|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
97-758 |
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: 1429.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 256
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 257 DIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFLPD 336
Cdd:cd14929 161 DIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDILGFLPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 337 EKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCAV 416
Cdd:cd14929 241 EKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTYAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 417 GALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKE 496
Cdd:cd14929 321 GALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 497 SIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFELVHYAG 576
Cdd:cd14929 401 GIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHFELVHYAG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 577 VVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKKRKKGASFQTVASLHKENLNKLMTNLKS 656
Cdd:cd14929 481 VVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQFGEKKRKKGASFQTVASLHKENLNKLMTNLKS 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 657 TAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVSSRKAAEE 736
Cdd:cd14929 561 TAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSSRKAAEE 640
|
650 660
....*....|....*....|..
gi 1981090065 737 LLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14929 641 LLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
97-758 |
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: 1243.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAAMIESR----KKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 252
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKkesgKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 253 SVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDIL 331
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADpELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 332 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQ 411
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 412 VTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQE 491
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 492 EYKKESIEWVSIGFGLDLQACIDLIEKP-MGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPdkKKFEAHFE 570
Cdd:cd01377 401 EYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKP--KKSEAHFI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 571 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAipfGEKKRKKGASFQTVASLHKENLNKL 650
Cdd:cd01377 479 LKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGG---GGKKKKKGGSFRTVSQLHKEQLNKL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 651 MTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSkFVSS 730
Cdd:cd01377 556 MTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKG-FDDG 634
|
650 660
....*....|....*....|....*...
gi 1981090065 731 RKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd01377 635 KAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
97-758 |
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: 1178.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAAMIESRKKQ---------GALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGA 247
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKaqflatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 248 RGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQ 326
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKpELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 327 AMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRG 406
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 407 QTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMF 486
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 487 VLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKK-KF 565
Cdd:cd14927 401 ILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKrKY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 566 EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFG---EKKRKKGASFQTVASL 642
Cdd:cd14927 481 EAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEDPKsgvKEKRKKAASFQTVSQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 643 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTF 722
Cdd:cd14927 561 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAI 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 1981090065 723 PKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14927 641 PDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
98-758 |
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: 1065.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 177
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 178 SGAGKTVNSKHIIQYFATIAAMIESRKKQ-----GALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 252
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKKKdskmkGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 253 SVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDIL 331
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKpELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 332 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQ 411
Cdd:cd14913 242 GFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 412 VTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQE 491
Cdd:cd14913 322 VHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 492 EYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFEL 571
Cdd:cd14913 402 EYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFSL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 572 VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKKRKKGASFQTVASLHKENLNKLM 651
Cdd:cd14913 482 IHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKLM 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 652 TNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVSSR 731
Cdd:cd14913 562 SNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSK 641
|
650 660
....*....|....*....|....*..
gi 1981090065 732 KAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14913 642 KACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
98-758 |
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: 985.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 177
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 178 SGAGKTVNSKHIIQYFATIAAMIESRKK-----QGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 252
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKdqtpgKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 253 SVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDIL 331
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKpELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 332 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQ 411
Cdd:cd14917 242 GFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 412 VTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQE 491
Cdd:cd14917 322 VIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 492 EYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFEL 571
Cdd:cd14917 402 EYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHFSL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 572 VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKKRKKGASFQTVASLHKENLNKLM 651
Cdd:cd14917 482 IHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKLM 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 652 TNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVSSR 731
Cdd:cd14917 562 TNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSR 641
|
650 660
....*....|....*....|....*..
gi 1981090065 732 KAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14917 642 KGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
98-758 |
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: 961.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 177
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 178 SGAGKTVNSKHIIQYFATIAAMIESRKK------QGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 251
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKKenpnanKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 252 SSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDI 330
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKpELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 331 LGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIE 410
Cdd:cd14916 242 LGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 411 QVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQ 490
Cdd:cd14916 322 QVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 491 EEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFE 570
Cdd:cd14916 402 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHFS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 571 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIP-FGEKKRKKGASFQTVASLHKENLNK 649
Cdd:cd14916 482 LVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSgKGKGGKKKGSSFQTVSALHRENLNK 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 650 LMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVS 729
Cdd:cd14916 562 LMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFID 641
|
650 660
....*....|....*....|....*....
gi 1981090065 730 SRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14916 642 SRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
85-758 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 959.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 85 IEDMAMLTHLNEASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDML 164
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 165 HNRENQSILFTGESGAGKTVNSKHIIQYFATIAAmIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMH 244
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSG-SGSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 245 FGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLvsANPSDFHFCS-CGAVTVESLDDAEEL 321
Cdd:pfam00063 160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGasAQLKKELRL--TNPKDYHYLSqSGCYTIDGIDDSEEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 322 LATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNE 401
Cdd:pfam00063 238 KITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 402 YVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAK-LSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQF 480
Cdd:pfam00063 318 TVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKtIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 481 FNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKLFDnHFGKSVHLQKPK 559
Cdd:pfam00063 398 FNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYS-TFSKHPHFQKPR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 560 PdkkKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGE----KKRKKGAS 635
Cdd:pfam00063 476 L---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESgkstPKRTKKKR 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 636 FQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYC 715
Cdd:pfam00063 553 FITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYR 632
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1981090065 716 ILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:pfam00063 633 ILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
98-758 |
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: 953.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 177
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 178 SGAGKTVNSKHIIQYFATIAAMIESRKK------QGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 251
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqpgkmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 252 SSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDI 330
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKpELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAIDI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 331 LGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIE 410
Cdd:cd14923 242 LGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 411 QVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQ 490
Cdd:cd14923 322 QVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 491 EEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFE 570
Cdd:cd14923 402 EEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHFS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 571 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKK--RKKGASFQTVASLHKENLN 648
Cdd:cd14923 482 LVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSGGSKKggKKKGSSFQTVSAVFRENLN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 649 KLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFV 728
Cdd:cd14923 562 KLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQFI 641
|
650 660 670
....*....|....*....|....*....|
gi 1981090065 729 SSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14923 642 DSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
99-758 |
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: 934.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 99 VLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGES 178
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 179 GAGKTVNSKHIIQYFATIAAMIESRKK-----QGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 253
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 254 VDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILG 332
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 333 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQV 412
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 413 TCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEE 492
Cdd:cd14918 323 YNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 493 YKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFELV 572
Cdd:cd14918 403 YKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFSLI 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 573 HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKKRKKGASFQTVASLHKENLNKLMT 652
Cdd:cd14918 483 HYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAKKKGSSFQTVSALFRENLNKLMT 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 653 NLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVSSRK 732
Cdd:cd14918 563 NLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDSKK 642
|
650 660
....*....|....*....|....*.
gi 1981090065 733 AAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14918 643 ASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
78-770 |
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: 932.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 78 NPPEFEMIEDMAMLTHLNEASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVAN 157
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 158 NAFQDMLHNRENQSILFTGESGAGKTVNSKHIIQYFATIAAmieSRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRF 237
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG---SNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 238 GKFIRMHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLvsANPSDFHFCS-CGAVTVES 314
Cdd:smart00242 158 GKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGasEELKKELGL--KSPEDYRYLNqGGCLTVDG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 315 LDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEA-DGTENADKAAFLMGINSSELVKCLIH 393
Cdd:smart00242 236 IDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTvKDKEELSNAAELLGVDPEELEKALTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 394 PRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFT 473
Cdd:smart00242 316 RKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 474 NEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKLfDNHFGKS 552
Cdd:smart00242 396 NEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKL-NQHHKKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 553 VHLQKPkpdKKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYmstdsaipfgEKKRKK 632
Cdd:smart00242 474 PHFSKP---KKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG----------VSNAGS 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 633 GASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQ 712
Cdd:smart00242 541 KKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQ 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1981090065 713 RYCILNPRTFPkSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFKAGFLGQLEAIRD 770
Cdd:smart00242 621 RYRVLLPDTWP-PWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
98-758 |
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: 932.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 177
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 178 SGAGKTVNSKHIIQYFATIAAMIESRKK-------QGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 250
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 251 LSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMD 329
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 330 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTI 409
Cdd:cd14915 242 ILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 410 EQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLE 489
Cdd:cd14915 322 QQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 490 QEEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHF 569
Cdd:cd14915 402 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAHF 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 570 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEK-KRKKGASFQTVASLHKENLN 648
Cdd:cd14915 482 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKgGKKKGSSFQTVSALFRENLN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 649 KLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFV 728
Cdd:cd14915 562 KLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFI 641
|
650 660 670
....*....|....*....|....*....|
gi 1981090065 729 SSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14915 642 DSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
98-758 |
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: 929.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 177
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 178 SGAGKTVNSKHIIQYFATIAAM-------IESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 250
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTgekkkeeATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 251 LSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMD 329
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 330 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTI 409
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 410 EQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLE 489
Cdd:cd14910 322 QQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 490 QEEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHF 569
Cdd:cd14910 402 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAHF 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 570 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEK-KRKKGASFQTVASLHKENLN 648
Cdd:cd14910 482 SLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKKgGKKKGSSFQTVSALFRENLN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 649 KLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFV 728
Cdd:cd14910 562 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFI 641
|
650 660 670
....*....|....*....|....*....|
gi 1981090065 729 SSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14910 642 DSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
98-758 |
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: 926.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 177
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 178 SGAGKTVNSKHIIQYFATIAAMIESRKK-------QGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 250
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 251 LSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMD 329
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 330 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTI 409
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 410 EQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLE 489
Cdd:cd14912 322 EQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 490 QEEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHF 569
Cdd:cd14912 402 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAHF 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 570 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKK---RKKGASFQTVASLHKEN 646
Cdd:cd14912 482 SLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGAKkggKKKGSSFQTVSALFREN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 647 LNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSK 726
Cdd:cd14912 562 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 641
|
650 660 670
....*....|....*....|....*....|..
gi 1981090065 727 FVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14912 642 FIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
97-758 |
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: 921.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAAM-IESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVD 255
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTgKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 256 IDIYLLEKSRVIFQQAGERNYHIFYQILSGQK-ELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFL 334
Cdd:cd14934 161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKpELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVLGFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 335 PDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTC 414
Cdd:cd14934 241 AEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQCNN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 415 AVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYK 494
Cdd:cd14934 321 SIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 495 KESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDK-KKFEAHFELVH 573
Cdd:cd14934 401 REGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKgKGPEAHFELVH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 574 YAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEnymstDSAIPFGEKKRKKGASFQTVASLHKENLNKLMTN 653
Cdd:cd14934 481 YAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFK-----EEEAPAGSKKQKRGSSFMTVSNFYREQLNKLMTT 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 654 LKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSkFVSSRKA 733
Cdd:cd14934 556 LHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FVDNKKA 634
|
650 660
....*....|....*....|....*
gi 1981090065 734 AEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14934 635 SELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
97-758 |
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: 908.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAAMI---ESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 253
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKktdEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 254 VDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQ-KELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILG 332
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSvPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 333 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQV 412
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 413 TCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEE 492
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 493 YKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEA-HFEL 571
Cdd:cd14909 401 YKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAaHFAI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 572 VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYmSTDSAIPFGEK--KRKKGASFQTVASLHKENLNK 649
Cdd:cd14909 481 AHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADH-AGQSGGGEQAKggRGKKGGGFATVSSAYKEQLNS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 650 LMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKfvS 729
Cdd:cd14909 560 LMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE--D 637
|
650 660
....*....|....*....|....*....
