32e-16 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 85.61 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 848 LRSAATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADaEDRCDLLIKTKI-QLEAK 926
Cdd:pfam01576 419 ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLrQLEDE 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 927 VKELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKA 1006
Cdd:pfam01576 498 RNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1007 LteahQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLegsLEQEKKVRMDLERVRRKLEGDLK------LSLESVMDLEND 1080
Cdd:pfam01576 578 L----QQELDDLLVDLDHQRQLVSNLEKKQKKFDQM---LAEEKAISARYAEERDRAEAEAReketraLSLARALEEALE 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1081 -KQQLEEKLKKKDFEMNEISSRIEDEQALVNQLH--KKIKELQARTEELEEELEADRASRAKVEKQRGDVARELEELSER 1157
Cdd:pfam01576 651 aKEELERTNKQLRAEMEDLVSSKDDVGKNVHELErsKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFE 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1158 LEEaggatSAQIEINKKRETDFLKLRRDLeEAMLHHEattaalRKKHADSVAelseqidslqrVKQKLEkerseakMEVD 1237
Cdd:pfam01576 731 RDL-----QARDEQGEEKRRQLVKQVREL-EAELEDE------RKQRAQAVA-----------AKKKLE-------LDLK 780
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1238 DLASTVEQLSKGKATSEKmcrlyedQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQ------- 1310
Cdd:pfam01576 781 ELEAQIDAANKGREEAVK-------QLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQedlaase 853
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1311 RAKNSLTQNVEELKKQLEEENKAKSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSKANAEVAQWRTKY--ETDAI 1388
Cdd:pfam01576 854 RARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELaaERSTS 933
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1389 QRTE----ELEEAKKKLVTRLQEAEESVEasnakcSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEW 1464
Cdd:pfam01576 934 QKSEsarqQLERQNKELKAKLQEMEGTVK------SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEV 1007
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 2045330442 1465 KQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQ 1523
Cdd:pfam01576 1008 LLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATES 1066
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1001-1869 |
4.56e-16 |
|
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: 84.64 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1001 TKEKKALTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVddLEGSLEQEKKVRMDLERVRRKLEGDLKLsLESVMDLEND 1080
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLK--EQAKKALEYYQLKEKLELEEEYLLYLDY-LKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1081 KQQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQRGDVARELEELSERLEE 1160
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1161 AGGATSAQIEINKKRETDFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLA 1240
Cdd:pfam02463 322 EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1241 STVEQLSKGKATSEKMCRLYEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNV 1320
Cdd:pfam02463 402 EEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1321 EELKKQLEEENKAKSALAHSLQSSRHDCDLLREQYDEEQE----AKAELQRALSKANAEVAQWRTKYETDAIQRTEELEE 1396
Cdd:pfam02463 482 LQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGgriiSAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1397 AKKKLVTRLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAAldkkqRNFDKVLAEWKQKYEECQSELE 1476
Cdd:pfam02463 562 ERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLE-----ADEDDKRAKVVEGILKDTELTK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1477 SSQKESRGLSTELF-----KLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAA 1551
Cdd:pfam02463 637 LKESAKAKESGLRKgvsleEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLK 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1552 LEEvegtlehEESKTLRIQLELNQIKADVDRKLAEKDEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLRKkmecDLN 1631
Cdd:pfam02463 717 LEA-------EELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREK----TEK 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1632 EMEVQLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQNDRARKLAE 1711
Cdd:pfam02463 786 LKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITK 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1712 HELLeateRVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLERMK 1791
Cdd:pfam02463 866 EELL----QELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELL 941
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 1792 KNMEQTVKDLQMRLDEAEQIALKGGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNL 1869
Cdd:pfam02463 942 LEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1630-1931 |
1.61e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1630 LNEMEVQLNHANRQASESQKLlRNLQVQIKDIQLELddTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQNDRARKL 1709
Cdd:COG1196 195 LGELERQLEPLERQAEKAERY-RELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1710 AEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLER 1789
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1790 MKKNMEQTVKDLQMRLDEAEQIALKGGKKQVQKLEARVkELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNL 1869
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL-EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2045330442 1870 ARLQDLIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQVNKLRVR 1931
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1428-1939 |
3.35e-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: 82.09 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1428 RLQTEIEDLVIDLERANAAAAALDKKQRNF-DKVLAEWKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETI 1506
Cdd:pfam15921 78 RVLEEYSHQVKDLQRRLNESNELHEKQKFYlRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1507 KrenkNLQEeiadlsDQISQGSKTIHELEKM---KKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQLElnQIKADVDRK 1583
Cdd:pfam15921 158 K----CLKE------DMLEDSNTQIEQLRKMmlsHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFR--SLGSAISKI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1584 LAEKDEEIDNLRrSHQRSMESMQTTLDAEAKSRNEAV--RLRKKMECDLNEMEVQLNHANRQASESQKLLRNLQVQIKDI 1661
Cdd:pfam15921 226 LRELDTEISYLK-GRIFPVEDQLEALKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1662 QlelddtvhqnEELKEQMALTERRNNLLSSEVEELRALLEQndrARKLAEHELLEATERVNLLHSQntglinqkkklesd 1741
Cdd:pfam15921 305 Q----------EQARNQNSMYMRQLSDLESTVSQLRSELRE---AKRMYEDKIEELEKQLVLANSE-------------- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1742 LSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLERMKKNMEQTVKDLQMRLDEAEQialkggkkQVQ 1821
Cdd:pfam15921 358 LTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM--------EVQ 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1822 KLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKR----------QAE 1891
Cdd:pfam15921 430 RLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERtvsdltaslqEKE 509
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2045330442 1892 EAEEQANSNLTKYR--------KLQHELDDAEE-RADMAETQVNKLRVRTRDQVSKV 1939
Cdd:pfam15921 510 RAIEATNAEITKLRsrvdlklqELQHLKNEGDHlRNVQTECEALKLQMAEKDKVIEI 566
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1260-1912 |
7.87e-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: 80.55 E-value: 7.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1260 YEDQMNEAKAKVDELQRQLNETN----TQRARAQAESGEVGRKLE----EREAMVSQLQRAKNSLTQNVEELKKQLEEEN 1331
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNelheKQKFYLRQSVIDLQTKLQemqmERDAMADIRRRESQSQEDLRNQLQNTVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1332 KAKSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALskANAEVAQWRTKYETDAIQRT-------------EELEEAK 1398
Cdd:pfam15921 156 AAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL--VDFEEASGKKIYEHDSMSTMhfrslgsaiskilRELDTEI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1399 KKLVTRLQEAEESVEASNAKCSS-LEKTKHRLQTEIEDLVIDLEranAAAAALDKKQrnfdkvlAEWKQKYEECQSELES 1477
Cdd:pfam15921 234 SYLKGRIFPVEDQLEALKSESQNkIELLLQQHQDRIEQLISEHE---VEITGLTEKA-------SSARSQANSIQSQLEI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1478 SQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEE-IADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVE 1556
Cdd:pfam15921 304 IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDkIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1557 GTLeHEESKTLRIQLELNQIKADVDrklAEKDEEIDNLRRS-HQRSMESmqttldaeakSRNEAVRLRKKMECDlNEMEV 1635
Cdd:pfam15921 384 ADL-HKREKELSLEKEQNKRLWDRD---TGNSITIDHLRRElDDRNMEV----------QRLEALLKAMKSECQ-GQMER 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1636 QLNhANRQASESQKLLRNLQVQIKDIQLELDDTVHQneelkeqmaLTERRNNLLSSE--VEELRALLEQNDRARKLAEHE 1713
Cdd:pfam15921 449 QMA-AIQGKNESLEKVSSLTAQLESTKEMLRKVVEE---------LTAKKMTLESSErtVSDLTASLQEKERAIEATNAE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1714 LLEATERVN-----LLHSQNTGLINQKKKLESDLSTLS-NEVDDAVQECRNAEEKakkaitdaamMAEELKKEQDTSSHL 1787
Cdd:pfam15921 519 ITKLRSRVDlklqeLQHLKNEGDHLRNVQTECEALKLQmAEKDKVIEILRQQIEN----------MTQLVGQHGRTAGAM 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1788 ERMKKNMEQTVKDLQMRLDEAEQIALKGGKKqVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKK 1867
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAK-IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRN 667
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2045330442 1868 NLARLQDLIDKLQakvKSYKRQAEEAEEQANSNLTKYRKLQHELD 1912
Cdd:pfam15921 668 ELNSLSEDYEVLK---RNFRNKSEEMETTTNKLKMQLKSAQSELE 709
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1009-1802 |
1.33e-14 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 79.78 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1009 EAHQQTLDDLQAEEDKVNTL-TKAKAKLEQQVDDLEGSLEQ---EKKVRMDLERVRRKLEGDLKLSLE-SVMDLENDKQQ 1083
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLRNQLQnTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1084 LEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARTEELEEELeaDRASRAKVEKQRGDVARELEELSERLEEAGG 1163
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEH--DSMSTMHFRSLGSAISKILRELDTEISYLKG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1164 ---ATSAQIEINKKRETDFLKL-----RRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKME 1235
Cdd:pfam15921 239 rifPVEDQLEALKSESQNKIELllqqhQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQ 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1236 VDDLASTVEQLskgKATSEKMCRLYEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEreaMVSQLQRAKNS 1315
Cdd:pfam15921 319 LSDLESTVSQL---RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK---LLADLHKREKE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1316 LTqnveelkkQLEEENKaksALAHSLQSSRHDCDLLREQYDEEQeakAELQR--ALSKANAEVAQWRTKYETDAIQRTEE 1393
Cdd:pfam15921 393 LS--------LEKEQNK---RLWDRDTGNSITIDHLRRELDDRN---MEVQRleALLKAMKSECQGQMERQMAAIQGKNE 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1394 LEEAKKKLVTRLQEAEES----VEASNAKCSSLEKTkhrlQTEIEDLVIDLERanaAAAALDKKQRNFDKVLAEWKQKYE 1469
Cdd:pfam15921 459 SLEKVSSLTAQLESTKEMlrkvVEELTAKKMTLESS----ERTVSDLTASLQE---KERAIEATNAEITKLRSRVDLKLQ 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1470 ECQsELESSQKESRGLSTELFKLKNSYEETLDHLETikrenknLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQ 1549
Cdd:pfam15921 532 ELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIEI-------LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR 603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1550 AALEEVEGTLEHEESKTLRIQ-----LELNQIK---ADVDRKLAEKD--EEIDNLRRSHQRSMESMQT-TLDAEAKSRNE 1618
Cdd:pfam15921 604 LELQEFKILKDKKDAKIRELEarvsdLELEKVKlvnAGSERLRAVKDikQERDQLLNEVKTSRNELNSlSEDYEVLKRNF 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1619 AVRlRKKMECDLNEMEVQLNHANRQASESQKLLRNlqvqikdiqLELDDTVHQNEELKEQMALTERRnnllsSEVEELRA 1698
Cdd:pfam15921 684 RNK-SEEMETTTNKLKMQLKSAQSELEQTRNTLKS---------MEGSDGHAMKVAMGMQKQITAKR-----GQIDALQS 748
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1699 LLEQNDRARKLAEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELK 1778
Cdd:pfam15921 749 KIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQ 828
|
810 820
....*....|....*....|....
gi 2045330442 1779 KEQDTSShleRMKKNMEQTVKDLQ 1802
Cdd:pfam15921 829 RQEQESV---RLKLQHTLDVKELQ 849
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
848-1535 |
1.74e-14 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 79.39 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 848 LRSAATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNladAEDRCDLLIKTKIQLEAKV 927
Cdd:pfam15921 250 LKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTV 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 928 KELMERLEDeeemsanvlaKKRKLEDECSELKKD--IDDLEITLAKVEKEKHATENkvKNLIEEMAAL------DETILK 999
Cdd:pfam15921 327 SQLRSELRE----------AKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQLQKLladlhkREKELS 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1000 LTKEK----------KALTEAH-QQTLDDLQAEEDKVNTLTKA-----KAKLEQQVDDLEG---SLEQEKKVRMDLERVR 1060
Cdd:pfam15921 395 LEKEQnkrlwdrdtgNSITIDHlRRELDDRNMEVQRLEALLKAmksecQGQMERQMAAIQGkneSLEKVSSLTAQLESTK 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1061 ---RKLEGDL---KLSLES----VMDLENDKQQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARTEELEEEL 1130
Cdd:pfam15921 475 emlRKVVEELtakKMTLESsertVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALK 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1131 EADRASRAKVEKQRGDVARELEELSERLEEAGG--ATSAQI--EINKKR-ETDFLKLRRDLEEAMLHH-EATTAALRKKH 1204
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAmqVEKAQLekEINDRRlELQEFKILKDKKDAKIRElEARVSDLELEK 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1205 ADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKVDELQRQLNETNTQ 1284
Cdd:pfam15921 635 VKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNT 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1285 RARAQAESG-----------EVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKAK---SALAHSLQSSRHDCDL 1350
Cdd:pfam15921 715 LKSMEGSDGhamkvamgmqkQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSqelSTVATEKNKMAGELEV 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1351 LREQYDEEQEAKAELQRALSKANAEVAQWRtkyetDAIQRTEElEEAKKKL-----VTRLQ----EAEESVEASNAKCSS 1421
Cdd:pfam15921 795 LRSQERRLKEKVANMEVALDKASLQFAECQ-----DIIQRQEQ-ESVRLKLqhtldVKELQgpgyTSNSSMKPRLLQPAS 868
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1422 LEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEEcQSELESSQKESRGLSTELFKLKNSYEETLD 1501
Cdd:pfam15921 869 FTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINE-EPTVQLSKAEDKGRAPSLGALDDRVRDCII 947
|
730 740 750
....*....|....*....|....*....|....*...
gi 2045330442 1502 HLE----TIKRENKNLQEEIADLSDQISQGSKTIHELE 1535
Cdd:pfam15921 948 ESSlrsdICHSSSNSLQTEGSKSSETCSREPVLLHAGE 985
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
980-1678 |
3.80e-14 |
|
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: 78.14 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 980 ENKVKNLIEEMAALDETILKLTKEKKALteahqqtLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERV 1059
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNL-------DKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1060 RRKLEGDLKLSLESVMDLENDKQQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEadrasraK 1139
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELN-------L 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1140 VEKQRgdvareleelserleeaggatsaqieINKKRETDFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQ 1219
Cdd:TIGR04523 178 LEKEK--------------------------LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1220 RVKQKLEKERSEAKMEvddLASTVEQLSKGKATSEKMCRLYED---QMNEAKAKVDELQRQLNETNTQ-----RARAQAE 1291
Cdd:TIGR04523 232 DNIEKKQQEINEKTTE---ISNTQTQLNQLKDEQNKIKKQLSEkqkELEQNNKKIKELEKQLNQLKSEisdlnNQKEQDW 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1292 SGEVGRKLEEREamvSQLQRAKNSLTQNveelkkqleeeNKAKSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSK 1371
Cdd:TIGR04523 309 NKELKSELKNQE---KKLEEIQNQISQN-----------NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1372 ANAEVAQWRtkyetdaiQRTEELEEAKKKLVTRLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALD 1451
Cdd:TIGR04523 375 LKKENQSYK--------QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1452 KKQRNFDKVLAEWKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTI 1531
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1532 HELEKMKKGLDMEKSDIQAALEEVEGTLEHEESKTlriqlelnqikadvdrKLAEKDEEIDNLRRShQRSMESMQTTLDA 1611
Cdd:TIGR04523 527 EKLESEKKEKESKISDLEDELNKDDFELKKENLEK----------------EIDEKNKEIEELKQT-QKSLKKKQEEKQE 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 1612 EAKSR-NEAVRLRKKMEcdlnEMEVQLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQ 1678
Cdd:TIGR04523 590 LIDQKeKEKKDLIKEIE----EKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
843-1628 |
6.12e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.87 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 843 KIKPLLRSAATEKELAALKEELAKLKEALEKSEVKRKELEEKQvsliqekndLALQLQAEQDNLADAEDRCDLLIKTKIQ 922
Cdd:PTZ00121 1201 KAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK---------KAEEERNNEEIRKFEEARMAHFARRQAA 1271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 923 LEAKVKELMERLEDEEEMSANVLAKKRKLEDECSELKKdiddleitlaKVEKEKHATENKVKnlIEEMAALDETILKLTK 1002
Cdd:PTZ00121 1272 IKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK----------KAEEAKKADEAKKK--AEEAKKKADAAKKKAE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1003 EKKALTEA----HQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVrmdlERVRRKLEGDLKLSLESVMDLE 1078
Cdd:PTZ00121 1340 EAKKAAEAakaeAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA----DEAKKKAEEDKKKADELKKAAA 1415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1079 NDKQQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQRGDVARELEELSERL 1158
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA 1495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1159 EEAGGATSAQIEINKKRETdflklRRDLEEAMLHHEATTAALRKKHADsvAELSEQIDSLQRVKQKLEKERSEAKMEVDD 1238
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADE-----AKKAEEAKKADEAKKAEEAKKADE--AKKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1239 LASTVEQLSKGKATSEKMcRLYEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQ 1318
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEA-KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1319 NVEELKKQLEEENKAKSALAHSLQSSRHDCDLLREQydEEQEAKAELQRALSKANAEVAQWRTKYETDAIQRTEELEEAK 1398
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA--EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1399 KKLVTRLQEAEESVEASNAKCSSLEKtkhrlqTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESS 1478
Cdd:PTZ00121 1726 EENKIKAEEAKKEAEEDKKKAEEAKK------DEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1479 QKESRGLSTELFKLKNSYEETL-DHLETIKRENKnlqeEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEG 1557
Cdd:PTZ00121 1800 IKDIFDNFANIIEGGKEGNLVInDSKEMEDSAIK----EVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKD 1875
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 1558 TLEHEESKTLRIQLELNQIKADVDRKLAEKDEEIDNlrrshqrsMESMQTTLDAEA-------KSRNEAVRLRKKMEC 1628
Cdd:PTZ00121 1876 LKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKN--------NDIIDDKLDKDEyikrdaeETREEIIKISKKDMC 1945
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1392-1943 |
7.91e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 76.98 E-value: 7.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1392 EELEEAKKKLVTRLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDK---VLAEWKQKY 1468
Cdd:TIGR04523 134 KENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELllsNLKKKIQKN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1469 EECQSELESSQKESRGLST-------ELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGL 1541
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDniekkqqEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1542 DMEKSDI-----QAALEEVEGTLEHEESKTLRIQLELNQIKadvdRKLAEKDEEIDNLRRShqrsmesmQTTLDAEAKSR 1616
Cdd:TIGR04523 294 KSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNN----KIISQLNEQISQLKKE--------LTNSESENSEK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1617 NEavrlrkkmecDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEEL 1696
Cdd:TIGR04523 362 QR----------ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1697 RALLEQNDRARKLAEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAE---EKAKKAITDAAMM 1773
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEkelKKLNEEKKELEEK 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1774 AEELKKEQDTS----SHLERMKKNMEQTVKDLQMRLDEAEQIALKGG-KKQVQKLEARVKELENELESEQRKSQEYQKVV 1848
Cdd:TIGR04523 512 VKDLTKKISSLkekiEKLESEKKEKESKISDLEDELNKDDFELKKENlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1849 RKYERRIKELsyqaeedKKNLARLQDLIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQVNKL 1928
Cdd:TIGR04523 592 DQKEKEKKDL-------IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEI 664
|
570
....*....|....*
gi 2045330442 1929 RVRTRDQVSKVSKLN 1943
Cdd:TIGR04523 665 IKKIKESKTKIDDII 679
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
32-76 |
8.11e-14 |
|
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: 67.07 E-value: 8.11e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2045330442 32 DGKKRAWIPDEKEAYIEIEIKELSGDKVIVETKDGRSLTVKEGDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
862-1686 |
2.22e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.33 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 862 EELAKLKEALEKSEVKRKELEEKQVSLI---------QEKNDLALQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELME 932
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDArkaeearkaEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAE 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 933 RLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEI-TLAKVEKEKHATE-----NKVKNLIEEMAALDETILKLTKEKKA 1006
Cdd:PTZ00121 1192 ELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAeAVKKAEEAKKDAEeakkaEEERNNEEIRKFEEARMAHFARRQAA 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1007 LTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKK---VRMDLERVRRKLEGDLKLSLESVMDLENDKQQ 1083
Cdd:PTZ00121 1272 IKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKadeAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1084 LE---EKLKKKDFEMNEISSRIEDEQALVNQLHKKIKEL----QARTEELEEELEADRASRAKVEKQRGDVARELEELSE 1156
Cdd:PTZ00121 1352 AEaaaDEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkkadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK 1431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1157 RleeaggATSAQIEINKKRETDflKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEkersEAKMEV 1236
Cdd:PTZ00121 1432 K------ADEAKKKAEEAKKAD--EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE----EAKKKA 1499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1237 DDLASTVEQLSKGKAT--SEKMCRLYEDQMNEAKAKVDELQR--------QLNETNTQRARAQAESGEVGRKLEEREAM- 1305
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAkkAEEAKKADEAKKAEEAKKADEAKKaeekkkadELKKAEELKKAEEKKKAEEAKKAEEDKNMa 1579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1306 VSQLQRAKNSLTQNVEELKKQLEEENKAKSALAHSLQSSRHDCDLLREQyDEEQEAKAELQRALSKANAEVAQWRTKYET 1385
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1386 DAIQRTEEL---EEAKKKLVTRLQEAEESVEASNAKCSSLEKTKhrlqtEIEDLVIDLERANAAAAALDKKQRNFDKVLA 1462
Cdd:PTZ00121 1659 NKIKAAEEAkkaEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-----KAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1463 EWKQKYEECQSELESSQKESRglstELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQisqgsKTIHELEKMKKGLD 1542
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDEE----EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE-----KRRMEVDKKIKDIF 1804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1543 MEKSDIQAALEevEGTLEHEESKtlriQLELNQIKADVDRK---LAEKDEEIDNLRRSHQRSMESMQTTLDAEAKSRNEA 1619
Cdd:PTZ00121 1805 DNFANIIEGGK--EGNLVINDSK----EMEDSAIKEVADSKnmqLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKE 1878
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 1620 VRLRKKMECDLNEmevQLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQN-EELKEQMALTERRN 1686
Cdd:PTZ00121 1879 DDEEEIEEADEIE---KIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDaEETREEIIKISKKD 1943
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
851-1436 |
2.82e-13 |
|
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: 75.48 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 851 AATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLIKTKIQL-----EA 925
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkkleEA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 926 KVKELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKV---KNLIEEMAALDETILKLTK 1002
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslERLQENLEGFSEGVKALLK 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1003 EKKALTEAHQQTLDDLQAEE-------------------DKVNTLTKAKAKLEQ-------------------QVDDLEG 1044
Cdd:TIGR02168 514 NQSGLSGILGVLSELISVDEgyeaaieaalggrlqavvvENLNAAKKAIAFLKQnelgrvtflpldsikgteiQGNDREI 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1045 SLEQEKKVRM--DLERVRRKLEGDLKLSLESVMDLENDKQQLEeKLKKKDFEMNEISSRIE-----------DEQALVNQ 1111
Cdd:TIGR02168 594 LKNIEGFLGVakDLVKFDPKLRKALSYLLGGVLVVDDLDNALE-LAKKLRPGYRIVTLDGDlvrpggvitggSAKTNSSI 672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1112 LHKK--IKELQARTEELEEELEADRASRAKVEKQRGDVARELEELSERLEEAggatsaqieinkkrETDFLKLRRDLEEA 1189
Cdd:TIGR02168 673 LERRreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL--------------SRQISALRKDLARL 738
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1190 MLHHEATTAALRKKHADsVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNEAKA 1269
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1270 KVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKAKSALAHSLQSSRHDCD 1349
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1350 LLREQYDEEQEAKAELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEESVEASNAKCSSLEKTKHRL 1429
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
....*..
gi 2045330442 1430 QTEIEDL 1436
Cdd:TIGR02168 978 ENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1017-1627 |
6.45e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1017 DLQAEED--KVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQLEEKLKKKDFE 1094
Cdd:COG1196 217 ELKEELKelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1095 MNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQRGDVAreleelserleeaggatsAQIEINKK 1174
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE------------------EELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1175 RETDFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSE---QIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLskgka 1251
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAElaaQLEELEEAEEALLERLERLEEELEELEEALAEL----- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1252 tsekmcrlyEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQ--NVEELKKQLEE 1329
Cdd:COG1196 434 ---------EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAArlLLLLEAEADYE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1330 ENKAKSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSkanAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAE 1409
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA---AALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1410 ESVEASNAkcsslektKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWkqkyeecQSELESSQKESRGLSTEL 1489
Cdd:COG1196 582 IRARAALA--------AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV-------AARLEAALRRAVTLAGRL 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1490 FKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEGTLEHEESKTLRI 1569
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 1570 QLELNQIKADVDRKLAEKDEEIDNLRRSHQRSMESmqttldaEAKSRNEAVRLRKKME 1627
Cdd:COG1196 727 EEQLEAEREELLEELLEEEELLEEEALEELPEPPD-------LEELERELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
849-1123 |
6.79e-13 |
|
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: 74.32 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 849 RSAATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLIKTKIQLEAKVK 928
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 929 ELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALT 1008
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1009 EAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSL-EQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQL--- 1084
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpv 987
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2045330442 1085 ----EEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQART 1123
Cdd:TIGR02168 988 nlaaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
853-1591 |
8.23e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 74.24 E-value: 8.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 853 TEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELME 932
Cdd:pfam02463 284 QEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 933 RLEDEEEMSANVLAKKRKLEDECSELKKDiddleitLAKVEKEKHATENKVKNLIE--EMAALDETILKLTKEKKALTEA 1010
Cdd:pfam02463 364 LQEKLEQLEEELLAKKKLESERLSSAAKL-------KEEELELKSEEEKEAQLLLElaRQLEDLLKEEKKEELEILEEEE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1011 HQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQLEEKLKK 1090
Cdd:pfam02463 437 ESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALI 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1091 KDFEMNEISS----RIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQRGDVARELEELSERLEEAGGats 1166
Cdd:pfam02463 517 KDGVGGRIISahgrLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKS--- 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1167 aqieINKKRETDFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQL 1246
Cdd:pfam02463 594 ----IAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLS 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1247 SKGKATSEKMCRLYEDQMNEAKAKVdelQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQ 1326
Cdd:pfam02463 670 ELTKELLEIQELQEKAESELAKEEI---LRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKID 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1327 LEEENKAKSALAHSLQSSRHDCDLLREQYDEEQEAKAEL------QRALSKANAEVAQWRTKYETDAIQRTEELEEAKKK 1400
Cdd:pfam02463 747 EEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKlkveeeKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQ 826
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1401 LVTRLQEAEESVEasNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQK 1480
Cdd:pfam02463 827 EEKIKEEELEELA--LELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE 904
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1481 ESRGLSTELFK-LKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLD----MEKSDIQAALEEV 1555
Cdd:pfam02463 905 ESQKLNLLEEKeNEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLakeeLGKVNLMAIEEFE 984
|
730 740 750
....*....|....*....|....*....|....*.
gi 2045330442 1556 EGTLEHEESKTLRIQLELNqiKADVDRKLAEKDEEI 1591
Cdd:pfam02463 985 EKEERYNKDELEKERLEEE--KKKLIRAIIEETCQR 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1630-1931 |
9.28e-13 |
|
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: 73.94 E-value: 9.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1630 LNEMEVQLNHANRQASESQKLlRNLQVQIKDIQLELddTVHQNEELKEQMalterrnnllssevEELRALLEQNDRARKL 1709
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERY-KELKAELRELELAL--LVLRLEELREEL--------------EELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1710 AEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLER 1789
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1790 MKKNMEQTVKDLQMRLdEAEQIALKGGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNL 1869
Cdd:TIGR02168 338 ELAELEEKLEELKEEL-ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2045330442 1870 ARLQDLI------------DKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQVNKLRVR 1931
Cdd:TIGR02168 417 ERLQQEIeellkkleeaelKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1475-1938 |
2.08e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1475 LESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEE 1554
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1555 VEGtLEHEESKTLRIQLELNQIKADVDRKLAEKDEEIDNLRRSHQRSMEsmqttLDAEAKSRNEAVRLRKKMECDLNEME 1634
Cdd:PRK03918 240 IEE-LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-----LKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1635 VQLNHANRQASESQKLLRnlqvqikdiqlELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQNDRARKLAEHEL 1714
Cdd:PRK03918 314 KRLSRLEEEINGIEERIK-----------ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1715 LEATERVNLLHSQntgLINQKKKLESDLSTLS---NEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEqdtssHLERMK 1791
Cdd:PRK03918 383 GLTPEKLEKELEE---LEKAKEEIEEEISKITariGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE-----HRKELL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1792 KNMEQTVKDLQMRLDEAEqialkggkKQVQKLEARVKELENELESEQRKSQEYQ--KVVRKYERRIKELSYQ-AEEDKKN 1868
Cdd:PRK03918 455 EEYTAELKRIEKELKEIE--------EKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEeLEKKAEE 526
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1869 LARLQDLIDKLQAKVKSYKRQAEEAEEQANsnltKYRKLQHELDDAEERADMAETQVNKLRVRTRDQVSK 1938
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLEELKK----KLAELEKKLDELEEELAELLKELEELGFESVEELEE 592
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1629-1922 |
2.86e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1629 DLNEMEVQLNHANRQASESQklLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQndrark 1708
Cdd:COG1196 221 ELKELEAELLLLKLRELEAE--LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE------ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1709 lAEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLE 1788
Cdd:COG1196 293 -LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1789 RMKKNMEQTVKDLQMRLDEAEQIALKgGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKN 1868
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAE-LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2045330442 1869 LARLQDLIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAEERADMAE 1922
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
839-1588 |
1.22e-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: 70.46 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 839 KLFFKIKPLLRSAATEKELAALKEELAKLKEALEKSE---------VKRKELEEKQVSLIQEKNDLAlQLQAEQDNLADA 909
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknsltetlkKEVKSLQNEKADLDRKLRKLD-QEMEQLNHHTTT 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 910 EDRCDLLIKTKIQLEAKVKELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEE 989
Cdd:TIGR00606 534 RTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 990 MAALDETILKLTKE--KKALTEAHQQTLDDLQAEEDKVNT----LTKAKAKLEQQVDDLEGS-------LEQEKKVRMDL 1056
Cdd:TIGR00606 614 LESKEEQLSSYEDKlfDVCGSQDEESDLERLKEEIEKSSKqramLAGATAVYSQFITQLTDEnqsccpvCQRVFQTEAEL 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1057 ERVRRKLEGDLKLSlesvmdlENDKQQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRAS 1136
Cdd:TIGR00606 694 QEFISDLQSKLRLA-------PDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKND 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1137 RAKVEKQRGDVareleelserleeaggatSAQIEINKKRETDFLKLRRDLEEamlhheatTAALRKKHADSVAELseQID 1216
Cdd:TIGR00606 767 IEEQETLLGTI------------------MPEEESAKVCLTDVTIMERFQME--------LKDVERKIAQQAAKL--QGS 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1217 SLQRVKQKLEKERSEAKMEVDDLASTVEQLskgkatsEKMCRLYEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVG 1296
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQHELDTVVSKIELN-------RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLV 891
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1297 RKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKAKSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSKANAEV 1376
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDY 971
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1377 AQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEESVEASNAKCSSLEKTKHRLQteIEDLVIDLERANAAAAaldkKQRN 1456
Cdd:TIGR00606 972 LKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRK--RENELKEVEEELKQHL----KEMG 1045
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1457 FDKVLaEWKQKYEECQSELESSQKESRGLSTELfklkNSYEETLDHLETIKREN--KNLQEEIADLSDQISQGSKTIHEL 1534
Cdd:TIGR00606 1046 QMQVL-QMKQEHQKLEENIDLIKRNHVLALGRQ----KGYEKEIKHFKKELREPqfRDAEEKYREMMIVMRTTELVNKDL 1120
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 2045330442 1535 EKMKKGLDMEKSDIQA-ALEEVEGTLEHEESKTLRIQ-LELNQIKADVDRKLAEKD 1588
Cdd:TIGR00606 1121 DIYYKTLDQAIMKFHSmKMEEINKIIRDLWRSTYRGQdIEYIEIRSDADENVSASD 1176
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
847-1305 |
2.71e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 847 LLRSAATEKELAALKEELAKLKEALEKSEVKRKELEEKqvslIQEKNDLALQLQAEQDNLADAEDRCDLLIKT----KIQ 922
Cdd:PRK02224 243 LEEHEERREELETLEAEIEDLRETIAETEREREELAEE----VRDLRERLEELEEERDDLLAEAGLDDADAEAvearREE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 923 LEAKVKELMERLEDE-------EEMSANVLAKKRKLEDECSELKKDIDDLeitlakvEKEKHATENKVKNLIEEMAALDE 995
Cdd:PRK02224 319 LEDRDEELRDRLEECrvaaqahNEEAESLREDADDLEERAEELREEAAEL-------ESELEEAREAVEDRREEIEELEE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 996 TIlkltkekKALTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQekkVRMDLERVRRKLEG--------DL 1067
Cdd:PRK02224 392 EI-------EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRT---ARERVEEAEALLEAgkcpecgqPV 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1068 KLS--LESVMDLENDKQQLEEKLKKKDFEMNEISSRIEDEQALV------NQLHKKIKELQARTEELEEELEADRASRAK 1139
Cdd:PRK02224 462 EGSphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaedriERLEERREDLEELIAERRETIEEKRERAEE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1140 VEKQRGDVARELEELSERleeaggATSAQIEINKKRET--DFLKLRRDLEEAM--LHHEATTAALRKKHADSVAELSEQI 1215
Cdd:PRK02224 542 LRERAAELEAEAEEKREA------AAEAEEEAEEAREEvaELNSKLAELKERIesLERIRTLLAAIADAEDEIERLREKR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1216 DSLQRvKQKLEKERSEAKME-VDDLASTVEQLSKGKATSEKmcrlyeDQMNEAKAKVDELQRQLNEtntQRARAQAESGE 1294
Cdd:PRK02224 616 EALAE-LNDERRERLAEKRErKRELEAEFDEARIEEAREDK------ERAEEYLEQVEEKLDELRE---ERDDLQAEIGA 685
|
490
....*....|.