gi 1981090065 730 SRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14909 638 PKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
33-1440 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 815.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 33 KCWIPDGENAYIEAEVKGSEDDGTVIVETAD---GESLSIKEDKIQQ--MNPPEFEMIEDMAMLTHLNEASVLHTLKRRY 107
Cdd:COG5022 11 GCWIPDEEKGWIWAEIIKEAFNKGKVTEEGKkedGESVSVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPAVLHNLEKRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 108 GQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGESGAGKTVNSK 187
Cdd:COG5022 91 NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 188 HIIQYFATIAAMIESRKKQgaLEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDIDIYLLEKSRVI 267
Cdd:COG5022 171 RIMQYLASVTSSSTVEISS--IEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 268 FQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVT-VESLDDAEELLATEQAMDILGFLPDEKYGCYKLTG 346
Cdd:COG5022 249 HQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQIFKILA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 347 AIMHFGNMKFKqKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYER 426
Cdd:COG5022 329 AILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 427 MFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFg 506
Cdd:COG5022 408 LFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY- 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 507 LDLQACIDLIEK--PMGILSILEEECMFPKATDLTFKTKLFDN-HFGKSVHLQKPKPDKKKfeahFELVHYAGVVPYNIS 583
Cdd:COG5022 487 FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVKHYAGDVEYDVE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 584 GWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTdsaipfgEKKRKkgasFQTVASLHKENLNKLMTNLKSTAPHFVR 663
Cdd:COG5022 563 GFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENI-------ESKGR----FPTLGSRFKESLNSLMSTLNSTQPHYIR 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 664 CINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNP---RTFPKSKFVSSRKAAEELLGS 740
Cdd:COG5022 632 CIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPsksWTGEYTWKEDTKNAVKSILEE 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 741 LEIDHTQYRFGITKVFFKAGFLGQLEAIRDERLSKVFTLFQARAQGKLMRIKFQKILEERDALILIQWNIRAFMAVKNWP 820
Cdd:COG5022 712 LVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYEL 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 821 WMRLFFKIKPLVKSSEVGEEVaGLKEECAQlqkaleksEFQREELKAKQVSLTQEKNDLIlqlqaeqetlanveeQCEWL 900
Cdd:COG5022 792 KWRLFIKLQPLLSLLGSRKEY-RSYLACII--------KLQKTIKREKKLRETEEVEFSL---------------KAEVL 847
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 901 IKSKIQLEARVKELSERVEEEEEINSelTARGRKLEDECFELKKEIDDLETM-LVKSEKEKRTTEHK---VKNLTEEVEF 976
Cdd:COG5022 848 IQKFGRSLKAKKRFSLLKKETIYLQS--AQRVELAERQLQELKIDVKSISSLkLVNLELESEIIELKkslSSDLIENLEF 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 977 LNEDISKL-----NRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCER---ELHKLE 1048
Cdd:COG5022 926 KTELIARLkkllnNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNfkkELAELS 1005
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1049 GNLKLNRESMENLESSQRHLAeELRKKELELSQMNSKVENEKGlvaqLQKTVKELQTQIKDLKEKLEAerttrAKMERER 1128
Cdd:COG5022 1006 KQYGALQESTKQLKELPVEVA-ELQSASKIISSESTELSILKP----LQKLKGLLLLENNQLQARYKA-----LKLRREN 1075
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1129 adltQDLADLNERLEEVGGSSLAQLEITKKQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAELegqVENLQQVKQK 1208
Cdd:COG5022 1076 ----SLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQL---VNTLEPVFQK 1148
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1209 LEKDksdlQLEVDDLLTrvEQMTRAKANAEKLCTLYEERLHEA-------TAKLDKVTQLANDLAAQKTKLWSES--GEF 1279
Cdd:COG5022 1149 LSVL----QLELDGLFW--EANLEALPSPPPFAALSEKRLYQSalydeksKLSSSEVNDLKNELIALFSKIFSGWprGDK 1222
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1280 LRRLEEKEALINQLSR--EKSNFTRQIEDLRGQLEKEtksqsALAHALQKAQRDCDLLREQYEEE--------QEVKAEL 1349
Cdd:COG5022 1223 LKKLISEGWVPTEYSTslKGFNNLNKKFDTPASMSNE-----KLLSLLNSIDNLLSSYKLEEEVLpatinsllQYINVGL 1297
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1350 HRTLSKVNAEMvqwRMKYENNVIQRTEDLEDAKKELAI-RLQEAAEamgvanarnaSLERARHQLQLELGDaLSDLGKVR 1428
Cdd:COG5022 1298 FNALRTKASSL---RWKSATEVNYNSEELDDWCREFEIsDVDEELE----------ELIQAVKVLQLLKDD-LNKLDELL 1363
|
1450
....*....|..
gi 1981090065 1429 SAAARLDQKQLQ 1440
Cdd:COG5022 1364 DACYSLNPAEIQ 1375
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
97-758 |
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: 786.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRR-SEAPPHIFAVANNAFQDMLHNRENQSILFT 175
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 176 GESGAGKTVNSKHIIQYFATIAA--MIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 253
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGsgSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 254 VDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQ-----KELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAM 328
Cdd:cd00124 161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLsdgarEELKLELLLSYYYLNDYLNSSGCDRIDGVDDAEEFQELLDAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 329 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREE--QLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRG 406
Cdd:cd00124 241 DVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 407 QTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQF--FIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWH 484
Cdd:cd00124 321 LTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEStsFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 485 MFVLEQEEYKKESIEWVSIGFgLDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKK 563
Cdd:cd00124 401 VFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 564 kfeaHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSsnrllaslfenymstdsaipfgekkrkkgasfqtvaSLH 643
Cdd:cd00124 480 ----EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG------------------------------------SQF 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 644 KENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRtFP 723
Cdd:cd00124 520 RSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPG-AT 598
|
650 660 670
....*....|....*....|....*....|....*
gi 1981090065 724 KSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd00124 599 EKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
97-758 |
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: 736.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAA------------MIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMH 244
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAskpkgsgavphpAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 245 FGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLAT 324
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 325 EQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVT 404
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 405 RGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFN 482
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLD-RTKRQgaSFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 483 WHMFVLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHfgkSVHlqkPKPDK 562
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH---SMH---PKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 563 KKFE--AHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSA------IPFGEKKRKkgA 634
Cdd:cd14911 474 TDFRgvADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAqqaltdTQFGARTRK--G 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 635 SFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRY 714
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1981090065 715 CILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14911 632 ELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
97-758 |
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: 725.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAAMIESRKK---QGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 253
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDhniPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 254 VDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKE--LHDLLLVSANpsDFHFCSCGAVTVESLDDAEELLATEQAMDIL 331
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEhlKSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 332 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQ 411
Cdd:cd14920 239 GFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 412 VTCAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLE 489
Cdd:cd14920 319 ADFAVEALAKATYERLFRWLVHRINKALD-RTKRQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 490 QEEYKKESIEWVSIGFGLDLQACIDLIEKPM---GILSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKpdKKKFE 566
Cdd:cd14920 398 QEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPR--QLKDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 567 AHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY-----MSTDSAIP---FGEKKRKKGASFQT 638
Cdd:cd14920 475 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdrivgLDQVTGMTetaFGSAYKTKKGMFRT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 639 VASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILN 718
Cdd:cd14920 555 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1981090065 719 PRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14920 635 PNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
98-758 |
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: 673.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQW-MIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAAmieSRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 256
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGG---SSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 257 DIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLVSANpSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFL 334
Cdd:cd01380 159 RTYLLEKSRVVFQAEEERNYHIFYQLCAAasLPELKELHLGSAE-DFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGIS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 335 PDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTC 414
Cdd:cd01380 238 EEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 415 AVGALSKSMYERMFKWLVARINRALDAKLSRQF--FIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEE 492
Cdd:cd01380 318 ARDALAKHIYAQLFDWIVDRINKALASPVKEKQhsFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 493 YKKESIEWVSIGFgLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSV-HLQKPKPDKKKfeahFEL 571
Cdd:cd01380 398 YVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkHFKKPRFSNTA----FIV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 572 VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRllaslfenymstdsaipfgeKKrkkgasfqTVASLHKENLNKLM 651
Cdd:cd01380 473 KHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR--------------------KK--------TVGSQFRDSLILLM 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 652 TNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKfvSSR 731
Cdd:cd01380 525 ETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRD--DKK 602
|
650 660
....*....|....*....|....*..
gi 1981090065 732 KAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd01380 603 KTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
97-758 |
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: 669.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAAMIESRKKQGA-------LEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARG 249
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSialshgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 250 MLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMD 329
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 330 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTI 409
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 410 EQVTCAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFV 487
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALD-KTKRQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 488 LEQEEYKKESIEWVSIGFGLDLQACIDLIEKPM---GILSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKpdKKK 564
Cdd:cd14932 400 LEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQ-GNNPKFQKPK--KLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 565 FEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY--------MSTDSAIPFGEKKRKKGAsF 636
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdrivgldkVAGMGESLHGAFKTRKGM-F 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 637 QTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCI 716
Cdd:cd14932 556 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1981090065 717 LNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14932 636 LTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
97-758 |
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: 648.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAAMIESRKKQ---GALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 253
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTsitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 254 VDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKEL--HDLLLVSANpsDFHFCSCGAVTVESLDDAEELLATEQAMDIL 331
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKmrSDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETLEAMSIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 332 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQ 411
Cdd:cd14921 239 GFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 412 VTCAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLE 489
Cdd:cd14921 319 ADFAIEALAKATYERLFRWILTRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 490 QEEYKKESIEWVSIGFGLDLQACIDLIEKPM---GILSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKPDKKKFE 566
Cdd:cd14921 398 QEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLKDKTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 567 ahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY----------MSTDSAIPFGEKKRKkgASF 636
Cdd:cd14921 477 --FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqmaKMTESSLPSASKTKK--GMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 637 QTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCI 716
Cdd:cd14921 553 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1981090065 717 LNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14921 633 LAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
97-758 |
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: 643.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 256
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 257 DIYLLEKSRVIFQQAGERNYHIFYQILSGQKE--LHDLLLVSANpsDFHFCSCGAVTVESLDDAEELLATEQAMDILGFL 334
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEhlKTDLLLEPYN--KYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 335 PDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTC 414
Cdd:cd14919 239 EEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 415 AVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEE 492
Cdd:cd14919 319 AIEALAKATYERMFRWLVLRINKALD-KTKRQgaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 493 YKKESIEWVSIGFGLDLQACIDLIEKPM---GILSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKPDKKKfeAHF 569
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK--ADF 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 570 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMS----------TDSAIPFGEKKRKkgASFQTV 639
Cdd:cd14919 475 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRiigldqvagmSETALPGAFKTRK--GMFRTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 640 ASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNP 719
Cdd:cd14919 553 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 632
|
650 660 670
....*....|....*....|....*....|....*....
gi 1981090065 720 RTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14919 633 NSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
97-758 |
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: 637.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAAMIESRKKQ-------GALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARG 249
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQnslalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 250 MLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILS--GQKELHDLLLVSANpsDFHFCSCGAVTVESLDDAEELLATEQA 327
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTgaGDKLRSELLLENYN--NYRFLSNGNVTIPGQQDKDLFTETMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 328 MDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQ 407
Cdd:cd15896 239 FRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 408 TIEQVTCAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHM 485
Cdd:cd15896 319 TQEQAEFAVEALAKATYERMFRWLVMRINKALD-KTKRQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 486 FVLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPM---GILSILEEECMFPKATDLTFKTKLFDNhfgKSVHLQKPKPDK 562
Cdd:cd15896 398 FILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQE---QGTHPKFFKPKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 563 KKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY--------MSTDSAIPFGEKKRKkgA 634
Cdd:cd15896 475 LKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVdrivgldkVSGMSEMPGAFKTRK--G 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 635 SFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRY 714
Cdd:cd15896 553 MFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1981090065 715 CILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd15896 633 EILTPNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
97-758 |
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: 617.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAAMIESRKKQGA---LEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 253
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 254 VDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVTVESlDDAEELLATEQAMDILGF 333
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 334 LPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVT 413
Cdd:cd14930 240 SHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 414 CAVGALSKSMYERMFKWLVARINRALDaKLSRQ--FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQE 491
Cdd:cd14930 320 FALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 492 EYKKESIEWVSIGFGLDLQACIDLIEKPM---GILSILEEECMFPKATDLTFKTKLFDNhfgKSVHLQKPKPDKKKFEAH 568
Cdd:cd14930 399 EYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQE---QGGHPKFQRPRHLRDQAD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 569 FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF---------ENYMSTDSAIPFGEKKRkkgASFQTV 639
Cdd:cd14930 476 FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegivglEQVSSLGDGPPGGRPRR---GMFRTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 640 ASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNP 719
Cdd:cd14930 553 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 632
|
650 660 670
....*....|....*....|....*....|....*....
gi 1981090065 720 RTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14930 633 NAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
98-758 |
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: 606.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYkGKRRSEaPPHIFAVANNAFQDMLHNRENQSILFTGE 177
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY-RQKLLD-SPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 178 SGAGKTVNSKHIIQYFATIAAmiesrkKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDID 257
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGG------GSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 258 IYLLEKSRVIFQQAGERNYHIFYQILSG-QKELHDLLLVSAnPSDFHFCS-CGAVTVESLDDAEELLATEQAMDILGFLP 335
Cdd:cd01383 154 TYLLEKSRVVQLANGERSYHIFYQLCAGaSPALREKLNLKS-ASEYKYLNqSNCLTIDGVDDAKKFHELKEALDTVGISK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 336 DEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCA 415
Cdd:cd01383 233 EDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 416 VGALSKSMYERMFKWLVARINRALDAKLSRQF-FIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYK 494
Cdd:cd01383 313 RDALAKAIYASLFDWLVEQINKSLEVGKRRTGrSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 495 KESIEWVSIGFgLDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKLfdnhfgkSVHLQKPKPDKKKFEAHFELVH 573
Cdd:cd01383 393 LDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-------KQHLKSNSCFKGERGGAFTIRH 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 574 YAGVVPYNISGWLEKNKDLLNETVVAVFQkSSNRLLASLFENYMSTDSAIPFGEKKRKKGASF-QTVASLHKENLNKLMT 652
Cdd:cd01383 465 YAGEVTYDTSGFLEKNRDLLHSDLIQLLS-SCSCQLPQLFASKMLDASRKALPLTKASGSDSQkQSVATKFKGQLFKLMQ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 653 NLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVSSRK 732
Cdd:cd01383 544 RLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLSTS 623
|
650 660
....*....|....*....|....*.
gi 1981090065 733 AAeeLLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd01383 624 VA--ILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
97-758 |
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: 605.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAAmiesrkKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 256
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISG------QHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 257 DIYLLEKSRVIFQQAGERNYHIFYQILSG----QKELHDLllvsANPSDFHFCSCG-AVTVESLDDAEELLATEQAMDIL 331
Cdd:cd01381 155 EQYLLEKSRIVSQAPDERNYHIFYCMLAGlsaeEKKKLEL----GDASDYYYLTQGnCLTCEGRDDAAEFADIRSAMKVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 332 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPRE--EQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTI 409
Cdd:cd01381 231 MFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 410 EQVTCAVGALSKSMYERMFKWLVARINRAL---DAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMF 486
Cdd:cd01381 311 EQALDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 487 VLEQEEYKKESIEWVSIGFgLDLQACIDLI-EKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLqKPKPDkkkF 565
Cdd:cd01381 391 KLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYL-KPKSD---L 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 566 EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMStdsaipFGEKKRKKGasfQTVASLHKE 645
Cdd:cd01381 466 NTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDIS------MGSETRKKS---PTLSSQFRK 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 646 NLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTfPKS 725
Cdd:cd01381 537 SLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGI-PPA 615
|
650 660 670
....*....|....*....|....*....|...
gi 1981090065 726 KFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd01381 616 HKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
98-758 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 604.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 177
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 178 SGAGKTVNSKHIIQYFATIAAMIESrkKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDID 257
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSES--EVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 258 IYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLVSaNPSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFLP 335
Cdd:cd01378 160 NYLLEKSRVVGQIKGERNFHIFYQLLKGasQEYLQELGLQR-PEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 336 DEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTEnADKAAFLMGINSSELVKCLIHPRIKVGNEY---VTRGQTIEQV 412
Cdd:cd01378 239 EEQDSIFRILAAILHLGNIQFAEDEEGNAAISDTSV-LDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 413 TCAVGALSKSMYERMFKWLVARINRALDAKLSRQ-FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFnwHMFVL--E 489
Cdd:cd01378 318 AYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIF--IELTLkaE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 490 QEEYKKESIEWVSIGFgLDLQACIDLIE-KPMGILSILEEECMFP-KATDLTFKTKLfDNHFGKSVHLQKPKPDKKKFEA 567
Cdd:cd01378 396 QEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHFELRRG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 568 HFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSaipfgeKKRKKGASFQTVASlhkenL 647
Cdd:cd01378 474 EFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDS------KKRPPTAGTKFKNS-----A 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 648 NKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKF 727
Cdd:cd01378 543 NALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDG 622
|
650 660 670
....*....|....*....|....*....|.
gi 1981090065 728 vSSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd01378 623 -TWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
98-758 |
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: 602.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 177
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 178 SGAGKTVNSKHIIQYFATIAAmiesrkKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDID 257
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTN------NHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 258 IYLLEKSRVIFQQAGERNYHIFYQILSG---QKELHDLLLVSaNPSDFHFCS-CGAVTVESLDDAEELLATEQAMDILGF 333
Cdd:cd14883 156 DYLLEQSRITFQAPGERNYHVFYQLLAGakhSKELKEKLKLG-EPEDYHYLNqSGCIRIDNINDKKDFDHLRLAMNVLGI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 334 LPDEKYGCYKLTGAIMHFGNMKFKQKPREE-QLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQV 412
Cdd:cd14883 235 PEEMQEGIFSVLSAILHLGNLTFEDIDGETgALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 413 TCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEE 492
Cdd:cd14883 315 RDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 493 YKKESIEWVSIGFGlDLQACIDLIEK-PMGILSILEEECMFPKATDLTFKTKLFDNHfgkSVHLQKPKPDKKKFEAHFEL 571
Cdd:cd14883 395 YEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH---EKHPYYEKPDRRRWKTEFGV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 572 VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF---ENYMSTDSAIPFGE----KKRKKGASfqTVASLHK 644
Cdd:cd14883 471 KHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtypDLLALTGLSISLGGdttsRGTSKGKP--TVGDTFK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 645 ENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPK 724
Cdd:cd14883 549 HQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSA 628
|
650 660 670
....*....|....*....|....*....|....
gi 1981090065 725 SKfVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14883 629 DH-KETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
97-758 |
5.43e-179 |
|
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: 557.29 E-value: 5.43e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 175
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 176 GESGAGKTVNSKHIIQYFATIAAMIESrkKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVD 255
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVT--EGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 256 IDIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLvsANPSDFHF---CSCgaVTVESLDDAEELLATEQAMDI 330
Cdd:cd01384 159 IRTYLLERSRVVQVSDPERNYHCFYQLCAGapPEDREKYKL--KDPKQFHYlnqSKC--FELDGVDDAEEYRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 331 LGFLPDEKYGCYKLTGAIMHFGNMKFKQKPreeqlEADGTENADK--------AAFLMGINSSELVKCLIHPRIKVGNEY 402
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGNIEFSKGE-----EDDSSVPKDEksefhlkaAAELLMCDEKALEDALCKRVIVTPDGI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 403 VTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFN 482
Cdd:cd01384 310 ITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 483 WHMFVLEQEEYKKESIEWVSIGFgLDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKLFDNhFGKSVHLQKPKPD 561
Cdd:cd01384 390 QHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPKLS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 562 KKKfeahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEnymstdsaiPFGEKKRKKGASFQTVAS 641
Cdd:cd01384 468 RTD----FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFP---------PLPREGTSSSSKFSSIGS 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 642 LHKENLNKLMTNLKSTAPHFVRCINPN-VNKiPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPR 720
Cdd:cd01384 535 RFKQQLQELMETLNTTEPHYIRCIKPNnLLK-PGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPE 613
|
650 660 670
....*....|....*....|....*....|....*...
gi 1981090065 721 TFPKSKfvSSRKAAEELLGSLEIDhtQYRFGITKVFFK 758
Cdd:cd01384 614 VLKGSD--DEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
97-758 |
1.18e-169 |
|
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: 532.21 E-value: 1.18e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 175
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 176 GESGAGKTVNSKHIIQYfatiaaMIESR-KKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSV 254
Cdd:cd01382 81 GESGAGKTESTKYILRY------LTESWgSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 255 DIDIYLLEKSRVIFQQAGERNYHIFYQILSG------QKELHDLLlvsanpsdfhfcscgavtvesLDDAEELLATEQAM 328
Cdd:cd01382 155 FVSHYLLEKSRICVQSKEERNYHIFYRLCAGapedlrEKLLKDPL---------------------LDDVGDFIRMDKAM 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 329 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREE----QLEADGTENADKAAFLMGINSSELVKCLIHpRIKVGNEYVT 404
Cdd:cd01382 214 KKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSgggcNVKPKSEQSLEYAAELLGLDQDELRVSLTT-RVMQTTRGGA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 405 RGQTI------EQVTCAVGALSKSMYERMFKWLVARINRALDAKLSrQFFIGILDITGFEILEYNSLEQLCINFTNEKLQ 478
Cdd:cd01382 293 KGTVIkvplkvEEANNARDALAKAIYSKLFDHIVNRINQCIPFETS-SYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 479 QFFNWHMFVLEQEEYKKESIEWVSIGFgLDLQACIDLIE-KPMGILSILEEECMFPKATdltfktklfDNHFGKSVHLQK 557
Cdd:cd01382 372 QFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPS---------DQHFTSAVHQKH 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 558 PK------PDKKKFEAHFELV--------HYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSai 623
Cdd:cd01382 442 KNhfrlsiPRKSKLKIHRNLRddegflirHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK-- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 624 pfGEKKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPN 703
Cdd:cd01382 520 --DSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPS 597
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1981090065 704 RLQYADFKQRY--------CILNPRTFPKSKFvssrKAaeelLGSLEIDhtqYRFGITKVFFK 758
Cdd:cd01382 598 RTSFHDLYNMYkkylppklARLDPRLFCKALF----KA----LGLNEND---FKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
97-758 |
3.18e-166 |
|
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: 522.80 E-value: 3.18e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAAmiesrkKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 256
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAG------STNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 257 DIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSAnpSDFHFCSC-GAVTVESLDDAEELLATEQAMDILGFLP 335
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSS--AAYGYLSLsGCIEVEGVDDVADFEEVVLAMEQLGFDD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 336 DEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENAD---KAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQ-TIEQ 411
Cdd:cd14872 233 ADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDvlkEVATLLGVDAATLEEALTSRLMEIKGCDPTRIPlTPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 412 VTCAVGALSKSMYERMFKWLVARINRALD-AKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQ 490
Cdd:cd14872 313 ATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 491 EEYKKESIEWVSIGFgLDLQACIDLIEK-PMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKpkpDKKKFEAHF 569
Cdd:cd14872 393 ALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYA---EVRTSRTEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 570 ELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEnymstdsaiPF-GEKKRKKgasfQTVASLHKENLN 648
Cdd:cd14872 469 IVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFP---------PSeGDQKTSK----VTLGGQFRKQLS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 649 KLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILnPRTFPKSKFV 728
Cdd:cd14872 536 ALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTIAKRVGP 614
|
650 660 670
....*....|....*....|....*....|
gi 1981090065 729 SSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14872 615 DDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
98-758 |
8.64e-166 |
|
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: 521.07 E-value: 8.64e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 177
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 178 SGAGKTVNSKHIIQYFATIaamieSRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDID 257
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-----GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARIS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 258 IYLLEKSRVIFQQAGERNYHIFYQILSG---QKELHDLLLVSANPSD-FHFCSCGAVTVESLD-DAEELLATEQAMDILG 332
Cdd:cd01379 157 EYLLEKSRVVHQAIGERNFHIFYYIYAGlaeDKKLAKYKLPENKPPRyLQNDGLTVQDIVNNSgNREKFEEIEQCFKVIG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 333 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEAD----GTENADKAAFLMGINSSELVKCLIHprikvgNEYVTRGQT 408
Cdd:cd01379 237 FTKEEVDSVYSILAAILHIGDIEFTEVESNHQTDKSsrisNPEALNNVAKLLGIEADELQEALTS------HSVVTRGET 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 409 I------EQVTCAVGALSKSMYERMFKWLVARINRALdaKLSR-----QFFIGILDITGFEILEYNSLEQLCINFTNEKL 477
Cdd:cd01379 311 IirnntvEEATDARDAMAKALYGRLFSWIVNRINSLL--KPDRsasdePLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 478 QQFFNWHMFVLEQEEYKKESIEWVSIGFG-----LDLqacidLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHfgKS 552
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 553 VHLQKPKPDkkkfEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLAslfenymstdsaipfgekkrkk 632
Cdd:cd01379 462 KYYWRPKSN----ALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR---------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 633 gasfQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQ 712
Cdd:cd01379 516 ----QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLK 591
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1981090065 713 RYCILnprTFPKSKFV-SSRKAAEELLGSLEIDHtqYRFGITKVFFK 758
Cdd:cd01379 592 RYYFL---AFKWNEEVvANRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
97-758 |
4.09e-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: 517.71 E-value: 4.09e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSeAPPHIFAVANNAFQDMLHNRENQSILFT 175
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSIS-KSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 176 GESGAGKTVNSKHIIQYFATiaAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHF---------G 246
Cdd:cd14888 80 GESGAGKTESTKYVMKFLAC--AGSEDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklkskrmsG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 247 ARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKEL-----------------HDLLLVSANPSDFH------ 303
Cdd:cd14888 158 DRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAkntglsyeendeklakgADAKPISIDMSSFEphlkfr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 304 --FCScGAVTVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFK-QKPREE--QLEADGTENADKAAF 378
Cdd:cd14888 238 ylTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEnNEACSEgaVVSASCTDDLEKVAS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 379 LMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALD-AKLSRQFFIGILDITGF 457
Cdd:cd14888 317 LLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGVLDIFGF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 458 EILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLI-EKPMGILSILEEECMFPKAT 536
Cdd:cd14888 397 ECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEECFVPGGK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 537 DLTFKTKLFDNHFG-KSVHLQKPKPDKkkfeahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN 615
Cdd:cd14888 476 DQGLCNKLCQKHKGhKRFDVVKTDPNS------FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 616 YMstDSAIPFGEKKRKkgasFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTR 695
Cdd:cd14888 550 YL--RRGTDGNTKKKK----FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQ 623
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1981090065 696 ICREGFPNRLQYADFKQRYCILNPrtfpkskfvssrkaaeellGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14888 624 VSRAGYPVRLSHAEFYNDYRILLN-------------------GEGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
97-758 |
1.16e-161 |
|
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: 510.86 E-value: 1.16e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 175
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 176 GESGAGKTVNSKHIIQYFATIAamiesrkkqGALED----QIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 251
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA---------GGLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 252 SSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFcSCGAVTVESLDDAEELLATEQAMDIL 331
Cdd:cd14903 152 VGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEALSLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 332 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLE--ADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTI 409
Cdd:cd14903 231 GVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 410 EQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLE 489
Cdd:cd14903 311 DQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 490 QEEYKKESIEWVSIGFgLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHf 569
Cdd:cd14903 391 QIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIK- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 570 elvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKKRKKGA-----SFQTVASLHK 644
Cdd:cd14903 469 ---HYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRrggalTTTTVGTQFK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 645 ENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPK 724
Cdd:cd14903 546 DSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGRNT 625
|
650 660 670
....*....|....*....|....*....|....*
gi 1981090065 725 SKFVssRKAAEELLGSLEIDH-TQYRFGITKVFFK 758
Cdd:cd14903 626 DVPV--AERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
97-758 |
1.04e-158 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 502.75 E-value: 1.04e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQ-KEVMAAYK-GKRRSEAPPHIFAVANNAFQDMLHNR----EN 169
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPlLYDvPGFDSQRKeEATASSPPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 170 QSILFTGESGAGKTVNSKHIIQYFATIAAMIESRKKQGA-------LEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIR 242
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGaanahesIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 243 MHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCG-AVTVESLDDAEEL 321
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 322 LATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQ--KPREEQLEADGTENADKAAFLMGINSSELVKCLIhPRIKVG 399
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLV-TQTTST 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 400 neyvTRGQ------TIEQVTCAVGALSKSMYERMFKWLVARINRA----------LDAKLSRQFFIGILDITGFEILEYN 463
Cdd:cd14892 320 ----ARGSvleiklTAREAKNALDALCKYLYGELFDWLISRINAChkqqtsgvtgGAASPTFSPFIGILDIFGFEIMPTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 464 SLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIEK-PMGILSILEEECMFP-KATDLTFK 541
Cdd:cd14892 396 SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 542 TKLFDNHFGKSVHLQKPkpdkkKFEA-HFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNrllaslfenymstd 620
Cdd:cd14892 475 TIYHQTHLDKHPHYAKP-----RFECdEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK-------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 621 saipfgekkrkkgasFQTvaslhkeNLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREG 700
Cdd:cd14892 536 ---------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREG 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981090065 701 FPNRLQYADFKQRYCIL---------NPRTfpKSKFVSSRKAAEELLGSLEIDHTQyrFGITKVFFK 758
Cdd:cd14892 594 FPIRRQFEEFYEKFWPLarnkagvaaSPDA--CDATTARKKCEEIVARALERENFQ--LGRTKVFLR 656
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
97-758 |
2.49e-156 |
|
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: 497.28 E-value: 2.49e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIaamieSRKKQGA-LEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVD 255
Cdd:cd01385 81 ESGSGKTESTNFLLHHLTAL-----SQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 256 IDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGA-VTVESLDDAEELLATEQAMDILGFL 334
Cdd:cd01385 156 VEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDcYTLEGEDEKYEFERLKQAMEMVGFL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 335 PDEKYGCYKLTGAIMHFGNMKFKQKP--REEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQV 412