gi 2045330442 1295 VGRKLEEREAM 1305
Cdd:PRK02224 686 VENELEELEEL 696
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
933-1542 |
2.80e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 933 RLEDEEEMSANVLAKKRKLEDECSELKKDI---DDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALtE 1009
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIkrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-E 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1010 AHQQTLDDLQAEEDKVNtltKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEgDLKLSLESVMDLENDKQQLEEKLK 1089
Cdd:PRK03918 235 ELKEEIEELEKELESLE---GSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1090 KKDFEMNEISSRIEDEQALVNQLHKKIKELQarteeleeeleadrasraKVEKQRGDVAReleelserleeaggatsaQI 1169
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLE------------------ELKKKLKELEK------------------RL 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1170 EINKKRETDFLKLRRDLEEAmlhheattAALRKKHAD-SVAELSEQIDSLQRVKQKLEKE-------RSEAKMEVDDLAS 1241
Cdd:PRK03918 355 EELEERHELYEEAKAKKEEL--------ERLKKRLTGlTPEKLEKELEELEKAKEEIEEEiskitarIGELKKEIKELKK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1242 TVEQLSKGKATSEKMCRLYEDQ-----MNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEERE------AMVSQLQ 1310
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkELAEQLK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1311 RAKNSLTQ-NVEELKKQLEEENKAKSALAH-SLQSSRHDCDLLREQydEEQEAKAELQRALSKANAEVAQWRTKYETDAI 1388
Cdd:PRK03918 507 ELEEKLKKyNLEELEKKAEEYEKLKEKLIKlKGEIKSLKKELEKLE--ELKKKLAELEKKLDELEEELAELLKELEELGF 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1389 QRTEELEEakkklvtRLQEAE----ESVEASNAkcsslEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEW 1464
Cdd:PRK03918 585 ESVEELEE-------RLKELEpfynEYLELKDA-----EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 1465 KQKYEEcqSELESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLsdqisqgSKTIHELEKMKKGLD 1542
Cdd:PRK03918 653 EKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER-------EKAKKELEKLEKALE 721
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1253-1912 |
3.11e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 68.59 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1253 SEKMCRLYEDQMNEAKakvdelqrqlnETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENK 1332
Cdd:pfam05483 73 SEGLSRLYSKLYKEAE-----------KIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1333 AKSALAHSLQSSRHDCDLLRE--------------QYDEEQEAKAELQRALSKANAEVAQWRTKYETDAIQRTEELEEAK 1398
Cdd:pfam05483 142 ENKDLIKENNATRHLCNLLKEtcarsaektkkyeyEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1399 KKLVTRLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESs 1478
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1479 qkesrglstelfkLKNSYEETLDHLETIKRENKNLQEEIADLSDQisqGSKTIHELEKMKKGLDMEKSDIQAALEEVEGT 1558
Cdd:pfam05483 301 -------------IKMSLQRSMSTQKALEEDLQIATKTICQLTEE---KEAQMEELNKAKAAHSFVVTEFEATTCSLEEL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1559 LEHEESKTLRIQLELNQIKADVDRKLAEKdEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLRKKMEcDLNEMEVQLN 1638
Cdd:pfam05483 365 LRTEQQRLEKNEDQLKIITMELQKKSSEL-EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAE-ELKGKEQELI 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1639 HAnRQASEsqKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELraLLEQndraRKLAEhellEAT 1718
Cdd:pfam05483 443 FL-LQARE--KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL--LLEN----KELTQ----EAS 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1719 ERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLERMKKNMEQTV 1798
Cdd:pfam05483 510 DMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1799 KDLQMRLDEAeqialkggKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKnlaRLQDLIDK 1878
Cdd:pfam05483 590 KILENKCNNL--------KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ---KFEEIIDN 658
|
650 660 670
....*....|....*....|....*....|....*..
gi 2045330442 1879 LQAKVKSYKRQAE---EAEEQANSNLTKYRKLQHELD 1912
Cdd:pfam05483 659 YQKEIEDKKISEEkllEEVEKAKAIADEAVKLQKEID 695
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1179-1866 |
5.35e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 67.82 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1179 FLKLRRDLEEAMLHHEATTAALRKKHaDSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCR 1258
Cdd:pfam05483 80 YSKLYKEAEKIKKWKVSIEAELKQKE-NKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1259 LYEDQMNEAKAKVDELQRQLNETNT----------------QRARAQAESG--EVGRKLEEREAMVSQL----QRAKNSL 1316
Cdd:pfam05483 159 LLKETCARSAEKTKKYEYEREETRQvymdlnnniekmilafEELRVQAENArlEMHFKLKEDHEKIQHLeeeyKKEINDK 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1317 TQNVEELKKQLEEENKAKSALAHSLQSSRHDCDLLREQ---YDEEQEAKAELQRALSKANAEVAQWRTKYETDAIQRTEE 1393
Cdd:pfam05483 239 EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKtklQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEED 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1394 LEEAKKKLVTRLQEAEESVEASNAKcssleKTKHRLQ-TEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYeecQ 1472
Cdd:pfam05483 319 LQIATKTICQLTEEKEAQMEELNKA-----KAAHSFVvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK---S 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1473 SELESSQKESRGLSTELFKLKN---SYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQ 1549
Cdd:pfam05483 391 SELEEMTKFKNNKEVELEELKKilaEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1550 AALEEVEGTLEHEESKTLRI----------QLELNQIKADVDRKLAEKDEEIDNLRRSHQRSMESMQTTLDAEAKSRNEA 1619
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNIELtahcdkllleNKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDEL 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1620 VRLRKKMECDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQLELDDtvhqneeLKEQMaltERRNNLLSSEVEELRAL 1699
Cdd:pfam05483 551 ESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN-------LKKQI---ENKNKNIEELHQENKAL 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1700 leqndRARKLAEHELLEATE-RVNLLHSQntgLINQKKKLESDLSTLSNEVDD---AVQECRNAEEKAKKAITDAAMMAE 1775
Cdd:pfam05483 621 -----KKKGSAENKQLNAYEiKVNKLELE---LASAKQKFEEIIDNYQKEIEDkkiSEEKLLEEVEKAKAIADEAVKLQK 692
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1776 ELKK--EQDTSSHLERMKKNMEQTVKDLQMRLDEaeqIALKGGKKQVQK-----LEARVKELENELESEQRKSQEYQKVV 1848
Cdd:pfam05483 693 EIDKrcQHKIAEMVALMEKHKHQYDKIIEERDSE---LGLYKNKEQEQSsakaaLEIELSNIKAELLSLKKQLEIEKEEK 769
|
730
....*....|....*...
gi 2045330442 1849 RKYERRIKELSYQAEEDK 1866
Cdd:pfam05483 770 EKLKMEAKENTAILKDKK 787
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
843-1698 |
7.81e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 67.69 E-value: 7.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 843 KIKPLLRSAATEKELAALKEELAKLKEALEKSEVK--RKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLIKTK 920
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELiiDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 921 IQLEA-KVKELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNliEEMAALDETILK 999
Cdd:pfam02463 234 LNEERiDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK--SELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1000 LTKEKKALTEahqqtldDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEgdlkLSLESVMDLEN 1079
Cdd:pfam02463 312 DEEKLKESEK-------EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLE----QLEEELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1080 DKQQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARteeleeeLEADRASRAKVEKQRGDVARELEELSERLE 1159
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKE-------EKKEELEILEEEEESIELKQGKLTEEKEEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1160 EAGGATSAQIEINKKRETDFLKLRRDLEEAMLHHEAttAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDL 1239
Cdd:pfam02463 454 EKQELKLLKDELELKKSEDLLKETQLVKLQEQLELL--LSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1240 ASTVEQLSKGKATSEKMCRLYEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQN 1319
Cdd:pfam02463 532 GDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1320 VEELKKQLEEENKAKSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSKANAEVAQWRTK-YETDAIQRTEELEEAK 1398
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKElLEIQELQEKAESELAK 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1399 KKLVTRLQEAEEsvEASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSEL--- 1475
Cdd:pfam02463 692 EEILRRQLEIKK--KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKsel 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1476 ---------ESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGS-KTIHELEKMKKGL-DME 1544
Cdd:pfam02463 770 slkekelaeEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKeEELEELALELKEEqKLE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1545 KSDIQAALEEVEGTLEHEESKTLRIQLELNQIKADVDRKLAEKDEEIDNLRRSHQRSmESMQTTLDAEAKSRNEAVRLRK 1624
Cdd:pfam02463 850 KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEES-QKLNLLEEKENEIEERIKEEAE 928
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2045330442 1625 KMECDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRA 1698
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEE 1002
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1496-1926 |
8.48e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1496 YEETLDHLETIKRENKNLqEEIADLSDQISQGSKTIHELEKMKKGLDMEKSdiQAALEEVEGTLEHEESKTLRIQLELNQ 1575
Cdd:COG4913 237 LERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1576 IKAdvdrKLAEKDEEIDNLRRSHQRS----MESMQTTLDAEAKSRNEAVRLRKKMECDLNEMEVQLNH-----------A 1640
Cdd:COG4913 314 LEA----RLDALREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeefaalraeA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1641 NRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQN-----DRARKLAehELL 1715
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlgldeAELPFVG--ELI 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1716 E----------ATERVnlLHSQNTGL-------------INQKK-----------------------------KLESDLS 1743
Cdd:COG4913 468 EvrpeeerwrgAIERV--LGGFALTLlvppehyaaalrwVNRLHlrgrlvyervrtglpdperprldpdslagKLDFKPH 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1744 TLSNEVDDAVQE------CRNAEE--KAKKAITDAAMMAEELKK-EQDTSSHLER---MKKNMEQTVKDLQMRLDEAEQi 1811
Cdd:COG4913 546 PFRAWLEAELGRrfdyvcVDSPEElrRHPRAITRAGQVKGNGTRhEKDDRRRIRSryvLGFDNRAKLAALEAELAELEE- 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1812 alkggkkQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQA-----EEDKKNLARLQDLIDKLQAKVKSY 1886
Cdd:COG4913 625 -------ELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEReiaelEAELERLDASSDDLAALEEQLEEL 697
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2045330442 1887 KRQAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQVN 1926
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1578-1943 |
1.33e-10 |
|
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: 67.02 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1578 ADVDRKLAEKDEEIDNLRRSHQRS---MESMQTTLDAEAKSRNEAVRLrKKMECDLNEMEVQLNHANRQASESQKllRNL 1654
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLdliIDEKRQQLERLRREREKAERY-QALLKEKREYEGYELLKEKEALERQK--EAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1655 QVQIKDIQLELDDTVHQNEELKEqmalterrnnllssEVEELRALLEQ-NDRARKLAEHELLEATERVNLLHSQntglin 1733
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEK--------------RLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAE------ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1734 qKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLERMKKNMEQTVKDLQMRLDEAEqial 1813
Cdd:TIGR02169 303 -IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD---- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1814 kggkKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEA 1893
Cdd:TIGR02169 378 ----KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2045330442 1894 EEQANSNL--------------TKYRKLQHELDDAEERADMAETQVNKLRVRTRDQVSKVSKLN 1943
Cdd:TIGR02169 454 EWKLEQLAadlskyeqelydlkEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLK 517
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
842-1280 |
1.35e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 842 FKIKPLLRSAATEKELAALKEELAKLKEALEKSEVKRKELEE---------KQVSLIQEKNDLALQLQAEQDNLADAEDR 912
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEElkkklkeleKRLEELEERHELYEEAKAKKEELERLKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 913 cdLLIKTKIQLEAKVKELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLE-----ITLAKVEKEKHATEN------ 981
Cdd:PRK03918 381 --LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkCPVCGRELTEEHRKElleeyt 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 982 -KVKNLIEEMAALDETILKLTKEKKALtEAHQQTLDDLQAEEDKVNTLTKAKAKLEQ-QVDDLEGSLEQEKKVRMDLERV 1059
Cdd:PRK03918 459 aELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1060 RRKLEGdLKLSLESVMDLENDKQQLEEKLKKKDFEMNEISSRIEDEQ-ALVNQLHKKIKELQARTEELEEELEADRASRA 1138
Cdd:PRK03918 538 KGEIKS-LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKELER 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1139 KVEKQRgdvareleelserlEEAGGATSAQIEINKKrETDFLKLRRDLEEA-MLHHEATTAALRKKHadsvAELSEQIDS 1217
Cdd:PRK03918 617 EEKELK--------------KLEEELDKAFEELAET-EKRLEELRKELEELeKKYSEEEYEELREEY----LELSRELAG 677
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2045330442 1218 LQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDqMNEAKAKVDELQRQLNE 1280
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER-VEELREKVKKYKALLKE 739
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1184-1879 |
1.48e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1184 RDLEEAmlHHEATTA-----ALR--KKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVddLASTVEQLSKGKATSEKM 1256
Cdd:COG4913 235 DDLERA--HEALEDAreqieLLEpiRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1257 CRLYEDQMNEAKAKVDELQRQLNETNTQR-ARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKAKS 1335
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1336 ALAHSLQSSRHDcdlLREQYDEEQEAKAELQRALSKANAEVAQWRTK---YETDAIQRTEELEEAKKKLVTRLQEAEESV 1412
Cdd:COG4913 391 ALLEALEEELEA---LEEALAEAEAALRDLRRELRELEAEIASLERRksnIPARLLALRDALAEALGLDEAELPFVGELI 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1413 EAsnakcssleKTKHRL-QTEIE--------DLVIDLERANAAAAALDK---KQR-NFDKVlaewkqkyEECQSELESSQ 1479
Cdd:COG4913 468 EV---------RPEEERwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPDPERPR 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1480 KESRGLSTEL-FK-------LKNSYEETLDHL-----ETIKRENKNLQEEiadlsDQISQgSKTIHELekmkkgldmeks 1546
Cdd:COG4913 531 LDPDSLAGKLdFKphpfrawLEAELGRRFDYVcvdspEELRRHPRAITRA-----GQVKG-NGTRHEK------------ 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1547 DIQAALEEVegtleheesktlriqlelNQIKADVDRKLAEKDEEIDNLRRSH---QRSMESMQTTLDAEAKSRNEAVRLR 1623
Cdd:COG4913 593 DDRRRIRSR------------------YVLGFDNRAKLAALEAELAELEEELaeaEERLEALEAELDALQERREALQRLA 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1624 KKMECDLNEMEVQ-----LNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRA 1698
Cdd:COG4913 655 EYSWDEIDVASAEreiaeLEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1699 LLEQNDRARKLAEHELLEAtERVNLLHSQNTGLInqKKKLESDLSTLSNEVDDAVQECRNAEEKAKK--------AITDA 1770
Cdd:COG4913 735 RLEAAEDLARLELRALLEE-RFAAALGDAVEREL--RENLEERIDALRARLNRAEEELERAMRAFNRewpaetadLDADL 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1771 AMMAEELKK-EQDTSSHL--------ERMKKNMEQTVKDLQMRLDEAEQIAlkggKKQVQKLEARVKELE-NE-----LE 1835
Cdd:COG4913 812 ESLPEYLALlDRLEEDGLpeyeerfkELLNENSIEFVADLLSKLRRAIREI----KERIDPLNDSLKRIPfGPgrylrLE 887
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 2045330442 1836 SEQRKSQEyqkvVRKYERRIKELS-----YQAEEDKKNLARLQDLIDKL 1879
Cdd:COG4913 888 ARPRPDPE----VREFRQELRAVTsgaslFDEELSEARFAALKRLIERL 932
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1211-1869 |
1.54e-10 |
|
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: 66.31 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1211 LSEQIDSLQRVKQKLEKERS---EAKMEVDDLASTVEQLskgkATSEKMCRLYEDQMNEAKAKVDELQRQLNETNtqrar 1287
Cdd:pfam07111 68 ISRQLQELRRLEEEVRLLREtslQQKMRLEAQAMELDAL----AVAEKAGQAEAEGLRAALAGAEMVRKNLEEGS----- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1288 aQAESGEVGRKLEEREAMVSQL-QRAKNSLTQNVEELKKQLEEENKAKSALAHSLQSSRHDCDLLREQYD---EEQEAKA 1363
Cdd:pfam07111 139 -QRELEEIQRLHQEQLSSLTQAhEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSktqEELEAQV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1364 ELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKkklvtRLQEAEESVEAsnakcsSLEKTKHRLQTEIEDLVIDLEra 1443
Cdd:pfam07111 218 TLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQ-----HLQEDRADLQA------TVELLQVRVQSLTHMLALQEE-- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1444 naaaaALDKKQRNFDKVLAEWKQKyeeCQSELESSQKESRGLSTELfklknsYEETLDHLETIKRenknLQEEIADLSDQ 1523
Cdd:pfam07111 285 -----ELTRKIQPSDSLEPEFPKK---CRSLLNRWREKVFALMVQL------KAQDLEHRDSVKQ----LRGQVAELQEQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1524 ISQGSKtihelekmkkgldmEKSDIQAALEEVEGTLEHEESKTLRIQLELNQIKaDVDRKLAEKDEEIDNLRRSHQRSME 1603
Cdd:pfam07111 347 VTSQSQ--------------EQAILQRALQDKAAEVEVERMSAKGLQMELSRAQ-EARRRQQQQTASAEEQLKFVVNAMS 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1604 SMQTTLDAEAKSRNEAVrlrkkmeCDLNEMEVQLNHANRQASESQKLLRNlQVQIKDIQLELDDTVHQNEELKEQMA--- 1680
Cdd:pfam07111 412 STQIWLETTMTRVEQAV-------ARIPSLSNRLSYAVRKVHTIKGLMAR-KVALAQLRQESCPPPPPAPPVDADLSlel 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1681 --LTERRNNLLSSEVEELRALLEQNDRARKLAEHELLEatervnllhsqntgLINQKKKLESDLSTLSNEVDDAVQECRN 1758
Cdd:pfam07111 484 eqLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQ--------------LSEVAQQLEQELQRAQESLASVGQQLEV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1759 AEEKAKKAITDAAMMAEELKKEQDT-----SSHLERMKKNMEQTVKDLQMRLDEA--EQIALKGGKKQVQKLEARVKELE 1831
Cdd:pfam07111 550 ARQGQQESTEEAASLRQELTQQQEIygqalQEKVAEVETRLREQLSDTKRRLNEArrEQAKAVVSLRQIQHRATQEKERN 629
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2045330442 1832 NELE--SEQRKSQEYQKVVrkyeRRIKELsyqaeEDKKNL 1869
Cdd:pfam07111 630 QELRrlQDEARKEEGQRLA----RRVQEL-----ERDKNL 660
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
847-1599 |
1.82e-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: 66.53 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 847 LLRSAATEKELAALKEELAKLKEALEKSEVKRKELEEKqvsliqeKNDLALQLQAEQDnlaDAEDRCDLLIKTKIQLEAK 926
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGK-------AELLTLRSQLLTL---CTPCMPDTYHERKQVLEKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 927 VKELMERLEDEEEMSANV------LAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATE--NKVKNLIEEMAALDE--- 995
Cdd:TIGR00618 228 LKHLREALQQTQQSHAYLtqkreaQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINraRKAAPLAAHIKAVTQieq 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 996 ---TILKLTKEKKALTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSle 1072
Cdd:TIGR00618 308 qaqRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQ-- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1073 svMDLENDKQQLEEKLKKKDFEMNE---ISSRIEDEQALVNQL--HKKIKELQARTEELEEELEADRASRAKVEKQRGDV 1147
Cdd:TIGR00618 386 --QQKTTLTQKLQSLCKELDILQREqatIDTRTSAFRDLQGQLahAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1148 ARELEELSERLEEAGGATSAQIEINKKRETDFL----KLRRDLEEAMLHHEATTAALRKKHADSvAELSEQIDSLQRVKQ 1223
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQETRKKAVVLARLlelqEEPCPLCGSCIHPNPARQDIDNPGPLT-RRMQRGEQTYAQLET 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1224 KLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRlyedQMNEAKAKVDELQrqlNETNTQRARAQAESGEVGRKLEERE 1303
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQ----CDNRSKEDIPNLQ---NITVRLQDLTEKLSEAEDMLACEQH 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1304 AMVSQLQRAKN----SLTQNVEELKKQLEEENKAKSALAHSLQSSRHDCDLLREQydeEQEAKAELQRALSKANAEVAQW 1379
Cdd:TIGR00618 616 ALLRKLQPEQDlqdvRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVL---PKELLASRQLALQKMQSEKEQL 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1380 RTKYETDAiQRTEELEEAKKKLVTRLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLviDLERANAAAAALDKKQRNFDK 1459
Cdd:TIGR00618 693 TYWKEMLA-QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKEL--MHQARTVLKARTEAHFNNNEE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1460 VLAEWK--QKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIKR-ENKNLQEEIADLSDQISQGSKTIHELeK 1536
Cdd:TIGR00618 770 VTAALQtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRLEEKSATLGEI-T 848
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2045330442 1537 MKKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQLELNQIKADVDRKLAEKDEEIDNLRRSHQ 1599
Cdd:TIGR00618 849 HQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQ 911
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
872-1866 |
2.23e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 66.22 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 872 EKSEVKRKELEEKQVSLIQEKN-DLALQLQAEQDNLADAEDrcdlLIKTKiqlEAKVKELMERLEDEEEMsanvLAKKRK 950
Cdd:TIGR00606 198 QGQKVQEHQMELKYLKQYKEKAcEIRDQITSKEAQLESSRE----IVKSY---ENELDPLKNRLKEIEHN----LSKIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 951 LEDECSELK-------KDIDDLEITLAKV-----EKEKHATENK---VKNLIEEMAALDETILKLTKEKKALTEAH---- 1011
Cdd:TIGR00606 267 LDNEIKALKsrkkqmeKDNSELELKMEKVfqgtdEQLNDLYHNHqrtVREKERELVDCQRELEKLNKERRLLNQEKtell 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1012 -QQTLDDLQAEEDKVNTLTKAKAKLEQQ----VDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQLEE 1086
Cdd:TIGR00606 347 vEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1087 KLKKKDFEMNEISSRIEDEQAL----VNQLHKKIKELQARTEELEEELEADRASRakveKQRGDVARELEelserleeag 1162
Cdd:TIGR00606 427 QADEIRDEKKGLGRTIELKKEIlekkQEELKFVIKELQQLEGSSDRILELDQELR----KAERELSKAEK---------- 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1163 gatSAQIEINKKRETDFLKLRRDLEEAMlhheattaalrKKHADSVAELSEQIDSLQRVkQKLEKERSEAKMEVDDLAST 1242
Cdd:TIGR00606 493 ---NSLTETLKKEVKSLQNEKADLDRKL-----------RKLDQEMEQLNHHTTTRTQM-EMLTKDKMDKDEQIRKIKSR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1243 VEQLSKGKATSEKMCRLYEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRaknsltqnvee 1322
Cdd:TIGR00606 558 HSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED----------- 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1323 lkkqleeenkaKSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSKANAEVAQWRTKYET------DAIQRTEELEE 1396
Cdd:TIGR00606 627 -----------KLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqRVFQTEAELQE 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1397 AKKKLVTRLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELE 1476
Cdd:TIGR00606 696 FISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1477 S---SQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEeiadlsdqiSQGSKTIHELEKMKKGLDMEKSDIQAALE 1553
Cdd:TIGR00606 776 TimpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQG---------SDLDRTVQQVNQEKQEKQHELDTVVSKIE 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1554 EVEGTLEHEESKTLRIQLELNQIKAdvdrklaekdeeidnlrrshqrsmesmqttldaEAKSRNEAVRLRKKMECDLNEM 1633
Cdd:TIGR00606 847 LNRKLIQDQQEQIQHLKSKTNELKS---------------------------------EKLQIGTNLQRRQQFEEQLVEL 893
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1634 EVQLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEElkeqmalterRNNLLSSEVEELRALLEQNDRARKLAEHE 1713
Cdd:TIGR00606 894 STEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKET----------SNKKAQDKVNDIKEKVKNIHGYMKDIENK 963
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1714 LLEATERvnllhsqntglinQKKKLESDLSTLSNEVDDAVQECRNAEE--KAKKAITDAAMMAEELKKEQDTSSHLERMK 1791
Cdd:TIGR00606 964 IQDGKDD-------------YLKQKETELNTVNAQLEECEKHQEKINEdmRLMRQDIDTQKIQERWLQDNLTLRKRENEL 1030
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2045330442 1792 KNMEQTVKDLqmrLDEAEQIALKGGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDK 1866
Cdd:TIGR00606 1031 KEVEEELKQH---LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1257-1924 |
3.75e-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: 65.24 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1257 CRLYEDQMNEAkAKVDELQRQLNETNTQRARAQAESGEVG---RKLEEREAMVSQLQRAKNS-LTQNVEELKKQLEEENK 1332
Cdd:pfam12128 230 IQAIAGIMKIR-PEFTKLQQEFNTLESAELRLSHLHFGYKsdeTLIASRQEERQETSAELNQlLRTLDDQWKEKRDELNG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1333 AKSALAHSLQSSRHDCDLLREQYDEEQEAKAElQRALSKANAEvaQWRTKYE---------TDAIQRTEELEEAKKKLVT 1403
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDADIE-TAAADQEQLP--SWQSELEnleerlkalTGKHQDVTAKYNRRRSKIK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1404 rlQEAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLE-----RANAAAAALDKKQRNFDKVLAEWK------------- 1465
Cdd:pfam12128 386 --EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALEselreQLEAGKLEFNEEEYRLKSRLGELKlrlnqatatpell 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1466 ----QKYEEC---QSELESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHEL---- 1534
Cdd:pfam12128 464 lqleNFDERIeraREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFlrke 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1535 -----EKMKKGLDME---KSDIQAaleEVEGTLEHEESKTLRIQLELNQIkaDVDRKLAEKDEeidnLRRSHQRSMESMQ 1606
Cdd:pfam12128 544 apdweQSIGKVISPEllhRTDLDP---EVWDGSVGGELNLYGVKLDLKRI--DVPEWAASEEE----LRERLDKAEEALQ 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1607 TTLDAEAKSRNEAVRLRKKMECDLNEMEVQLNhANRQASESQKLLRNlqvqikdiqlelddtVHQNEELKEQMALTERRn 1686
Cdd:pfam12128 615 SAREKQAAAEEQLVQANGELEKASREETFART-ALKNARLDLRRLFD---------------EKQSEKDKKNKALAERK- 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1687 NLLSSEVEELRALLEQNDRARKLAehelLEATERVNLLHSqnTGLINQKKKLESDLSTLSNEVDDAVQecrnAEEKAKKA 1766
Cdd:pfam12128 678 DSANERLNSLEAQLKQLDKKHQAW----LEEQKEQKREAR--TEKQAYWQVVEGALDAQLALLKAAIA----ARRSGAKA 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1767 ITDA--AMMAEELKK---EQDTSSHLERMKKNMEQTVKDLQMRLDEAeqialkggkkqvqkleARVKELENELESEQRks 1841
Cdd:pfam12128 748 ELKAleTWYKRDLASlgvDPDVIAKLKREIRTLERKIERIAVRRQEV----------------LRYFDWYQETWLQRR-- 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1842 QEYQKVVRKYERRIKELsyqaeedKKNLARLQDLIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAEERADMA 1921
Cdd:pfam12128 810 PRLATQLSNIERAISEL-------QQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSE 882
|
...
gi 2045330442 1922 ETQ 1924
Cdd:pfam12128 883 QAQ 885
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
851-1316 |
4.05e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 851 AATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLAL---QLQAEQDNLADAEDRCDLLIKTKIQLEAKV 927
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESlegSKRKLEEKIRELEERIEELKKEIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 928 KELMERLEDEEEMSA------NVLAKKRKLEDECSELKKDIDDLEITLAKVEK---EKHATENKVKNLIEEMAALDETIL 998
Cdd:PRK03918 283 KELKELKEKAEEYIKlsefyeEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEERHE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 999 KLTKEKKALTEAHQ-------QTLDDLQAE-----------EDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVR 1060
Cdd:PRK03918 363 LYEEAKAKKEELERlkkrltgLTPEKLEKEleelekakeeiEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCG 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1061 RKLEGDLKLSL-----ESVMDLENDKQQLEEKLKKKDFEMNEISSRIEDEQALV--NQLHKKIKELQARTEELEEELEAD 1133
Cdd:PRK03918 443 RELTEEHRKELleeytAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEELEK 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1134 RASRA-KVEKQRGDVARELEELSERLEEAGGATSAQIEINKKREtdflKLRRDLEEamLHHEattaaLRKKHADSVAELS 1212
Cdd:PRK03918 523 KAEEYeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD----ELEEELAE--LLKE-----LEELGFESVEELE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1213 EQIDSLqrvkQKLEKERSEAKMEVDDLASTVEQLSKGKAT---SEKMCRLYEDQMNEAKAKVDELQRQLNETNTQRARAQ 1289
Cdd:PRK03918 592 ERLKEL----EPFYNEYLELKDAEKELEREEKELKKLEEEldkAFEELAETEKRLEELRKELEELEKKYSEEEYEELREE 667
|
490 500
....*....|....*....|....*....
gi 2045330442 1290 AE--SGEVGRKLEEREAMVSQLQRAKNSL 1316
Cdd:PRK03918 668 YLelSRELAGLRAELEELEKRREEIKKTL 696
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1508-1924 |
4.20e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1508 RENKNLQEEIADLSDQISQgsktIHELEKMKKGLDMEKSDIQAALEEVEGtlEHEESKTLRIQLELNQIKADVDRKLAEK 1587
Cdd:COG4717 71 KELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELRE--ELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1588 DEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLRKKMECDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQLELDD 1667
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1668 TVHQNEELKEQMALTERRNNLLSSEVE-----ELRALLEQNDRARKLAEHELLEATERVNLLHSQNTGLINQKKKLESDL 1742
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLlliaaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1743 STLsnevdDAVQECRNAEEKAKKAITDAAMMAEELKKEqdtssHLERMKKNMEQTVKDLQMRLDEAEQIALKGGKKQVQK 1822
Cdd:COG4717 305 EEL-----QALPALEELEEEELEELLAALGLPPDLSPE-----ELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1823 LEARVK-ELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQDliDKLQAKVKSYKRQAEEAEEQANSNL 1901
Cdd:COG4717 375 LLAEAGvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELR 452
|
410 420
....*....|....*....|...
gi 2045330442 1902 TKYRKLQHELDDAEERADMAETQ 1924
Cdd:COG4717 453 EELAELEAELEQLEEDGELAELL 475
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
848-1441 |
4.76e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 848 LRSAATEKELAALKEELAKLKEALEKSEVKRKELEEKqvsliqekndlalqlqaeqdnladaedrcdlliktKIQLEAKV 927
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQ-----------------------------------REQARETR 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 928 KELMERLEDEEEmsanvlakKRkleDECSELKKDIDDLEITLAKVEKEKHAtenkvknLIEEMAALDETILKLTKEKKAL 1007
Cdd:PRK02224 237 DEADEVLEEHEE--------RR---EELETLEAEIEDLRETIAETEREREE-------LAEEVRDLRERLEELEEERDDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1008 teahqqtLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQekkVRMDLERVRRKLEGdlklSLESVMDLENDKQQLEEK 1087
Cdd:PRK02224 299 -------LAEAGLDDADAEAVEARREELEDRDEELRDRLEE---CRVAAQAHNEEAES----LREDADDLEERAEELREE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1088 LKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQRGDVARELeelserleeaggatsa 1167
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE---------------- 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1168 qieinKKRETDFLKLRRDLEEAmlhhEATTAALR----------KKHADSVAELSEQIDslqrvkqKLEKERSEAKMEVD 1237
Cdd:PRK02224 429 -----AELEATLRTARERVEEA----EALLEAGKcpecgqpvegSPHVETIEEDRERVE-------ELEAELEDLEEEVE 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1238 DLASTVEQLSKGKATSEKMCRLYE------DQMNEAKAKVDELQRQLNETNTQ-----------RARAQAESGEVGRKLE 1300
Cdd:PRK02224 493 EVEERLERAEDLVEAEDRIERLEErredleELIAERRETIEEKRERAEELRERaaeleaeaeekREAAAEAEEEAEEARE 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1301 EREAMVSQLQRAKNSLTQ--NVEELKKQLEEENKAKSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSKANAEVAQ 1378
Cdd:PRK02224 573 EVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAR 652
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2045330442 1379 WR----TKYETDAIQRTEELEEAKKKLVTRLQEAEESVEasnakcsSLEKTKHRLqTEIEDLVIDLE 1441
Cdd:PRK02224 653 EDkeraEEYLEQVEEKLDELREERDDLQAEIGAVENELE-------ELEELRERR-EALENRVEALE 711
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
847-1064 |
6.13e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 6.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 847 LLRSAATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLIKTKIQLEAK 926
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 927 VKELMERLEDEEEMSANVLAKKRKLEDEcSELK-----KDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLT 1001
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQ-PPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2045330442 1002 KEKKALTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLE 1064
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
916-1778 |
7.25e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 64.68 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 916 LIKTKIQLEAKVKELMERLEDEEEMSANVLAKKrklEDECSELKKDIDDLEITLAKVEKekhatenkvknLIEEMAALDE 995
Cdd:TIGR00606 211 YLKQYKEKACEIRDQITSKEAQLESSREIVKSY---ENELDPLKNRLKEIEHNLSKIMK-----------LDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 996 TILKLTKEKKALTEAHQQTlddLQAEEDKVNTLTKAKAK----LEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDlklsl 1071
Cdd:TIGR00606 277 RKKQMEKDNSELELKMEKV---FQGTDEQLNDLYHNHQRtvreKERELVDCQRELEKLNKERRLLNQEKTELLVE----- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1072 ESVMDLENDKQQleEKLKKKDFEMNEISSRIE--------DEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQ 1143
Cdd:TIGR00606 349 QGRLQLQADRHQ--EHIRARDSLIQSLATRLEldgfergpFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1144 RGDvareleELSERLEEAGGATSAQIEINKKRETDFLKLRRDLEEA---MLHHEATTAALRKKHAD-SVAELSEQIDSLQ 1219
Cdd:TIGR00606 427 QAD------EIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLegsSDRILELDQELRKAERElSKAEKNSLTETLK 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1220 RVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKVDELQRQLNETNTQ------RARAQAESG 1293
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnKKQLEDWLH 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1294 EVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKAKSALAHSL------QSSRHDCDLLREQYDEEQEAKAELQR 1367
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLAG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1368 ALSKANAEVAQWRTKYET------DAIQRTEELEEAKKKLVTRLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLE 1441
Cdd:TIGR00606 661 ATAVYSQFITQLTDENQSccpvcqRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIID 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1442 RANAAAAALDKKQRNFDKVLAEWKQKYEECQSELES---SQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEeiA 1518
Cdd:TIGR00606 741 LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTimpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQG--S 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1519 DLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQLELNQIKADVDR------KLAEKDEEID 1592
Cdd:TIGR00606 819 DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRrqqfeeQLVELSTEVQ 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1593 NLRR--SHQRSMESMQTTLDAEAKSRNEAVRLRKKMECDLNEMEVQ---------------------------------- 1636
Cdd:TIGR00606 899 SLIReiKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNdikekvknihgymkdienkiqdgkddylkqkete 978
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1637 LNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLlsSEVEELRA----------LLEQNDRA 1706
Cdd:TIGR00606 979 LNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENEL--KEVEEELKqhlkemgqmqVLQMKQEH 1056
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2045330442 1707 RKLaEHELLEATERVNLLHSQNTGLINQKKKLESDLSTlsnevddavQECRNAEEKAKKAITDAAMMAEELK 1778
Cdd:TIGR00606 1057 QKL-EENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE---------PQFRDAEEKYREMMIVMRTTELVNK 1118
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
862-1690 |
1.03e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 63.91 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 862 EELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLAdaedRCDLLIKTkIQLEAKVKELMERLEDEEEMS 941
Cdd:TIGR00606 319 RELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIR----ARDSLIQS-LATRLELDGFERGPFSERQIK 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 942 ANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALTEAHQQTLDDLQAE 1021
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1022 EDKVNTLTKAKAKLEQ-----QVDDLEGSLEQEKKVRMDLERVRRKLEGDL------KLSLESVMDLENDKQQLEEKLKK 1090
Cdd:TIGR00606 474 LELDQELRKAERELSKaeknsLTETLKKEVKSLQNEKADLDRKLRKLDQEMeqlnhhTTTRTQMEMLTKDKMDKDEQIRK 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1091 KDFE-MNEISSRIED---EQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQRGDVARELEELSERLEEAGGATS 1166
Cdd:TIGR00606 554 IKSRhSDELTSLLGYfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCG 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1167 AQIEinkkrETDFLKLRRDLEEAMlHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLastveql 1246
Cdd:TIGR00606 634 SQDE-----ESDLERLKEEIEKSS-KQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDL------- 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1247 skgkatsEKMCRLYEDQMNEAKAKVDELQRQLNE----TNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEE 1322
Cdd:TIGR00606 701 -------QSKLRLAPDKLKSTESELKKKEKRRDEmlglAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETL 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1323 LKKQLEEENKAKSALAhslqssrhDCDLLREQYDEEQEAKAELQRALSKANAeVAQWRTKYETDaiQRTEELEEAKKKLV 1402
Cdd:TIGR00606 774 LGTIMPEEESAKVCLT--------DVTIMERFQMELKDVERKIAQQAAKLQG-SDLDRTVQQVN--QEKQEKQHELDTVV 842
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1403 TRLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLERanaaaaaldkkQRNFDKVLAEWKQKYEECQSELESSQKES 1482
Cdd:TIGR00606 843 SKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR-----------RQQFEEQLVELSTEVQSLIREIKDAKEQD 911
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1483 RGLSTELFKLKNSYEETLDHLETikrENKNLQEEIADLSDQISQGSKTIHELEK-MKKGLDMEKSDIQAALEEVEGTLEH 1561
Cdd:TIGR00606 912 SPLETFLEKDQQEKEELISSKET---SNKKAQDKVNDIKEKVKNIHGYMKDIENkIQDGKDDYLKQKETELNTVNAQLEE 988
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1562 EESKTLRIQLELNQIKADVDRKLAEKDEEIDNL-RRSHQRSMESMQTTLDAEAKSRNEAVRLRKKMEcdLNEMEVQLNHA 1640
Cdd:TIGR00606 989 CEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtLRKRENELKEVEEELKQHLKEMGQMQVLQMKQE--HQKLEENIDLI 1066
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1641 NRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLS 1690
Cdd:TIGR00606 1067 KRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELV 1116
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
857-1312 |
1.08e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 857 LAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDlalQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELMERLED 936
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELK---EAEEKEEEYAELQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 937 EEEMSAN--VLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKaltEAHQQT 1014
Cdd:COG4717 121 LEKLLQLlpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE---EELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1015 LDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMD--LENDKQQLEEKLKKKD 1092
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLalLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1093 FEMNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQRGDVARELEELSERLEEAGGATSAQIEIN 1172
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1173 KKREtdflklRRDLEEamlHHEATTAALRKKHADSVAELSEQIDSLQRvKQKLEKERSEAKMEVDDLASTVEQLSKGKAT 1252
Cdd:COG4717 358 ELEE------ELQLEE---LEQEIAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDE 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2045330442 1253 SEkmcrlYEDQMNEAKAKVDELQRQLNETNTQRARAQAE------SGEVGRKLEEREAMVSQLQRA 1312
Cdd:COG4717 428 EE-----LEEELEELEEELEELEEELEELREELAELEAEleqleeDGELAELLQELEELKAELREL 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1286-1935 |
1.16e-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: 63.93 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1286 ARAQAESGEVGRKLEEREAMVS----QLQRAKNSLTQNVEELKKQLEEENKAKSALAHSLQSSRHDCDLLREQYDEEQEA 1361
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDekrqQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1362 KAELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLE 1441
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1442 RANAAAAALDKKQRNFDKVLAEW-------KQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQ 1514
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRDKLteeyaelKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1515 EEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEGTLEheesktlriqlELNQIKADVDRKLAEKDEEIDNL 1594
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE-----------QLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1595 RRshqrsmesmqttldaeaksrneavRLRKKmECDLNEMEVQLnhanRQASESQKLLRNLQVQIKDIQLELDDTVHQNEE 1674
Cdd:TIGR02169 482 EK------------------------ELSKL-QRELAEAEAQA----RASEERVRGGRAVEEVLKASIQGVHGTVAQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1675 LKEQMALTerrnnLLSSEVEELRALLEQNDrarklaehelLEATERVNLLHSQNTGL-----INQKKKLESDLSTLSNE- 1748
Cdd:TIGR02169 533 VGERYATA-----IEVAAGNRLNNVVVEDD----------AVAKEAIELLKRRKAGRatflpLNKMRDERRDLSILSEDg 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1749 -VDDAVQ--ECRNAEEKA-KKAITDAAMMAE-ELKKEQDTSSHL-----ERMKKNMEQTVKDLQMRLDEAEQIALKGgkk 1818
Cdd:TIGR02169 598 vIGFAVDlvEFDPKYEPAfKYVFGDTLVVEDiEAARRLMGKYRMvtlegELFEKSGAMTGGSRAPRGGILFSRSEPA--- 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1819 QVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEAEEQAN 1898
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
650 660 670
....*....|....*....|....*....|....*..
gi 2045330442 1899 SNLTKYRKLQHELDDAEERADMAETQVNKLRVRTRDQ 1935
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS 791
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
848-1064 |
1.37e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 63.11 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 848 LRSAATEKELAALKEELAKLKEALEKSEVKRKELEEKQ--VSLIQEKNDLALQLQAEQDNLADAEDRcdlliktKIQLEA 925
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAE-------LAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 926 KVKELMERLEDEEEMSANVLAkkrklEDECSELKKDIDDLEITLAkvEKEKHATEN--KVKNLIEEMAALdetilkltke 1003
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL---------- 303
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2045330442 1004 KKALTEAHQQTLDDLQAEedkVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLE 1064
Cdd:COG3206 304 RAQLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1473-1943 |
1.47e-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: 63.12 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1473 SELESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAAL 1552
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1553 EEVEgtleheeSKTLRIQLELNQIKAdVDRKLAEKDEEIDNLRRSHQrsmeSMQTTLDAEAKSRNEAVRLRKKMECDLNE 1632
Cdd:TIGR04523 190 DKIK-------NKLLKLELLLSNLKK-KIQKNKSLESQISELKKQNN----QLKDNIEKKQQEINEKTTEISNTQTQLNQ 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1633 MEVQLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQmalteRRNNLLSseveELRALLEQNDRARKLAEH 1712
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ-----KEQDWNK----ELKSELKNQEKKLEEIQN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1713 ELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVddavqecrnaEEKAKKAitdaammaEELKKEQDtsSHLERmKK 1792
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESENSEKQREL----------EEKQNEI--------EKLKKENQ--SYKQE-IK 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1793 NMEQTVKDLQMRLDEAEQIAlkggkkqvQKLEARVKELENELEseqrksqeyqkvvrKYERRIKELSYQAEEDKKNLARL 1872
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLN--------QQKDEQIKKLQQEKE--------------LLEKEIERLKETIIKNNSEIKDL 445
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2045330442 1873 QDLIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQVNKLRVRTRDQVSKVSKLN 1943
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT 516
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1351-1906 |
2.27e-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: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1351 LREQYDEEQEAKAELQRALSKANAEVAQwrTKYETdAIQRTEELEEAKKKLVTRLQEAEESVEASNAKCSSLEKTKHRLQ 1430
Cdd:COG4913 260 LAERYAAARERLAELEYLRAALRLWFAQ--RRLEL-LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1431 TE-IEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDhleTIKRE 1509
Cdd:COG4913 337 GDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA---EAEAA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1510 NKNLQEEIADLSDQISqgsktihELEKMKKGLDmekSDIQAALEEVEGTLEHEESKtLRIQLELNQIKADvdrklaekDE 1589
Cdd:COG4913 414 LRDLRRELRELEAEIA-------SLERRKSNIP---ARLLALRDALAEALGLDEAE-LPFVGELIEVRPE--------EE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1590 E----IDNLRRSHQRSMesmqttL--DAEAKSRNEAV-RLRKKMECDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQ 1662
Cdd:COG4913 475 RwrgaIERVLGGFALTL------LvpPEHYAAALRWVnRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFR 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1663 LELDDTVHQN---------EELK-EQMALTerRNNLLSSEveelRALLEQNDRARKLAEHEL-LEATERVNLLHSQNTGL 1731
Cdd:COG4913 549 AWLEAELGRRfdyvcvdspEELRrHPRAIT--RAGQVKGN----GTRHEKDDRRRIRSRYVLgFDNRAKLAALEAELAEL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1732 INQKKKLESDLSTLSNEVdDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLERMKKNMeQTVKDLQMRLDEAEQi 1811
Cdd:COG4913 623 EEELAEAEERLEALEAEL-DALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQLEELEA- 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1812 ALKGGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIK-ELSYQAEEDKKNL---ARLQDLIDKLQAKVKSYK 1887
Cdd:COG4913 700 ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERFAAAlgdAVERELRENLEERIDALR 779
|
570
....*....|....*....
gi 2045330442 1888 RQAEEAEEQANSNLTKYRK 1906
Cdd:COG4913 780 ARLNRAEEELERAMRAFNR 798
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
848-1281 |
2.82e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.36 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 848 LRSAATEK--ELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQaeqdnlaDAEDRCDLLIKTKIQLEA 925
Cdd:PRK02224 354 LEERAEELreEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG-------NAEDFLEELREERDELRE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 926 KVKELMERLEDEEemsaNVLAKKRKLEDE--CSELKKDIDDLEITLAKVEKEKhatenKVKNLIEEMAALDETILKLtke 1003
Cdd:PRK02224 427 REAELEATLRTAR----ERVEEAEALLEAgkCPECGQPVEGSPHVETIEEDRE-----RVEELEAELEDLEEEVEEV--- 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1004 kkaltEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQ 1083
Cdd:PRK02224 495 -----EERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1084 LEEKLKKKDFEMNEISSRIE------DEQALVNQLHKKIKELQARteeleeeleadRASRAKVEKQRGDvareleelser 1157
Cdd:PRK02224 570 AREEVAELNSKLAELKERIEslerirTLLAAIADAEDEIERLREK-----------REALAELNDERRE----------- 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1158 leeaggatsaqiEINKKRETdflklRRDLEEAmlHHEATTAALRKKHA----------DSVAELSEQIDSLQR----VKQ 1223
Cdd:PRK02224 628 ------------RLAEKRER-----KRELEAE--FDEARIEEAREDKEraeeyleqveEKLDELREERDDLQAeigaVEN 688
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2045330442 1224 KLEkERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAK-VDELQRQLNET 1281
Cdd:PRK02224 689 ELE-ELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRnVETLERMLNET 746
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1205-1421 |
2.87e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1205 ADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKVDELQRQLNETNTQ 1284
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1285 RARAQAESGEVGRKLEEREAM-----------VSQLQRAKNSLTQNVEELKKQLEEENKAKSALAHSLQSSRHDCDLLRE 1353
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 1354 QYDEEQEAKAELQRALSKANAEVAQWRTKYETDAiQRTEELEEAKKKLVTRLQEAEESVEASNAKCSS 1421
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
975-1717 |
3.10e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 975 EKHATENKVKNLIEEMAALDETilkltkeKKALTEAHQQtLDDLQAEEDKVNTLTKAKAKLEQQVDDLEgsleqekkvRM 1054
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERA-------HEALEDAREQ-IELLEPIRELAERYAAARERLAELEYLRA---------AL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1055 DLERVRRKLEgdlklslesvmDLENDKQQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQArteeleeeleaDR 1134
Cdd:COG4913 282 RLWFAQRRLE-----------LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG-----------DR 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1135 ASRAKVEKQRgdvareleelserleeaggATSAQIEINKKREtDFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQ 1214
Cdd:COG4913 340 LEQLEREIER-------------------LERELEERERRRA-RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1215 IDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATsekmcrlYEDQMNEAKakvDELQRQLNETNTQ---------- 1284
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN-------IPARLLALR---DALAEALGLDEAElpfvgeliev 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1285 RARAQAESGEVGRKL----------EEREAMVSqlqRAKNSL-------TQNVEELKKQLEEENKAKSALAHSLQSSRHD 1347
Cdd:COG4913 470 RPEEERWRGAIERVLggfaltllvpPEHYAAAL---RWVNRLhlrgrlvYERVRTGLPDPERPRLDPDSLAGKLDFKPHP 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1348 C-----DLLREQYD----EEQEAKAELQRALSKAnAEVAQWRTKYE--------------TDAIQRTEELEEAKKKLVTR 1404
Cdd:COG4913 547 FrawleAELGRRFDyvcvDSPEELRRHPRAITRA-GQVKGNGTRHEkddrrrirsryvlgFDNRAKLAALEAELAELEEE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1405 LQEAEESVEASNAKCSSLEKTKHRLQ--TEIEDLVIDLERANAAaaaldkkqrnfdkvLAEWKQKYEecqsELESSQKES 1482
Cdd:COG4913 626 LAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAERE--------------IAELEAELE----RLDASSDDL 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1483 RGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEkmkkglDMEKSDIQAALEEVEGTLeHE 1562
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE------DLARLELRALLEERFAAA-LG 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1563 ESKTLRIQLELNQIKADVDRKLAEKDEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLRKKMECD-LNEMEVQLNHAN 1641
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDgLPEYEERFKELL 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1642 RQASESQK--LLRNLQVQIKDIQLELDDTvhqNEELKE---------QMALTERRNnllsSEVEELRALLEQNDRARKLA 1710
Cdd:COG4913 841 NENSIEFVadLLSKLRRAIREIKERIDPL---NDSLKRipfgpgrylRLEARPRPD----PEVREFRQELRAVTSGASLF 913
|
....*..
gi 2045330442 1711 EHELLEA 1717
Cdd:COG4913 914 DEELSEA 920
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1677-1905 |
3.68e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1677 EQMALTERRNNLLSSEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQEC 1756
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1757 RNAEEKAKKAITDAAMMAE----ELKKEQDTSSHLERMKKNMEQTVKDLQMRLDE--AEQIALKGGKKQVQKLEARVKEL 1830
Cdd:COG4942 100 EAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2045330442 1831 ENELESEQRK----SQEYQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAkvksykRQAEEAEEQANSNLTKYR 1905
Cdd:COG4942 180 LAELEEERAAlealKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA------EAAAAAERTPAAGFAALK 252
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
912-1606 |
3.68e-09 |
|
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: 61.91 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 912 RCDLLIKTKIQLEAKVKELMERLEDEEEMSANVLAKKRKLEDECSELKKDI----DDLEITLAKVEKEKHATENKVKNLI 987
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 988 EEMAALDETILKLTKEKKALTEAH--QQTLDDLQAEEDKVNTLTKAKAKLEQ-------------------QVDDLEGSL 1046
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAVLEETQErinrarkaaplaahikavtQIEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1047 EQEKKVRM-DLERVRRKLEGDLK--LSLESVMDLENDKQQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQART 1123
Cdd:TIGR00618 313 HTELQSKMrSRAKLLMKRAAHVKqqSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1124 EELeeeleadRASRAKVEKQRGDVARELEELSERLEEAGGATSAQIEINKKREtdflklRRDLEEAMLHHEATTAALRKK 1203
Cdd:TIGR00618 393 QKL-------QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQR------YAELCAAAITCTAQCEKLEKI 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1204 HADSVAE-LSEQIDSLQRVKQKLEKERSEAKMEvddlASTVEQLSKGKATSEKMCRLYEDQMNEAKAKVDELQRQLNETN 1282
Cdd:TIGR00618 460 HLQESAQsLKEREQQLQTKEQIHLQETRKKAVV----LARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1283 TQRARAQAESGEVGRKLEEREamvsQLQRAKNSLTQNVEELKKQLEEENKAKSALAHSLQSSRHDCDLLREQYDEEQEAK 1362
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERK----QRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1363 AELQRALSKANAEVAQWRTKYETDAIQRTEELEE-AKKKLVTRLQEAEESVEASNAKCSSLEKTKHR------LQTEIED 1435
Cdd:TIGR00618 612 CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLtALHALQLTLTQERVREHALSIRVLPKELLASRqlalqkMQSEKEQ 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1436 LVID---LERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELessQKESRGLSTELFKLKNSYEETLDHLETIKrENKN 1512
Cdd:TIGR00618 692 LTYWkemLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDL---AAREDALNQSLKELMHQARTVLKARTEAH-FNNN 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1513 LQEEIADLSDQisQGSKTIHELEKMKKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQLELNQIKADVDRKLAEKDEEID 1592
Cdd:TIGR00618 768 EEVTAALQTGA--ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLG 845
|
730
....*....|....
gi 2045330442 1593 NLRRSHQRSMESMQ 1606
Cdd:TIGR00618 846 EITHQLLKYEECSK 859
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1212-1915 |
4.59e-09 |
|
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: 61.91 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1212 SEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKVDELQRQLnETNTQRARAQAE 1291
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR-EAQEEQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1292 SGEVGRKLEEREAMVSQLQRAKNSLTQnveelkkqleeENKAKSALAHSLQSSRHDCDLlREQYDEEQEAKAELQRALSK 1371
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVLEETQERINR-----------ARKAAPLAAHIKAVTQIEQQA-QRIHTELQSKMRSRAKLLMK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1372 ANAEVAQwrtKYETDAIQRTEELEEAKKKLVTRLQEAEESVEASNAKCSSLEktkHRLQTEIEDLVIDLERANAAAAALD 1451
Cdd:TIGR00618 330 RAAHVKQ---QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT---QHIHTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1452 KKQRNFDKVLAEwKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQgSKTI 1531
Cdd:TIGR00618 404 ILQREQATIDTR-TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQT-KEQI 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1532 HELEKMKKGLDMEKSDIQAALE-EVEGTLEHEESKtlriqlelnQIKADVDRKLAEKDEEIDNLRRSHQRSMESMQTTLD 1610
Cdd:TIGR00618 482 HLQETRKKAVVLARLLELQEEPcPLCGSCIHPNPA---------RQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1611 AEaksrneavrlRKKMECDLNEME-----------------------------------VQLNHANRQASESQKLLRNLQ 1655
Cdd:TIGR00618 553 SE----------RKQRASLKEQMQeiqqsfsiltqcdnrskedipnlqnitvrlqdlteKLSEAEDMLACEQHALLRKLQ 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1656 VQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEElRALLEQNDRARKLAEHELLEATERVnlLHSQNTGL---I 1732
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVRE-HALSIRVLPKELLASRQLALQKMQS--EKEQLTYWkemL 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1733 NQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAITD----AAMMAEELKKEQDTS-SHLERMKKNMEQTVKDLQMRLDE 1807
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAredaLNQSLKELMHQARTVlKARTEAHFNNNEEVTAALQTGAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1808 AEQIAlkggkkqvQKLEARVKELENELESEQRKSQEYQKVVRKYErriKELSYQAEEDKKNLARLQDLIDKLQAKVKSYK 1887
Cdd:TIGR00618 780 LSHLA--------AEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE---DILNLQCETLVQEEEQFLSRLEEKSATLGEIT 848
|
730 740 750
....*....|....*....|....*....|.
gi 2045330442 1888 RQAEEAEE---QANSNLTKYRKLQHELDDAE 1915
Cdd:TIGR00618 849 HQLLKYEEcskQLAQLTQEQAKIIQLSDKLN 879
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1389-1848 |
4.99e-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: 61.24 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1389 QRTEELE-------EAKKKLV---TRLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFD 1458
Cdd:pfam05622 14 QRCHELDqqvsllqEEKNSLQqenKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1459 KVLAEWKQKYEEcqseLESSQKESRGLSTELFKLKNS-------------YEETLDHLETIKRENKNLQEEIADLSDQIS 1525
Cdd:pfam05622 94 KEVLELQHRNEE----LTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNAEYMQRTL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1526 QGSKTIHELEKMKKGLDMEKSDIQaaleEVEGTLEHEESKTLRIQLELNQIKADVDRKLAEKD----------EEIDNLR 1595
Cdd:pfam05622 170 QLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKErliierdtlrETNEELR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1596 RSHQRSMESMQTTLDAEAKSRNEAVRLRKKMECDLNEMEVQLNHANRQASESQKLlrNLQVQIKDIQLELDDTVHQNEEL 1675
Cdd:pfam05622 246 CAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEG--SYRERLTELQQLLEDANRRKNEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1676 KEQMALTERRNNLLSSEVEELRALLEQNDrarklaehelleatervnllhSQNTGLINQKKKLESDLSTLsNEVDDAVQE 1755
Cdd:pfam05622 324 ETQNRLANQRILELQQQVEELQKALQEQG---------------------SKAEDSSLLKQKLEEHLEKL-HEAQSELQK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1756 CRNA-EEKAKKAITDAAMMAEEL-----KKEQDTSSHLERMKKNMEQT---VKDLQMRLDEAEQIALKGGKKQVQKLEAR 1826
Cdd:pfam05622 382 KKEQiEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKAksvIKTLDPKQNPASPPEIQALKNQLLEKDKK 461
|
490 500
....*....|....*....|...
gi 2045330442 1827 VKELENELE-SEQRKSQEYQKVV 1848
Cdd:pfam05622 462 IEHLERDFEkSKLQREQEEKLIV 484
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1021-1930 |
5.22e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 61.60 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1021 EEDKVNTLTKAKAkLEQQVDDLEG------SLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQLEEKLKKKDFE 1094
Cdd:TIGR00606 158 QEDSNWPLSEGKA-LKQKFDEIFSatryikALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1095 mNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRasraKVEKQRGDVARELEELSERLEEAGGATSAQIEINKK 1174
Cdd:TIGR00606 237 -REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALK----SRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1175 R-----ETDFLKLRRDL-----EEAMLHHEATTAALRKK----HADSVAELSEQIDSL-QRVKQKLEKERSE----AKME 1235
Cdd:TIGR00606 312 RtvrekERELVDCQRELeklnkERRLLNQEKTELLVEQGrlqlQADRHQEHIRARDSLiQSLATRLELDGFErgpfSERQ 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1236 VDDLASTVEQLSKGKA-TSEKMCRLYEDQMNEAKAKVDELQrqlNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKN 1314
Cdd:TIGR00606 392 IKNFHTLVIERQEDEAkTAAQLCADLQSKERLKQEQADEIR---DEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEG 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1315 SLTQNVEELKKQLeeenKAKSALAHSLQSSRHDCDLLREQYdeEQEAKAELQRALSKANAEVAQWRTKYETdaiqRTEEL 1394
Cdd:TIGR00606 469 SSDRILELDQELR----KAERELSKAEKNSLTETLKKEVKS--LQNEKADLDRKLRKLDQEMEQLNHHTTT----RTQME 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1395 EEAKKKLVTRLQEAEESVEASNAKCS---------SLEKTKHRLQTEIEDLVIDLeranaaaaaldkkqRNFDKVLAEWK 1465
Cdd:TIGR00606 539 MLTKDKMDKDEQIRKIKSRHSDELTSllgyfpnkkQLEDWLHSKSKEINQTRDRL--------------AKLNKELASLE 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1466 QKYEECQSELESSQKESRGLSTELFKLKNSYEETLDhLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEK 1545
Cdd:TIGR00606 605 QNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESD-LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVC 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1546 SDIQAALEEVEGTLEHEESKTLRIQLELNQIKADVDRKLAEKDEEIDnlrrshqrSMESMQTTLDAEAKSRNEAVRLRKK 1625
Cdd:TIGR00606 684 QRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLG--------LAPGRQSIIDLKEKEIPELRNKLQK 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1626 MECDLNEMEVQLnhanrqaSESQKLLRNLQVQIKDIQLELDDtVHQNEELKEQMALTERRNNLLSSEVE--ELRALLEQN 1703
Cdd:TIGR00606 756 VNRDIQRLKNDI-------EEQETLLGTIMPEEESAKVCLTD-VTIMERFQMELKDVERKIAQQAAKLQgsDLDRTVQQV 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1704 DRARKLAEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNE---VDDAVQECRNAEEKAKKAITDAAMMAEELKKE 1780
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEklqIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA 907
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1781 QDTSSHLERMKKNMEQTVKDLQMRLDEAEQIA---LKGGKKQVQKLEARVKELENELEsEQRKSQEYQKvvrkyERRIKE 1857
Cdd:TIGR00606 908 KEQDSPLETFLEKDQQEKEELISSKETSNKKAqdkVNDIKEKVKNIHGYMKDIENKIQ-DGKDDYLKQK-----ETELNT 981
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2045330442 1858 LSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQaeeaEEQANSNLTKyRKLQHELDDAEERADMAETQVNKLRV 1930
Cdd:TIGR00606 982 VNAQLEECEKHQEKINEDMRLMRQDIDTQKIQ----ERWLQDNLTL-RKRENELKEVEEELKQHLKEMGQMQV 1049
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1208-1848 |
5.94e-09 |
|
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: 61.30 E-value: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1208 VAELSEQIDSLQRVKQKLEKERSEAKMEvddlastveqLSKGKATSEKMCRLYEDQMNEAKAKVDELQRQLNETNTQRaR 1287
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIE----------LEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEAL-R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1288 AQAE--------SGEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKAKSALAHSLQSSRHDCDLLREQYDEEQ 1359
Cdd:pfam05557 73 EQAElnrlkkkyLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1360 EAKAELQRALSKANAEVAQWRT------KYETDAiqrtEELEEAKKKL--VTRLQEAEESVEASNAKCSSLEKTKHRLQT 1431
Cdd:pfam05557 153 QLRQNLEKQQSSLAEAEQRIKElefeiqSQEQDS----EIVKNSKSELarIPELEKELERLREHNKHLNENIENKLLLKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1432 EIEDLVIDLERanaaaaaldkkqrnfdkvlaewkqkYEECQSELESSQKESRGLSTEL---FKLKNSYEETLDHLETIKR 1508
Cdd:pfam05557 229 EVEDLKRKLER-------------------------EEKYREEAATLELEKEKLEQELqswVKLAQDTGLNLRSPEDLSR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1509 ENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQlelnqikadvdRKLAEKD 1588
Cdd:pfam05557 284 RIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ-----------RRVLLLT 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1589 EEIDNLR---RSHQRSMeSMQTTLDAEAKSRNEAVRLRKKMECDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQlel 1665
Cdd:pfam05557 353 KERDGYRailESYDKEL-TMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALR--- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1666 ddtvhQNEELKEQMALTERRNNlLSSEVEELRAlleQNDRARKlaEHELLEaterVNLLHSQNTGLINQKKKLESDLStl 1745
Cdd:pfam05557 429 -----QQESLADPSYSKEEVDS-LRRKLETLEL---ERQRLRE--QKNELE----MELERRCLQGDYDPKKTKVLHLS-- 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1746 SNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSSHL-ERMKKNMEQTVKDLQMRLDEAEqialkggkKQVQKLE 1824
Cdd:pfam05557 492 MNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLpETTSTMNFKEVLDLRKELESAE--------LKNQRLK 563
|
650 660
....*....|....*....|....