Cdd:cd01385 236 PETQRQIFSVLSAVLHLGNIEYKKKAyhRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 413 TCAVGALSKSMYERMFKWLVARINRALDAKLS----RQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVL 488
Cdd:cd01385 316 IATRDAMAKCLYSALFDWIVLRINHALLNKKDleeaKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 489 EQEEYKKESIEWVSIGFgLDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKlFDNHFGKSVHLQKPkpdkKKFEA 567
Cdd:cd01385 396 EQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKP----QVMEP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 568 HFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSN------------------------RLLASLFE--------- 614
Cdd:cd01385 470 AFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSafvreligidpvavfrwavlraffRAMAAFREagrrraqrt 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 615 ---NYMSTDSAIPFGEKKRKK------GASFQTvaslhkeNLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQL 685
Cdd:cd01385 550 aghSLTLHDRTTKSLLHLHKKkkppsvSAQFQT-------SLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQL 622
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1981090065 686 RCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKfvSSRKaaeELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd01385 623 RYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSK--EDIK---DFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
97-756 |
3.75e-156 |
|
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: 495.46 E-value: 3.75e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAY------KGKRRSEAPPHIFAVANNAFQDMLHNRE-- 168
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 169 --NQSILFTGESGAGKTVNSKHIIQYFATIAamieSRKKQGA-------LEDQIMQANTILEAFGNAKTLRNDNSSRFGK 239
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVS----SATTHGQnaterenVRDRVLESNPILEAFGNARTNRNNNSSRFGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 240 FIRMHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLVSANPSDFHFCSCGAVTVESLDD 317
Cdd:cd14901 157 FIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGasSDELHALGLTHVEEYKYLNSSQCYDRRDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 318 AEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPRE-EQLEADGTENADKAAFLMGINSSELVKCLIHPRI 396
Cdd:cd14901 237 SVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEgGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 397 KVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLS--RQFFIGILDITGFEILEYNSLEQLCINFTN 474
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 475 EKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKLFDNhFGKSV 553
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 554 HLQKPKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASlfenymstdsaipfgekkrkkg 633
Cdd:cd14901 475 SFSVSKLQQGK--RQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS---------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 634 asfqTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQR 713
Cdd:cd14901 531 ----TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHT 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1981090065 714 YCILNPRTfpKSKFVSSRKAAEELLGSLEI------DHTQYRFGITKVF 756
Cdd:cd14901 607 YSCLAPDG--ASDTWKVNELAERLMSQLQHselnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
97-758 |
2.25e-154 |
|
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: 490.80 E-value: 2.25e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAamiesrKKQGAL-EDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFgARGMLSSVD 255
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN------QRRNNLvTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 256 IDIYLLEKSRVIFQQAGERNYHIFYQILSG----QKELHDLLlvsaNPSDFHFC----SCGAVTVESLDDAEELLAteqA 327
Cdd:cd01387 154 TSQYLLEKSRIVTQAKNERNYHVFYELLAGlpaqLRQKYGLQ----EAEKYFYLnqggNCEIAGKSDADDFRRLLA---A 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 328 MDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPRE---EQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVT 404
Cdd:cd01387 227 MQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 405 RGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWH 484
Cdd:cd01387 307 TPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKH 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 485 MFVLEQEEYKKESIEWVSIGFgLDLQACIDLI-EKPMGILSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKPDkk 563
Cdd:cd01387 387 VFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPRMP-- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 564 kfEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMS-TDSAIPFGEKKRKKGASFQ--TVA 640
Cdd:cd01387 463 --LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAqTDKAPPRLGKGRFVTMKPRtpTVA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 641 SLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPR 720
Cdd:cd01387 541 ARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVAL 620
|
650 660 670
....*....|....*....|....*....|....*....
gi 1981090065 721 TFPKS-KFVSSRKAAEELLGSLEIDhtQYRFGITKVFFK 758
Cdd:cd01387 621 KLPRPaPGDMCVSLLSRLCTVTPKD--MYRLGATKVFLR 657
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
97-758 |
1.81e-153 |
|
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: 488.52 E-value: 1.81e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAF----QDMLHNRENQS 171
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtqliQSGVLDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 172 ILFTGESGAGKTVNSKHIIQYFATI-------------AAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFG 238
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARItsgfaqgasgegeAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 239 KFIRMHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKE--LHDLLLVSANPSDFHFCSCGAVtvESLD 316
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEalRERLKLQTPVEYFYLRGECSSI--PSCD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 317 DAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGT-ENADKAAFLMGINSSELVKCLIHPR 395
Cdd:cd14890 239 DAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 396 IKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNE 475
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 476 KLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGILSILE--EEC--MFPKATDLTFKTKLFDNHFG 550
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFItlDDCwrFKGEEANKKFVSQLHASFGR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 551 KSV------------HLQKPKPDKKKfeaHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLlaslfenyms 618
Cdd:cd14890 478 KSGsggtrrgssqhpHFVHPKFDADK---QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI---------- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 619 tdsaipfgekkrkKGASfqtVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICR 698
Cdd:cd14890 545 -------------REVS---VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQ 608
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 699 EGFPNRLQYADFKQRYCILNPRTFPKSKFVssrkaaEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14890 609 QGFALREEHDSFFYDFQVLLPTAENIEQLV------AVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
97-758 |
1.30e-149 |
|
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: 477.36 E-value: 1.30e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 175
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 176 GESGAGKTVNSKHIIQYFATIAAMI---ESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 252
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSlelSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 253 SVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCS-CGAVTVESLDDAEELLATEQAMDIL 331
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 332 GFLPDEKYGCYKLTGAIMHFGNMKFkqkpreeqLEADGTENADKAAF-----LMGINSSELVKCLIHPRIKVGNEYVTRG 406
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKTALgrsaeLLGLDPTQLTDALTQRSMFLRGEEILTP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 407 QTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQfFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMF 486
Cdd:cd14873 313 LNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 487 VLEQEEYKKESIEWVSIGFgLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLfdnhfgKSVHLQKPKPDKKKFE 566
Cdd:cd14873 392 SLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKL------HSQHANNHFYVKPRVA 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 567 AH-FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSA-IPFGEKKRKKgasfQTVASLHK 644
Cdd:cd14873 465 VNnFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQdTLKCGSKHRR----PTVSSQFK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 645 ENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTfpk 724
Cdd:cd14873 541 DSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNL--- 617
|
650 660 670
....*....|....*....|....*....|....
gi 1981090065 725 SKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14873 618 ALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
97-758 |
4.34e-147 |
|
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: 469.94 E-value: 4.34e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKR-RSEAPPHIFAVANNAFQDMLHNRENQSILFT 175
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 176 GESGAGKTVNSKHIIQYFATIaamieSRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVD 255
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKL-----SPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 256 IDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQA-------M 328
Cdd:cd14897 156 IDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDSEELEYYRQMfhdltniM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 329 DILGFLPDEKYGCYKLTGAIMHFGNMKFkqkprEEQLEADGTENADK-----AAFLMGINSSELVKCLIHPRIKVGNEYV 403
Cdd:cd14897 236 KLIGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVNTIRGERI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 404 TRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAK-----LSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQ 478
Cdd:cd14897 311 QSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDkdfqiMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 479 QFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLI-EKPMGILSILEEECMFPKATDLTFKTKLfDNHFGKSVHLQK 557
Cdd:cd14897 391 QYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVA 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 558 PKPDKKKFEAHfelvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMstdsaipfgekkrkkgasfq 637
Cdd:cd14897 469 SPGNRVAFGIR----HYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSYF-------------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 638 tvaslhKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCIL 717
Cdd:cd14897 525 ------KRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEI 598
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1981090065 718 NPrtFPKSKFVSSRKAAEELLGSLEIDhtQYRFGITKVFFK 758
Cdd:cd14897 599 CD--FSNKVRSDDLGKCQKILKTAGIK--GYQFGKTKVFLK 635
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
99-758 |
1.12e-143 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 461.30 E-value: 1.12e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 99 VLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDML----HNRENQSILF 174
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 175 TGESGAGKTVNSKHIIQYfatiaaMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFgARGMLSSV 254
Cdd:cd14889 83 SGESGAGKTESTKLLLRQ------IMELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 255 DIDIYLLEKSRVIFQQAGERNYHIFYQILSG----QKELHDLLlvsaNPSDFHFCSCGAVTVESLD----DAEELLateQ 326
Cdd:cd14889 156 KINEYLLEKSRVVHQDGGEENFHIFYYMFAGisaeDRENYGLL----DPGKYRYLNNGAGCKREVQywkkKYDEVC---N 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 327 AMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQkpreEQLEADGTENADK-----AAFLMGINSSELVKCLIHPRIKVGNE 401
Cdd:cd14889 229 AMDMVGFTEQEEVDMFTILAGILSLGNITFEM----DDDEALKVENDSNgwlkaAAGQFGVSEEDLLKTLTCTVTFTRGE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 402 YVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQF---FIGILDITGFEILEYNSLEQLCINFTNEKLQ 478
Cdd:cd14889 305 QIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVelrEIGILDIFGFENFAVNRFEQACINLANEQLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 479 QFFNWHMFVLEQEEYKKESIEWVSIGFgLDLQACIDL-IEKPMGILSILEEECMFPKATDLTFKTKLfDNHFGKSVHLQK 557
Cdd:cd14889 385 YFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYGK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 558 PKPDKKKfeahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMS-TDSAIPFGEKKRKKGASF 636
Cdd:cd14889 463 SRSKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSrTGTLMPRAKLPQAGSDNF 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 637 -----QTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFK 711
Cdd:cd14889 539 nstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFA 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1981090065 712 QRYCILnprtFPKSKFVSSRKAAEELLGSLEIdhTQYRFGITKVFFK 758
Cdd:cd14889 619 ERYKIL----LCEPALPGTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
98-717 |
6.29e-137 |
|
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: 441.67 E-value: 6.29e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAY-----------KGKRRSEAPPHIFAVANNAFQDMLH 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 166 NR----ENQSILFTGESGAGKTVNSKHIIQYFATI-----AAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSR 236
Cdd:cd14900 82 GLngvmSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 237 FGKFIRMHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHdlllvsanpsdfhfcscgavtvESLD 316
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAA----------------------RKRD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 317 DAEELLAteqAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENA-------DKAAFLMGINSSELVK 389
Cdd:cd14900 220 MYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 390 CLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRAL---DAKLSRQ--FFIGILDITGFEILEYNS 464
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGglHFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 465 LEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLI-EKPMGILSILEEECMFPKATDLTFKTK 543
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLASK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 544 LFdNHFGKSVHLQKPKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQkssnrllaslfenymstdsai 623
Cdd:cd14900 456 LY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV--------------------- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 624 pfgekkrkKGASFqtvaslhKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPN 703
Cdd:cd14900 512 --------YGLQF-------KEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPI 576
|
650
....*....|....
gi 1981090065 704 RLQYADFKQRYCIL 717
Cdd:cd14900 577 RLLHDEFVARYFSL 590
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
97-737 |
7.95e-136 |
|
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: 7.95e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYK--------GKRRSEAPPHIFAVANNAFQDMLHN- 166
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 167 RENQSILFTGESGAGKTVNSKHIIQYFATIAAMIESRKKQGA----LEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIR 242
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSdaveIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 243 MHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG-QKELHDLLLVSAN----PSDFHFCSCGAVTVESLDD 317
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGaDKTLLDLLGLQKGgkyeLLNSYGPSFARKRAVADKY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 318 AEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFK---QKPREEQLEADGTENADKAAFLMGINSSELVKCLIHP 394
Cdd:cd14902 241 AQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTaenGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 395 RIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFF---------IGILDITGFEILEYNSL 465
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 466 EQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKL 544
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGSNQALSTKF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 545 FDNHFGksvhlqkpkpdkkkfEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIP 624
Cdd:cd14902 480 YRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSPGAD 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 625 FGEKKRKKGASFQT--VASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFP 702
Cdd:cd14902 545 NGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYS 624
|
650 660 670
....*....|....*....|....*....|....*
gi 1981090065 703 NRLQYADFKQRYCILNPrtFPKSKFVSSRKAAEEL 737
Cdd:cd14902 625 VRLAHASFIELFSGFKC--FLSTRDRAAKMNNHDL 657
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
97-758 |
5.25e-131 |
|
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: 425.90 E-value: 5.25e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 175
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 176 GESGAGKTVNSKHIIQYFATIAAmieSRKKQGAleDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVD 255
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTI--AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 256 IDIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILGF 333
Cdd:cd14904 156 CETYLLEKSRVVSIAEGERNYHIFYQLLAGlsSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 334 LPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGtENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVT 413
Cdd:cd14904 236 DNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNG-SQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 414 CAVGALSKSMYERMFKWLVARINRAL---DAKLSRQffIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQ 490
Cdd:cd14904 315 ENRDALAKAIYSKLFDWMVVKINAAIstdDDRIKGQ--IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 491 EEYKKESIEWVSIGFGlDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNH--FGKSVHLQKPKPDKKKFEAH 568
Cdd:cd14904 393 EEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKRTQFIIN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 569 felvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIpfGEKKRKKGASFQTVASLHKENLN 648
Cdd:cd14904 472 ----HYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETK--EGKSGKGTKAPKSLGSQFKTSLS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 649 KLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILnprtFPKSKFV 728
Cdd:cd14904 546 QLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM----FPPSMHS 621
|
650 660 670
....*....|....*....|....*....|..