gi 2045330442 1825 arvkelenelESEQRKSQEYQKVV 1848
Cdd:pfam05557 564 ----------EVFQAKIQEFRDVC 577
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
922-1145 |
6.18e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 922 QLEAKVKELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLT 1001
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1002 KEKKALTEAHQ----QTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDL 1077
Cdd:COG4942 104 EELAELLRALYrlgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1078 ENDKQQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQA--RTEELEEELEADRASRAKVEKQRG 1145
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAliARLEAEAAAAAERTPAAGFAALKG 253
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
854-1546 |
6.45e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.19 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 854 EKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELMER 933
Cdd:TIGR04523 53 EKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 934 LEDEEEMSANVLAKKRKLEDECSELKKDIDDLEitlakveKEKHATENKVKNLIEEMAALDETILKLTKEKKALteahQQ 1013
Cdd:TIGR04523 133 KKENKKNIDKFLTEIKKKEKELEKLNNKYNDLK-------KQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL----EL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1014 TLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESvmdLENDKQQLEEKLKkkdf 1093
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE---QNKIKKQLSEKQK---- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1094 EMNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQRgdvareleelserleeaggaTSAQIEINK 1173
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEE--------------------IQNQISQNN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1174 KRETDFLKLRRDLEEAMLHHEATTAalrkkhadsvaELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATS 1253
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENS-----------EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1254 EKMCRLYEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVeelkkqleeenka 1333
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL------------- 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1334 kSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSKANAEVAQWrTKYETDAIQRTEELEEAKKKLVTRLQEAEESVE 1413
Cdd:TIGR04523 471 -KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL-TKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1414 A--SNAKCSSLEKTKHRLQTEIEDLVID----LERANAAAAALDKKQRNFDKV---LAEWKQKYEECQSELESSQKESRG 1484
Cdd:TIGR04523 549 KddFELKKENLEKEIDEKNKEIEELKQTqkslKKKQEEKQELIDQKEKEKKDLikeIEEKEKKISSLEKELEKAKKENEK 628
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2045330442 1485 LSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKS 1546
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELS 690
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1340-1881 |
6.92e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1340 SLQSSRHDCDLLREQYDEEQEAKAELQRALSKANAEVAQWRtkyetdaiQRTEELEEAKKKLVTRLQEAEESVEASNAKC 1419
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR--------EELETLEAEIEDLRETIAETEREREELAEEV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1420 SSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQKESRGLSTELFKLKNSYEEt 1499
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1500 ldhletIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQLELNQIKAD 1579
Cdd:PRK02224 361 ------LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1580 VdRKLAEKDEEIDNLRRShQRSMESMQTTLDAEAKSRNEAVRLRK-KMECDLNEMEVQLNHANrQASESQKLLRNLQVQI 1658
Cdd:PRK02224 435 L-RTARERVEEAEALLEA-GKCPECGQPVEGSPHVETIEEDRERVeELEAELEDLEEEVEEVE-ERLERAEDLVEAEDRI 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1659 KDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTGLINQKKKL 1738
Cdd:PRK02224 512 ERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1739 EsDLSTLSNEVDDAVQECRNAEEKAKkaitDAAMMAEELKkeqdtsshlERMKKNMEQtVKDLQMRLDEAeqiALKGGKK 1818
Cdd:PRK02224 592 E-RIRTLLAAIADAEDEIERLREKRE----ALAELNDERR---------ERLAEKRER-KRELEAEFDEA---RIEEARE 653
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2045330442 1819 QVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELsyqaEEDKKNLARLQDLIDKLQA 1881
Cdd:PRK02224 654 DKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL----EELRERREALENRVEALEA 712
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
849-1319 |
7.16e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 849 RSAATEKELAALKEELAKLKEaLEKSEVKRKELEEKQVSLIQEKNDLAL-------QLQAEQDNLADAEDRCDLLIKTKI 921
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKrlsrleeEINGIEERIKELEEKEERLEELKK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 922 QLEaKVKELMERLEDEEEMSANVLAKKRKLEDECSELK-KDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKL 1000
Cdd:PRK03918 346 KLK-ELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1001 TKEKKALTEAHQQ--TLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLS-LESVMD- 1076
Cdd:PRK03918 425 KKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIkLKELAEq 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1077 LENDKQQLE----EKLKKKDFE---MNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEadrasraKVEKQRGDVAR 1149
Cdd:PRK03918 505 LKELEEKLKkynlEELEKKAEEyekLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD-------ELEEELAELLK 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1150 ELEELSERLEEAGGATSAQIEINKKRETDFLKLRRDLEEAmlhhEATTAALRKKHADSVAELSEQIDSLQRVKQKL-EKE 1228
Cdd:PRK03918 578 ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELERE----EKELKKLEEELDKAFEELAETEKRLEELRKELeELE 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1229 RSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKVDELQRQLNEtntqRARAQAESGEVGRKLEEREAMVSQ 1308
Cdd:PRK03918 654 KKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE----REKAKKELEKLEKALERVEELREK 729
|
490
....*....|.
gi 2045330442 1309 LQRAKNSLTQN 1319
Cdd:PRK03918 730 VKKYKALLKER 740
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
943-1610 |
7.20e-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: 60.80 E-value: 7.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 943 NVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEtilKLTKEKKALTEAHQqtldDLQAEE 1022
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLND---KLKKNKDKINKLNS----DLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1023 DKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQLEEKLKKKDFEMNEISSRI 1102
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1103 EDEQALVNQLHKKIKELQArteeleeeleadrasraKVEKQRGDVARELEELSERLEEAGGATSAQIEINKKrETDFLKL 1182
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKK-----------------KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK-TTEISNT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1183 RRDLEEamlhheattaaLRKKHADSVAELSEQIDSLQRVKQK---LEKERSEAKMEVDDLASTVEQ-----LSKGKATSE 1254
Cdd:TIGR04523 252 QTQLNQ-----------LKDEQNKIKKQLSEKQKELEQNNKKikeLEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1255 KMCRLYEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELkkqleeeNKAK 1334
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL-------ESQI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1335 SALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSKANAEVAQwrtkyETDAIQRTEELEEAKKKLVTRL----QEAEE 1410
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK-----NNSEIKDLTNQDSVKELIIKNLdntrESLET 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1411 SVEASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQKESRGLSTELF 1490
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1491 KL-----KNSYEETLDHL-----------ETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEE 1554
Cdd:TIGR04523 549 KDdfelkKENLEKEIDEKnkeieelkqtqKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 2045330442 1555 VEGTLEHEESKTLRIQLELNQIKADVDRKLAEKDEEIDNLRRSHQRSMESMQTTLD 1610
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKD 684
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1337-1943 |
1.54e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.92 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1337 LAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSKANAEVAQWRTKYE--TDAIQRTEELEEAKKKLVTRLQEAEESVEA 1414
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1415 SNAKCSSLEKTKHRLQtEIEDLVIDLERANAAAAALDKKQrnfdkvLAEWKQKYEECQSELESSQKESRGLStELFKLKN 1494
Cdd:PRK01156 268 ELEKNNYYKELEERHM-KIINDPVYKNRNYINDYFKYKND------IENKKQILSNIDAEINKYHAIIKKLS-VLQKDYN 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1495 SYEETldhletiKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQLELN 1574
Cdd:PRK01156 340 DYIKK-------KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1575 QIKADVDR---KLAEKDEEIDNLRrSHQRSMESMQTTLDAEAKSRNEAVRLRKKMECDLnemevqLNHANRQASESQKLL 1651
Cdd:PRK01156 413 EINVKLQDissKVSSLNQRIRALR-ENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHI------INHYNEKKSRLEEKI 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1652 RNLQVQIKDIqlelddtvhqNEELKEQMALTERrnnLLSSEVEELrallEQNDRARKLAEHELleatervnllhsqntgl 1731
Cdd:PRK01156 486 REIEIEVKDI----------DEKIVDLKKRKEY---LESEEINKS----INEYNKIESARADL----------------- 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1732 inqkKKLESDLSTLsnevddavqecRNAEEKAKKAITD-AAMMAEELkkEQDTSSHLERMKKNMEQTVKDLQMRLDEAeq 1810
Cdd:PRK01156 532 ----EDIKIKINEL-----------KDKHDKYEEIKNRyKSLKLEDL--DSKRTSWLNALAVISLIDIETNRSRSNEI-- 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1811 ialkggKKQVQKLEARVKELENELESEQrksqeyqKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQA 1890
Cdd:PRK01156 593 ------KKQLNDLESRLQEIEIGFPDDK-------SYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQI 659
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2045330442 1891 EEAEE----------QANSNLTKYRKLQHELDDAEERADMAETQVNKLRVRTRDQVSKVSKLN 1943
Cdd:PRK01156 660 AEIDSiipdlkeitsRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDIN 722
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1350-1692 |
1.55e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 59.52 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1350 LLREQYDEEQEAKAELQRALSKANAEVAQWRTKYETDaiqrTEELEEAKKKLVTRLQEAEESVEASNAKCSSLEK----- 1424
Cdd:pfam07888 31 LLQNRLEECLQERAELLQAQEAANRQREKEKERYKRD----REQWERQRRELESRVAELKEELRQSREKHEELEEkykel 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1425 --------------------TKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEE---CQSELESSQKE 1481
Cdd:pfam07888 107 sasseelseekdallaqraaHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAErkqLQAKLQQTEEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1482 SRGLSTELFKLKNSYEETLDHLETikrenknLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEG---T 1558
Cdd:pfam07888 187 LRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGlgeE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1559 LEHEESKTLRIQLELNQIK---ADVDRKLAEKDEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLRKKMECDLNE--- 1632
Cdd:pfam07888 260 LSSMAAQRDRTQAELHQARlqaAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEerm 339
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 1633 ----MEVQLNH---ANR-QASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSE 1692
Cdd:pfam07888 340 erekLEVELGRekdCNRvQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADA 407
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
851-1229 |
2.30e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 851 AATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQekndlALQLQAEQDNLADAEDRCDlliktkiqleakvkEL 930
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQR-----LAEYSWDEIDVASAEREIA--------------EL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 931 MERLEDEEEMSANVlakkRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKaltEA 1010
Cdd:COG4913 674 EAELERLDASSDDL----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR---LE 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1011 HQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKvrmDLERVRRK-------LEGDLKLSLESVMD------- 1076
Cdd:COG4913 747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE---ELERAMRAfnrewpaETADLDADLESLPEylalldr 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1077 LENDK-QQLEEKLKK--KDFEMNEISsriedeqALVNQLHKKIKELQARTeeleeeleaDR--ASRAKVEKQRGdvarel 1151
Cdd:COG4913 824 LEEDGlPEYEERFKEllNENSIEFVA-------DLLSKLRRAIREIKERI---------DPlnDSLKRIPFGPG------ 881
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 1152 eelserleeaggaTSAQIEINKKRETDFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKER 1229
Cdd:COG4913 882 -------------RYLRLEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRSEEEESDRRWRAR 946
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
843-1025 |
2.89e-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: 56.47 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 843 KIKPLLRSAATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRcdlliktkiq 922
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 923 lEAKVKELMERLEDEEEMSAnvlakkrkLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTK 1002
Cdd:COG1579 75 -IKKYEEQLGNVRNNKEYEA--------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
170 180
....*....|....*....|...
gi 2045330442 1003 EKKALTEAHQQTLDDLQAEEDKV 1025
Cdd:COG1579 146 ELDEELAELEAELEELEAEREEL 168
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
948-1533 |
3.30e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 948 KRKLEDECSELKKDIDDLEITLAKVEKEKHATE--NKVKNLIEEMAALDETILKLTKEKKALT-EAHQQTLDDLQAEEDK 1024
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1025 vntLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLES-VMDLENDKQQLEEKLKKKDFEMNEISSRIE 1103
Cdd:COG4913 300 ---LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEReIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1104 DEQALVNQLHKKIKELQARTEELEEELEADRAS-RAKVEKQRGDVAreleelserleeaggATSAQIEINKKRET----D 1178
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEALAEaEAALRDLRRELR---------------ELEAEIASLERRKSnipaR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1179 FLKLRRDLEEAM------------------------------LHHEATTAALRKKHADSVAELSEQIDSLQRVK-QKLEK 1227
Cdd:COG4913 442 LLALRDALAEALgldeaelpfvgelievrpeeerwrgaiervLGGFALTLLVPPEHYAAALRWVNRLHLRGRLVyERVRT 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1228 ERSEAKMEVDDLASTVEQLS-KGKATSEKMCRLYEDQMNEAK-AKVDELQRqlnetnTQRA-------RAQAESGEVG-- 1296
Cdd:COG4913 522 GLPDPERPRLDPDSLAGKLDfKPHPFRAWLEAELGRRFDYVCvDSPEELRR------HPRAitragqvKGNGTRHEKDdr 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1297 --------------RKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKAKSALAHSLQSSRHDCDLlrEQYDEEQEAK 1362
Cdd:COG4913 596 rrirsryvlgfdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV--ASAEREIAEL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1363 AELQRALSKANAEVaqwrtkyetdaiqrtEELEEAKKKLVTRLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLER 1442
Cdd:COG4913 674 EAELERLDASSDDL---------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1443 ANAAAAA------------------LDKKQRNFDKVLAEWKQKYEECQSELESSQKE--------SRGLSTELfklkNSY 1496
Cdd:COG4913 739 AEDLARLelralleerfaaalgdavERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaeTADLDADL----ESL 814
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1497 EETLDHLETIKRE-------------NKNLQEEIADLSDQISQGSKTIHE 1533
Cdd:COG4913 815 PEYLALLDRLEEDglpeyeerfkellNENSIEFVADLLSKLRRAIREIKE 864
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1627-1864 |
3.32e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1627 ECDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQndRA 1706
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--RA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1707 RKLAEHELLEATERVnLLHSQNTG-LINQkkklESDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTss 1785
Cdd:COG3883 93 RALYRSGGSVSYLDV-LLGSESFSdFLDR----LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE-- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2045330442 1786 hLERMKKNMEQTVKDLQMRLDEAEQialkggkkQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEE 1864
Cdd:COG3883 166 -LEAAKAELEAQQAEQEALLAQLSA--------EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1466-1685 |
5.33e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1466 QKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEK 1545
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1546 SDIQAALEEVEGTLeHEESKTLRIQLELNQIKA-DVDRKLaekdEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLRK 1624
Cdd:COG4942 100 EAQKEELAELLRAL-YRLGRQPPLALLLSPEDFlDAVRRL----QYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2045330442 1625 KMECDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERR 1685
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
922-1319 |
8.23e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 57.21 E-value: 8.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 922 QLEAKVKELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLT 1001
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1002 KEKKALTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDK 1081
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1082 QQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQRGDVAreleelserlEEA 1161
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS----------SMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1162 GGATSAQIEINKKR-ETDFLKLR-RDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDL 1239
Cdd:pfam07888 265 AQRDRTQAELHQARlQAAQLTLQlADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1240 ASTVEQlskgkatsEKMCRLYedQMNEAKAKVDELQRQLNETNTQRARAQAESGEV---GRKLEEREAMVSQLQRAKNSL 1316
Cdd:pfam07888 345 EVELGR--------EKDCNRV--QLSESRRELQELKASLRVAQKEKEQLQAEKQELleyIRQLEQRLETVADAKWSEAAL 414
|
...
gi 2045330442 1317 TQN 1319
Cdd:pfam07888 415 TST 417
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1357-1931 |
8.27e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.42 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1357 EEQEAKAELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKK---------------------KLVTRLQEAEESVEAS 1415
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKiieaqrkaiqelqfenekvslKLEEEIQENKDLIKEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1416 NAK---CSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKkqrNFDKVLAewkqKYEECQSELESSQKESRglstelFKL 1492
Cdd:pfam05483 151 NATrhlCNLLKETCARSAEKTKKYEYEREETRQVYMDLNN---NIEKMIL----AFEELRVQAENARLEMH------FKL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1493 KNSYEEtLDHLEtikrenKNLQEEIADLSDQISQGSKTIHELE-KMKkgldmeksDIQAALEEVEGTLEHEESKTlriQL 1571
Cdd:pfam05483 218 KEDHEK-IQHLE------EEYKKEINDKEKQVSLLLIQITEKEnKMK--------DLTFLLEESRDKANQLEEKT---KL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1572 ELNQIKADVDRKlAEKDEEIDNLRRSHQRSMeSMQTTLDaeaksrnEAVRLRKKMECDLNE-MEVQLNHANRQASESQKL 1650
Cdd:pfam05483 280 QDENLKELIEKK-DHLTKELEDIKMSLQRSM-STQKALE-------EDLQIATKTICQLTEeKEAQMEELNKAKAAHSFV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1651 LRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRAL-----LEQNDRARKLAEHE-LLEATERVNLL 1724
Cdd:pfam05483 351 VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFknnkeVELEELKKILAEDEkLLDEKKQFEKI 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1725 HSQNTGlinQKKKLESDLSTLSNEVDD---AVQECRNAEEKAKKAITDaamMAEELKKEQ----DTSSHLERM---KKNM 1794
Cdd:pfam05483 431 AEELKG---KEQELIFLLQAREKEIHDleiQLTAIKTSEEHYLKEVED---LKTELEKEKlkniELTAHCDKLlleNKEL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1795 EQTVKDLQMRLdEAEQIALKGGKKQVQKLearVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQD 1874
Cdd:pfam05483 505 TQEASDMTLEL-KKHQEDIINCKKQEERM---LKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEY 580
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 2045330442 1875 LIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQVNKLRVR 1931
Cdd:pfam05483 581 EVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIK 637
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1168-1724 |
8.58e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 8.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1168 QIEINKKRETDFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSE----QIDSLQRVKQKLEKERSEAKMEVDDLASTV 1243
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1244 EQLSKGKATSEKMcrlYEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEel 1323
Cdd:COG4913 369 AALGLPLPASAEE---FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL-- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1324 kkqleeenKAKSALAHSLQSSRHD----CDLLrEQYDEEQEAKAELQRAL----------SKANAEVAQW------RTKY 1383
Cdd:COG4913 444 --------ALRDALAEALGLDEAElpfvGELI-EVRPEEERWRGAIERVLggfaltllvpPEHYAAALRWvnrlhlRGRL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1384 ETDAIQRTEELEEAKK--------KLVTRLQEAEESVEASNA------KCSSLE------------------KTKHRLQT 1431
Cdd:COG4913 515 VYERVRTGLPDPERPRldpdslagKLDFKPHPFRAWLEAELGrrfdyvCVDSPEelrrhpraitragqvkgnGTRHEKDD 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1432 EI---EDLVIDlERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQKESRGLStelfKLKNSYEETLDHLEtikr 1508
Cdd:COG4913 595 RRrirSRYVLG-FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ----RLAEYSWDEIDVAS---- 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1509 enknLQEEIADLSDQISQGSKTIHELEKMKKGLDmeksDIQAALEEVEGTLEheesktlriqlELNQIKADVDRKLAEKD 1588
Cdd:COG4913 666 ----AEREIAELEAELERLDASSDDLAALEEQLE----ELEAELEELEEELD-----------ELKGEIGRLEKELEQAE 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1589 EEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLRKKMECDLNEMEVQLNHANRQASESQKLLRNLQVQIK----DIQLE 1664
Cdd:COG4913 727 EELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNrewpAETAD 806
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2045330442 1665 LDDTVHQNEELKEQmaLTE-RRNNLLSSEVEELRALLEQNDR-----ARKLAEhELLEATERVNLL 1724
Cdd:COG4913 807 LDADLESLPEYLAL--LDRlEEDGLPEYEERFKELLNENSIEfvadlLSKLRR-AIREIKERIDPL 869
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
847-1374 |
2.47e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.88 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 847 LLRSAATEKE---------LAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLI 917
Cdd:pfam05483 244 LLLIQITEKEnkmkdltflLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAT 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 918 KTKIQLEAKVKELMERLEDEE--------EMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEE 989
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKaahsfvvtEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 990 MAALDETILKLTKEKKALTEAHQ--QTLDDLQAEEDKVNTLTKAKaklEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDL 1067
Cdd:pfam05483 404 EVELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQELIFLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1068 KLSLESVMDLENDKQQLEEKLKKKDFEMNEISSRIEDEQALVN----QLHKKIKELQARTEELEEELEADRASRAKVEKQ 1143
Cdd:pfam05483 481 EKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIInckkQEERMLKQIENLEEKEMNLRDELESVREEFIQK 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1144 RGDVARELEELSERLEEAGGATSAQIEINKKRETDFLKLRRDLEEAM-----LHHEatTAALRKKhadSVAElSEQIDSL 1218
Cdd:pfam05483 561 GDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNknieeLHQE--NKALKKK---GSAE-NKQLNAY 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1219 QRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKmcRLYEdQMNEAKAKVDELQRQLNETNTqraRAQAESGEVGRK 1298
Cdd:pfam05483 635 EIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEE--KLLE-EVEKAKAIADEAVKLQKEIDK---RCQHKIAEMVAL 708
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2045330442 1299 LEEREAMVSQLQRAKNSltqNVEELKKQLEEENKAKSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRALSKANA 1374
Cdd:pfam05483 709 MEKHKHQYDKIIEERDS---ELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTA 781
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1364-1783 |
2.68e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1364 ELQRALSKANAEVAQWRTKYET--DAIQRTEELEEAKKKLVTRLQEAEESVEASnakcsSLEKTKHRLQTEIEDLVIDLE 1441
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEEleELEEELEELEAELEELREELEKLEKLLQLL-----PLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1442 RANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQKESRGlstELFKLKNSYEETLDHLETIKRENKNLQEEIADLS 1521
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1522 DQISQGSKTiHELEKMKKGLDMEKSD--IQAALEEVEGTLEHEESKTLRI-------------QLELNQIKADVDRKLAE 1586
Cdd:COG4717 227 EELEQLENE-LEAAALEERLKEARLLllIAAALLALLGLGGSLLSLILTIagvlflvlgllalLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1587 KDEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLRKKMECDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQLELD 1666
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1667 DTVHQNEELKEQMALTERRNNL---LSSEVEELRALLEQNDRAR-----KLAEHELLEATERVNLLHSQNTGLINQKKKL 1738
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELeeqLEELLGELEELLEALDEEEleeelEELEEELEELEEELEELREELAELEAELEQL 465
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2045330442 1739 ESD--LSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDT 1783
Cdd:COG4717 466 EEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1479-1864 |
3.89e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.13 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1479 QKESRGLSTELFKLKNSYeetldhleTIKRENKNLQE-EIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEG 1557
Cdd:pfam17380 239 RKESFNLAEDVTTMTPEY--------TVRYNGQTMTEnEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1558 TLEH----EESKTLRiQLELNQ---IKADVDRKLAEKDEEIDNLRRS-HQRSMESMqttldaeaKSRNEAVRLRKKMECD 1629
Cdd:pfam17380 311 EVERrrklEEAEKAR-QAEMDRqaaIYAEQERMAMERERELERIRQEeRKRELERI--------RQEEIAMEISRMRELE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1630 LNEMEVQL-NHANRQ---ASESQKLL-RNLQVQIKDIQLELDDTVHQNEELKEqmalterrnnllssevEELRALLEQND 1704
Cdd:pfam17380 382 RLQMERQQkNERVRQeleAARKVKILeEERQRKIQQQKVEMEQIRAEQEEARQ----------------REVRRLEEERA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1705 RARKLAEHELLEATERVNLLHSQNTGliNQKKKLEsdlstlsneVDDAVQECRNAEEKAKKaitdaaMMAEELKKEQDTS 1784
Cdd:pfam17380 446 REMERVRLEEQERQQQVERLRQQEEE--RKRKKLE---------LEKEKRDRKRAEEQRRK------ILEKELEERKQAM 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1785 SHLERMKKNMEQTVKDLQMRLDEAEQ--IALKGGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQA 1862
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAIYEEERrrEAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
|
..
gi 2045330442 1863 EE 1864
Cdd:pfam17380 589 AE 590
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1535-1913 |
6.19e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 54.91 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1535 EKMKKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQLELNQIKA----DVDRKLAEKDEEIDNLRRSHQRSMESMQTTLD 1610
Cdd:PLN02939 48 KKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTssddDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1611 AEAKSRNEAVRLRKKMECDLNEMEVQ-LNHANRQASESQKLlrnlQVQIKDIQLELDDTVHQNEELKEQMALTErrnnLL 1689
Cdd:PLN02939 128 FQLEDLVGMIQNAEKNILLLNQARLQaLEDLEKILTEKEAL----QGKINILEMRLSETDARIKLAAQEKIHVE----IL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1690 SSEVEELRALLEQNDRARKLAEHELleaTERVNLLHSQNTGLINQKKKLESDLStlsnevddavqECRNAEEKAKKaitd 1769
Cdd:PLN02939 200 EEQLEKLRNELLIRGATEGLCVHSL---SKELDVLKEENMLLKDDIQFLKAELI-----------EVAETEERVFK---- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1770 aammaeelkkeqdtsshLERMKKNMEQTVKDLQMRLDEAEQIALKGGKKQVQKLEARVKELENELESEQRKSQEYQKVVR 1849
Cdd:PLN02939 262 -----------------LEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLD 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 1850 KY---ERRIKELSYQAEEdkKNLARLQ-DLIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDD 1913
Cdd:PLN02939 325 QNqdlRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQD 390
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
867-1601 |
6.75e-07 |
|
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: 54.84 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 867 LKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLIKtkiqleaKVKELMERLEDEEEMSANVLA 946
Cdd:pfam12128 214 PKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHF-------GYKSDETLIASRQEERQETSA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 947 KKRkledecSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALTEAHQQTLDDLQAE----E 1022
Cdd:pfam12128 287 ELN------QLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSElenlE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1023 DKVNTLTKAKAKLEQQVDDLEGSLEQEKKVrmDLERVRRKL----EGDLKLSLESVMDLENDKQQLEEKLKKKDFEMNE- 1097
Cdd:pfam12128 361 ERLKALTGKHQDVTAKYNRRRSKIKEQNNR--DIAGIKDKLakirEARDRQLAVAEDDLQALESELREQLEAGKLEFNEe 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1098 ---ISSRIEDEQALVNQLHKKIKELQARTEELEEELEADR---ASRAKVEKQRGDVARELEELSERLEEAGGATSAQIEi 1171
Cdd:pfam12128 439 eyrLKSRLGELKLRLNQATATPELLLQLENFDERIERAREeqeAANAEVERLQSELRQARKRRDQASEALRQASRRLEE- 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1172 nKKRETDFLKLRRDLEEAMLHHeattaALRKKHADSVAELSEQIDSLQRVKQKLEKERSEA----------------KME 1235
Cdd:pfam12128 518 -RQSALDELELQLFPQAGTLLH-----FLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGsvggelnlygvkldlkRID 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1236 VDDLASTVEQLSKGKATSEK-------MCRLYEDQMNEAKAKVDELQRQlnETNTQRARAQAESgEVGRKLEEREAMVSQ 1308
Cdd:pfam12128 592 VPEWAASEEELRERLDKAEEalqsareKQAAAEEQLVQANGELEKASRE--ETFARTALKNARL-DLRRLFDEKQSEKDK 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1309 LQRAknsLTQNVEELKKQLEEENKAKSALAHSLQS-SRHDCDLLREQYDEEQEAKAELQRALSKANAEVAQWRTKYETDA 1387
Cdd:pfam12128 669 KNKA---LAERKDSANERLNSLEAQLKQLDKKHQAwLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGA 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1388 IQRTEELEEAKKKLVTRLQEAEESVEasnakcsslektkhRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQK 1467
Cdd:pfam12128 746 KAELKALETWYKRDLASLGVDPDVIA--------------KLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPR 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1468 YEECQSELESSQKESRGlstELFKLKnsyeetldhlETIKRENKNLQEEIADLSDQisqgsktIHELEKMKKGLDMEKSD 1547
Cdd:pfam12128 812 LATQLSNIERAISELQQ---QLARLI----------ADTKLRRAKLEMERKASEKQ-------QVRLSENLRGLRCEMSK 871
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 2045330442 1548 I-QAALEEVEGTLEHEESKTLRIQLELNQIKADVDRKLAEKDEEIDNLRRSHQRS 1601
Cdd:pfam12128 872 LaTLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADHSGS 926
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
656-683 |
9.33e-07 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 50.81 E-value: 9.33e-07
10 20
....*....|....*....|....*...
gi 2045330442 656 SQLHKENLNKLMTNLRSTQPHFVRCIIP 683
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1479-1928 |
9.36e-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: 54.06 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1479 QKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQI---SQGSKTIHELEKMKKGLdmekSDIQAALEEV 1555
Cdd:pfam10174 122 QSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLqskGLPKKSGEEDWERTRRI----AEAEMQLGHL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1556 EGTLEHEESKTLRIQLEL---NQIKADVDRKLA------EKDEEIDNLRRSHQRSMESMQTTldaeaksRNEAVRLRKKM 1626
Cdd:pfam10174 198 EVLLDQKEKENIHLREELhrrNQLQPDPAKTKAlqtvieMKDTKISSLERNIRDLEDEVQML-------KTNGLLHTEDR 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1627 ECDLNEMEVQLNHANRQASESQKLLRNLQ---VQIKDIQLELDDTVHQN-------EELKEQMALTERRNNLLSSEVEEL 1696
Cdd:pfam10174 271 EEEIKQMEVYKSHSKFMKNKIDQLKQELSkkeSELLALQTKLETLTNQNsdckqhiEVLKESLTAKEQRAAILQTEVDAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1697 RALLEQNDRARKLAEHELLEATERVNLL-----HSQNTGLINQKK--KLESDLSTLSNEVDDAVQECRNAEEKAKKAITD 1769
Cdd:pfam10174 351 RLRLEEKESFLNKKTKQLQDLTEEKSTLageirDLKDMLDVKERKinVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTD 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1770 AAMMAEELKKEQDTSSHLERMKKNM-EQTVKDLQMRLDEAEQI--ALKGGKKQVQKLEARVKELENELESEQRKSQEYQK 1846
Cdd:pfam10174 431 SSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESLkkENKDLKEKVSALQPELTEKESSLIDLKEHASSLAS 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1847 VVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQakvksykrQAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQVN 1926
Cdd:pfam10174 511 SGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVE 582
|
..
gi 2045330442 1927 KL 1928
Cdd:pfam10174 583 RL 584
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
855-1533 |
9.43e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.87 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 855 KELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELMERL 934
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 935 EDEEEMSANVLAKKRKLEDECSELKKDIddleitlakvekEKHAT-ENKVKNLIEEMAALDETILKLTKEKKALTEAhqq 1013
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKI------------QKNKSlESQISELKKQNNQLKDNIEKKQQEINEKTTE--- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1014 tlddLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKlslesvmDLENDKQQ-----LEEKL 1088
Cdd:TIGR04523 248 ----ISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS-------DLNNQKEQdwnkeLKSEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1089 KKKDFEMNEISSRIEDEQALVNQLHKKIKEL-QARTEELEEELEADRASRAKVEKQRgdvareleelserleeaggATSA 1167
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLkKELTNSESENSEKQRELEEKQNEIE-------------------KLKK 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1168 QIEINKKRETDFLKLRRDLEEAMLHHEATTaalrkkhadsvAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLS 1247
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLN-----------QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1248 KGKATSEKMCRLYEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQL 1327
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1328 EEENKAKSALAHSLQS---------SRHDCDLLREQYDEEQEAKAEL---QRALSKANAEVAQWRTKYETDAIQRTEELE 1395
Cdd:TIGR04523 527 EKLESEKKEKESKISDledelnkddFELKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1396 EaKKKLVTRLQEAEESVEASNAKCSSLEKT----KHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEEC 1471
Cdd:TIGR04523 607 E-KEKKISSLEKELEKAKKENEKLSSIIKNikskKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDW 685
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2045330442 1472 QSELESSQKESRglsteLFKLKNSYEETL-DHLETIKRENKNLQEEIADLSDQISQGSKTIHE 1533
Cdd:TIGR04523 686 LKELSLHYKKYI-----TRMIRIKDLPKLeEKYKEIEKELKKLDEFSKELENIIKNFNKKFDD 743
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
852-1413 |
9.77e-07 |
|
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: 9.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 852 ATEKELAALKEELAKLKEALEKSEVKRK------ELEEKQVSLIQEKNDLA-LQLQAEQDNLADAEDRCDLLIKTKIQLE 924
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREqiellePIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 925 AKVKELMERLEDEEEMSANVLAKKRKLEDECSELK-KDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKE 1003
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1004 KKALTEAHQQTLDDLQAEEDKV-NTLTKAKAKLEQQVDDLEgSLEQE------KKVRMD--LERVRRKLEGDLKLSLESV 1074
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALeEALAEAEAALRDLRRELR-ELEAEiaslerRKSNIParLLALRDALAEALGLDEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1075 ------MDLENDKQQLE---EKLkkkdfeMNEISSRI--EDEQ-----ALVNQLHKKIK----ELQARTEELEEELEADR 1134
Cdd:COG4913 461 pfvgelIEVRPEEERWRgaiERV------LGGFALTLlvPPEHyaaalRWVNRLHLRGRlvyeRVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1135 ASRAKVEKQRGDvareleelserleeAGGATSAQIEinkkRETDFLK------LRRD----LEEAMLHHEATtaalRKKH 1204
Cdd:COG4913 535 SLAGKLDFKPHP--------------FRAWLEAELG----RRFDYVCvdspeeLRRHpraiTRAGQVKGNGT----RHEK 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1205 ADSVAELS---------EQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMcrlyeDQMNEAKAKVDELQ 1275
Cdd:COG4913 593 DDRRRIRSryvlgfdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRL-----AEYSWDEIDVASAE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1276 RQLNETNTQRARAQAESGEVgRKLEEREAmvsQLQRAKNSLTQnveelkkQLEEENKAKSALAHSLQSSRHDCDLLREQY 1355
Cdd:COG4913 668 REIAELEAELERLDASSDDL-AALEEQLE---ELEAELEELEE-------ELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1356 DEEQEAKAELQRalskanAEVAQWRTKYETDAIQRT--EELEEAKKKLVTRLQEAEESVE 1413
Cdd:COG4913 737 EAAEDLARLELR------ALLEERFAAALGDAVERElrENLEERIDALRARLNRAEEELE 790
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1597-1841 |
1.03e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1597 SHQRSMESMQTTLDAEAKSRNEAVRLRKKMECDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELK 1676
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1677 EQmaLTERRNNLlsseVEELRALLEQNDRAR---KLAEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLsnevddav 1753
Cdd:COG4942 97 AE--LEAQKEEL----AELLRALYRLGRQPPlalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL-------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1754 QECRNAEEKAKKAITDAAMMAEELKKEqdtsshLERMKKNMEQTVKDLQMRLDEAEQiALKGGKKQVQKLEARVKELENE 1833
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAA------LEALKAERQKLLARLEKELAELAA-ELAELQQEAEELEALIARLEAE 235
|
....*...
gi 2045330442 1834 LESEQRKS 1841
Cdd:COG4942 236 AAAAAERT 243
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1488-1837 |
1.28e-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: 53.15 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1488 ELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAAL-------EEVEGTL- 1559
Cdd:pfam19220 49 RLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELrdktaqaEALERQLa 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1560 -EHEESKTLRIQLELNQIKADV-DRKLAEKDEEIDNLRRSHQRsmesmqttldAEAKSRneavRLRKKMEcdlnEMEVQL 1637
Cdd:pfam19220 129 aETEQNRALEEENKALREEAQAaEKALQRAEGELATARERLAL----------LEQENR----RLQALSE----EQAAEL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1638 NHANRQASESQKLLRNLQVQIKDIQLELDDT-------VHQNEELKEQMAlTERrnNLLSSEVEELRALLEQNDRARKLA 1710
Cdd:pfam19220 191 AELTRRLAELETQLDATRARLRALEGQLAAEqaereraEAQLEEAVEAHR-AER--ASLRMKLEALTARAAATEQLLAEA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1711 EHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQEcRNAEEKAKKAITD-AAMMAEELKkeqDTSSHLER 1789
Cdd:pfam19220 268 RNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQ-FQEMQRARAELEErAEMLTKALA---AKDAALER 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2045330442 1790 MkknmEQTVKDLQMRLDEAEQIALKggkkQVQKLEARVKELENELESE 1837
Cdd:pfam19220 344 A----EERIASLSDRIAELTKRFEV----ERAALEQANRRLKEELQRE 383
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1671-1908 |
1.29e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1671 QNEELKEQMALTERRNNLLSSEVEELRALLEQNDRARK--LAEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNE 1748
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1749 VDDAVQECRNAEEKAKKAITDAAMmaeelkkeqdtsshlermkKNMEQTVKDLQMRLDEAEQIaLKGGKKQVQKLEARVK 1828
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVI-------------------QQLRAQLAELEAELAELSAR-YTPNHPDVIALRAQIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1829 ELENELESE-QRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQdlidKLQAKVKSYKRQAEEAEEQANSNLTKYRKL 1907
Cdd:COG3206 302 ALRAQLQQEaQRILASLEAELEALQAREASLQAQLAQLEARLAELP----ELEAELRRLEREVEVARELYESLLQRLEEA 377
|
.
gi 2045330442 1908 Q 1908
Cdd:COG3206 378 R 378
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1501-1738 |
1.33e-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: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1501 DHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQLELNQIKADv 1580
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1581 drkLAEKDEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLRKKMECDLNEMEVQLNHANRQASESQKLLRNLQVQIKD 1660
Cdd:COG4942 99 ---LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1661 IQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQNDRARKLAEHEL--LEATERVNLLHSQNTGLINQKKKL 1738
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIarLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
815-1911 |
2.06e-06 |
|
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: 53.13 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 815 RREALMIIQWNIRAfntvkhwpwmKLFFKIKPLLRSAAT-----EKELAALKEELAKLKEALEKSEVKRKELEEKQVSLI 889
Cdd:TIGR01612 523 KNIIGFDIDQNIKA----------KLYKEIEAGLKESYElaknwKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEID 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 890 QEK---NDLALQLQAEQDNLADAEDrcdlLIKTKIQLEAKVKELMERLEDEEEMSANVLAKKRKLEDEC-----SELKK- 960
Cdd:TIGR01612 593 DEIiyiNKLKLELKEKIKNISDKNE----YIKKAIDLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIystikSELSKi 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 961 ---DIDDLEITLAKVEKEkhateNKVKNlIEEMAALDETILKLTKEKKALTEAHQQTLddlqaeEDKVNTLTKAKAKLEQ 1037
Cdd:TIGR01612 669 yedDIDALYNELSSIVKE-----NAIDN-TEDKAKLDDLKSKIDKEYDKIQNMETATV------ELHLSNIENKKNELLD 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1038 QVddlegsLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQLEEKLKKKDFEMNEISSRIEDEQALVNqlhkkIK 1117
Cdd:TIGR01612 737 II------VEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDN-----IK 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1118 ELQARTEELEEELEADRASRAKVEkqrgdvareleelserleeaggaTSAQIEINKKRETDFLK-------LRRDLEEAM 1190
Cdd:TIGR01612 806 DEDAKQNYDKSKEYIKTISIKEDE-----------------------IFKIINEMKFMKDDFLNkvdkfinFENNCKEKI 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1191 -LHHEATTAALRKKHA----DSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQmN 1265
Cdd:TIGR01612 863 dSEHEQFAELTNKIKAeisdDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKICENTKESIEKFHNKQ-N 941
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1266 EAKAKVDELQRQLNETNT--QRARAQAESGEVGRKLEE----REAMVSQLQRAKNSLTQNVeelkkqleeeNKAKSALAH 1339
Cdd:TIGR01612 942 ILKEILNKNIDTIKESNLieKSYKDKFDNTLIDKINELdkafKDASLNDYEAKNNELIKYF----------NDLKANLGK 1011
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1340 SLQssrhdcDLLREQYDEEQEAKAELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEaeESVEASNAKC 1419
Cdd:TIGR01612 1012 NKE------NMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNK--EILEEAEINI 1083
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1420 SSLEKTKHRLQT-EIEDLVidLERANAAAAALDKKQRNFDKVlaewKQKYEECQSELESSQKESRGLSTELFKLKNSYEE 1498
Cdd:TIGR01612 1084 TNFNEIKEKLKHyNFDDFG--KEENIKYADEINKIKDDIKNL----DQKIDHHIKALEEIKKKSENYIDEIKAQINDLED 1157
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1499 TLDhlETIKREN-KNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDiQAALEEVEGtleheesktlrIQLELNQik 1577
Cdd:TIGR01612 1158 VAD--KAISNDDpEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKD-KTSLEEVKG-----------INLSYGK-- 1221
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1578 aDVDRKLAEKDEEIDNLRRSHQRSMESMQTTLDaEAKSRNEAVRLRKKMECDLN-EMEVqLNHANRQASESQKLLRNLQV 1656
Cdd:TIGR01612 1222 -NLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLD-EIKEKSPEIENEMGIEMDIKaEMET-FNISHDDDKDHHIISKKHDE 1298
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1657 QIKDIQlelddtvhqNEELKeqmaLTErrNNLLSSEVEELRALLEQNdrarklaeheLLEATER---VNLLHSQNTGLIN 1733
Cdd:TIGR01612 1299 NISDIR---------EKSLK----IIE--DFSEESDINDIKKELQKN----------LLDAQKHnsdINLYLNEIANIYN 1353
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1734 QKKklesdLSTLSNEVDDaVQECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLERMKKNMEQTVKDlqmrldeaeqial 1813
Cdd:TIGR01612 1354 ILK-----LNKIKKIIDE-VKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDD------------- 1414
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1814 kggkKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAE----------EDKK---------NLARLQD 1874
Cdd:TIGR01612 1415 ----KDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEmadnksqhilKIKKdnatndhdfNINELKE 1490
|
1130 1140 1150
....*....|....*....|....*....|....*..
gi 2045330442 1875 LIDklqaKVKSYKRQAEEAEEQANSNLTKYRKLQHEL 1911
Cdd:TIGR01612 1491 HID----KSKGCKDEADKNAKAIEKNKELFEQYKKDV 1523
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1585-1815 |
3.22e-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: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1585 AEKDEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLRKKMECDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQLE 1664
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1665 LDDtvhQNEELKEQMALTERRNN------LLSSE----VEELRALLEQNDRARKLAEHELLEATERvnlLHSQNTGLINQ 1734
Cdd:COG4942 99 LEA---QKEELAELLRALYRLGRqpplalLLSPEdfldAVRRLQYLKYLAPARREQAEELRADLAE---LAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1735 KKKLESDLSTLSNE---VDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTsshLERMKKNMEQTVKDLQMRLDEAEQI 1811
Cdd:COG4942 173 RAELEALLAELEEEraaLEALKAERQKLLARLEKELAELAAELAELQQEAEE---LEALIARLEAEAAAAAERTPAAGFA 249
|
....
gi 2045330442 1812 ALKG 1815
Cdd:COG4942 250 ALKG 253
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1262-1478 |
3.67e-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: 51.30 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1262 DQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKAKSALAHSL 1341
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1342 QSSRHD-CDLLREQYDEEQEAKAELqrALSKANAEVAQWRTKY----------ETDAIQRT-EELEEAKKKLVTRLQEAE 1409
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYlkylaparreQAEELRADlAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2045330442 1410 ESVEASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESS 1478
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1359-1590 |
4.00e-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: 51.30 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1359 QEAKAELQRALSKANAEVAQwrtkyetdAIQRTEELEEAKKKLVTRLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLVI 1438
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAE--------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1439 DLERANAAaaaLDKKQRNFDKVLAEWKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIA 1518
Cdd:COG4942 91 EIAELRAE---LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2045330442 1519 DLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQLELNQIKADVDRKLAEKDEE 1590
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1688-1942 |
4.53e-06 |
|
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: 51.98 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1688 LLSSEVEELRALLEQN------DRARKLAEHELLEATE---RVNLLHsqntglinqkKKLESDLSTLSNEVDDAV--QEC 1756
Cdd:TIGR02168 149 IIEAKPEERRAIFEEAagiskyKERRKETERKLERTREnldRLEDIL----------NELERQLKSLERQAEKAEryKEL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1757 RNAEEKAKKAItdAAMMAEELKKEQDTsshLERMKKNMEQTVKDLQMRLDEAEQialkggkkQVQKLEARVKELENELES 1836
Cdd:TIGR02168 219 KAELRELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEELRLEVSELEEEIEE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1837 EQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLqakvksyKRQAEEAEEQANSNLTKYRKLQHELDDAEE 1916
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL-------ESKLDELAEELAELEEKLEELKEELESLEA 358
|
250 260 270
....*....|....*....|....*....|...
gi 2045330442 1917 RAD-------MAETQVNKLRVRTRDQVSKVSKL 1942
Cdd:TIGR02168 359 ELEeleaeleELESRLEELEEQLETLRSKVAQL 391
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1694-1926 |
4.62e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1694 EELRALLEQNDRARKlAEHELLEATERVNLLhsqntglinqkkkleSDLSTLSNEVDDAVQECRNAEE-----KAKKAIT 1768
Cdd:COG4913 225 EAADALVEHFDDLER-AHEALEDAREQIELL---------------EPIRELAERYAAARERLAELEYlraalRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1769 DAAMMAEELKKEQDTSSHLERMKKNMEQTVKDLQMRLDEAE-QIALKGGkkqvqkleARVKELENELESEQRKSQEYQKV 1847
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEaQIRGNGG--------DRLEQLEREIERLERELEERERR 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1848 VRKYERRIKELSYQAEEDKKNLARLQdliDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAE-ERADMAETQVN 1926
Cdd:COG4913 361 RARLEALLAALGLPLPASAEEFAALR---AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEaEIASLERRKSN 437
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1547-1892 |
4.98e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1547 DIQAALEEVEGTLEH-EESKTLR------IQLELNQIKADVDR---KLAEKDEEIDNLRRSHQRSMESMqttldaeAKSR 1616
Cdd:PRK04863 234 DMEAALRENRMTLEAiRVTQSDRdlfkhlITESTNYVAADYMRhanERRVHLEEALELRRELYTSRRQL-------AAEQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1617 NEAVRLRKKMEcDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTErrnnLLSSEVEEL 1696
Cdd:PRK04863 307 YRLVEMARELA-ELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQADLEELEERLEEQNEVVE----EADEQQEEN 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1697 RALLEQN----DRARK-LAEH-ELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAEekakKAITDA 1770
Cdd:PRK04863 382 EARAEAAeeevDELKSqLADYqQALDVQQTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE----QEATEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1771 AMMAEElkKEQDTSSHLERMKKNME---------------QTVKDLQMRLDEAEQIAlkggkKQVQKLEARVKELENELE 1835
Cdd:PRK04863 458 LLSLEQ--KLSVAQAAHSQFEQAYQlvrkiagevsrseawDVARELLRRLREQRHLA-----EQLQQLRMRLSELEQRLR 530
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2045330442 1836 SEQRKSQ-----------------EYQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEE 1892
Cdd:PRK04863 531 QQQRAERllaefckrlgknlddedELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPA 604
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
853-1119 |
5.90e-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: 51.56 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 853 TEKELAALKEELAKLKEALEKsevKRKELEEKQVSLIQEKNDL--------ALQLQAEQDNLADAEDRCDLLIKTKIQLE 924
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSE---KQKELEQNNKKIKELEKQLnqlkseisDLNNQKEQDWNKELKSELKNQEKKLEEIQ 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 925 AKVKELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEK 1004
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1005 KALTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQL 1084
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
250 260 270
....*....|....*....|....*....|....*
gi 2045330442 1085 EEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKEL 1119
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1761-1943 |
6.12e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1761 EKAKKAItdaammaeELKKEQDTSSHLERMKK--NMEQTVKDLQMRLDEAEQiALKGGKKQVQKLEARVKELENELESEQ 1838
Cdd:COG1196 210 EKAERYR--------ELKEELKELEAELLLLKlrELEAELEELEAELEELEA-ELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1839 RKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAEERA 1918
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180
....*....|....*....|....*
gi 2045330442 1919 DMAETQVNKLRVRTRDQVSKVSKLN 1943
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELA 385
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1752-1943 |
7.49e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1752 AVQECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLERMKKNMEQTVKDLQMRLDEAEQiALKGGKKQVQKLEARVKELE 1831
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-ELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1832 NELESEQrksQEYQKVVRKY---------------------ERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQA 1890
Cdd:COG4942 97 AELEAQK---EELAELLRALyrlgrqpplalllspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2045330442 1891 EEAEEQANSNLTKYRKLQHELDDAEERADMAETQVNKLRVRTRDQVSKVSKLN 1943
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1038-1591 |
7.97e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1038 QVDDL-EGSLEQEKKVRMDLERVRRKLEGDLKLS--LESVMDLENDKQQLEEKLKKKDFEMNEISSRIEDEQALVNQLHK 1114
Cdd:PRK01156 139 EMDSLiSGDPAQRKKILDEILEINSLERNYDKLKdvIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1115 KIKELQ------------ARTEELEEELEADRASR-----AKVEKQRGDVARELEELSERLEEAGGATSAQIEINKKRET 1177
Cdd:PRK01156 219 EIERLSieynnamddynnLKSALNELSSLEDMKNRyeseiKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYIN 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1178 DFLKLRRDLEEAMLHHEATTAALRKKHAD--SVAELS---EQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLskgkat 1252
Cdd:PRK01156 299 DYFKYKNDIENKKQILSNIDAEINKYHAIikKLSVLQkdyNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSI------ 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1253 sEKMCRLYEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENK 1332
Cdd:PRK01156 373 -ESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNG 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1333 AKSALAHSLQSSRHDCDLLREQYDEE----QEAKAELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKL------- 1401
Cdd:PRK01156 452 QSVCPVCGTTLGEEKSNHIINHYNEKksrlEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIesaradl 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1402 ------VTRLQEAEESVEASNAKCSSLE------KTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYE 1469
Cdd:PRK01156 532 edikikINELKDKHDKYEEIKNRYKSLKledldsKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFP 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1470 ECQSELESSQKEsrgLSTELFKLKNSYEEtldhLETIKRENKNLQEEIADLSDQISQgsktIHELEKMKKGLDMEKSDIQ 1549
Cdd:PRK01156 612 DDKSYIDKSIRE---IENEANNLNNKYNE----IQENKILIEKLRGKIDNYKKQIAE----IDSIIPDLKEITSRINDIE 680
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2045330442 1550 AALEEVEGTLEHEES---------KTLRIQL-ELNQIKADVDRKLaEKDEEI 1591
Cdd:PRK01156 681 DNLKKSRKALDDAKAnrarlestiEILRTRInELSDRINDINETL-ESMKKI 731
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1462-1918 |
8.33e-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: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1462 AEWKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLdhletikrenKNLQEEIADLSDQISQGSKTIHELEKMKKGL 1541
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERK----------QVLEKELKHLREALQQTQQSHAYLTQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1542 DmEKSDIQAALEEVEGTLEheESKTLRIQLELNQIKADVDRK---LAEKDEEIDNLRRSHQRSMESMQTTLDAEAKSRNE 1618
Cdd:TIGR00618 253 E-EQLKKQQLLKQLRARIE--ELRAQEAVLEETQERINRARKaapLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1619 AVRLRK------KMECDLNEMEVQLNHaNRQASESQKLLRnlqvQIKDIQLELDDTVHQneeLKEQMALTERRNNLLSSE 1692
Cdd:TIGR00618 330 RAAHVKqqssieEQRRLLQTLHSQEIH-IRDAHEVATSIR----EISCQQHTLTQHIHT---LQQQKTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1693 VEELRALL------------EQNDRARKLAEHELLEATERVNLLHSQNTGLI-NQKKKLESDLSTLSNEVDDAVQECRNA 1759
Cdd:TIGR00618 402 LDILQREQatidtrtsafrdLQGQLAHAKKQQELQQRYAELCAAAITCTAQCeKLEKIHLQESAQSLKEREQQLQTKEQI 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1760 EEKAKKAITDAAMMAEELKKEQdtsshLERMKKNMEQTVKDLQMRLDEAEQIALKGGKKQVQKLEARVKELENELESEQR 1839
Cdd:TIGR00618 482 HLQETRKKAVVLARLLELQEEP-----CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1840 KSQEY-------QKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELD 1912
Cdd:TIGR00618 557 QRASLkeqmqeiQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ 636
|
....*.
gi 2045330442 1913 DAEERA 1918
Cdd:TIGR00618 637 CSQELA 642
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1688-1918 |
8.91e-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: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1688 LLSSEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAI 1767
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1768 TDAAMMAEELKKEQDT-SSHLERMKKNMEQTVKDLQMRLDEAEQIAlkggkKQVQKLEARVKELENELESEQRKSQEYQK 1846
Cdd:COG4942 90 KEIAELRAELEAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAV-----RRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2045330442 1847 VVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAEERA 1918
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1208-1600 |
9.32e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1208 VAELSEQIDSLQRVK---QKLEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQmneakAKVDELQRQLNETNTQ 1284
Cdd:COG4717 73 LKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY-----QELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1285 RARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQnveelkkqleEENKAKSALAHSLQSSRHDCDLLREQYDEEQEAKAE 1364
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEE----------LLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1365 LQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRL--------------------------------QEAEESV 1412
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALlallglggsllsliltiagvlflvlgllallfLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1413 EASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQS-ELESSQKESRGLSTELFK 1491
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1492 LKN-SYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKmkkglDMEKSDIQAALEEVEGTLEHEESKTLRIQ 1570
Cdd:COG4717 378 EAGvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----ALDEEELEEELEELEEELEELEEELEELR 452
|
410 420 430
....*....|....*....|....*....|
gi 2045330442 1571 LELNQIKADVDRklAEKDEEIDNLRRSHQR 1600
Cdd:COG4717 453 EELAELEAELEQ--LEEDGELAELLQELEE 480
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
950-1908 |
9.92e-06 |
|
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: 51.21 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 950 KLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLT-----KEKKALTEAHQQTL----DDLQA 1020
Cdd:TIGR01612 1108 KYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVAdkaisNDDPEEIEKKIENIvtkiDKKKN 1187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1021 EEDKVNTLTKAKAKLEQQvddlEGSLEQEKKVRMD---------LERV---RRKLEGDLKLSLESVMDLENDKQQLEEKL 1088
Cdd:TIGR01612 1188 IYDEIKKLLNEIAEIEKD----KTSLEEVKGINLSygknlgklfLEKIdeeKKKSEHMIKAMEAYIEDLDEIKEKSPEIE 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1089 KKKDFEMNeissrIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKqrgdvareleelserleeaggATSAQ 1168
Cdd:TIGR01612 1264 NEMGIEMD-----IKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIE---------------------DFSEE 1317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1169 IEINKKRETdflkLRRDLEEAMLHHEATTAALRK----KHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDD---LAS 1241
Cdd:TIGR01612 1318 SDINDIKKE----LQKNLLDAQKHNSDINLYLNEianiYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKsekLIK 1393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1242 TVEQLSKGKATSEKMCRLYEDQ-MNEAKAKVDELQRQL--NETNTQRARAQAESGEVGRKL----------EEREAMVSQ 1308
Cdd:TIGR01612 1394 KIKDDINLEECKSKIESTLDDKdIDECIKKIKELKNHIlsEESNIDTYFKNADENNENVLLlfkniemadnKSQHILKIK 1473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1309 LQRAKNSLTQNVEELKKQLEEENKAKSALAHSLQSSRHDCDLLrEQYdeeqeaKAELQRALSKANA-EVAQWRTKYETDA 1387
Cdd:TIGR01612 1474 KDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELF-EQY------KKDVTELLNKYSAlAIKNKFAKTKKDS 1546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1388 IQRTEELEEAKKKLVTRLQEAEEsveasnaKCSSLEKTKHRlqteIEDLVIDLERANAAAAALDKKQRNFDKVL---AEW 1464
Cdd:TIGR01612 1547 EIIIKEIKDAHKKFILEAEKSEQ-------KIKEIKKEKFR----IEDDAAKNDKSNKAAIDIQLSLENFENKFlkiSDI 1615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1465 KQKYEECQSELESSQKESRGLS-----TELFKLKNSYEETLDHLETIKRENKNLQE----------EIADLSDQISQGSK 1529
Cdd:TIGR01612 1616 KKKINDCLKETESIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQKKNIEDkkkeldeldsEIEKIEIDVDQHKK 1695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1530 T--IHELEKMKKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQLElnqiKADVDRKLAEKDEEIDNLRRSHQRSMESMQT 1607
Cdd:TIGR01612 1696 NyeIGIIEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLE----GIDPNEKLEEYNTEIGDIYEEFIELYNIIAG 1771
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1608 TLDAEAK--------------SRNEAVR---LRKKMECDLNEMEVqlNHANRQASESQKLLRNLQV----QIKDIQLELD 1666
Cdd:TIGR01612 1772 CLETVSKepitydeikntrinAQNEFLKiieIEKKSKSYLDDIEA--KEFDRIINHFKKKLDHVNDkftkEYSKINEGFD 1849
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1667 DTVHQNEELKEQmalTERRN--NLLSSEVEELRALLEQNDRARKL-AEHELLEATERVNLLH--SQNTGLINQKKKLESD 1741
Cdd:TIGR01612 1850 DISKSIENVKNS---TDENLlfDILNKTKDAYAGIIGKKYYSYKDeAEKIFINISKLANSINiqIQNNSGIDLFDNINIA 1926
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1742 -LSTLSNEVDDAVQECRNAEEKAK---------KAITDAAMMAEEL-KKEQDTsshLERMKKNMEQTVKdlqMRLDEAEQ 1810
Cdd:TIGR01612 1927 iLSSLDSEKEDTLKFIPSPEKEPEiytkirdsyDTLLDIFKKSQDLhKKEQDT---LNIIFENQQLYEK---IQASNELK 2000
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1811 IALKGGKKQVQKLEARVKEL---ENELESEQRKSQEYQKVVR-KYERRIKELSYQAEEDKKNLARLQDL----------- 1875
Cdd:TIGR01612 2001 DTLSDLKYKKEKILNDVKLLlhkFDELNKLSCDSQNYDTILElSKQDKIKEKIDNYEKEKEKFGIDFDVkameekfdndi 2080
|
1050 1060 1070
....*....|....*....|....*....|....*
gi 2045330442 1876 --IDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQ 1908
Cdd:TIGR01612 2081 kdIEKFENNYKHSEKDNHDFSEEKDNIIQSKKKLK 2115
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1710-1899 |
1.02e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1710 AEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDT-SSHLE 1788
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1789 RMKKNMEQTVK-----------DLQMRLDEAEQIAlKGGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKE 1857
Cdd:COG3883 94 ALYRSGGSVSYldvllgsesfsDFLDRLSALSKIA-DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2045330442 1858 LSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEAEEQANS 1899
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1544-1916 |
1.27e-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: 50.44 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1544 EKSDIQAALEEVEGTLEHEESKTlrIQLELNQIKADVDRKLAEKDEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLR 1623
Cdd:pfam13166 90 ESIEIQEKIAKLKKEIKDHEEKL--DAAEANLQKLDKEKEKLEADFLDECWKKIKRKKNSALSEALNGFKYEANFKSRLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1624 KKMECDLNEMEVQLNHANRQASESQKLLRNLQ----VQIKDIQLeldDTVHQNEELKEQMALTE------RRNNLLSSEV 1693
Cdd:pfam13166 168 REIEKDNFNAGVLLSDEDRKAALATVFSDNKPeiapLTFNVIDF---DALEKAEILIQKVIGKSsaieelIKNPDLADWV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1694 EELRALLEQN-------------DRARKLAEHELLEATERVNLLHSQNTGLINQKKKLE------SDLSTLSNEVDDAVQ 1754
Cdd:pfam13166 245 EQGLELHKAHldtcpfcgqplpaERKAALEAHFDDEFTEFQNRLQKLIEKVESAISSLLaqlpavSDLASLLSAFELDVE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1755 ECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLERMKKNMEQtVKDLQMRLDEaeQIALKggKKQVQKLEARVKELENEL 1834
Cdd:pfam13166 325 DIESEAEVLNSQLDGLRRALEAKRKDPFKSIELDSVDAKIES-INDLVASINE--LIAKH--NEITDNFEEEKNKAKKKL 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1835 E---SEQRKS--QEYQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEaeeqANSNLTKYRKLQH 1909
Cdd:pfam13166 400 RlhlVEEFKSeiDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADE----INKLLKAFGFGEL 475
|
....*..
gi 2045330442 1910 ELDDAEE 1916
Cdd:pfam13166 476 ELSFNEE 482
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1657-1938 |
1.32e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1657 QIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALL-EQNDRARKLAEhELLEATERVNLLHSQNTGLINQK 1735
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRdELNAQVKELRE-EAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1736 KKLESDLSTLSNEVDDAVQEcRNAEEKAKKAITDAAMMAEELKKEQDTSSHLERMKKNMEQTVKDLQMRLDEAEQIalkg 1815
Cdd:COG1340 81 DELNEKLNELREELDELRKE-LAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKA---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1816 gkkqvqklearvKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEAEE 1895
Cdd:COG1340 156 ------------LEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQE 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2045330442 1896 QANSNLTKYRKLQHELDDAEERADMAETQVNKLRVRTRDQVSK 1938
Cdd:COG1340 224 KADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1621-1771 |
1.43e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1621 RLRKKMECDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQmaLTERRNNllssevEELRAL- 1699
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ--LGNVRNN------KEYEALq 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2045330442 1700 --LEQNDRARKLAEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAITDAA 1771
Cdd:COG1579 96 keIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1655-1868 |
1.64e-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: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1655 QVQIKDIQLELDDTVHQNEELKEQ---MALTERRNNLLSSEVEELRALLEQNDRARKLAEHELLEatERVNLLHSQN--- 1728
Cdd:pfam13166 282 TEFQNRLQKLIEKVESAISSLLAQlpaVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEA--KRKDPFKSIElds 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1729 -TGLINQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAItdAAMMAEELKKEQDTsshLERMKKNMEQTVKDLQMRLDE 1807
Cdd:pfam13166 360 vDAKIESINDLVASINELIAKHNEITDNFEEEKNKAKKKL--RLHLVEEFKSEIDE---YKDKYAGLEKAINSLEKEIKN 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2045330442 1808 AEqialkggkKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRikELSYQAEEDKKN 1868
Cdd:pfam13166 435 LE--------AEIKKLREEIKELEAQLRDHKPGADEINKLLKAFGFG--ELELSFNEEGKG 485
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1639-1870 |
2.42e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1639 HANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQndrarklAEHELLEAT 1718
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-------AEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1719 ERVN--LLHSQNTGLINqkkkleSDLSTL--SNEVDDAVQECRnaeekAKKAITDA-AMMAEELKKEQDTsshLERMKKN 1793
Cdd:COG3883 86 EELGerARALYRSGGSV------SYLDVLlgSESFSDFLDRLS-----ALSKIADAdADLLEELKADKAE---LEAKKAE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2045330442 1794 MEQTVKDLQMRLDEAEQiALKGGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLA 1870
Cdd:COG3883 152 LEAKLAELEALKAELEA-AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
907-1168 |
2.50e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 907 ADAEDRCDLLIKTKIQLEAKVKELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNL 986
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 987 IEEMAALDETILKLTkekkALTEAhqQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKvrmdlervrrklegd 1066
Cdd:COG3883 92 ARALYRSGGSVSYLD----VLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA--------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1067 lklslesvmDLENDKQQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQRGD 1146
Cdd:COG3883 151 ---------ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
250 260
....*....|....*....|..
gi 2045330442 1147 VARELEELSERLEEAGGATSAQ 1168
Cdd:COG3883 222 AAAAAAAAAAAAAAAAAAAAAA 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1761-1935 |
2.61e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1761 EKAKKAITDAAMMAEELKKEQDTSSHLERMKKNMEQTVKDLQMRLDEAEQIalkggkKQVQKLEARVKELENELESEQRK 1840
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1841 SQEyqkvVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQA-EEAEEQANSNLTKYRKLQHELDDAEERAD 1919
Cdd:COG4717 148 LEE----LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*.
gi 2045330442 1920 MAETQVNKLRVRTRDQ 1935
Cdd:COG4717 224 ELEEELEQLENELEAA 239
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
854-1060 |
3.45e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 854 EKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLIKTKIQLEAKvkelMER 933
Cdd:pfam07888 79 ESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE----LER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 934 LEDEEEMSanvLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEkkaLTEAHQQ 1013
Cdd:pfam07888 155 MKERAKKA---GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK---LTTAHRK 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2045330442 1014 TLDDLQAEEDkVNTLTKAKAKLEQQVDDLEGSLE----QEKKVRMDLERVR 1060
Cdd:pfam07888 229 EAENEALLEE-LRSLQERLNASERKVEGLGEELSsmaaQRDRTQAELHQAR 278
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
856-1119 |
4.68e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.39 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 856 ELAALKEELAKLKEALEKSEVKrkELEEKQVSLIQEKNDLALQLQAeqdnladaedrcdlliktkiqleaKVKELMERLE 935
Cdd:PRK05771 10 LIVTLKSYKDEVLEALHELGVV--HIEDLKEELSNERLRKLRSLLT------------------------KLSEALDKLR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 936 DEeeMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEkhatenkVKNLIEEMAALDETILKLTKEKKALT--EAHQQ 1013
Cdd:PRK05771 64 SY--LPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERLEpwGNFDL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1014 TLDDLQAEED---KVNTLTKAKAKLEQQVDDLEGSLEQEKKvrmdlervrrkleGDLKLSLesVMDLENDKQQLEEKLKK 1090
Cdd:PRK05771 135 DLSLLLGFKYvsvFVGTVPEDKLEELKLESDVENVEYISTD-------------KGYVYVV--VVVLKELSDEVEEELKK 199
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2045330442 1091 KDFE-------------MNEISSRIEDEQALVNQLHKKIKEL 1119
Cdd:PRK05771 200 LGFErleleeegtpselIREIKEELEEIEKERESLLEELKEL 241
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
856-1121 |
4.95e-05 |
|
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: 48.15 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 856 ELAALKEELAKLKEALEKS-------EVKRKELEE-----KQVSLIQEKNDLALQlqaeqdNLADAEDRCDLLIKTKIQL 923
Cdd:pfam05622 112 EAQALKDEMDILRESSDKVkkleatvETYKKKLEDlgdlrRQVKLLEERNAEYMQ------RTLQLEEELKKANALRGQL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 924 EA---KVKELMERLEDE--------------EEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHA------TE 980
Cdd:pfam05622 186 ETykrQVQELHGKLSEEskkadklefeykklEEKLEALQKEKERLIIERDTLRETNEELRCAQLQQAELSQAdallspSS 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 981 NKVKNLIEEM--AALDETILKLTKEKKALTEAH-----------QQTLDDLQAEEDKVNT-LTKAKAK---LEQQVDDLE 1043
Cdd:pfam05622 266 DPGDNLAAEImpAEIREKLIRLQHENKMLRLGQegsyrerltelQQLLEDANRRKNELETqNRLANQRileLQQQVEELQ 345
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 1044 GSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQLEEKlkkkdfemneissriedEQALVNQLHKKIKELQA 1121
Cdd:pfam05622 346 KALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEEL-----------------EPKQDSNLAQKIDELQE 406
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
846-1007 |
5.28e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 846 PLLRSAATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLIKTKIQLEA 925
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 926 KVKELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDL-------EITLAKVEKEKHATENKVKNLIEEMAALDETIL 998
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaIEEYEELEERYDFLSEQREDLEEARETLEEAIE 819
|
....*....