gi 1981090065 729 -SSRKAAEELLGSL-EIDHTQYRFGITKVFFK 758
Cdd:cd14904 622 kDVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
97-726 |
1.34e-130 |
|
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: 425.21 E-value: 1.34e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGK--------RRSEAPPHIFAVANNAFQDMLHNR 167
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 168 ENQSILFTGESGAGKTVNSKHIIQYFATIAA--------------MIESRKKQGALEDQIMQANTILEAFGNAKTLRNDN 233
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 234 SSRFGKFIRMHFGAR-GMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLVSANPSDFHFC--SCG 308
Cdd:cd14907 161 SSRFGKYVSILVDKKkRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGadQQLLQQLGLKNQLSGDRYDYlkKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 309 AVTVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQK--PREEQLEADGTENADKAAFLMGINSSE 386
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDStlDDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 387 LVKCLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRAL--------DAKLSRQFFIGILDITGFE 458
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 459 ILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIE-WVS-IGFgLDLQACIDLIEK-PMGILSILEEECMFPKA 535
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdYLNqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 536 TDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEahfeLVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFen 615
Cdd:cd14907 480 TDEKLLNKIKKQHKNNSKLIFPNKINKDTFT----IRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF-- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 616 YMSTDSAIPFGEKKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTR 695
Cdd:cd14907 554 SGEDGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIR 633
|
650 660 670
....*....|....*....|....*....|..
gi 1981090065 696 ICREGFPNRLQYADFKQRYCILNP-RTFPKSK 726
Cdd:cd14907 634 VRKQGYPYRKSYEDFYKQYSLLKKnVLFGKTK 665
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
59-818 |
1.49e-128 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 424.83 E-value: 1.49e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 59 VETADGESLSIKEDKIQQMNPP-EFEMIEDMAMLTHLNEASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVM 137
Cdd:PTZ00014 71 IDPPTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 138 AAYKGKRRSEA-PPHIFAVANNAFQDMLHNRENQSILFTGESGAGKTVNSKHIIQYFATIAAMIESRKKQGAledqIMQA 216
Cdd:PTZ00014 151 RRYRDAKDSDKlPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNA----IMAA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 217 NTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG-----QKELHD 291
Cdd:PTZ00014 227 NPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGandemKEKYKL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 292 LLLvsanpSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTE 371
Cdd:PTZ00014 307 KSL-----EEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAIS 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 372 NADKAAF-----LMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQ 446
Cdd:PTZ00014 382 DESLEVFneaceLLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFK 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 447 FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSIL 526
Cdd:PTZ00014 462 VFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSIL 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 527 EEECMFPKATDLTFkTKLFDNHFGKSVHLQKPKPDKKKfeaHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSN 606
Cdd:PTZ00014 542 EDQCLAPGGTDEKF-VSSCNTNLKNNPKYKPAKVDSNK---NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPN 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 607 RLLASLFENYMSTDSAIpfgekkrKKGasfQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLR 686
Cdd:PTZ00014 618 PLVRDLFEGVEVEKGKL-------AKG---QLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLH 687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 687 CNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKfVSSRKAAEELLGSLEIDHTQYRFGITKVFFKAGFLGQLE 766
Cdd:PTZ00014 688 SLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSS-LDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELT 766
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1981090065 767 AIRDERLSKVFTLFQArAQGKLMRIKFQKILEER-DALILIQWNIRAFMAVKN 818
Cdd:PTZ00014 767 QIQREKLAAWEPLVSV-LEALILKIKKKRKVRKNiKSLVRIQAHLRRHLVIAE 818
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
97-758 |
1.19e-126 |
|
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: 413.29 E-value: 1.19e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRY---GQwMIYTYSGLFCVTINPYKWLPVYQKEvmaAYKGKRRSEAPPHIFAVANNAFQDMLHNRE---NQ 170
Cdd:cd14891 1 AGILHNLEERSkldNQ-RPYTFMANVLIAVNPLRRLPEPDKS---DYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 171 SILFTGESGAGKTVNSKHIIQY------------FATIAAMIESRKKQGA-LEDQIMQANTILEAFGNAKTLRNDNSSRF 237
Cdd:cd14891 77 SIVISGESGAGKTETSKIILRFlttravggkkasGQDIEQSSKKRKLSVTsLDERLMDTNPILESFGNAKTLRNHNSSRF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 238 GKFIRMHFGARGM-LSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCS-CGAVTVESL 315
Cdd:cd14891 157 GKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 316 DDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKA----AFLMGINSSELVKCL 391
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEAlataAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 392 IHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILE-YNSLEQLCI 470
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 471 NFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLI-EKPMGILSILEEECMFPKATDLTFKTKLfDNHF 549
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETL-HKTH 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 550 GKSVHLQKPKPDKKKFEahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFqKSSNRLLASLFEnymstdsaipfgekk 629
Cdd:cd14891 475 KRHPCFPRPHPKDMREM--FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLL-ASSAKFSDQMQE--------------- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 630 rkkgasfqtvaslhkenlnkLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYAD 709
Cdd:cd14891 537 --------------------LVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAE 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1981090065 710 FKQRYCILNPrTFPKSKFVSSRKA-AEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14891 597 LVDVYKPVLP-PSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
97-726 |
3.18e-125 |
|
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: 410.84 E-value: 3.18e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYK--GKRRS---EAP----PHIFAVANNAFQDMLHN- 166
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 167 RENQSILFTGESGAGKTVNSKHIIQYFATI------AAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKF 240
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLgngeegAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 241 IRMHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG-------QKELHDLLLVSAN-PSDFHFCSCG-AVT 311
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGgdeeeheKYEFHDGITGGLQlPNEFHYTGQGgAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 312 VESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENAD---KAAFLMGINSSELV 388
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKclaRVAKLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 389 KCLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQF--FIGILDITGFEILEYNSLE 466
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrsSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 467 QLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGILSILEEECMFP-KATDLTFKTKL 544
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 545 FDNHFGKSvhlQKPKPDKKKFEAH--------FELVHYAGVVPYNI-SGWLEKNKDLLNETVvavfqkssnrllASLFEN 615
Cdd:cd14908 480 YETYLPEK---NQTHSENTRFEATsiqktkliFAVRHFAGQVQYTVeTTFCEKNKDEIPLTA------------DSLFES 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 616 ymstdsaipfgekkrkkGASFqtvaslhKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTR 695
Cdd:cd14908 545 -----------------GQQF-------KAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVR 600
|
650 660 670
....*....|....*....|....*....|.
gi 1981090065 696 ICREGFPNRLQYADFKQRYCILNPrTFPKSK 726
Cdd:cd14908 601 VARSGYPVRLPHKDFFKRYRMLLP-LIPEVV 630
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
97-758 |
6.34e-124 |
|
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: 405.70 E-value: 6.34e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIaamieSRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFgARGMLSSVDI 256
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL-----YQDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 257 DIYLLEKSRVIFQQAGERNYHIFYQILSG----QKElhdLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILG 332
Cdd:cd14896 155 SHYLLETSRVVFQAQAERSFHVFYELLAGldpeERE---QLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 333 FLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENAD--KAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIE 410
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 411 QVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFF--IGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVL 488
Cdd:cd14896 312 GAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 489 EQEEYKKESIEWVSIgFGLDLQACIDLI-EKPMGILSILEEECMFPKATDLTFKTKLFDNHfGKSVHLQKPKPDKKKFEA 567
Cdd:cd14896 392 EEEECQRELLPWVPI-PQPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQLPLPVFTV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 568 HfelvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENymstdsaipfGEKKRKKGASFQTVASLHKENL 647
Cdd:cd14896 470 R----HYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE----------AEPQYGLGQGKPTLASRFQQSL 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 648 NKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRtfpKSKF 727
Cdd:cd14896 536 GDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSE---RQEA 612
|
650 660 670
....*....|....*....|....*....|..
gi 1981090065 728 VSSRKAAEELLGSLEIDHTQ-YRFGITKVFFK 758
Cdd:cd14896 613 LSDRERCGAILSQVLGAESPlYHLGATKVLLK 644
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
98-758 |
1.30e-121 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 401.25 E-value: 1.30e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQ----KEVMAAYKGKrrseaPPHIFAVANNAFQDM---LH---- 165
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYDlhkyREEMPGWTAL-----PPHVFSIAEGAYRSLrrrLHepga 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 166 NRENQSILFTGESGAGKTVNSKHIIQYFATIA----AMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFI 241
Cdd:cd14895 77 SKKNQTILVSGESGAGKTETTKFIMNYLAESSkhttATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 242 RMHFGARGMLSSV-----DIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKE--LHDLLLVSANPSDFHFCSCGAVTV-- 312
Cdd:cd14895 157 RMFFEGHELDTSLrmigtSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADdmKLELQLELLSAQEFQYISGGQCYQrn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 313 ESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENA------------------D 374
Cdd:cd14895 237 DGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqhlD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 375 KAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDaklSRQF------- 447
Cdd:cd14895 317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASP---QRQFalnpnka 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 448 -------FIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGLDlQACIDLIE-KP 519
Cdd:cd14895 394 ankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEqRP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 520 MGILSILEEECMFPKATDLTFKTKLFDNHFGKSvHLQKPKPDKKKFEahFELVHYAGVVPYNISGWLEKNKDLLNETVVA 599
Cdd:cd14895 473 SGIFSLLDEECVVPKGSDAGFARKLYQRLQEHS-NFSASRTDQADVA--FQIHHYAGAVRYQAEGFCEKNKDQPNAELFS 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 600 VFQKSSNRLLASLFENY-MSTDSAIPFGE---KKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGI 675
Cdd:cd14895 550 VLGKTSDAHLRELFEFFkASESAELSLGQpklRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQ 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 676 LDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYcilnpRTFPKSKFVSSRKAAeELLGSLEIDHTQyrFGITKV 755
Cdd:cd14895 630 FDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQY-----RLLVAAKNASDATAS-ALIETLKVDHAE--LGKTRV 701
|
...
gi 1981090065 756 FFK 758
Cdd:cd14895 702 FLR 704
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
839-1915 |
3.55e-115 |
|
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: 393.77 E-value: 3.55e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 839 EEVAGLKEEcaQLQKALE---KSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELS 915
Cdd:pfam01576 4 EEEMQAKEE--ELQKVKErqqKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 916 ERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAH 995
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 996 QQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKK 1075
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1076 ELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEI 1155
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1156 TKKQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKA 1235
Cdd:pfam01576 322 RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1236 NAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKET 1315
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEET 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1316 KSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYEnNVIQRTEDLEDAKKELAIRLQEAAEA 1395
Cdd:pfam01576 482 RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLE-EDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1396 MGVANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQ-----KHEESQALLDASQKEVQALS 1470
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAisaryAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1471 tellkLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKI 1550
Cdd:pfam01576 641 -----LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAK 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1551 LHFQLELLEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSE 1630
Cdd:pfam01576 716 LRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREE 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1631 ATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYT 1710
Cdd:pfam01576 796 AVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGAS 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1711 QNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLA 1790
Cdd:pfam01576 876 GKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQ 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1791 EAEQMALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNY 1870
Cdd:pfam01576 956 EMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQL 1035
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*
gi 1981090065 1871 KQQVEVAETQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIK 1915
Cdd:pfam01576 1036 KRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
97-758 |
9.85e-115 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 379.72 E-value: 9.85e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKG-KRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 175
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 176 GESGAGKTVNSKHIIQYFATIAAMIESRKKQGAledqIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVD 255
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAKSGNMDLRIQTA----IMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 256 IDIYLLEKSRVIFQQAGERNYHIFYQILSG----QKELHDLLLVSanpsDFHFCSCGAVTVESLDDAEELLATEQAMDIL 331
Cdd:cd14876 157 VVAFLLEKSRIVTQDDNERSYHIFYQLLKGadseMKSKYHLLGLK----EYKFLNPKCLDVPGIDDVADFEEVLESLKSM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 332 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAF-----LMGINSSELVKCLIHPRIKVGNEYVTRG 406
Cdd:cd14876 233 GLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVDDAAAISNESLEVFkeacsLLFLDPEALKRELTVKVTKAGGQEIEGR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 407 QTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMF 486
Cdd:cd14876 313 WTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 487 VLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTF----KTKLFDNhfgksvhlQKPKPDK 562
Cdd:cd14876 393 ERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFvsacVSKLKSN--------GKFKPAK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 563 KKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENymstdsaIPFGEKKRKKGasfQTVASL 642
Cdd:cd14876 465 VDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG-------VVVEKGKIAKG---SLIGSQ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 643 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPrTF 722
Cdd:cd14876 535 FLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDL-GI 613
|
650 660 670
....*....|....*....|....*....|....*.