gi 2045330442 999 KLTKEKKAL 1007
Cdd:COG1196 820 EIDRETRER 828
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1184-1914 |
5.89e-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: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1184 RDLEEAMLHHEATtAALRKKHADSVAELSEQIDSLQRVKQKL-EKERSEAKMEvDDLASTVEQLSK---GKATSEKMCRl 1259
Cdd:COG3096 275 RHANERRELSERA-LELRRELFGARRQLAEEQYRLVEMARELeELSARESDLE-QDYQAASDHLNLvqtALRQQEKIER- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1260 YEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGrklEEREAMVSQL---QRAKNSLTQNVEELKKQLEEENKAKSA 1336
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAE---EEVDSLKSQLadyQQALDVQQTRAIQYQQAVQALEKARAL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1337 LAHSLQSSRHDCDLLREQYDEEQEAKA---ELQRALSKANAEVAQWRTKYE-----TDAIQRTEELEEAKKKLVT--RLQ 1406
Cdd:COG3096 429 CGLPDLTPENAEDYLAAFRAKEQQATEevlELEQKLSVADAARRQFEKAYElvckiAGEVERSQAWQTARELLRRyrSQQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1407 EAEESVEASNAKCSSLEKTKHRLQteiedlviDLERANAAAAALDKKQRN----FDKVLAEWKQKYEECQSELESSQKES 1482
Cdd:COG3096 509 ALAQRLQQLRAQLAELEQRLRQQQ--------NAERLLEEFCQRIGQQLDaaeeLEELLAELEAQLEELEEQAAEAVEQR 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1483 RGLSTELFKLKNSYEEtldhLETIKRENKNLQEEIADLSDQISQgsktihELEkmkkgldmEKSDIQAALEEVegtLEHE 1562
Cdd:COG3096 581 SELRQQLEQLRARIKE----LAARAPAWLAAQDALERLREQSGE------ALA--------DSQEVTAAMQQL---LERE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1563 -ESKTLRiqlelnqikadvdRKLAEKDEEID-NLRRSHQRSMESmqttlDAEAKSRNEavRLRKKMECDLNEmEVQLNHA 1640
Cdd:COG3096 640 rEATVER-------------DELAARKQALEsQIERLSQPGGAE-----DPRLLALAE--RLGGVLLSEIYD-DVTLEDA 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1641 ---------NRQA------SESQKLLRNLQVQIKDIQL------ELDDTVHQNEELKEQMALTERRNNLLSSEVEEL--- 1696
Cdd:COG3096 699 pyfsalygpARHAivvpdlSAVKEQLAGLEDCPEDLYLiegdpdSFDDSVFDAEELEDAVVVKLSDRQWRYSRFPEVplf 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1697 -RALLEQndRARKL-AEHELLE---ATERVNL-----LHSQNTGLINQKKKL------ESDLSTLS---NEVDDAVQECR 1757
Cdd:COG3096 779 gRAAREK--RLEELrAERDELAeqyAKASFDVqklqrLHQAFSQFVGGHLAVafapdpEAELAALRqrrSELERELAQHR 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1758 NAEEKAKKAITDAAMMAEELKKEQDTSSHLErmKKNMEQTVKDLQMRLDEAEQ----IALKGgkKQVQKLEARVKELENE 1833
Cdd:COG3096 857 AQEQQLRQQLDQLKEQLQLLNKLLPQANLLA--DETLADRLEELREELDAAQEaqafIQQHG--KALAQLEPLVAVLQSD 932
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1834 LESEQRKSQEYQKVVRKYER-------------RIKELSYQAEEDKknLARLQDLIDKLQAKVksykRQAEEAEEQANsn 1900
Cdd:COG3096 933 PEQFEQLQADYLQAKEQQRRlkqqifalsevvqRRPHFSYEDAVGL--LGENSDLNEKLRARL----EQAEEARREAR-- 1004
|
810
....*....|....
gi 2045330442 1901 lTKYRKLQHELDDA 1914
Cdd:COG3096 1005 -EQLRQAQAQYSQY 1017
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1645-1889 |
6.66e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1645 SESQKLL----RNLQVQIKDIQLELDdtvHQNEELKEQMALTERRNNLLSSEVEELRALLEQNDRARKLAEHELLEATER 1720
Cdd:PHA02562 166 SEMDKLNkdkiRELNQQIQTLDMKID---HIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1721 VNLLHSQNTGLINQKKKLESDLSTLSNEVDDAvqecrNAEEKAKKAITDAAMMAEELKKEQDTSSHLERMKKNMEQTVKD 1800
Cdd:PHA02562 243 LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQF-----QKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1801 LQMRLDEAEQIalkggKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQ 1880
Cdd:PHA02562 318 LDTAIDELEEI-----MDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV 392
|
....*....
gi 2045330442 1881 AKVKSYKRQ 1889
Cdd:PHA02562 393 KTKSELVKE 401
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
858-1523 |
6.71e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 858 AALKEELAKLKEALEKSEVKRKELEEKQVSliQEKNDLALQLQAEQDNLADAEDR-----CDLLIKTKIQLEAKVKELME 932
Cdd:pfam05483 99 AELKQKENKLQENRKIIEAQRKAIQELQFE--NEKVSLKLEEEIQENKDLIKENNatrhlCNLLKETCARSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 933 RLEDEEEMSAN----------------VLAKKRKLEDECsELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDET 996
Cdd:pfam05483 177 EREETRQVYMDlnnniekmilafeelrVQAENARLEMHF-KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENK 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 997 ILKLTKEKKALTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKvrmdlerVRRKLEGDLKLSLESVMD 1076
Cdd:pfam05483 256 MKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMS-------TQKALEEDLQIATKTICQ 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1077 LENDKQQLEEKLKKKDFEMNEISSRIEDEQALVNQLhkkikelqARTEELEEELEADRASRAKVEKQRGDVARELEELSE 1156
Cdd:pfam05483 329 LTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEL--------LRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFK 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1157 RLEEAGGATSAQIEINKKRETDFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEV 1236
Cdd:pfam05483 401 NNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1237 DDlastvEQLSKGKATSEKMCRLYEDQ--MNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKN 1314
Cdd:pfam05483 481 EK-----EKLKNIELTAHCDKLLLENKelTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVRE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1315 SLTQN-------VEELKKQLEEENKAKSALAHSLQSSRHDCDLLREQYDEEQEAKAELQ---RALSKANAEVAQWRTKYE 1384
Cdd:pfam05483 556 EFIQKgdevkckLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHqenKALKKKGSAENKQLNAYE 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1385 TDAIQRTEELEEAKKKL------------VTRLQEAEESVEASNAKCSSLEKTK------HRLQTEIEDLVIDLERanaA 1446
Cdd:pfam05483 636 IKVNKLELELASAKQKFeeiidnyqkeieDKKISEEKLLEEVEKAKAIADEAVKlqkeidKRCQHKIAEMVALMEK---H 712
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2045330442 1447 AAALDKKQRNFDKVLAEWKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIKRENknlQEEIADLSDQ 1523
Cdd:pfam05483 713 KHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEA---KENTAILKDK 786
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
860-1114 |
7.77e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.89 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 860 LKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLiktkiqlEAKVKELMERLEDEEE 939
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL-------QTEVDALRLRLEEKES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 940 MSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKAL------TEAHQQ 1013
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLqtdssnTDTALT 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1014 TLDDLQAEEDKV-NTLTKAKAKLEQQVDDlegSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQLEEKLKKKD 1092
Cdd:pfam10174 440 TLEEALSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKD 516
|
250 260
....*....|....*....|....*.
gi 2045330442 1093 FEMN----EISSRIEDEQALVNQLHK 1114
Cdd:pfam10174 517 SKLKsleiAVEQKKEECSKLENQLKK 542
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
851-1010 |
8.66e-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: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 851 AATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLAD--------------------AE 910
Cdd:COG3883 33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrsggsvsyldvllgSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 911 DRCDLLIKTKI--QLEAKVKELMERLEDEEEMSANvlaKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIE 988
Cdd:COG3883 113 SFSDFLDRLSAlsKIADADADLLEELKADKAELEA---KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
170 180
....*....|....*....|..
gi 2045330442 989 EMAALDETILKLTKEKKALTEA 1010
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAA 211
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1458-1657 |
9.86e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1458 DKVLAEWKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKtihELEKM 1537
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE---ELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1538 -----KKGLD-------MEKSDIQAALEEVEgTLEHEESKTLRIQLELNQIKADVDRKLAEKDEEIDNLRRShQRSMESM 1605
Cdd:COG3883 92 aralyRSGGSvsyldvlLGSESFSDFLDRLS-ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL-KAELEAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2045330442 1606 QTTLDAEaksRNEAVRLRKKMECDLNEMEVQLNHANRQASESQKLLRNLQVQ 1657
Cdd:COG3883 170 KAELEAQ---QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1351-1711 |
1.07e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1351 LREQYDEEQEAKAELQRALSKANAEVAQWRTKYET-DAIQRTEELEEAKKKLVTRLQEAEESVEASNAKCSSLEktkhRL 1429
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQLlPLYQELEALEAELAELPERLEELEERLEELRELEEELE----EL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1430 QTEIEDLVIDLERANAAAAALDKKQrnfdkvLAEWKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIKRE 1509
Cdd:COG4717 169 EAELAELQEELEELLEQLSLATEEE------LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1510 NKNLQEE-----------IADLSDQISQGSKTIHEL-----------------EKMKKGLDMEKSDIQAALEEVEGTLEH 1561
Cdd:COG4717 243 ERLKEARlllliaaallaLLGLGGSLLSLILTIAGVlflvlgllallflllarEKASLGKEAEELQALPALEELEEEELE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1562 EESKTLRIQLELNQIKA-----------DVDRKLAEKDEEIDNLRRSHQRS--MESMQTTLDAEAKSRNEAVRLRKKMEC 1628
Cdd:COG4717 323 ELLAALGLPPDLSPEELlelldrieelqELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKE 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1629 DLNEMEVQLNHAN--RQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQNDRA 1706
Cdd:COG4717 403 ELEELEEQLEELLgeLEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELK 482
|
....*
gi 2045330442 1707 RKLAE 1711
Cdd:COG4717 483 AELRE 487
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1424-1895 |
1.10e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1424 KTKHRLQTEIEDLVIDLERANAAAAALDKKQRNfdkvLAEWKQKYEECQSELESSQKESRGLSTELfklknSYEETLDHL 1503
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEE----LEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1504 ETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQLELNQIKADVDRK 1583
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1584 LAEKDEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRL------------RKKMECDLNEMEVQLNHANRQASESQKLL 1651
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglgGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1652 RNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQNDRARKLaEHELLEATERVNLLHSQNtgl 1731
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL-LREAEELEEELQLEELEQ--- 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1732 iNQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLErmKKNMEQTVKDLQMRLDEAEQi 1811
Cdd:COG4717 371 -EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD--EEELEEELEELEEELEELEE- 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1812 ALKGGKKQVQKLEARVKELENELESEQRKSQEYQKvvrkyERRIKELsyqaEEDKKNLARLQDLIDKLQAKVKSYKRQA- 1890
Cdd:COG4717 447 ELEELREELAELEAELEQLEEDGELAELLQELEEL-----KAELREL----AEEWAALKLALELLEEAREEYREERLPPv 517
|
....*.
gi 2045330442 1891 -EEAEE 1895
Cdd:COG4717 518 lERASE 523
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1400-1578 |
1.13e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 46.55 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1400 KLVTRLQEAEESVEAsnaKCSSLEKTKHRLQTEIEDLVIDLERanaaaaaLDKKQRNFDKVLAEWKQKYEECQSELESSQ 1479
Cdd:smart00787 123 KTFARLEAKKMWYEW---RMKLLEGLKEGLDENLEGLKEDYKL-------LMKELELLNSIKPKLRDRKDALEEELRQLK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1480 KESRGL----STELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKmkkgldmEKSDIQAALEEV 1555
Cdd:smart00787 193 QLEDELedcdPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT-------EIAEAEKKLEQC 265
|
170 180
....*....|....*....|...
gi 2045330442 1556 EGTLEHEESKtlrIQLELNQIKA 1578
Cdd:smart00787 266 RGFTFKEIEK---LKEQLKLLQS 285
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
953-1199 |
1.18e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 953 DECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEkkalteahqqtlddLQAEEDKVNTLTKAK 1032
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR--------------IRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1033 AKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEG----DLKLSLESVMDLENDKQQLEEKLKKKDFEMNEISSRIEDEQAL 1108
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1109 VNQLHKKIKELQARTEELEEELEADRASRAKVEKQRGDVARELEelserleeaggATSAQIEINKKRETDFLKLRRDLEE 1188
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA-----------ELAAELAELQQEAEELEALIARLEA 234
|
250
....*....|.
gi 2045330442 1189 AMLHHEATTAA 1199
Cdd:COG4942 235 EAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1072-1292 |
1.34e-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: 46.30 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1072 ESVMDLENDKQQLEEKLKKKDFEMNEISSRIEDEQAL-------VNQLHKKIKELQARTEELEEELEADRASRAKVEKQR 1144
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQlaalerrIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1145 GDVARELEELSERLEEAGGATSAQIEINKKRETDFLKLRRDLEEAMLHHEATTAALRKKhadsVAELSEQIDSLQRVKQK 1224
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 1225 LEKERSEAKMEVDDLASTVEQLSKGKATSEKMCRLYEDQMNEAKAKVDELQRQLNETNTQRARAQAES 1292
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
847-1122 |
1.35e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 847 LLRSAAT-EKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEdrcdlliktKI-QLE 924
Cdd:PRK04863 284 HLEEALElRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQE---------KIeRYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 925 AKVKELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKV-----EKEKHATE-NKVKNLIEEMAAL----- 993
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYqqaldVQQTRAIQyQQAVQALERAKQLcglpd 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 994 ------DETILKLTKEKKALTEAH---QQTLDDLQA---EEDKVNTLTKAKA---------------------------- 1033
Cdd:PRK04863 435 ltadnaEDWLEEFQAKEQEATEELlslEQKLSVAQAahsQFEQAYQLVRKIAgevsrseawdvarellrrlreqrhlaeq 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1034 --KLEQQVDDLEGSLEQEKkvrmDLERVRRKLEGDLKLSLESVMDLENDKQQLEEKLKKKDFEMNEISSRIEDEQALVNQ 1111
Cdd:PRK04863 515 lqQLRMRLSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
|
330
....*....|.
gi 2045330442 1112 LHKKIKELQAR 1122
Cdd:PRK04863 591 LQARIQRLAAR 601
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
850-1064 |
1.36e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 850 SAATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDlliktkiQLEAKVKE 929
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 930 LMERLEDeeemSANVLAKKRKLEDECSELK--KDIDDLEITLAKVEKEKHATENKVKNLIEEMAALdetilkltKEKKAL 1007
Cdd:COG3883 84 RREELGE----RARALYRSGGSVSYLDVLLgsESFSDFLDRLSALSKIADADADLLEELKADKAEL--------EAKKAE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 1008 TEAHQQTLDDLQAE-EDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLE 1064
Cdd:COG3883 152 LEAKLAELEALKAElEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
851-1111 |
1.36e-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: 47.07 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 851 AATEKELAALKEELAKLKEALEKSEVKR----KELEEKQVSLIQEKNDLALQLQAEQDnladaEDRCDLLIKTKIQLEAK 926
Cdd:pfam18971 599 AVAEAKSTGNYDEVKKAQKDLEKSLRKRehleKEVEKKLESKSGNKNKMEAKAQANSQ-----KDEIFALINKEANRDAR 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 927 VKELMERLEdeeemsanvlAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKnliEEMAALDETI--LKLTKEK 1004
Cdd:pfam18971 674 AIAYTQNLK----------GIKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAE---ETLKALKGSVkdLGINPEW 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1005 KALTEAHQQTLDDLQAEEDK-VNTLTKAKAKLEQQVDDLEGSLEQEKKV-RMDLERVRRKLEGDLKLSLESVMDLEN-DK 1081
Cdd:pfam18971 741 ISKVENLNAALNEFKNGKNKdFSKVTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKNfSK 820
|
250 260 270
....*....|....*....|....*....|.
gi 2045330442 1082 QQLEEKLKK-KDFEMNEISSRIEDEQALVNQ 1111
Cdd:pfam18971 821 EQLAQQAQKnEDFNTGKNSELYQSVKNSVNK 851
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1064-1319 |
1.37e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1064 EGDLKLSLESVMDLENDKQQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARTEELEEEleadrasrakVEKQ 1143
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE----------IEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1144 RGDVAREleelserleeaggATSAQIEINKKRETDFLKLRRDLEEAMlhheaTTAALRKKHADSVAELseqIDSLQRVKQ 1223
Cdd:COG3883 85 REELGER-------------ARALYRSGGSVSYLDVLLGSESFSDFL-----DRLSALSKIADADADL---LEELKADKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1224 KLEKERSEAKMEVDDLASTVEQLSKGKATsekmcrlYEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEERE 1303
Cdd:COG3883 144 ELEAKKAELEAKLAELEALKAELEAAKAE-------LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
250
....*....|....*.
gi 2045330442 1304 AMVSQLQRAKNSLTQN 1319
Cdd:COG3883 217 AAAAAAAAAAAAAAAA 232
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1356-1477 |
1.39e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1356 DEEQEAKAELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKklvtRLQEAEESVEasnAKCSSLEKTKHRLQTEIED 1435
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEK----RLLQKEENLD---RKLELLEKREEELEKKEKE 118
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2045330442 1436 lvidleranaaaaaLDKKQRNFDKVLAEWKQKYEECQSELES 1477
Cdd:PRK12704 119 --------------LEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
867-1099 |
1.42e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 47.24 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 867 LKEALEKSEVKRKELEEKQVSLIQE---KNDLALQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELM-ERLEDEEEMSA 942
Cdd:PLN03188 1045 PEKKLEQERLRWTEAESKWISLAEElrtELDASRALAEKQKHELDTEKRCAEELKEAMQMAMEGHARMlEQYADLEEKHI 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 943 NVLAKKRKLEDECSELKKD-------------IDDL--EITLAKVEKEKHAT----ENK-----VKNLIEEMAALDETIL 998
Cdd:PLN03188 1125 QLLARHRRIQEGIDDVKKAaaragvrgaeskfINALaaEISALKVEREKERRylrdENKslqaqLRDTAEAVQAAGELLV 1204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 999 KLTKEKKALTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEgslEQEKKVRMDLERVRRKLEGDLKLSLESVMDLE 1078
Cdd:PLN03188 1205 RLKEAEEALTVAQKRAMDAEQEAAEAYKQIDKLKRKHENEISTLN---QLVAESRLPKEAIRPACNDDCMAKYDAGEPLS 1281
|
250 260
....*....|....*....|....*
gi 2045330442 1079 NDKQQLEEKL----KKKDFEMNEIS 1099
Cdd:PLN03188 1282 EGDQQWREEFepfyKKEDGELSKLA 1306
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1468-1680 |
1.49e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1468 YEECQSELESSQKEsrglstELFKLKNSYEETLDHLETIKRENKNLQEEIADLsdqISQGSKTIHELEKMKKGLDMEKSD 1547
Cdd:PHA02562 200 YNKNIEEQRKKNGE------NIARKQNKYDELVEEAKTIKAEIEELTDELLNL---VMDIEDPSAALNKLNTAAAKIKSK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1548 IQAALEEVEGTLEHEESKTLRIQLElnqikaDVDRKLAEKDEEIDNLrrshQRSMESMQTTLDAEAKSRNEAVRLRKK-- 1625
Cdd:PHA02562 271 IEQFQKVIKMYEKGGVCPTCTQQIS------EGPDRITKIKDKLKEL----QHSLEKLDTAIDELEEIMDEFNEQSKKll 340
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2045330442 1626 -MECDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMA 1680
Cdd:PHA02562 341 eLKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKS 396
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1489-1911 |
1.50e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 46.77 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1489 LFKLKNSYEEtLDHLETIKRE--NKNLQEEIADLSdQISQGSKTIHELEKMKKG----LDMEKSDIQAALEEVEGTLE-H 1561
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKVK-KLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELNDkY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1562 EESKTLRIQLELNQIKADVDRKLAEKDEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLR-------KKMECDLNEME 1634
Cdd:pfam06160 80 RFKKAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRfsygpaiDELEKQLAEIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1635 VQLNHANrQASESQKLlrnlqVQIKDIQLELDDTVHQNEELKEQM-ALTERRNNLLSSEVEELRA----LLEQNdraRKL 1709
Cdd:pfam06160 160 EEFSQFE-ELTESGDY-----LEAREVLEKLEEETDALEELMEDIpPLYEELKTELPDQLEELKEgyreMEEEG---YAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1710 AEHELLEATERVNLLHSQNTGLINQK--KKLESDLSTLSNEVDdAVQECRNAEEKAKKaitdaammaeELKKEQDT-SSH 1786
Cdd:pfam06160 231 EHLNVDKEIQQLEEQLEENLALLENLelDEAEEALEEIEERID-QLYDLLEKEVDAKK----------YVEKNLPEiEDY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1787 LERMKKNMEQTVKDLQM-----RLDEAEQIALKGGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKElsyq 1861
Cdd:pfam06160 300 LEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEE---- 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1862 aeedkknlarlqdlIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHEL 1911
Cdd:pfam06160 376 --------------IEEEQEEFKESLQSLRKDELEAREKLDEFKLELREI 411
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1194-1437 |
1.56e-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: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1194 EATTAALRKKHADSVAELSEQIDSLQRVKQKLEkersEAKMEVDDLASTVEQLSkgkatsekmcrLYEDqmNEAKAKVDE 1273
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLD----QLKEQLQLLNKLLPQAN-----------LLAD--ETLADRLEE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1274 LQRQLNETNtqraRAQAESGEVGRKLEEREAMVSQLQR---AKNSLTQNVEELKKQLEEENKAKSALAHSLQSSRH---- 1346
Cdd:COG3096 898 LREELDAAQ----EAQAFIQQHGKALAQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHfsye 973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1347 --------DCDL---LREQYDEEQEAKAELQRALSKANAEVAQW-----------RTKYET--DAIQRTEELE-----EA 1397
Cdd:COG3096 974 davgllgeNSDLnekLRARLEQAEEARREAREQLRQAQAQYSQYnqvlaslkssrDAKQQTlqELEQELEELGvqadaEA 1053
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2045330442 1398 KKKLVTRLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLV 1437
Cdd:COG3096 1054 EERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQ 1093
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
853-1091 |
1.69e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 853 TEKELAALKEE---LAKLKEALEKSEVKRKELEEKQVSliqeknDLALQLQAEQDN---LADAEDRCDlliktkiQLEAK 926
Cdd:PRK01156 488 IEIEVKDIDEKivdLKKRKEYLESEEINKSINEYNKIE------SARADLEDIKIKineLKDKHDKYE-------EIKNR 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 927 VKEL-MERLEDEEEMSANVLAKKRKLEDEC-----SELKKDIDDLEITLAKVEKE----KHATENKVKNLIEEMAALDET 996
Cdd:PRK01156 555 YKSLkLEDLDSKRTSWLNALAVISLIDIETnrsrsNEIKKQLNDLESRLQEIEIGfpddKSYIDKSIREIENEANNLNNK 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 997 IlKLTKEKKALTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMD 1076
Cdd:PRK01156 635 Y-NEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINE 713
|
250
....*....|....*
gi 2045330442 1077 LENDKQQLEEKLKKK 1091
Cdd:PRK01156 714 LSDRINDINETLESM 728
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
848-986 |
2.08e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 848 LRSAATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQL-QAEQDNLADAEDRCDLLIKTKIQLEAK 926
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERR 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2045330442 927 VKELMERL-----------EDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNL 986
Cdd:COG4913 361 RARLEALLaalglplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1757-1923 |
2.14e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1757 RNAEEKAKKAITDAAMMAEELKKEqdtsshLERMKKNMEQTVKDlqmrldeaEQIALKggkkqvQKLEARVKELENELES 1836
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKE------AEAIKKEALLEAKE--------EIHKLR------NEFEKELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1837 EQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEAEEQAnSNLTKYRKLQHELDDAEE 1916
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI-SGLTAEEAKEILLEKVEE 165
|
....*....
gi 2045330442 1917 --RADMAET 1923
Cdd:PRK12704 166 eaRHEAAVL 174
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1787-1905 |
2.22e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.73 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1787 LERMKK-NMEQTVKDLQMRLDEAE------QIALKGGKKQVQKLEARVKELENELESEQRKSQEYQkvvrkyeRRIKELS 1859
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEaersrlQALLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2045330442 1860 YQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEE-------AEEQANSNLTKYR 1905
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADlgrrlnvALAQRVQELNRYR 196
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
847-1104 |
2.39e-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: 46.32 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 847 LLRSAATEKELAALKEELAKLKEALEKSEVKRKELEekqvsliQEKNDLalqlqaeQDNLADAEDRCDLLIKTKIQLEAK 926
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQ-------QERDEL-------ADEIASGASGKSALQDEKRRLEAR 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 927 VKELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETIlkLTKEKKA 1006
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTV--KSKFKSS 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1007 LteahqqtlddlqaeedkvntltkakAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQLEE 1086
Cdd:pfam01576 969 I-------------------------AALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKD 1023
|
250
....*....|....*...
gi 2045330442 1087 KLKKKDFEMNEISSRIED 1104
Cdd:pfam01576 1024 QAEKGNSRMKQLKRQLEE 1041
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1735-1935 |
2.42e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1735 KKKLESDLSTLSNEVDDaVQECRNAEEKAKKAI---TDAAMMAEELKKEQDTSSHLERMKK-----NMEQTVKDLQMRLD 1806
Cdd:COG4913 220 EPDTFEAADALVEHFDD-LERAHEALEDAREQIellEPIRELAERYAAARERLAELEYLRAalrlwFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1807 EAEQiALKGGKKQVQKLEARVKELENELES--EQRKSQEYQKVVRkYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVK 1884
Cdd:COG4913 299 ELRA-ELARLEAELERLEARLDALREELDEleAQIRGNGGDRLEQ-LEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2045330442 1885 SYKRQAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQVNKLRVRTRDQ 1935
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1461-1859 |
2.63e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 45.66 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1461 LAEWKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETikrENKNLQEEIADLSDQISQGSKTIHELEKMKKG 1540
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKE---ELRQSREKHEELEEKYKELSASSEELSEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1541 LDMEKSDIQAALEEVEGTLEHEESKTLRIQLELNQIKADVDRKLAEKDEEidnlrrshQRSMESMQTTLDAeakSRNEAV 1620
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE--------EAERKQLQAKLQQ---TEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1621 RLRKKMECDLNEMEVQLNHANRQASESQKLLRNL-QVQIKDIQLELddTVHQNEELKEQMALTERRNNLLSsevEELRAL 1699
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLtTAHRKEAENEA--LLEELRSLQERLNASERKVEGLG---EELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1700 LEQNDRARKLAEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVD---DAVQECRNAEEKAKKAITDAAMMAEE 1776
Cdd:pfam07888 264 AAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEadkDRIEKLSAELQRLEERLQEERMEREK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1777 LKKEqdtsshLERMKknmeqtvkdlqmrldEAEQIALKGGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIK 1856
Cdd:pfam07888 344 LEVE------LGREK---------------DCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
...
gi 2045330442 1857 ELS 1859
Cdd:pfam07888 403 TVA 405
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1640-1911 |
2.71e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.98 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1640 ANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMA-----LTERRNNLLS---------SEVEE-LRALLEQND 1704
Cdd:PRK04778 103 AKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEqlkdlYRELRKSLLAnrfsfgpalDELEKqLENLEEEFS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1705 RARKLAEH-ELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKA---ITDAAMMAE--ELK 1778
Cdd:PRK04778 183 QFVELTESgDYVEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEgyhLDHLDIEKEiqDLK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1779 KE-QDTSSHLERMK-KNMEQTVKDLQMRLD------EAEQIALKGGKKQVQKLE---ARVKELENELESE-QRKSQEYQ- 1845
Cdd:PRK04778 263 EQiDENLALLEELDlDEAEEKNEEIQERIDqlydilEREVKARKYVEKNSDTLPdflEHAKEQNKELKEEiDRVKQSYTl 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1846 -----KVVRKYERRIKELSYQAEEDKKNLA-----------RLQDL------IDKLQAKVKSYKRQAEEAEEQANSNLTK 1903
Cdd:PRK04778 343 neselESVRQLEKQLESLEKQYDEITERIAeqeiayselqeELEEIlkqleeIEKEQEKLSEMLQGLRKDELEAREKLER 422
|
....*...
gi 2045330442 1904 YRKLQHEL 1911
Cdd:PRK04778 423 YRNKLHEI 430
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1459-1664 |
2.72e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1459 KVLAEWKQKYEECQSEL--ESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKnlqeeIADLSDQISQGSKTIHELEK 1536
Cdd:COG3206 152 AVANALAEAYLEQNLELrrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1537 MKKGLDMEKSDIQAALEEVEGTLE------HEESKTLRIQLELNQIkADVDRKLAEK--------------DEEIDNLRR 1596
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGsgpdalPELLQSPVIQQLRAQL-AELEAELAELsarytpnhpdvialRAQIAALRA 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2045330442 1597 SHQRSMESMQTTLDAEAKS--------RNEAVRLRKKMEcDLNEMEVQLNHANRQASESQKLLRNLQVQIKDIQLE 1664
Cdd:COG3206 306 QLQQEAQRILASLEAELEAlqareaslQAQLAQLEARLA-ELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1018-1233 |
3.22e-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: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1018 LQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQLEEKLKKKDFEMNE 1097
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1098 ISSRIEDEQALVNQLHKKI--KELQARTEELEEELEADRASRA-----KVEKQRGDVARELEELSERLEEAGGATSAQIE 1170
Cdd:COG4942 95 LRAELEAQKEELAELLRALyrLGRQPPLALLLSPEDFLDAVRRlqylkYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2045330442 1171 INKKRETDFLKLRRDLEEAMLHHEATTAALRKK---HADSVAELSEQIDSLQRVKQKLEKERSEAK 1233
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKElaeLAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
781-1048 |
4.23e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 781 LEEMRDERLAKVLTLLQAAARGKIMRTELMKMNERREALMIIQwnirafntvkhwpwmKLFFKIkplLRSAATEKELAAL 860
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA---------------EYSWDE---IDVASAEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 861 KEE----------LAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRcdLLIKTKIQLEAKVKEL 930
Cdd:COG4913 674 EAElerldassddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR--LEAAEDLARLELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 931 MERLEdEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKE-KHATENKVKNLIEEMAALDETILKLT-------- 1001
Cdd:COG4913 752 EERFA-AALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALLDrleedglp 830
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2045330442 1002 ----KEKKALTEAHQQTLDDLQAEedkvntLTKAKAKLEQQVDDLEGSLEQ 1048
Cdd:COG4913 831 eyeeRFKELLNENSIEFVADLLSK------LRRAIREIKERIDPLNDSLKR 875
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1787-1909 |
4.60e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1787 LERMKKNMEQTVKDLQMRLDEAEQIALKGGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDK 1866
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREI 461
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2045330442 1867 KN---LARLQDLIDKLQAKVKSYKRQAEEAEEQANSnLTKYRKLQH 1909
Cdd:COG2433 462 RKdreISRLDREIERLERELEEERERIEELKRKLER-LKELWKLEH 506
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1213-1434 |
4.80e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1213 EQIDSLQRVKQK---LEKERSEAKMEVDDLASTVEQLsKGKATSEKMCRLyedqmneAKAKVDELQRQLNETNTQRARAQ 1289
Cdd:PRK11281 70 ALLDKIDRQKEEteqLKQQLAQAPAKLRQAQAELEAL-KDDNDEETRETL-------STLSLRQLESRLAQTLDQLQNAQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1290 AESGEVGRKLeerEAMVSQLQRAKNSLTQNVeelkKQLEEENKAKSALAHSLQSSRHDcdlLREQYDEEQ---EAKAELQ 1366
Cdd:PRK11281 142 NDLAEYNSQL---VSLQTQPERAQAALYANS----QRLQQIRNLLKGGKVGGKALRPS---QRVLLQAEQallNAQNDLQ 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2045330442 1367 RALSKANA---EVAQWRTKYETDAIQRTEELEEAKKKLVT--RLQEAEESV-EASNAKCSSLEKTKHRLQTEIE 1434
Cdd:PRK11281 212 RKSLEGNTqlqDLLQKQRDYLTARIQRLEHQLQLLQEAINskRLTLSEKTVqEAQSQDEAARIQANPLVAQELE 285
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
854-1006 |
4.86e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 854 EKELAAlKEELAKLKEALEK-SEVKRKELEEKQVSLIQEKNDLalqlqaeqdnladaEDRCDLLIKTKIQLEAKVKELME 932
Cdd:PRK12704 57 EALLEA-KEEIHKLRNEFEKeLRERRNELQKLEKRLLQKEENL--------------DRKLELLEKREEELEKKEKELEQ 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 933 RLEDEEEMSANVLAKKRKLEDE---CSELKKDiDDLEITLAKVEKE-KHATENKVKNlIEEMAaldetilKLTKEKKA 1006
Cdd:PRK12704 122 KQQELEKKEEELEELIEEQLQElerISGLTAE-EAKEILLEKVEEEaRHEAAVLIKE-IEEEA-------KEEADKKA 190
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
854-1103 |
5.39e-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: 44.84 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 854 EKELAALKEELAKLKEALEKSEVK--RKELEEKQVSLIQEKNDLAL------QLQAE-QDNLADAEDRCDLLIKTKIQLE 924
Cdd:pfam06160 152 EKQLAEIEEEFSQFEELTESGDYLeaREVLEKLEEETDALEELMEDipplyeELKTElPDQLEELKEGYREMEEEGYALE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 925 AKvkELMERLEDEEEMSANVLAKKRKL-----EDECSELKKDIDDLEITLakvEKEKHAtENKVKNLIEEMAALDETILK 999
Cdd:pfam06160 232 HL--NVDKEIQQLEEQLEENLALLENLeldeaEEALEEIEERIDQLYDLL---EKEVDA-KKYVEKNLPEIEDYLEHAEE 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1000 LTKEKKALTEAHQQ--TLDDlqAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKV----RMDLERVRRKLEG---DLKLS 1070
Cdd:pfam06160 306 QNKELKEELERVQQsyTLNE--NELERVRGLEKQLEELEKRYDEIVERLEEKEVAyselQEELEEILEQLEEieeEQEEF 383
|
250 260 270
....*....|....*....|....*....|...
gi 2045330442 1071 LESVMDLENDKQQLEEKLKKKDFEMNEISSRIE 1103
Cdd:pfam06160 384 KESLQSLRKDELEAREKLDEFKLELREIKRLVE 416
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1646-1851 |
5.77e-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: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1646 ESQKLLRNLQvqikDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQNDRARKLAEHELLEATERVNLLH 1725
Cdd:COG1579 4 EDLRALLDLQ----ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1726 SQNTGLINQKkklesDLSTLSNEVDDAVQECRNAEEKAKKAItdaammaEELKKEQDTSSHLERMKKNMEQTVKDLQMRL 1805
Cdd:COG1579 80 EQLGNVRNNK-----EYEALQKEIESLKRRISDLEDEILELM-------ERIEELEEELAELEAELAELEAELEEKKAEL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2045330442 1806 DEAEQIAlkggKKQVQKLEARVKELENELESEQRKsqEYQKVVRKY 1851
Cdd:COG1579 148 DEELAEL----EAELEELEAEREELAAKIPPELLA--LYERIRKRK 187
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
982-1468 |
6.28e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 982 KVKNLIEEMAALDETIlkltKEKKALTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLE------GSLEQEKKVRMD 1055
Cdd:COG4717 65 KPELNLKELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllqllPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1056 LERVRRKLEgDLKLSLESVMDLENDKQQLEEKLKKKDFEMNEISSRI-EDEQALVNQLHKKIKELQARTEELEEELEADR 1134
Cdd:COG4717 141 LAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1135 ASRAKVEKQRGDVARELEELSERLEEAGGATSAQIeinkkretdfLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQ 1214
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARLLLLI----------AAALLALLGLGGSLLSLILTIAGVLFLVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1215 IDSLQRVKQKLEKERSEAkmevdDLASTVEQLSKgkatsEKMCRLYEDQMNEAKAKVDELQRQLNE-TNTQRARAQAESg 1293
Cdd:COG4717 290 FLLLAREKASLGKEAEEL-----QALPALEELEE-----EELEELLAALGLPPDLSPEELLELLDRiEELQELLREAEE- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1294 evgrklEEREAMVSQLQRAKNSLTQNveelkkqleeenkaksALAHSLQSSRHDCDLLREqYDEEQEAKAELQRALSKAN 1373
Cdd:COG4717 359 ------LEEELQLEELEQEIAALLAE----------------AGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1374 AEVAQWRTKYETDAI-QRTEELEEAKKKLVTRLQEAEESVEASNAKCSSLEK--TKHRLQTEIEDLVIDLERANAAAAAL 1450
Cdd:COG4717 416 GELEELLEALDEEELeEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEWAAL 495
|
490
....*....|....*...
gi 2045330442 1451 DKKQRNFDKVLAEWKQKY 1468
Cdd:COG4717 496 KLALELLEEAREEYREER 513
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
851-1521 |
6.33e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.83 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 851 AATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSL---------IQEKNDLALQLQAEQDN--LADAEDRCDLLIKT 919
Cdd:pfam12128 326 ALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLkaltgkhqdVTAKYNRRRSKIKEQNNrdIAGIKDKLAKIREA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 920 KIQLEAKVKELMERLEDE-----EEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEkEKHATENKVKNLIEEMAALD 994
Cdd:pfam12128 406 RDRQLAVAEDDLQALESElreqlEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLL-QLENFDERIERAREEQEAAN 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 995 ETILKLTKEKKALTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQekkvrmdlerVRRKLEGDLKLSLESV 1074
Cdd:pfam12128 485 AEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLH----------FLRKEAPDWEQSIGKV 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1075 MDLEN------DKQQLEEKLKKkdfEMNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQRgdva 1148
Cdd:pfam12128 555 ISPELlhrtdlDPEVWDGSVGG---ELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQL---- 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1149 releelserleeagGATSAQIEINKKRETDflkLRRDLEEAMLhheattaalrkkhadSVAELSEQIDSLQRVKQK-LEK 1227
Cdd:pfam12128 628 --------------VQANGELEKASREETF---ARTALKNARL---------------DLRRLFDEKQSEKDKKNKaLAE 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1228 ERSEAKMEVDDLASTVEQLskgkatsekmcrlyedqMNEAKAKVDELQRQLNETNTQraraqaesgevgrKLEEREAMVS 1307
Cdd:pfam12128 676 RKDSANERLNSLEAQLKQL-----------------DKKHQAWLEEQKEQKREARTE-------------KQAYWQVVEG 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1308 QLQRAKNSLTQNVEELKKQLEEENKA-KSALAHSLQSSRHDCDLLREQYDEEQEAKAELQRAlSKANAEVAQWRTKYETD 1386
Cdd:pfam12128 726 ALDAQLALLKAAIAARRSGAKAELKAlETWYKRDLASLGVDPDVIAKLKREIRTLERKIERI-AVRRQEVLRYFDWYQET 804
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1387 AIQRteeleeaKKKLVTRLQEAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQ 1466
Cdd:pfam12128 805 WLQR-------RPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKE 877
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 2045330442 1467 KYEECQSELESSQKESRGlstELFKLKNSYEEtldhlETIKRENKNLQEEIADLS 1521
Cdd:pfam12128 878 DANSEQAQGSIGERLAQL---EDLKLKRDYLS-----ESVKKYVEHFKNVIADHS 924
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
841-1122 |
6.56e-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: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 841 FFKIKPLLRSA-----ATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEkndlalqLQAEQDNLADAEDrcdl 915
Cdd:pfam06160 81 FKKAKKALDEIeelldDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKT-------LLANRFSYGPAID---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 916 liktkiQLEAKVKELMERLEDEEEMSAN---VLAKK--RKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEM 990
Cdd:pfam06160 150 ------ELEKQLAEIEEEFSQFEELTESgdyLEAREvlEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREM 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 991 A----ALDEtiLKLTKEKKALTEAHQQTLDDLqaEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGD 1066
Cdd:pfam06160 224 EeegyALEH--LNVDKEIQQLEEQLEENLALL--ENLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDY 299
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 1067 LKlslesvmDLENDKQQLEEKLK--KKDFEMNeissriEDEQALVNQLHKKIKELQAR 1122
Cdd:pfam06160 300 LE-------HAEEQNKELKEELErvQQSYTLN------ENELERVRGLEKQLEELEKR 344
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
773-1118 |
6.56e-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: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 773 FKAGLLGHLEEMRDERLAKVLTLLQAAArgKIMRTELMK-----MNERREALmiIQWNIRAFNTVKHWPWMKLFF----K 843
Cdd:pfam15818 5 FKTSLLEALEELRMRREAETQYEEQIGK--IIVETQELKwqketLQNQKETL--AKQHKEAMAVFKKQLQMKMCAleeeK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 844 IKPLLRSAATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLIKTKIQL 923
Cdd:pfam15818 81 GKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLHLLAKEDHHKQLNEIEKYYATITGQFGLVKENHGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 924 EAKVKELMErledeeeMSANVLAKKRKLEDECSELKKDIDDLEITLAKVE---KEKHATEN--------KVKNLIEEMAA 992
Cdd:pfam15818 161 EQNVQEAIQ-------LNKRLSALNKKQESEICSLKKELKKVTSDLIKSKvtcQYKMGEENinltikeqKFQELQERLNM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 993 LDETILKLTKEKKALTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEgslEQEKKVRMDLERVRRKLegdlKLSLE 1072
Cdd:pfam15818 234 ELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALK---ENNQTLERDNELQREKV----KENEE 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2045330442 1073 SVMDLENDKQQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKE 1118
Cdd:pfam15818 307 KFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQE 352
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1861-1937 |
6.86e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 6.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2045330442 1861 QAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQVNKLRVRTRDQVS 1937
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
847-1021 |
7.01e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 847 LLRSAATEKELAAlkEELAK--LKEALEKSEVKRKEleekqvsLIQEKNDLALQLQAEQDNlaDAEDRcdlliktkiqlE 924
Cdd:PRK12704 24 VRKKIAEAKIKEA--EEEAKriLEEAKKEAEAIKKE-------ALLEAKEEIHKLRNEFEK--ELRER-----------R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 925 AKVKELMERLEDEEEmsaNVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMaaldETILKLTKEk 1004
Cdd:PRK12704 82 NELQKLEKRLLQKEE---NLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL----ERISGLTAE- 153
|
170
....*....|....*..
gi 2045330442 1005 kaltEAHQQTLDDLQAE 1021
Cdd:PRK12704 154 ----EAKEILLEKVEEE 166
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
985-1187 |
7.11e-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: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 985 NLIEEMAALDETILKLTKE----KKALTEAhQQTLDDLQAEEDKVNTLTKAKAkLEQQVDDLEGSLEQEKKVRMDLERVR 1060
Cdd:COG3206 165 NLELRREEARKALEFLEEQlpelRKELEEA-EAALEEFRQKNGLVDLSEEAKL-LLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1061 RKLEGDLKLSLESVMDLENDK--QQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRA 1138
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2045330442 1139 KVEKQRGDVARELEElserleeaggATSAQIEINKKRETDFLKLRRDLE 1187
Cdd:COG3206 323 EALQAREASLQAQLA----------QLEARLAELPELEAELRRLEREVE 361
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1469-1815 |
7.44e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1469 EECQSELESSQKeSRGLSTELFKLKNSYEETLDHL---ETIKRENKNLQEEIADLSDQISQGSKtihELEKMKKGLDMEK 1545
Cdd:PRK11281 39 ADVQAQLDALNK-QKLLEAEDKLVQQDLEQTLALLdkiDRQKEETEQLKQQLAQAPAKLRQAQA---ELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1546 SDIQAALeevegTLEHEESKTLRIQLELNQIKADvdrkLAEKDEEIDNLRRSHQRSmesmQTTLDAEAKsRNEAVRLRKK 1625
Cdd:PRK11281 115 RETLSTL-----SLRQLESRLAQTLDQLQNAQND----LAEYNSQLVSLQTQPERA----QAALYANSQ-RLQQIRNLLK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1626 mecdlnemevQLNHANRQASESQKLLRNLQVQIKDIQLELddtvhqneelkeqmalterrnnllsseveeLRALLEQNDR 1705
Cdd:PRK11281 181 ----------GGKVGGKALRPSQRVLLQAEQALLNAQNDL------------------------------QRKSLEGNTQ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1706 ARKLAEHELLEATERVNLLHSQNT---GLINQKKKLESdlstlsnevDDAVQECRNAEEKAKkaITDAAMMAEELKKEQD 1782
Cdd:PRK11281 221 LQDLLQKQRDYLTARIQRLEHQLQllqEAINSKRLTLS---------EKTVQEAQSQDEAAR--IQANPLVAQELEINLQ 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2045330442 1783 TSSHLERMKKNMEQTVKD-LQMR--LDEA--------EQI-ALKG 1815
Cdd:PRK11281 290 LSQRLLKATEKLNTLTQQnLRVKnwLDRLtqsernikEQIsVLKG 334
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
908-1122 |
7.71e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 908 DAEDRCDLLIKTKIQLEAKVKELMERLED-EEEMSAnvLAKKRKLEDECSELKKDIDDLEitlakvekekhATENKVKNL 986
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEAlEAELDA--LQERREALQRLAEYSWDEIDVA-----------SAEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 987 IEEMAALDETILKLTKEKKALTEAHQQtlddLQAEEDKVNTLTKAKAKLEQQVDDLEgslEQEKKVRMDLERVRRKLEGD 1066
Cdd:COG4913 674 EAELERLDASSDDLAALEEQLEELEAE----LEELEEELDELKGEIGRLEKELEQAE---EELDELQDRLEAAEDLARLE 746
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2045330442 1067 LKLSLESVMDLENDKQQLEEKLKkkdfemnEISSRIEDEQALVNQLHKKIKELQAR 1122
Cdd:COG4913 747 LRALLEERFAAALGDAVERELRE-------NLEERIDALRARLNRAEEELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1267-1481 |
7.79e-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: 43.98 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1267 AKAKVDELQRQL-------NETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKAKSALAH 1339
Cdd:COG4942 18 QADAAAEAEAELeqlqqeiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1340 SLQSSRHD-CDLLREQYDEEQEAKAELqrALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEESVEASNAK 1418
Cdd:COG4942 98 ELEAQKEElAELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2045330442 1419 cssLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQKE 1481
Cdd:COG4942 176 ---LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1819-1924 |
8.22e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1819 QVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEAeeqan 1898
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV----- 85
|
90 100
....*....|....*....|....*.
gi 2045330442 1899 SNLTKYRKLQHELDDAEERADMAETQ 1924
Cdd:COG1579 86 RNNKEYEALQKEIESLKRRISDLEDE 111
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
1463-1577 |
8.29e-04 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 43.56 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1463 EWKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEkmKKGLd 1542
Cdd:COG4026 132 ELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELL--KKRL- 208
|
90 100 110
....*....|....*....|....*....|....*
gi 2045330442 1543 MEKSDIQAALEEVEGTLEHEESKTLRIQLELNQIK 1577
Cdd:COG4026 209 LEVFSLEELWKELFPEELPEEDFIYFATENLKPGK 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1261-1715 |
8.68e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1261 EDQMNEAKAKVDE---LQRQLNETNTQRARAQAESGEvgrkLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKAKSAL 1337
Cdd:COG4717 77 EEELKEAEEKEEEyaeLQEELEELEEELEELEAELEE----LREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1338 AHSLQSSRhdcdlLREQYDEEQEAKAELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEESVEASNA 1417
Cdd:COG4717 153 ERLEELRE-----LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1418 KCSSLEKTKHRLQTE-----------IEDLVIDLERANAAAAALDKKQRNFDKVLAE---WKQKYEECQSELESSQKESR 1483
Cdd:COG4717 228 ELEQLENELEAAALEerlkearllllIAAALLALLGLGGSLLSLILTIAGVLFLVLGllaLLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1484 GLSTELFKLKNsyEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKgldmeksdiQAALEEVEgtlehee 1563
Cdd:COG4717 308 QALPALEELEE--EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE---------ELQLEELE------- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1564 sktLRIQLELNQIKADVDRKLAEKDEEIDNlRRSHQRSMESMQTTLDAEAKSRNEAVRLRkkmecDLNEMEVQLNHANRQ 1643
Cdd:COG4717 370 ---QEIAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEAL-----DEEELEEELEELEEE 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2045330442 1644 ASESQKLLRNLQVQIKDIQLELDDTVHQNE--ELKEQMALTERRNNLLSSEVEELRALLEQNDRARKLAEHELL 1715
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
854-1119 |
8.77e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 854 EKELAALKEELAKLKEALEKSEVkrKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELM-- 931
Cdd:PRK04778 255 EKEIQDLKEQIDENLALLEELDL--DEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKee 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 932 -ERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLtkekkaltea 1010
Cdd:PRK04778 333 iDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKL---------- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1011 hQQTLDDLQAEEdkvntlTKAKAKLEQqvddlegsleqekkVRMDLERVRRKLEgdlKLSL----ESVMDL----ENDKQ 1082
Cdd:PRK04778 403 -SEMLQGLRKDE------LEAREKLER--------------YRNKLHEIKRYLE---KSNLpglpEDYLEMffevSDEIE 458
|
250 260 270
....*....|....*....|....*....|....*..
gi 2045330442 1083 QLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKEL 1119
Cdd:PRK04778 459 ALAEELEEKPINMEAVNRLLEEATEDVETLEEETEEL 495
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1467-1838 |
9.23e-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: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1467 KYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKS 1546
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1547 DIQAALeeveGTLEHEESKTLRIqleLNQIKADVDRKLAEKDEEIDNLRR----------SHQRSMESMQTTL-DAEAKS 1615
Cdd:pfam10174 433 NTDTAL----TTLEEALSEKERI---IERLKEQREREDRERLEELESLKKenkdlkekvsALQPELTEKESSLiDLKEHA 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1616 RNEAVRLRKKmECDLNEMEVQLNHANRQASEsqkllrnLQVQIKDIQlELDDTVHQNEELKEQMALTERR-------NNL 1688
Cdd:pfam10174 506 SSLASSGLKK-DSKLKSLEIAVEQKKEECSK-------LENQLKKAH-NAEEAVRTNPEINDRIRLLEQEvarykeeSGK 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1689 LSSEVEELRALL-----EQNDRARKLAEHELLEATErvnlLHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAEEKA 1763
Cdd:pfam10174 577 AQAEVERLLGILrevenEKNDKDKKIAELESLTLRQ----MKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNS 652
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2045330442 1764 KKAITDAAMMAEElkkeqDTSSHLERMKKNMEQTVKDLQMRldEAEQIALKGgkkqvqkleARVKELENELESEQ 1838
Cdd:pfam10174 653 QQLQLEELMGALE-----KTRQELDATKARLSSTQQSLAEK--DGHLTNLRA---------ERRKQLEEILEMKQ 711
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1731-1927 |
9.54e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1731 LINQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTsshLERMKKNMEQTVKDLQMRLDEAEQ 1810
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE---IEERREELGERARALYRSGGSVSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1811 IALKGGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELsyqaeedKKNLARLQDLIDKLQAKVKSYKRQA 1890
Cdd:COG3883 105 LDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAEL-------EAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 2045330442 1891 EEAEEQANSNLTKYRKLQHELDDAEERADMAETQVNK 1927
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
869-1541 |
9.90e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 869 EALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLAdaedrcdlliktkiqleakvkELMERLEDEEEMSANVLAKK 948
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELE---------------------NIKKQIADDEKSHSITLKEI 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 949 RKLEDECSELKKDIDDLEITLakvekekhatenkvknliEEMAALDETILKLTKEKKalteahqQTLDDLQAEEDKVNtl 1028
Cdd:PRK01156 221 ERLSIEYNNAMDDYNNLKSAL------------------NELSSLEDMKNRYESEIK-------TAESDLSMELEKNN-- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1029 tkakakleqqvdDLEGSLEQEKKVRMDLERVRRklegdlklslESVMDLENDKQQLEEKlkkkdfemNEISSRIEDEQAL 1108
Cdd:PRK01156 274 ------------YYKELEERHMKIINDPVYKNR----------NYINDYFKYKNDIENK--------KQILSNIDAEINK 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1109 VNQLHKKIKELQarteeleeeleADRASRAKVEKQRGDVARELEELSERLEEAGGATSAQIEINKKRETDFLKLRR---D 1185
Cdd:PRK01156 324 YHAIIKKLSVLQ-----------KDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERmsaF 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1186 LEEAMLHHEATTAALRKKHAD---SVAELSEQIDSLQRVKQKLEkersEAKMEVDDLASTVEQLSK--------GKATSE 1254
Cdd:PRK01156 393 ISEILKIQEIDPDAIKKELNEinvKLQDISSKVSSLNQRIRALR----ENLDELSRNMEMLNGQSVcpvcgttlGEEKSN 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1255 KMCRLYEDQMNEAKAKVDELQRQLNETNTQRARAQA-ESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKA 1333
Cdd:PRK01156 469 HIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKrKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKY 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1334 KSALAhslQSSRHDCDLLREQYDEEQEAKAElqralskanaevaqwRTKYETDAIQ-RTEELEEAKKKLVTRLQEAEESV 1412
Cdd:PRK01156 549 EEIKN---RYKSLKLEDLDSKRTSWLNALAV---------------ISLIDIETNRsRSNEIKKQLNDLESRLQEIEIGF 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1413 EASNakcSSLEKTKHRLQTEIEDL---VIDLERANAAAAALDKKQRNFDKVLAEwKQKYEECQSELESSQKESrglSTEL 1489
Cdd:PRK01156 611 PDDK---SYIDKSIREIENEANNLnnkYNEIQENKILIEKLRGKIDNYKKQIAE-IDSIIPDLKEITSRINDI---EDNL 683
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2045330442 1490 FKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGL 1541
Cdd:PRK01156 684 KKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1800-1938 |
1.04e-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: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1800 DLQMRLDEAEQIalkggKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDK- 1878
Cdd:COG1579 11 DLQELDSELDRL-----EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNv 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 1879 --------LQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQVNKLRVRTRDQVSK 1938
Cdd:COG1579 86 rnnkeyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1741-1906 |
1.05e-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: 42.60 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1741 DLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLERMKKNMEQTVKDLQMRLDEAEQiALKGGKKQV 1820
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-QLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1821 QklearVKELENELESEQRKsqeyqkvVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEAEEQANSN 1900
Cdd:COG1579 90 E-----YEALQKEIESLKRR-------ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
....*.
gi 2045330442 1901 LTKYRK 1906
Cdd:COG1579 158 LEELEA 163
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1654-1924 |
1.16e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.91 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1654 LQVQIKDIQLEL-------DDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQNDrarklaehELLEATERVNLLHS 1726
Cdd:pfam05622 64 LQKQLEQLQEENfrletarDDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEMD--------ILRESSDKVKKLEA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1727 QntgLINQKKKLEsDLSTLSNEVddavqecRNAEEKAKKAITDAAMMAEELKKEQDTSSHLERMKKNmeqtVKDLQMRLD 1806
Cdd:pfam05622 136 T---VETYKKKLE-DLGDLRRQV-------KLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQ----VQELHGKLS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1807 EAEQIALK---GGKKQVQKLEARVKELEN---------ELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNL--ARL 1872
Cdd:pfam05622 201 EESKKADKlefEYKKLEEKLEALQKEKERliierdtlrETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEImpAEI 280
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2045330442 1873 QDLIDKLQAKVKSYKRQAEEAEEQansnltKYRKLQHELDDAEERADMAETQ 1924
Cdd:pfam05622 281 REKLIRLQHENKMLRLGQEGSYRE------RLTELQQLLEDANRRKNELETQ 326
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1465-1902 |
1.32e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.91 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1465 KQKYEECQSELESSQKESRGLS------TELFKLKNSYEETLDHLETIKRENKNLQEE---IADLSDQISQGSKTIHELE 1535
Cdd:COG5022 833 RETEEVEFSLKAEVLIQKFGRSlkakkrFSLLKKETIYLQSAQRVELAERQLQELKIDvksISSLKLVNLELESEIIELK 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1536 KMKKGLDMEKSDIQAaleevegtlehEESKTLRIQLELNQIKADVDRKLAEKDEEidNLRRSHQRSMESMQTTLDAEAKS 1615
Cdd:COG5022 913 KSLSSDLIENLEFKT-----------ELIARLKKLLNNIDLEEGPSIEYVKLPEL--NKLHEVESKLKETSEEYEDLLKK 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1616 RNEAVRLRKKMECDLNEMEVQLNHANRQ---ASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTE-RRNNLLSS 1691
Cdd:COG5022 980 STILVREGNKANSELKNFKKELAELSKQygaLQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKlKGLLLLEN 1059
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1692 EVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQ----ECRNAEEKAKKAI 1767
Cdd:COG5022 1060 NQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMiklnLLQEISKFLSQLV 1139
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1768 TDAAMMAEELKKEQDTSSHLERMKKNMEQTVKDLQMRLDEAEQIALKGGKKQVQKLEARVKELENELESEQRKSQEYQKV 1847
Cdd:COG5022 1140 NTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFSGWPR 1219
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2045330442 1848 VRKYERRIKELSYQAEEDK-----------------KNLARLQDLIDKLQAKVKSYKRQAEEAEEQANSNLT 1902
Cdd:COG5022 1220 GDKLKKLISEGWVPTEYSTslkgfnnlnkkfdtpasMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQ 1291
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1349-1524 |
1.35e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 43.88 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1349 DLLREQYDEEQE-AKAELQR---ALSKAnaevaqwRTKYETDaIQRTEE----LEEAKKKLVTRLQEAEESVEASNAKCS 1420
Cdd:pfam10168 542 QVFREEYLKKHDlAREEIQKrvkLLKLQ-------KEQQLQE-LQSLEEerksLSERAEKLAEKYEEIKDKQEKLMRRCK 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1421 SLEKtkhRLQTEIEDLvIDLERANAAA-AALDKKQRNFDKVLAEWKQKYEECQSELESSQKESRglstelfklKNSYEET 1499
Cdd:pfam10168 614 KVLQ---RLNSQLPVL-SDAEREMKKElETINEQLKHLANAIKQAKKKMNYQRYQIAKSQSIRK---------KSSLSLS 680
|
170 180
....*....|....*....|....*
gi 2045330442 1500 LDHLETIKRENKNLQEEIADLSDQI 1524
Cdd:pfam10168 681 EKQRKTIKEILKQLGSEIDELIKQV 705
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1438-1625 |
1.52e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1438 IDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIK---------R 1508
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvrnnK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1509 ENKNLQEEIADLSDQISqgsktihELEKMKKGLDMEKSDIQAALEEVEGTLEHEESktlriqlELNQIKADVDRKLAEKD 1588
Cdd:COG1579 90 EYEALQKEIESLKRRIS-------DLEDEILELMERIEELEEELAELEAELAELEA-------ELEEKKAELDEELAELE 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 2045330442 1589 EEIDNLRRshQRsmESMQTTLDAEAKSRNEAVRLRKK 1625
Cdd:COG1579 156 AELEELEA--ER--EELAAKIPPELLALYERIRKRKN 188
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1728-1925 |
1.71e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.40 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1728 NTGLINQKKKLESDLSTLSNEVDDAvqecrnaeEKAKKAITDAAMMAEEL-KKEQDTSSHLERMKKNMEQTVKDLQMRLD 1806
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENAHKIQI--------EILEKELSSLAQETEELqKKATQTLAKAQQVNAESERTLGHAKELAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1807 EAEQIALKGgKKQVQKLEARVKELENELESE-QRKSQEYQKVVRkyERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKS 1885
Cdd:pfam06008 90 AIKNLIDNI-KEINEKVATLGENDFALPSSDlSRMLAEAQRMLG--EIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2045330442 1886 YKRQAEEAEEQANSNLTKYrklQHELDDAEERADMAETQV 1925
Cdd:pfam06008 167 PQEENKALANALRDSLAEY---EAKLSDLRELLREAAAKT 203
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1547-1928 |
1.77e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1547 DIQAALEEVEGTLEH-EESKTLR------IQLELNQIKADVDRKLAEKDEEID---NLRRSHQRSMESMqttldAEAKSR 1616
Cdd:COG3096 233 DMEAALRENRMTLEAiRVTQSDRdlfkhlITEATNYVAADYMRHANERRELSEralELRRELFGARRQL-----AEEQYR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1617 neAVRLRKKMEcDLNEMEVQLNHANRQASESQKLLRN---LQVQIKDIQLELDD----TVHQN---EELKEQMALTERRN 1686
Cdd:COG3096 308 --LVEMARELE-ELSARESDLEQDYQAASDHLNLVQTalrQQEKIERYQEDLEElterLEEQEevvEEAAEQLAEAEARL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1687 NLLSSEVEEL--------RALLEQNDRArkLAEHELLEATERVNLL----------------------HSQNTGLINQKK 1736
Cdd:COG3096 385 EAAEEEVDSLksqladyqQALDVQQTRA--IQYQQAVQALEKARALcglpdltpenaedylaafrakeQQATEEVLELEQ 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1737 KLeSDLSTLSNEVDDAVQ---------ECRNAEEKAKKAITDA------AMMAEELKKEQDTSSHLERMKKNMEQTVKDL 1801
Cdd:COG3096 463 KL-SVADAARRQFEKAYElvckiagevERSQAWQTARELLRRYrsqqalAQRLQQLRAQLAELEQRLRQQQNAERLLEEF 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1802 QMR----LDEAEQIALkggkkQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQDLID 1877
Cdd:COG3096 542 CQRigqqLDAAEELEE-----LLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLRE 616
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2045330442 1878 KLQAKVKSykrqAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQVNKL 1928
Cdd:COG3096 617 QSGEALAD----SQEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1787-1938 |
1.79e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1787 LERMKKNMEQTVKDLQMRLDEAEQiALKGGKKQVQKLEARVKELENELESEQRKSQEYQK---VVRKyERRIKELSYQAE 1863
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgNVRN-NKEYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2045330442 1864 EDKKNLARLQDLIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQVNKLRVRTRDQVSK 1938
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1483-1596 |
1.82e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1483 RGLSTE--LFKLKNsyEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKmkkgldmEKSDIQAALEEVEGTLE 1560
Cdd:COG2433 374 RGLSIEeaLEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA-------EVEELEAELEEKDERIE 444
|
90 100 110
....*....|....*....|....*....|....*.