gi 1981090065 723 PKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14876 614 ANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
97-756 |
4.30e-111 |
|
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: 369.56 E-value: 4.30e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEA-PPHIFAVANNAFQDMLHNRE--NQSI 172
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 173 LFTGESGAGKTVNSKHIIQYFATIAA---MIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARG 249
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAsptSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 250 MLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVTVESlDDAEellATEQAMD 329
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNLEE-DCFE---VTREAML 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 330 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQ---LEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRG 406
Cdd:cd14880 237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQpcqPMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQVFK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 407 QTIEQVTCAV--GALSKSMYERMFKWLVARINRALDAKLSR-QFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNW 483
Cdd:cd14880 317 KPCSRAECDTrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 484 HMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGILSILEEECMFPKATDLT-FKTKLfdnhfgKSVHLQKPKPD 561
Cdd:cd14880 397 HYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSAAqLQTRI------ESALAGNPCLG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 562 KKKF--EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF--------ENYMSTDSAIPfgekkrk 631
Cdd:cd14880 470 HNKLsrEPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFpanpeektQEEPSGQSRAP------- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 632 kgasFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFK 711
Cdd:cd14880 543 ----VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFV 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1981090065 712 QRYCILNPRTFPKSKFVSSRKAAEELLGSLEIdhtqyrfGITKVF 756
Cdd:cd14880 619 ERYKLLRRLRPHTSSGPHSPYPAKGLSEPVHC-------GRTKVF 656
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
97-714 |
2.96e-109 |
|
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: 366.34 E-value: 2.96e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYK-------GKRRSEA---PPHIFAVANNAFQDMLH 165
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 166 NRENQSILFTGESGAGKTVNSKHIIQYFA------------TIAAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDN 233
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnnnltnSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 234 SSRFGKFIRMHF-GARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG-----QKELHDLLLVSANPSDFHFC-- 305
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLnq 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 306 SCGAVTVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKP--REEQLEADGTENA---------- 373
Cdd:cd14899 241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPhkGDDTVFADEARVMssttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 374 DKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQF------ 447
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 448 ---------FIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGLDlQACIDLIE- 517
Cdd:cd14899 401 vddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEh 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 518 KPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETV 597
Cdd:cd14899 480 RPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 598 VAVFQKSSNRLLASL-----FENYMSTDSAIPFGEKKRKKGASFQ---TVASLHKENLNKLMTNLKSTAPHFVRCINPNV 669
Cdd:cd14899 560 AQLLAGSSNPLIQALaagsnDEDANGDSELDGFGGRTRRRAKSAIaavSVGTQFKIQLNELLSTVRATTPRYVRCIKPND 639
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1981090065 670 NKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRY 714
Cdd:cd14899 640 SHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
97-758 |
3.81e-109 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 365.09 E-value: 3.81e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAAMIESRKKQgaleDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 256
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSV----EKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 257 DIYLLEKSRVIFQQAGERNYHIFYQILSG-----QKELH-DLLLVS--------ANPSDFHfcscgavtveslDDAEELL 322
Cdd:cd01386 157 QTLLLERSRVARRPEGESNFNVFYYLLAGadaalRTELHlNQLAESnsfgivplQKPEDKQ------------KAAAAFS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 323 ATEQAMDILGFLPDEKYGCYKLTGAIMHFGN---MKFKQKPREEQLEadgTENADKAAFLMGINSSELVKCLIHPRIKVG 399
Cdd:cd01386 225 KLQAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFAR---PEWAQRAAYLLGCTLEELSSAIFKHHLSGG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 400 NEYVTRGQTIEQVTC------------AVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYN---- 463
Cdd:cd01386 302 PQQSTTSSGQESPARsssggpkltgveALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqr 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 464 --SLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEwVSIGFGLD-LQACIDLIEK---------------PMGILSI 525
Cdd:cd01386 382 gaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVE-VDFDLPELsPGALVALIDQapqqalvrsdlrdedRRGLLWL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 526 LEEECMFPKATDLTFKTKLFdNHFGKSVHLQKPKPDKKKFEA-HFELVHYAGV--VPYNISGWLEKNK-DLLNETVVAVF 601
Cdd:cd01386 461 LDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLL 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 602 QkSSNRLLASLfenymstdsaipfgekkRKKGASFQTvaslhKENLNKLMTNLKSTAPHFVRCINPNVNKIPG------- 674
Cdd:cd01386 540 Q-ESQKETAAV-----------------KRKSPCLQI-----KFQVDALIDTLRRTGLHFVHCLLPQHNAGKDerstssp 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 675 -----ILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNP----RTFPKSKFVSSRKAAEELLGSLEIDH 745
Cdd:cd01386 597 aagdeLLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPpltkKLGLNSEVADERKAVEELLEELDLEK 676
|
730
....*....|...
gi 1981090065 746 TQYRFGITKVFFK 758
Cdd:cd01386 677 SSYRIGLSQVFFR 689
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
97-718 |
6.48e-107 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 359.29 E-value: 6.48e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRR-SEAPPHIFAVANNAFQDMLHNRENQSILF 174
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 175 TGESGAGKTVNSKHIIQYF-----ATIAAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHF-GAR 248
Cdd:cd14906 81 SGESGSGKTEASKTILQYLintssSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFrSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 249 GMLSSVDIDIYLLEKSRVIFQ-QAGERNYHIFYQILSG-QKELHDLLLVSANPSDFHFCSCGAVTVESL----------- 315
Cdd:cd14906 161 GKIDGASIETYLLEKSRISHRpDNINLSYHIFYYLVYGaSKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsnh 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 316 ----DDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKP---REEQLEADGTENADKAAFLMGINSSELV 388
Cdd:cd14906 241 nnktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 389 KCLIHPRIKVGNE--YVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRA---------LDAKLSRQ--FFIGILDIT 455
Cdd:cd14906 321 QALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKfnqntqsndLAGGSNKKnnLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 456 GFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFgLDLQACIDLIE-KPMGILSILEEECMFPK 534
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 535 ATDLTFKTKlfdnhFGKSVHlQKPKPDKKKF-EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF 613
Cdd:cd14906 480 GSEQSLLEK-----YNKQYH-NTNQYYQRTLaKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 614 enymSTDSAIPFGEKKRKKGASfqTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEG 693
Cdd:cd14906 554 ----QQQITSTTNTTKKQTQSN--TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNT 627
|
650 660
....*....|....*....|....*.
gi 1981090065 694 TRICREGFPNRLQYADFKQRY-CILN 718
Cdd:cd14906 628 IKVRKMGYSYRRDFNQFFSRYkCIVD 653
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
97-758 |
7.02e-103 |
|
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: 346.03 E-value: 7.02e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMI-YTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEA-PPHIFAVANNAF-QDMLHNRENQSIL 173
Cdd:cd14875 1 ATLLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFnAIFVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 174 FTGESGAGKTVNSKHIIQYFATIAAMIESRKKQGALEDQIMQ----ANTILEAFGNAKTLRNDNSSRFGKFIRMHF-GAR 248
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFdPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 249 GMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG-----QKELHDLllvsANPSDFHFCSCG------AVTVESLDD 317
Cdd:cd14875 161 GVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGlspeeKKELGGL----KTAQDYKCLNGGntfvrrGVDGKTLDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 318 AEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENAdKAAFLMGINSSELVKCLIhprIK 397
Cdd:cd14875 237 AHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLRECFL---VK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 398 VGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKL--SRQFFIGILDITGFEILEYNSLEQLCINFTNE 475
Cdd:cd14875 313 SKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNSFEQLCINYANE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 476 KLQQFFNWHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIE-KPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVH 554
Cdd:cd14875 393 SLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 555 LQKPK---PDKkkfeahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFenymSTDSaipfGEKKRK 631
Cdd:cd14875 472 FVLPKstiPNQ------FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLL----STEK----GLARRK 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 632 kgasfQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFK 711
Cdd:cd14875 538 -----QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFC 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1981090065 712 QRYCILNPRTfPKSKFVSSR--KAAEELLGS----LEIDHTQYRFGITKVFFK 758
Cdd:cd14875 613 RYFYLIMPRS-TASLFKQEKysEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
97-758 |
1.08e-98 |
|
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: 333.39 E-value: 1.08e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRS-----EAPPHIFAVANNAFQDMLHNRENQ 170
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 171 SILFTGESGAGKTVNSKHIIQYFATIAAMiESRKKQGAledqIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 250
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHST-SSTDVQSL----ILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 251 LSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG----QKELHDLLLVSAnpsdFHFCSCG-AVTVESLDDAEELLATE 325
Cdd:cd14886 156 LKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGlspeEKKSLGFKSLES----YNFLNASkCYDAPGIDDQKEFAPVR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 326 QAMDILgFLPDEKYGCYKLTGAIMHFGNMKFKQKPR---EEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEY 402
Cdd:cd14886 232 SQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNET 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 403 VTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFN 482
Cdd:cd14886 311 IISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 483 WHMFVLEQEEYKKESIEWVSIGFGlDLQACIDLIEKP-MGILSILEEECMFPKATDLTF----KTKLFDNHFGKSvhlqk 557
Cdd:cd14886 391 NQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFtsscKSKIKNNSFIPG----- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 558 pkpdkKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIpfgekkrkKGasfQ 637
Cdd:cd14886 465 -----KGSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNM--------KG---K 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 638 TVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCIL 717
Cdd:cd14886 529 FLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKIL 608
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1981090065 718 NPRTFPKSKFVSSRKAA-EELLGSLEIDHTQYRFGITKVFFK 758
Cdd:cd14886 609 ISHNSSSQNAGEDLVEAvKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
97-758 |
3.79e-98 |
|
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: 331.21 E-value: 3.79e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEvmaaYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFatiaamIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDI 256
Cdd:cd14937 77 ESGSGKTEASKLVIKYY------LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 257 DIYLLEKSRVIFQQAGERNYHIFYQILSG-QKELHDLLLVSANpSDFHFCSCGAVTVESLDDAEELLATEQAMDILGfLP 335
Cdd:cd14937 151 EIFLLENIRVVSQEEEERGYHIFYQIFNGmSQELKNKYKIRSE-NEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMN-MH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 336 DEKYGCYKLTGAIMHFGNMKFKQ-----KPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIE 410
Cdd:cd14937 229 DMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 411 QVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQ 490
Cdd:cd14937 309 ESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKET 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 491 EEYKKESIEWVSIGFGLDlQACIDLIEKPMGILSILEEECMFPKATDLTFkTKLFDNHFGKSVHLQKPKPDKKKfeaHFE 570
Cdd:cd14937 389 ELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYASTKKDINK---NFV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 571 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAipfgekKRKKGASFQtvaslHKENLNKL 650
Cdd:cd14937 464 IKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESL------GRKNLITFK-----YLKNLNNI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 651 MTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRIcREGFPNRLQYADFKQRYCILNPRTFPKSKFVSS 730
Cdd:cd14937 533 ISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDK 611
|
650 660
....*....|....*....|....*...