gi 2045330442 1561 HEESKTLRIQLELNQiKADVDRKLAEKDEEIDNLRR 1596
Cdd:COG2433 445 RLERELSEARSEERR-EIRKDREISRLDREIERLER 479
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
778-1263 |
1.96e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 778 LGHLEEMRDERLAKVLTLLQAAARGKIMRTELMKMNERREALMIIQwnirafntvKHWPWMKLFFKIKPLLrsAATEKEL 857
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL---------QLLPLYQELEALEAEL--AELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 858 AALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRcdlliktkiqLEAKVKELMERLEde 937
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE----------LQQRLAELEEELE-- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 938 eemsanvlakkrKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIE-EMAALDETILKLTKEKKALTEAhqqTLD 1016
Cdd:COG4717 217 ------------EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAaALLALLGLGGSLLSLILTIAGV---LFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1017 DLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQLEEKLKKKdfemn 1096
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA----- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1097 eissRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAkvEKQRGDVARELEELSERLEEAGGATSAQIEINKKR- 1175
Cdd:COG4717 357 ----EELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA--EEYQELKEELEELEEQLEELLGELEELLEALDEEEl 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1176 ETDFLKLRRDLEEAmlhheattAALRKKHADSVAELSEQIDSLQRVK--QKLEKERSEAKMEVDDLASTVEQLSKGKATS 1253
Cdd:COG4717 431 EEELEELEEELEEL--------EEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEEWAALKLALELL 502
|
490
....*....|
gi 2045330442 1254 EKMCRLYEDQ 1263
Cdd:COG4717 503 EEAREEYREE 512
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
874-1248 |
1.97e-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: 43.21 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 874 SEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKELMERLEdeeEMSANVLAKKRKLED 953
Cdd:pfam09731 70 SVVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALE---EVLKEAISKAESATA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 954 ECSELKKDiddleitlakvekEKHATENKVKNLIEEMAALDETILKLTKEKKALTEAHQQTLDDLQAEEDKVNTlTKAKA 1033
Cdd:pfam09731 147 VAKEAKDD-------------AIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEE-EAAPP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1034 KLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQLEEKL--------KKKDFEMNEISSRIEDE 1105
Cdd:pfam09731 213 LLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFpdiipvlkEDNLLSNDDLNSLIAHA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1106 QALVNQLHKKIKELQARteeleeeleADRASRAKVEKQRGDVARELEELSERLEEAGGATSAQIEINKKRETdfLKLRRD 1185
Cdd:pfam09731 293 HREIDQLSKKLAELKKR---------EEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFERER--EEIRES 361
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2045330442 1186 LEEAM---LHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSK 1248
Cdd:pfam09731 362 YEEKLrteLERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNELLANLKGLEK 427
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1598-1918 |
2.04e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1598 HQRSMESMQttlDAEAKSRNEAVRLRKKMECDLNEMEVQlnhanRQASESQKLLrnlqvqikdiQLELDDTVHQNEElKE 1677
Cdd:pfam17380 280 HQKAVSERQ---QQEKFEKMEQERLRQEKEEKAREVERR-----RKLEEAEKAR----------QAEMDRQAAIYAE-QE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1678 QMALtERRNNLLSSEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQECR 1757
Cdd:pfam17380 341 RMAM-ERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1758 NAEEKAKKAITDAamMAEELKK-EQDTSSHLERMK-KNMEQTVKDLQMRLDEAEQialkggkkQVQKLEARVKELENELE 1835
Cdd:pfam17380 420 VEMEQIRAEQEEA--RQREVRRlEEERAREMERVRlEEQERQQQVERLRQQEEER--------KRKKLELEKEKRDRKRA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1836 SEQRKsqeyqKVVRK--YERRIKELsyqaEEDKKNLARLQDLIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDD 1913
Cdd:pfam17380 490 EEQRR-----KILEKelEERKQAMI----EEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRK 560
|
....*.
gi 2045330442 1914 A-EERA 1918
Cdd:pfam17380 561 AtEERS 566
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
915-1051 |
2.07e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.31 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 915 LLIKTKIQLEAK----------VKELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITL-AKVEKEKHATENKV 983
Cdd:smart00787 120 QLVKTFARLEAKkmwyewrmklLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALeEELRQLKQLEDELE 199
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2045330442 984 KNLIEEMAALDETILKLTKEKKALTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKK 1051
Cdd:smart00787 200 DCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1261-1487 |
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: 42.51 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1261 EDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKAKSALAHS 1340
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1341 LQSSRHDCDLL---------------REQYDEEQEAKAELQRALSKANAEVAQwrtkYETDAIQRTEELEEAKKKLVTRL 1405
Cdd:COG3883 95 LYRSGGSVSYLdvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEA----KKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1406 QEAEESVEASNAKCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQKESRGL 1485
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
..
gi 2045330442 1486 ST 1487
Cdd:COG3883 251 AA 252
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1461-1737 |
2.29e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1461 LAEWKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKG 1540
Cdd:COG4372 61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1541 LDMEKSDIQAALEEVEGTLEHEESKTLRIQLELNQIkadvdrKLAEKDEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAV 1620
Cdd:COG4372 141 LQSEIAEREEELKELEEQLESLQEELAALEQELQAL------SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1621 RLRKKMECDLNEMEvqlnhANRQASESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALL 1700
Cdd:COG4372 215 ELAEELLEAKDSLE-----AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
250 260 270
....*....|....*....|....*....|....*..
gi 2045330442 1701 EQNDRARKLAEHELLEATERVNLLHSQNTGLINQKKK 1737
Cdd:COG4372 290 EAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1351-1610 |
2.32e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.21 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1351 LREQYDEEQEAKAELQRALSKANAEVAQWRTKYETDAIQRTeELEEAKKKLVTRLQEAEESVEASNAKCSSLE------K 1424
Cdd:pfam00038 59 LRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRT-SAENDLVGLRKDLDEATLARVDLEAKIESLKeelaflK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1425 TKHrlQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEEcQSELESSQKEsrglstelfklknsyeetldhlE 1504
Cdd:pfam00038 138 KNH--EEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEE-IAAKNREEAE----------------------E 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1505 TIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEGTLEHEESktlRIQLELNQIKadvdRKL 1584
Cdd:pfam00038 193 WYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEE---RYELQLADYQ----ELI 265
|
250 260
....*....|....*....|....*.
gi 2045330442 1585 AEKDEEIDNLRRSHQRSMESMQTTLD 1610
Cdd:pfam00038 266 SELEAELQETRQEMARQLREYQELLN 291
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
847-1121 |
2.37e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 847 LLRSAATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLalqLQAEQDNLADAEDrcdlLIKTKIQLEAK 926
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL---VNAGSERLRAVKD----IKQERDQLLNE 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 927 VKELMERLEDeeeMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNlieeMAALDETILKLTKEKKA 1006
Cdd:pfam15921 662 VKTSRNELNS---LSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS----MEGSDGHAMKVAMGMQK 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1007 LTEAHQQTLDDLQAeedKVNTLTKAKAKLEQQVDDLEgslEQEKKVRMDLERV---RRKLEGDLKLSLESVMDLENDKQQ 1083
Cdd:pfam15921 735 QITAKRGQIDALQS---KIQFLEEAMTNANKEKHFLK---EEKNKLSQELSTVateKNKMAGELEVLRSQERRLKEKVAN 808
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2045330442 1084 LEEKLKKKDFEMNE---ISSRIEDEQALVNQLHK-KIKELQA 1121
Cdd:pfam15921 809 MEVALDKASLQFAEcqdIIQRQEQESVRLKLQHTlDVKELQG 850
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
811-934 |
2.48e-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: 40.18 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 811 KMNERREALMIIQWNIRAFNTVK-HWPwmklffKIKPLLRSAATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLI 889
Cdd:cd21759 40 KILYRREALIKIQKTVRGYLARKkHRP------RIKGLRKIRALEKQLKEMEEIASQLKKDKDKWTKQVKELKKEIDALI 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2045330442 890 QE-KNDlalqlqaEQDNLADAEDRCDlliktkiQLEAKVKELMERL 934
Cdd:cd21759 114 KKiKTN-------DMITRKEIDKLYN-------ALVKKVDKQLAEL 145
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1673-1859 |
2.65e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1673 EELKEQMALTERRNNLLSSEVEELRAL---------LEQndRARKLAEHE-LLEATERV-NLLHSQNTGLINQKKKLESD 1741
Cdd:COG0497 175 EELRADEAERARELDLLRFQLEELEAAalqpgeeeeLEE--ERRRLSNAEkLREALQEAlEALSGGEGGALDLLGQALRA 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1742 LSTLSnEVDDAVQEcrnaeekAKKAITDAAMMAEELkkeqdtSSHLERMKKNME---QTVKDLQMRLDEAEQIALKGGK- 1817
Cdd:COG0497 253 LERLA-EYDPSLAE-------LAERLESALIELEEA------ASELRRYLDSLEfdpERLEEVEERLALLRRLARKYGVt 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2045330442 1818 -KQV----QKLEARVKELENELESEQRKSQEYQKVVRKYERRIKELS 1859
Cdd:COG0497 319 vEELlayaEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLS 365
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
843-975 |
2.72e-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: 42.00 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 843 KIKPLLRSAATE---KELAALKEELAKLKEaleksevKRKELEEKQVSLIQEKNDLALQLQAEQDNLADAEDRCDLLIKT 919
Cdd:pfam15294 118 KLEPLNEGGGSAllhMEIERLKEENEKLKE-------RLKTLESQATQALDEKSKLEKALKDLQKEQGAKKDVKSNLKEI 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2045330442 920 KiQLEAKVKELMERLEDEEEMSANVLAkkrKLEDECSELKKDIDDLEITLAKVEKE 975
Cdd:pfam15294 191 S-DLEEKMAALKSDLEKTLNASTALQK---SLEEDLASTKHELLKVQEQLEMAEKE 242
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1570-1931 |
2.73e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.89 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1570 QLELNQIKADVDRKLAEKDEEIDNLRRSHQRSMESMQTTLDAEAKSRneavrlRKKMECDLNEMEVQL-NHANRQASESQ 1648
Cdd:NF041483 82 QIQADQLRADAERELRDARAQTQRILQEHAEHQARLQAELHTEAVQR------RQQLDQELAERRQTVeSHVNENVAWAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1649 KLLRNLQVQIKDIqleLDDTVHQNEEL-----KEQMALTERRNNLLSSEVEELRALLEQN-DRARKLAEHEL-------L 1715
Cdd:NF041483 156 QLRARTESQARRL---LDESRAEAEQAlaaarAEAERLAEEARQRLGSEAESARAEAEAIlRRARKDAERLLnaastqaQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1716 EATERVNLLHSQNTGLINQKKKLESDLSTLS----NEVDDAVQECRNAEEKAKKAITDAA---MMAEELKKEQDTSSHLE 1788
Cdd:NF041483 233 EATDHAEQLRSSTAAESDQARRQAAELSRAAeqrmQEAEEALREARAEAEKVVAEAKEAAakqLASAESANEQRTRTAKE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1789 RMKKNMEQTVKDLQMRLDEAEQiALKGGKKQVQKLEARVKELENELESEQRKSQeyqkvVRKYERRIKELSYQAEEDKKN 1868
Cdd:NF041483 313 EIARLVGEATKEAEALKAEAEQ-ALADARAEAEKLVAEAAEKARTVAAEDTAAQ-----LAKAARTAEEVLTKASEDAKA 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2045330442 1869 LARlqdlidklqAKVKSYKRQAEEAEEQANSNLTKYRKLQHEL-----DDAEE-RADMAETQVNKLRVR 1931
Cdd:NF041483 387 TTR---------AAAEEAERIRREAEAEADRLRGEAADQAEQLkgaakDDTKEyRAKTVELQEEARRLR 446
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
932-1119 |
2.82e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 932 ERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMA-------ALDETILKLTKEK 1004
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQelrekrdELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1005 KALTE---AHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEG-------SLEQEKKVRMDLERVRRKLEGdlklsLESV 1074
Cdd:COG1340 81 DELNEklnELREELDELRKELAELNKAGGSIDKLRKEIERLEWrqqtevlSPEEEKELVEKIKELEKELEK-----AKKA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2045330442 1075 MDLENDKQQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKEL 1119
Cdd:COG1340 156 LEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIEL 200
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1616-1882 |
2.93e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1616 RNEAVRLRKKMECDLNEMEVQLNHANRQASEsqkllrnLQVQIKDIQLELDDTVHQNEELKEQMAL--TERRNNLLSSEV 1693
Cdd:pfam15905 89 RGEQDKRLQALEEELEKVEAKLNAAVREKTS-------LSASVASLEKQLLELTRVNELLKAKFSEdgTQKKMSSLSMEL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1694 EELRALLEQNDRARKLAEHEL---LEATERvNLLHSQNTgLINQKKKLesdlstLSNEVDDAVQECRNaeEKAKKAITDA 1770
Cdd:pfam15905 162 MKLRNKLEAKMKEVMAKQEGMegkLQVTQK-NLEHSKGK-VAQLEEKL------VSTEKEKIEEKSET--EKLLEYITEL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1771 AMMAEELKKEQDTSSHLERMKKNMEQTVKDLQMRLDEAEQIAlkggKKQVQKLEARVKELENELEseqrksqeyqKVVRK 1850
Cdd:pfam15905 232 SCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQEL----SKQIKDLNEKCKLLESEKE----------ELLRE 297
|
250 260 270
....*....|....*....|....*....|..
gi 2045330442 1851 YERRIKELSYQAEEDKKNLARLQDLIDKLQAK 1882
Cdd:pfam15905 298 YEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1796-1944 |
3.04e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1796 QTVKDLQMRLDEAEQiALKGGKKQVQKLEA----RVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLAR 1871
Cdd:PHA02562 181 QQIQTLDMKIDHIQQ-QIKTYNKNIEEQRKkngeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1872 LQDLIDKLQAKVKSYKR----------------QAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQVNKLrvrtRDQ 1935
Cdd:PHA02562 260 LNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEF----NEQ 335
|
....*....
gi 2045330442 1936 VSKVSKLNT 1944
Cdd:PHA02562 336 SKKLLELKN 344
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
854-1114 |
3.13e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.53 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 854 EKELAALKEELAKlkeALEKSEVKRKELEEKQVSLIQEKN-DLA-----LQLQAEQDNLADAEDRCDLL------IKTKI 921
Cdd:PLN03229 485 QERLENLREEFSK---ANSQDQLMHPVLMEKIEKLKDEFNkRLSrapnyLSLKYKLDMLNEFSRAKALSekkskaEKLKA 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 922 QLEAKVKELMERLEDEEEMSAnvlakkRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMaALDETILKlt 1001
Cdd:PLN03229 562 EINKKFKEVMDRPEIKEKMEA------LKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSM-GLEVIGVT-- 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1002 keKKALTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEK--------KVRMDLERVRRKLEGDLKLSLES 1073
Cdd:PLN03229 633 --KKNKDTAEQTPPPNLQEKIESLNEEINKKIERVIRSSDLKSKIELLKlevakaskTPDVTEKEKIEALEQQIKQKIAE 710
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2045330442 1074 VMDLENDKQQLEEKLKkkdfemnEISSRIEDEQALVNQLHK 1114
Cdd:PLN03229 711 ALNSSELKEKFEELEA-------ELAAARETAAESNGSLKN 744
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1742-1928 |
3.37e-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: 41.17 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1742 LSTLSNEVDDAVQECRNAEEK---AKKAITDAAMMAEELKKE-QDTSSHLERMKKNMEQTVKDLQM---RLDEAEQiALK 1814
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKleeAEKRAEKAEAEVAALNRRiQLLEEELERTEERLAEALEKLEEaekAADESER-GRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1815 GGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKYERRIK----ELSYQAEEDKKNLARLQDLIDKLQ---AKVKSYK 1887
Cdd:pfam00261 82 VLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVvvegDLERAEERAELAESKIVELEEELKvvgNNLKSLE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2045330442 1888 RQAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQVNKL 1928
Cdd:pfam00261 162 ASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL 202
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
847-1141 |
3.43e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 847 LLRSAATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQDNLAdaedrcdlliktkiQLEAK 926
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA--------------QAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 927 VKELMERLEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKka 1006
Cdd:COG4372 103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE-- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1007 LTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKVRMDLERVRRKLEGDLKLSLESVMDLENDKQQLEE 1086
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2045330442 1087 KLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVE 1141
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1694-1914 |
3.53e-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: 41.17 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1694 EELRALLEQNDRAR---KLAEHELLEATERVNLLHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAITDA 1770
Cdd:pfam00261 1 KKMQQIKEELDEAEerlKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1771 AMMAEELKKEQDTSSHLERMKKNMEQTVKDLQMRLDEAE------QIALKGGKKQVQKLEARVKELENELE--------- 1835
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVArklvvvEGDLERAEERAELAESKIVELEEELKvvgnnlksl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1836 --SEQRKSQ---EYQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRqaeeaeeqansnltKYRKLQHE 1910
Cdd:pfam00261 161 eaSEEKASEredKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKE--------------KYKAISEE 226
|
....
gi 2045330442 1911 LDDA 1914
Cdd:pfam00261 227 LDQT 230
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
838-1105 |
3.76e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.34 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 838 MKLFF----KIKPLLRSAA-TEKELAALK---------EELAKLKEALEKSEVKRKELEEKQVSLIQEKNDLALQLQAEQ 903
Cdd:PTZ00108 1094 MPIWSltkeKVEKLNAELEkKEKELEKLKnttpkdmwlEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPK 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 904 DNLADAEDRCDlliKTKIQLEAKVKELMERLEDEEEMSanvLAKKRKLEDECSELKKDIDDLEITLAKVEKEKHATENKV 983
Cdd:PTZ00108 1174 LKKKEKKKKKS---SADKSKKASVVGNSKRVDSDEKRK---LDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKK 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 984 KNLIEEMAALDETILK--------LTKEKKALTEAHQQTLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQ-EKKVRM 1054
Cdd:PTZ00108 1248 NNSSKSSEDNDEFSSDdlskegkpKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAAlKKKKKS 1327
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2045330442 1055 DLERVRRKlegdlKLSLESVMDLENDKQQLEEKLKKKdfemnEISSRIEDE 1105
Cdd:PTZ00108 1328 EKKTARKK-----KSKTRVKQASASQSSRLLRRPRKK-----KSDSSSEDD 1368
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1076-1245 |
4.03e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1076 DLENDKQQLEEKLKKKDFEMNEISSRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQRGDVARELEELs 1155
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1156 erleeaggATSAQIEINKKRETDFLKLRRDLEEAMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKME 1235
Cdd:COG1579 93 --------ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|
gi 2045330442 1236 VDDLASTVEQ 1245
Cdd:COG1579 165 REELAAKIPP 174
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1099-1312 |
4.10e-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: 41.67 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1099 SSRIEDEQALVNQLHKKIKELQARTEELEEELEADRASRAKVEKQRGDVARELEELSERLEeaggATSAQIEINKKRETd 1178
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAELAELEKEIA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1179 flKLRRDLEE----------AMLHHEATTAALRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSK 1248
Cdd:COG4942 94 --ELRAELEAqkeelaellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2045330442 1249 GKATSEKMCRLYEDQMNEAKAKVDELQRQLNETNTQRARAQAESGEVGRKLEEREAMVSQLQRA 1312
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1389-1572 |
4.15e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.28 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1389 QRTEELEEAKKKLVTRLQEA--EESVEASNAKCSSLEKTKHR----------LQTEIEDLVIDL----ERANAAAAALDK 1452
Cdd:pfam09787 14 QKAARILQSKEKLIASLKEGsgVEGLDSSTALTLELEELRQErdllreeiqkLRGQIQQLRTELqeleAQQQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1453 KQRNFDKVLAEWKQKYEECQSELESSQKESRGLSTELFKLKNSYEETLdhletikrenKNLQEEIADLSDQI---SQGSK 1529
Cdd:pfam09787 94 QLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRI----------KDREAEIEKLRNQLtskSQSSS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2045330442 1530 TIHELEKMKKGLDMEKSDIQAALEEVEgtlehEESKTLRIQLE 1572
Cdd:pfam09787 164 SQSELENRLHQLTETLIQKQTMLEALS-----TEKNSLVLQLE 201
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1183-1524 |
4.40e-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: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1183 RRDLEEAMLHHEATTAalRKKHADSVAELSEQIDSLQRVKQKLEKERSEAkmeVDDLASTVEQLSKGKATSEKMCRLYED 1262
Cdd:pfam15964 382 KRAQEKEALRKEMKKE--REELGATMLALSQNVAQLEAQVEKVTREKNSL---VSQLEEAQKQLASQEMDVTKVCGEMRY 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1263 QMNEAKAKVDELQRQLNETNTQraraqaesgeVGRKLEEREAMVSQLQRAKNSLTQNVEELKKQLEEENKAKSALAHSLQ 1342
Cdd:pfam15964 457 QLNQTKMKKDEAEKEHREYRTK----------TGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLG 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1343 SSRHDCDLLREQYDEEQEAKAElqraLSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEESV-----EASNA 1417
Cdd:pfam15964 527 ESEHQLHLTRLEKESIQQSFSN----EAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFiaklkEECCT 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1418 KCSSLEKTKHRLQTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEECQSELESSQKESRGLSTELFKLKNSYE 1497
Cdd:pfam15964 603 LAKKLEEITQKSRSEVEQLSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQLDKHCQATAQQLVQLLSKQN 682
|
330 340
....*....|....*....|....*..
gi 2045330442 1498 ETLdhletikRENKNLQEEIADLSDQI 1524
Cdd:pfam15964 683 QLF-------KERQNLTEEVQSLRSQV 702
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1631-1941 |
4.41e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1631 NEMEVQLNHAnrqaSESQKLLRNLQVQIKDIQLELDDTVHQNEELKEQMaltERRNNLLSSEVEELRALLEQndrARKLA 1710
Cdd:pfam17380 268 NEFLNQLLHI----VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREV---ERRRKLEEAEKARQAEMDRQ---AAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1711 EHELLeATERVNLLHSqntglINQKKKLESDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTS-SHLER 1789
Cdd:pfam17380 338 EQERM-AMERERELER-----IRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKiLEEER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1790 MKKNMEQTVKDLQMRLDEAEqialkGGKKQVQKL-EARVKELENELESEQRKSQEYQKVVR-KYERRIKELSYQAEEDKK 1867
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEE-----ARQREVRRLeEERAREMERVRLEEQERQQQVERLRQqEEERKRKKLELEKEKRDR 486
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2045330442 1868 nlARLQDLIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELDDAEERADMAETQVNKL-----RVRTRDQVSKVSK 1941
Cdd:pfam17380 487 --KRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQqemeeRRRIQEQMRKATE 563
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1348-1563 |
4.62e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1348 CDLLREQYDEEQEAKAELQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLVTRLQEAEESVEASNAKCSSLEKTKH 1427
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1428 RLQTEIEDLV------IDLERANAAAAAL----DKKQRNFDKVLAEWKQKYEECQSELESS-------QKESRGLSTELF 1490
Cdd:PRK05771 118 ELEQEIERLEpwgnfdLDLSLLLGFKYVSvfvgTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvvLKELSDEVEEEL 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2045330442 1491 KlKNSYEE-TLDHLETIKRENKNLQEEIADLSDQIsqgSKTIHELEKMKKGLDmekSDIQAALEEVEGTLEHEE 1563
Cdd:PRK05771 198 K-KLGFERlELEEEGTPSELIREIKEELEEIEKER---ESLLEELKELAKKYL---EELLALYEYLEIELERAE 264
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1566-1867 |
4.77e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1566 TLRIQLELnqikadVDRKLAEKDEEIDNLRRSHQRSMESMQTTLD--------AEAKSRNEAVRLRKKMECDLNEMEVQL 1637
Cdd:PRK04863 790 QLRAEREE------LAERYATLSFDVQKLQRLHQAFSRFIGSHLAvafeadpeAELRQLNRRRVELERALADHESQEQQQ 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1638 NHANRQASESQKLLRNLQVQIKdiqlELDDTVHQN--EELKEQMALTE------RRNNLLSSEVEELRALL----EQNDR 1705
Cdd:PRK04863 864 RSQLEQAKEGLSALNRLLPRLN----LLADETLADrvEEIREQLDEAEeakrfvQQHGNALAQLEPIVSVLqsdpEQFEQ 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1706 ARK---LAEHELLEATERVNLL-----------HSQNTGLINQkkklESDLS-TLSNEVDDAVQECRNAEEKAKKAITDA 1770
Cdd:PRK04863 940 LKQdyqQAQQTQRDAKQQAFALtevvqrrahfsYEDAAEMLAK----NSDLNeKLRQRLEQAEQERTRAREQLRQAQAQL 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1771 AMMAEELKKEQDTSSHLERMKKNMEQTVKDLQMRLDEAEQIALKGGKKQVQKL----EARVKELENELESEQRKSQEYQK 1846
Cdd:PRK04863 1016 AQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARRDELHARlsanRSRRNQLEKQLTFCEAEMDNLTK 1095
|
330 340
....*....|....*....|.
gi 2045330442 1847 VVRKYERRIKELSYQAEEDKK 1867
Cdd:PRK04863 1096 KLRKLERDYHEMREQVVNAKA 1116
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1351-1594 |
5.18e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.99 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1351 LREQYDEEQEAKAE--LQRALSKANAEVAQWRTKYETDAIQRTEELEEAKKKLvTRLQEAEESVEASNAKCSSLEKTKHR 1428
Cdd:COG5022 832 LRETEEVEFSLKAEvlIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQL-QELKIDVKSISSLKLVNLELESEIIE 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1429 L-QTEIEDLVIDLERANAAAAALDKKQRNFDKVLAEWKQKYEecQSELESSQKESRGLSTELFKLKN---SYEETLDHLE 1504
Cdd:COG5022 911 LkKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVK--LPELNKLHEVESKLKETSEEYEDllkKSTILVREGN 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1505 TIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQaaleevegtLEHEESKTLRIQLELNQIKADVDRKL 1584
Cdd:COG5022 989 KANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASK---------IISSESTELSILKPLQKLKGLLLLEN 1059
|
250
....*....|
gi 2045330442 1585 AEKDEEIDNL 1594
Cdd:COG5022 1060 NQLQARYKAL 1069
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1823-1938 |
5.27e-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: 41.25 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1823 LEARVKELENELESEQRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQDLidklQAKVKSYKRQAeeaeEQANSNLT 1902
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAA----QAAVKAAQAQL----AQAQIDLA 127
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2045330442 1903 KYRKL-------QHELDDAEERADMAETQVNKLrVRTRDQVSK 1938
Cdd:pfam00529 128 RRRVLapiggisRESLVTAGALVAQAQANLLAT-VAQLDQIYV 169
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1724-1912 |
6.66e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1724 LHSQNTGLINQKKKLESDLSTLSNEVDDAVQECRNAE---EKAKKAITDAAMMAEelkkeqDTSSHLE-------RMKKN 1793
Cdd:PHA02562 197 IKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKaeiEELTDELLNLVMDIE------DPSAALNklntaaaKIKSK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1794 MEQTVKDLQMRLDEAE----QIALKGGKKQVQKLEARVKELENELESEQRKSQEYQKVVRKY---ERRIKELSYQAEEDK 1866
Cdd:PHA02562 271 IEQFQKVIKMYEKGGVcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFneqSKKLLELKNKISTNK 350
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2045330442 1867 KNLA-------RLQDLIDKLQAKVKSYKRQAEEAEEQANSNLTKYRKLQHELD 1912
Cdd:PHA02562 351 QSLItlvdkakKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKY 403
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1500-1801 |
6.70e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1500 LDHLETIKRENKNLQEEIADLSDQISQGSKTIHELEKMKKGLDMEKSDIQAALEEVEGTLEHEESKTLRIQLELNQIKAD 1579
Cdd:PLN02939 155 LEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1580 vdrKLAEKDEeidnlrrshqrsMESMQTTLDAEAKSRNEAVRLRKK---MECDLNEMEVQLNHANRQASESQKL-LRNLQ 1655
Cdd:PLN02939 235 ---NMLLKDD------------IQFLKAELIEVAETEERVFKLEKErslLDASLRELESKFIVAQEDVSKLSPLqYDCWW 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1656 VQIKDIQLELDDTVHQneelKEQMALTERRNNLLSSEVEELRALLEQNDRARklaehellEATERVNLLHsqntglinQK 1735
Cdd:PLN02939 300 EKVENLQDLLDRATNQ----VEKAALVLDQNQDLRDKVDKLEASLKEANVSK--------FSSYKVELLQ--------QK 359
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2045330442 1736 -KKLESDLSTLSNEVDDAVQecrnaeekakkaitdaaMMAEELKKEQDTSSHL--ERMKKNMEQTVKDL 1801
Cdd:PLN02939 360 lKLLEERLQASDHEIHSYIQ-----------------LYQESIKEFQDTLSKLkeESKKRSLEHPADDM 411
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1582-1944 |
6.74e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1582 RKLAEKDEEIDNLRRSHQRSMESMQTTLDAEAKSRNEAVRLRKKMECDLNEMEVQLNHANRQASESQKLLRNLQVQIKDI 1661
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1662 QLELDDTVHQNEELKEQMALTERRNNLLSSEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTGLINQKKKLESD 1741
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1742 LSTLsnEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSSHLERMKKNMEQTVKDLQMRLDEAEQIALKGGKKQVQ 1821
Cdd:COG4372 166 LAAL--EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1822 KLEARVKELENELESE-QRKSQEYQKVVRKYERRIKELSYQAEEDKKNLARLQDLIDKLQAKVKSYKRQAEEAEEQANSN 1900
Cdd:COG4372 244 LEEDKEELLEEVILKEiEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2045330442 1901 LTKYRKLQHELDDAEERADMAETQVNKLRVRTRDQVSKVSKLNT 1944
Cdd:COG4372 324 LAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1738-1942 |
6.99e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 41.46 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1738 LESDLSTLSNEVDDAVQECRNAEE-KAKKAITDAAMMAEELKKEQDTSSHLERMKKNMEQTVKDLQMRLDEAEQIALKGG 1816
Cdd:PLN03188 1030 QAPPLNTIPESTDESPEKKLEQERlRWTEAESKWISLAEELRTELDASRALAEKQKHELDTEKRCAEELKEAMQMAMEGH 1109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1817 KKQVQKLeARVKELENELESEQRKSQEYQKVVRKYERR--------------IKELSYQAEEDKKNLARLQDLIDKLQAK 1882
Cdd:PLN03188 1110 ARMLEQY-ADLEEKHIQLLARHRRIQEGIDDVKKAAARagvrgaeskfinalAAEISALKVEREKERRYLRDENKSLQAQ 1188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2045330442 1883 VksykRQAEEAEEQANSNLTKYRKLQHELDDAEERADMAE-------TQVNKLRVRTRDQVSKVSKL 1942
Cdd:PLN03188 1189 L----RDTAEAVQAAGELLVRLKEAEEALTVAQKRAMDAEqeaaeayKQIDKLKRKHENEISTLNQL 1251
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
854-1055 |
8.22e-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: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 854 EKELAALKEelAKLKEALEKSEVKRKELEEkqvsLIQEKNDLALQLQAEQDNLADAedRCDLLiKTKIQLEAKVKELMER 933
Cdd:pfam09787 24 EKLIASLKE--GSGVEGLDSSTALTLELEE----LRQERDLLREEIQKLRGQIQQL--RTELQ-ELEAQQQEEAESSREQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 934 LEDEEEMSANVLAKKRKLEDECSELKKDIDDLEITLAKVE-------KEKHATENKVKNLIEEMAALDETILKLTKEKKA 1006
Cdd:pfam09787 95 LQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKatlqsriKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2045330442 1007 LTEA---HQQTLDDLQAEEdkvNTLTKAKAKLEQQVDDLEGSLEQEKKVRMD 1055
Cdd:pfam09787 175 LTETliqKQTMLEALSTEK---NSLVLQLERMEQQIKELQGEGSNGTSINME 223
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
841-1122 |
9.06e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 841 FFKIKPLLRSA-----ATEKELAALKEELAKLKEALEKSEVKRKELEEKQVSLIQEkndlalqLQAEQDNLADAEDrcdl 915
Cdd:PRK04778 100 FRKAKHEINEIeslldLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKS-------LLANRFSFGPALD---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 916 liktkiQLEAKVKELMERLEDEEEMSAN---VLAKK--RKLEDECSELKKDIDDLEITLAKVEKEKHATENKVKN----L 986
Cdd:PRK04778 169 ------ELEKQLENLEEEFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 987 IEEMAALDEtiLKLTKEKKALTEAHQQTLDDLQAEEdkvntLTKAKAKLEQ---QVDDLEGSLEQEKKVRMDLERVRRKL 1063
Cdd:PRK04778 243 VEEGYHLDH--LDIEKEIQDLKEQIDENLALLEELD-----LDEAEEKNEEiqeRIDQLYDILEREVKARKYVEKNSDTL 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2045330442 1064 EGDLKLSLEsvmdlENDKQQLEEKLKKKDFEMNeissriEDEQALVNQLHKKIKELQAR 1122
Cdd:PRK04778 316 PDFLEHAKE-----QNKELKEEIDRVKQSYTLN------ESELESVRQLEKQLESLEKQ 363
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1211-1408 |
9.15e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1211 LSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKATSEkmcrlYEDQMNEAKAKVDELQRQLNETNTQRARAQA 1290
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2045330442 1291 ESGEVGRKLEEREAMVSQLQRaknsltqnveelkkqleeeNKAKSALAHSLQSSRHDCDLLREQYDEE----QEAKAELQ 1366
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQ-------------------SPVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIA 301
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2045330442 1367 RALSKANAEVAQWRTKYETD---AIQRTEELEEAKKKLVTRLQEA 1408
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAEleaLQAREASLQAQLAQLEARLAEL 346
|
|
| |