gi 1981090065 731 RKAAEELLGSLEIDhtQYRFGITKVFFK 758
Cdd:cd14937 612 EKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
97-758 |
2.24e-95 |
|
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: 324.08 E-value: 2.24e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAY---KGKRRSEAPPHIFAVANNAFQDMLHNRENQSIL 173
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 174 FTGESGAGKTVNSKHIIQYFATiaamiESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGAR-GMLS 252
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTC-----RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERkKHLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 253 SVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGA----VTVESLDDAEELLATEQAM 328
Cdd:cd14878 156 GARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMredvSTAERSLNREKLAVLKQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 329 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQT 408
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 409 IEQVTCAVGALSKSMYERMFKWLVARINRAL----DAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWH 484
Cdd:cd14878 316 IQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 485 MFVLEQEEYKKESIEWVSIGFGLDLQACIDLI-EKPMGILSILEEECMFPKATDLTFKTKLFD-------NHFGKSVHLQ 556
Cdd:cd14878 396 LFLQEQTECVQEGVTMETAYSPGNQTGVLDFFfQKPSGFLSLLDEESQMIWSVEPNLPKKLQSllessntNAVYSPMKDG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 557 KPKPDKKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTdsaipfgekkrkkgasf 636
Cdd:cd14878 476 NGNVALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLVT----------------- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 637 qtVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCI 716
Cdd:cd14878 539 --IASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKP 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1981090065 717 LnPRTFPKSKfvssRKAAEELLGSLEIDHTQ---YRFGITKVFFK 758
Cdd:cd14878 617 L-ADTLLGEK----KKQSAEERCRLVLQQCKlqgWQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
98-722 |
3.49e-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: 312.22 E-value: 3.49e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKwlPVYQKEVMAAYKgKRRSEAPPHIFAVANNAFQDMLHNrENQSILFTGE 177
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 178 SGAGKTVNSKHIIQYfatiaaMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFgaRGMLSSVDID 257
Cdd:cd14898 78 SGSGKTENAKLVIKY------LVERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKITGAKFE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 258 IYLLEKSRVIFQQAGERNYHIFYQILSGQkelhDLLLvsanPSDFHFCSCGAVTVESLDD-AEELLATEQAMDILGFLPD 336
Cdd:cd14898 150 TYLLEKSRVTHHEKGERNFHIFYQFCASK----RLNI----KNDFIDTSSTAGNKESIVQlSEKYKMTCSAMKSLGIANF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 337 EKYGCYKLtgAIMHFGNMKFKQkprEEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCAV 416
Cdd:cd14898 222 KSIEDCLL--GILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 417 GALSKSMYERMFKWLVARINRALDAKLSRQffIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKE 496
Cdd:cd14898 297 NSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 497 SIEWVSIGFgLDLQACIDLIEKPMGILSILEEECMFPKAT--DLTFKTKLFDNHFGKSvhlqkpkpdkkKFEAHFELVHY 574
Cdd:cd14898 375 GIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNGFINT-----------KARDKIKVSHY 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 575 AGVVPYNISGWLEKNKDllnetvvavfqkssnrllaslfenymsTDSAIPFGEKKRKKGASFQTVASLHKENLNKLMTNL 654
Cdd:cd14898 443 AGDVEYDLRDFLDKNRE---------------------------KGQLLIFKNLLINDEGSKEDLVKYFKDSMNKLLNSI 495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1981090065 655 KSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTF 722
Cdd:cd14898 496 NETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLF 563
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
112-758 |
1.42e-84 |
|
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: 294.63 E-value: 1.42e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 112 IYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGESGAGKTVNSKHIIQ 191
Cdd:cd14887 24 IYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQSILISGESGAGKTETSKHVLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 192 YFATIAAMIESRKKQGaLEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDIDIYLLEKSRVIFQQA 271
Cdd:cd14887 104 YLAAVSDRRHGADSQG-LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 272 GERNYHIFYQILSGQK--ELHDLLLVSANPsdfhfcscgavtvESLDdaeeLLATEQAMDILGFLPDEKYGCYKLTGAIM 349
Cdd:cd14887 183 DEFSFHIFYALCNAAVaaATQKSSAGEGDP-------------ESTD----LRRITAAMKTVGIGGGEQADIFKLLAAIL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 350 HFGNMKF--KQKPRE-------------EQLEADGTENADKAAFLMGINSSE--------LVKCLIHPRIKVGNEYV--- 403
Cdd:cd14887 246 HLGNVEFttDQEPETskkrkltsvsvgcEETAADRSHSSEVKCLSSGLKVTEasrkhlktVARLLGLPPGVEGEEMLrla 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 404 --------TRGQ-TIEQVTCAVGALSKSMYERMFKWLVARINRAL-------------DAKLSRQF-FIGILDITGFEIL 460
Cdd:cd14887 326 lvsrsvreTRSFfDLDGAAAARDAACKNLYSRAFDAVVARINAGLqrsakpsesdsdeDTPSTTGTqTIGILDLFGFEDL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 461 E---YNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKES--IEWVSIGFGLDLQACIDLIEKP---------------- 519
Cdd:cd14887 406 RnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQDCSAFPFSFPLASTLTSSPsstspfsptpsfrsss 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 520 --------MGILSILEEE-CMFPKATDLTFKTKLFDNHFGK----SVHLQKPKPDKKKFEAHFELVHYAGVVPYNISGWL 586
Cdd:cd14887 486 afatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKNITPALSRENLEFTVSHFACDVTYDARDFC 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 587 EKNKDLLNETVVAVFQKSSNRLLaslfENYMSTDSAIPFGEKKRKkgasfqTVASLHKENLNKLMTNLKSTAPHFVRCIN 666
Cdd:cd14887 566 RANREATSDELERLFLACSTYTR----LVGSKKNSGVRAISSRRS------TLSAQFASQLQQVLKALQETSCHFIRCVK 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 667 PNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFpkSKFVSSRKAAEELLGSLEIDHT 746
Cdd:cd14887 636 PNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMAL--REALTPKMFCKIVLMFLEINSN 713
|
730
....*....|..
gi 1981090065 747 QYRFGITKVFFK 758
Cdd:cd14887 714 SYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
94-757 |
6.20e-83 |
|
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: 287.14 E-value: 6.20e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 94 LNEASVLHTLKRRYGQWMIYTY---SGLfcVTINPYKWLPVYQKEVMAAYK-------GKRRSEAPPHIFAVANNAFQDM 163
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 164 LHNRENQSILFTGESGAGKTVNSKHIIQYFATIAAmieSRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRM 243
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSS---HSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 244 HFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG-QKELHDLLLVSaNPSDF-----HFCSCGAVTVESlDD 317
Cdd:cd14879 156 QFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGaSPEERQHLGLD-DPSDYallasYGCHPLPLGPGS-DD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 318 AEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFkqkpreeQLEADGTENA---------DKAAFLMGINSSELV 388
Cdd:cd14879 234 AEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEF-------TYDHEGGEESavvkntdvlDIVAAFLGVSPEDLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 389 KCLIHpRIKvgneYVTRgqtiEQVTC---AVGA------LSKSMYERMFKWLVARINRALdAKLSRQF--FIGILDITGF 457
Cdd:cd14879 307 TSLTY-KTK----LVRK----ELCTVfldPEGAaaqrdeLARTLYSLLFAWVVETINQKL-CAPEDDFatFISLLDFPGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 458 EIL---EYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKE--SIEWVSIgfgLDLQACIDLI-EKPMGILSILEEEC- 530
Cdd:cd14879 377 QNRsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEgvSVPATSY---FDNSDCVRLLrGKPGGLLGILDDQTr 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 531 MFPKATDLTFKTKL---FDNHfgKSVHLQKPKPDKKKFeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVavfqkssnr 607
Cdd:cd14879 454 RMPKKTDEQMLEALrkrFGNH--SSFIAVGNFATRSGS-ASFTVNHYAGEVTYSVEGFLERNGDVLSPDFV--------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 608 llaSLFenymstdsaipfgekkrkKGASFqtvaslHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRC 687
Cdd:cd14879 522 ---NLL------------------RGATQ------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRS 574
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 688 NGVLEGTRICREGFPNRLQYADFKQRYcilnPRTFPKSKFVSSRKAAEELLGSLEIDhtqYRFGITKVFF 757
Cdd:cd14879 575 LGLPELAARLRVEYVVSLEHAEFCERY----KSTLRGSAAERIRQCARANGWWEGRD---YVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
97-705 |
1.22e-74 |
|
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: 264.08 E-value: 1.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEA-------PPHIFAVANNAFQDMLHNRE 168
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 169 NQSILFTGESGAGKTVNSKHIIQYFatiaAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGAR 248
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYF----HYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 249 ---------GMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLVS-------ANPSDFHFCSCGAV 310
Cdd:cd14884 157 entqknmfnGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlsDEDLARRNLVRncgvyglLNPDESHQKRSVKG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 311 TVESLDDAEELLATEQAMDILGF------LPDEKYGCYKLT------GAIMHFGNMKFKQkpreeqleadgtenadkAAF 378
Cdd:cd14884 237 TLRLGSDSLDPSEEEKAKDEKNFvallhgLHYIKYDERQINeffdiiAGILHLGNRAYKA-----------------AAE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 379 LMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRAL------------DAKLSRQ 446
Cdd:cd14884 300 CLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdneDIYSINE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 447 FFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIgfglDLQACIDLIEKPMGILSIL 526
Cdd:cd14884 380 AIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSD----VAPSYSDTLIFIAKIFRRL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 527 EEECMFP----KATDLTFKTKLFDNH----------FGK-SVHLQKPKPDKKKFEAH-FELVHYAGVVPYNISGWLEKNK 590
Cdd:cd14884 456 DDITKLKnqgqKKTDDHFFRYLLNNErqqqlegkvsYGFvLNHDADGTAKKQNIKKNiFFIRHYAGLVTYRINNWIDKNS 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 591 DLLNETVVAVFQKSSNRLLASLFENymstdsaipfgekkrKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVN 670
Cdd:cd14884 536 DKIETSIETLISCSSNRFLREANNG---------------GNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAK 600
|
650 660 670
....*....|....*....|....*....|....*
gi 1981090065 671 KIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRL 705
Cdd:cd14884 601 MLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKI 635
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
98-724 |
3.43e-73 |
|
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: 258.12 E-value: 3.43e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKwlpvyqkEVMAA--YKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 175
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYR-------DVGNPltLTSTRSSPLAPQLLKVVQEAVRQQSETGYPQAIILS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 176 GESGAGKTVNSKHIIQYFATIAAmiesrkkqGALEDQIMQ----ANTILEAFGNAKTLRNDNSSRFGKFIRMHFgARGML 251
Cdd:cd14881 75 GTSGSGKTYASMLLLRQLFDVAG--------GGPETDAFKhlaaAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDGAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 252 SSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSG--QKELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMD 329
Cdd:cd14881 146 YRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGlsQEERVKLHLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKACLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 330 ILG--FLpdekyGCYKLTGAIMHFGNMKFKQKPREEQLEADGTEnADKAAFLMGINSSELVKCLIhprIKVGNeyvTRGQ 407
Cdd:cd14881 226 ILGipFL-----DVVRVLAAVLLLGNVQFIDGGGLEVDVKGETE-LKSVAALLGVSGAALFRGLT---TRTHN---ARGQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 408 TIEQVtCAVG-------ALSKSMYERMFKWLVARIN--RALDAKLSRQF---FIGILDITGFEILEYNSLEQLCINFTNE 475
Cdd:cd14881 294 LVKSV-CDANmsnmtrdALAKALYCRTVATIVRRANslKRLGSTLGTHAtdgFIGILDMFGFEDPKPSQLEHLCINLCAE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 476 KLQQFFNWHMFVLEQEEYKKESIEW-VSIGFgLDLQACIDLIEK-PMGILSILEEECMfPKATDLTFKTKLFDNHFGKSV 553
Cdd:cd14881 373 TMQHFYNTHIFKSSIESCRDEGIQCeVEVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPR 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 554 HLQKPKPDKKKfeahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSnrllaslfenymstdsaIPFGekkrkkg 633
Cdd:cd14881 451 LFEAKPQDDRM----FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN-----------------CNFG------- 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 634 asFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQR 713
Cdd:cd14881 503 --FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNAR 580
|
650
....*....|.
gi 1981090065 714 YCILNPRTFPK 724
Cdd:cd14881 581 YRLLAPFRLLR 591
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
98-717 |
5.93e-70 |
|
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: 248.89 E-value: 5.93e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 177
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 178 SGAGKTVNSKHIIQYFATIAAMiesrkKQGALEdQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDID 257
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDG-----NRGATG-RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 258 IYLLEKSRVIFQQAGERNYHIFYQI---LSGQKELHDLLL------------VSANPSDFHFC-SCGAVTVESLDDAEEL 321
Cdd:cd14882 156 MYQLEKLRVSTTDGNQSNFHIFYYFydfIEAQNRLKEYNLkagrnyrylripPEVPPSKLKYRrDDPEGNVERYKEFEEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 322 LateQAMDilgFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEadGTENADKAAFLMGINSSELVKCLIHPRIKVGNE 401
Cdd:cd14882 236 L---KDLD---FNEEQLETVRKVLAAILNLGEIRFRQNGGYAELE--NTEIASRVAELLRLDEKKFMWALTNYCLIKGGS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 402 YVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINraldAKLS--RQFF-----IGILDITGFEILEYNSLEQLCINFTN 474
Cdd:cd14882 308 AERRKHTTEEARDARDVLASTLYSRLVDWIINRIN----MKMSfpRAVFgdkysISIHDMFGFECFHRNRLEQLMVNTLN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 475 EKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECmfpkatdltfKTKLFDNHFGKSVH 554
Cdd:cd14882 384 EQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDAS----------RSCQDQNYIMDRIK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 555 lQKPKPDKKKFEAH-FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMStdsaipfgEKKRKKG 633
Cdd:cd14882 454 -EKHSQFVKKHSAHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQV--------RNMRTLA 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 634 ASFQTvASLhkENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQR 713
Cdd:cd14882 525 ATFRA-TSL--ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRR 601
|
....
gi 1981090065 714 YCIL 717
Cdd:cd14882 602 YQFL 605
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
98-722 |
3.15e-68 |
|
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: 244.62 E-value: 3.15e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSeAPPHIFAVANNAFQDMLHNRENQSILFTGE 177
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPFLHSQELVRNYNQRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 178 SGAGKTVNSKHIIQYFATIAAmieSRKKQgaLEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDID 257
Cdd:cd14905 81 SGSGKSENTKIIIQYLLTTDL---SRSKY--LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 258 IYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCS-CGAVTVESLDDAEELLATEQAMDILGFlPD 336
Cdd:cd14905 156 SYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNqGGSISVESIDDNRVFDRLKMSFVFFDF-PS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 337 EKYG-CYKLTGAIMHFGNMKFKQKprEEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTieqvtca 415
Cdd:cd14905 235 EKIDlIFKTLSFIIILGNVTFFQK--NGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENRDS------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 416 vgaLSKSMYERMFKWLVARINRALDAKlSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKK 495
Cdd:cd14905 306 ---LARSLYSALFHWIIDFLNSKLKPT-QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 496 ESIEWVS-IGFGlDLQACIDLIEKpmgILSILEEECMFPKATDLTFKTKLfdNHFGKSVHLQKPKPDKkkfeahFELVHY 574
Cdd:cd14905 382 ERIPWMTpISFK-DNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--QNFLSRHHLFGKKPNK------FGIEHY 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 575 AGVVPYNISGWLEKNKDL-------------------------LNETVVAVFQ-----KSSNRLLASLFENYMSTDSAIP 624
Cdd:cd14905 450 FGQFYYDVRGFIIKNRDEilqrtnvlhknsitkylfsrdgvfnINATVAELNQmfdakNTAKKSPLSIVKVLLSCGSNNP 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 625 ------------------FGEKKRKKGASFQTVASLHKEnlnklmTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLR 686
Cdd:cd14905 530 nnvnnpnnnsgggggggnSGGGSGSGGSTYTTYSSTNKA------INNSNCDFHFIRCIKPNSKKTHLTFDVKSVNEQIK 603
|
650 660 670
....*....|....*....|....*....|....*...
gi 1981090065 687 CNGVLEGTRICREGFPNRLQYADFKQRYCIL--NPRTF 722
Cdd:cd14905 604 SLCLLETTRIQRFGYTIHYNNKIFFDRFSFFfqNQRNF 641
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
97-717 |
1.61e-67 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 241.31 E-value: 1.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 97 ASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYkgkrrseappHIFAVANNAFQDMLHNREN-QSILFT 175
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 176 GESGAGKTVNSKHIIQYFATIAAMIESRKKQGALEdqimqanTILEAFGNAKTLRNDNSSRFGKFIRMHFgARGMLSSVD 255
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAIE-------SVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 256 IDIYL-LEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFL 334
Cdd:cd14874 143 LKYTVpLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 335 PDEKYGCYKLTGAIMHFGNMKFKQKPR---EEQLEADGTENADK-AAFLMGINSSELVKCLIhPRIKVGNEYvtrgqTIE 410
Cdd:cd14874 223 DDHCISIYKIISTILHIGNIYFRTKRNpnvEQDVVEIGNMSEVKwVAFLLEVDFDQLVNFLL-PKSEDGTTI-----DLN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 411 QVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFfIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQ 490
Cdd:cd14874 297 AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV-ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 491 EEYKKESIEwvsigfgLDLQ--ACID-------LIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPD 561
Cdd:cd14874 376 VDYAKDGIS-------VDYKvpNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNKE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 562 KKKFEAHfelvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMS-TDSAIPFGEKKRKKGAsfQTVA 640
Cdd:cd14874 449 RLEFGVR----HCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSnTSDMIVSQAQFILRGA--QEIA 522
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1981090065 641 slhkENLNKLMTnlkstapHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRY-CIL 717
Cdd:cd14874 523 ----DKINGSHA-------HFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYrCLL 589
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
100-757 |
1.05e-66 |
|
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: 241.80 E-value: 1.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 100 LHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRR----------SEAPPHIFAVANNAFQDMLHNREN 169
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 170 QSILFTGESGAGKTVNSKHIIQYFATIAAMIESRK----KQGALE---DQIMQANTILEAFGNAKTLRNDNSSRFGKFIR 242
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPdsegASGVLHpigQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 243 MHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKE---LHDLLLVSANPSDFHFCSCGA--VTVESLD- 316
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdptLRDSLEMNKCVNEFVMLKQADplATNFALDa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 317 -DAEELLATEQAMDIlgfLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENA----------DKAAFLMGINSS 385
Cdd:cd14893 244 rDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTvsdaqscalkDPAQILLAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 386 ELVKCLIHPRIKV-------GNEYVTRGQ--TIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSR---------QF 447
Cdd:cd14893 321 EVEPVVLDNYFRTrqffskdGNKTVSSLKvvTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksnivinSQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 448 FIGILDITGFEILE--YNSLEQLCINFTNEKLQQFF-------NWHMFVLEQEEYKKESIEWVSIGFGLDLQACIDLIE- 517
Cdd:cd14893 401 GVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvqntlaiNFSFLEDESQQVENRLTVNSNVDITSEQEKCLQLFEd 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 518 KPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVhLQKPKPD----------KKKFEAHFELVHYAGVVPYNISGWLE 587
Cdd:cd14893 481 KPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGG-LSRPNMGadttneylapSKDWRLLFIVQHHCGKVTYNGKGLSS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 588 KNKDLLNETVVAVFQKSSNRLLASLFENYM---STDSAIPFGEKKRKKGASFQTVASLHKENLN--------------KL 650
Cdd:cd14893 560 KNMLSISSTCAAIMQSSKNAVLHAVGAAQMaaaSSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadAL 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 651 MTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYcilnprtfpkSKFVSS 730
Cdd:cd14893 640 LHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY----------KNVCGH 709
|
730 740 750
....*....|....*....|....*....|.
gi 1981090065 731 RKAAEELLGSLE----IDHTQYRFGITKVFF 757
Cdd:cd14893 710 RGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
119-243 |
1.71e-52 |
|
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: 182.16 E-value: 1.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 119 FCVTINPYKWLPVY-QKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGESGAGKTVNSKHIIQYFATIA 197
Cdd:cd01363 1 VLVRVNPFKELPIYrDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1981090065 198 A----------MIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRM 243
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 ... |
98-756 |
7.33e-46 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 178.49 E-value: 7.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 98 SVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSE-APPHIFAVANNAFQDMLHNRENQSILFTG 176
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 177 ESGAGKTVNSKHIIQYFATIAA------------------MIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFG 238
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKgsrrlptnlndqeednihNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 239 KFIRMHFGARgMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVTVESLDDA 318
Cdd:cd14938 162 KFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 319 EELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQL-----------------------EADGTENADK 375
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAFRKKSLlmgknqcgqninyetilselensEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 376 ----AAFLMGINSSELVKCLIHPRIkVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFF--- 448
Cdd:cd14938 321 nlllACKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININtny 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 449 IGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGLDLQACID-LIEKPMGILSILE 527
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNlLVGPTEGSLFSLL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 528 EECMFPKATDLTFKTKLFDNHFGKSVHLQKpKPDKKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNR 607
Cdd:cd14938 480 ENVSTKTIFDKSNLHSSIIRKFSRNSKYIK-KDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSENE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 608 LLASL--FENYMSTDS--------AIPFGEK--KRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNK-IPG 674
Cdd:cd14938 559 YMRQFcmFYNYDNSGNiveekrrySIQSALKlfKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKrELC 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 675 ILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPrtfpkskfvSSRKAAEELLGSLEIDHTQYRFGITK 754
Cdd:cd14938 639 SFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 1981090065 755 VF 756
Cdd:cd14938 710 IF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
849-1739 |
7.77e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 129.79 E-value: 7.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 849 AQLQKAlEKSEFQREELKAKQVSL-TQEKNDLILQLQAEQETLANVEEQCEwlikskiQLEARVKELSERVEEEEEINSE 927
Cdd:TIGR02168 207 RQAEKA-ERYKELKAELRELELALlVLRLEELREELEELQEELKEAEEELE-------ELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 928 LTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEE 1007
Cdd:TIGR02168 279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1008 KLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELsqmnskve 1087
Cdd:TIGR02168 359 ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL-------- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1088 nEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGgsslAQLEITKKQETKFQKLH 1167
Cdd:TIGR02168 431 -EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ----ARLDSLERLQENLEGFS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1168 RDMEEATLhfettsaslkkrHADSLAELEGQVENLQQVKQKLEKDKS-DLQLEVDDLLtrVEQMTRAKANAEKLctlyee 1246
Cdd:TIGR02168 506 EGVKALLK------------NQSGLSGILGVLSELISVDEGYEAAIEaALGGRLQAVV--VENLNAAKKAIAFL------ 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1247 rlheATAKLDKVTQLANDLAAQkTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLeketksqsALAHALQ 1326
Cdd:TIGR02168 566 ----KQNELGRVTFLPLDSIKG-TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV--------LVVDDLD 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1327 KAQRdcdLLREQYEEEQEVKAELHRTL---------SKVNAEMVQWRMKYENNViQRTEDLEDAKKELAIRLQEAAEAMG 1397
Cdd:TIGR02168 633 NALE---LAKKLRPGYRIVTLDGDLVRpggvitggsAKTNSSILERRREIEELE-EKIEELEEKIAELEKALAELRKELE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1398 VANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLK 1477
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1478 NTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLEL 1557
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1558 LEAKAELERKLSEKDEEIENfrrkqqctIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQ 1637
Cdd:TIGR02168 869 EELESELEALLNERASLEEA--------LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1638 LQIQIKDL-QMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEqtergrrLSEEELLEATERINLFYTQNTSLL 1716
Cdd:TIGR02168 941 LQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNL-------AAIEEYEELKERYDFLTAQKEDLT 1013
|
890 900
....*....|....*....|...
gi 1981090065 1717 SQKKKLEADVARMQKEAEEVVQE 1739
Cdd:TIGR02168 1014 EAKETLEEAIEEIDREARERFKD 1036
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1073-1912 |
4.17e-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: 127.48 E-value: 4.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1073 RKKELElSQMNSKVENekglVAQLQKTVKELQTQIKDLKEKLE-AERTTRAKMERERADLTQDLADLNERLEEVggssLA 1151
Cdd:TIGR02168 173 RRKETE-RKLERTREN----LDRLEDILNELERQLKSLERQAEkAERYKELKAELRELELALLVLRLEELREEL----EE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1152 QLEITKKQETKFQKLHRDMEEATLHFETTSASLKKRHaDSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMT 1231
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELE-EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1232 RAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQL 1311
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1312 EKETKSQSALAHALQKAQRDCDLLREQYEEEQevKAELHRTLSKVNAEMVQWRMKYEnNVIQRTEDLEDAKKELAIRLQE 1391
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELE-RLEEALEELREELEEAEQALDA 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1392 AAEAMGVANARNASLERARHQLQlelgdalsdlGKVRSAAARLDQKQLQSGkaladwkqkheesqalldasqkeVQALST 1471
Cdd:TIGR02168 480 AERELAQLQARLDSLERLQENLE----------GFSEGVKALLKNQSGLSG-----------------------ILGVLS 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1472 ELLKLKNTYEESIvgqETLRREnkNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKIL 1551
Cdd:TIGR02168 527 ELISVDEGYEAAI---EAALGG--RLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFL 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1552 HFQLELLEAKAELERKLS----------EKDEEIENFRR-KQQCTIDSLQSSL-----------DSEAKSRIEVTRLKKK 1609
Cdd:TIGR02168 602 GVAKDLVKFDPKLRKALSyllggvlvvdDLDNALELAKKlRPGYRIVTLDGDLvrpggvitggsAKTNSSILERRREIEE 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1610 MEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTER 1689
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1690 GRRLSEEELLEATERInlfytqnTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIA 1769
Cdd:TIGR02168 762 EIEELEERLEEAEEEL-------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1770 HLERTRENMEQTITDLQKRLAEAE------QMALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELT 1843
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAaeieelEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1844 YQAEEDKKNLSRMQTQMDKLQLKVQNYKQQV-EVAETQANQYLSKYKKQQHELNEVKERAEVAESQVNKL 1912
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
213-698 |
4.28e-24 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 110.60 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 213 IMQANTILEAFGNAKTLRNDNSSRFGKF--IRMHFGARG---MLSSVDIDIYLLEKSRVIFQQA------GERNYHIFYQ 281
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERGresgdqNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 282 ILSG----------QKELH-DLLLVSA----NPSDFHFCscGAVTVESL--DDAEELLATEQAMDILGFLPDEKYGCYKL 344
Cdd:cd14894 329 MVAGvnafpfmrllAKELHlDGIDCSAltylGRSDHKLA--GFVSKEDTwkKDVERWQQVIDGLDELNVSPDEQKTIFKV 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 345 TGAIMHFGNMKFKQKPREEQL--EADGTENA-DKAAFLMGINSSE-LVKCLIHPRIKVGNEYVTRGQTIE--QVTCAVGA 418
Cdd:cd14894 407 LSAVLWLGNIELDYREVSGKLvmSSTGALNApQKVVELLELGSVEkLERMLMTKSVSLQSTSETFEVTLEkgQVNHVRDT 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 419 LSKSMYERMFKWLVARINRA--------------LDAKLSRQ---FFIGILDITGFEILEYNSLEQLCINFTNEKLQqff 481
Cdd:cd14894 487 LARLLYQLAFNYVVFVMNEAtkmsalstdgnkhqMDSNASAPeavSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY--- 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 482 nwhmfvleQEEYKKESIEWVSIGFGLDLQACIDLI---EKPMGILSILEEECMFPKATDLTF-----KTKLFDNHFGKSV 553
Cdd:cd14894 564 --------AREEQVIAVAYSSRPHLTARDSEKDVLfiyEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIYDRN 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 554 HLQKPKPDKKKFEAH-----------FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYM----- 617
Cdd:cd14894 636 SSRLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSqlgws 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 618 -STDSAIPFGEKKRKKGAsfQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRI 696
Cdd:cd14894 716 pNTNRSMLGSAESRLSGT--KSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEI 793
|
..
gi 1981090065 697 CR 698
Cdd:cd14894 794 CR 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
941-1795 |
3.46e-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: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 941 ELKKEIDDLE-TMLVKS----EKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAkvvqEAHQQTLDDLHMEEEKLSSLSKA 1015
Cdd:TIGR02169 215 ALLKEKREYEgYELLKEkealERQKEAIERQLASLEEELEKLTEEISELEKRL----EEIEQLLEELNKKIKDLGEEEQL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1016 NLKleQQVDELEGALEQerkarmncerelhkLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQ 1095
Cdd:TIGR02169 291 RVK--EKIGELEAEIAS--------------LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1096 LQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKFQKLHRDM---EE 1172
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIagiEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1173 ATLHFETTsaslKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLltrveqmtrakanaeklctlyEERLHEAT 1252
Cdd:TIGR02169 435 KINELEEE----KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV---------------------EKELSKLQ 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1253 AKLDKvtqlandLAAQKTKLWSESGEFLRRLEEKEA-------LINQLSREKSNFTRQIEdlrgqleketksqSALAHAL 1325
Cdd:TIGR02169 490 RELAE-------AEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGSVGERYATAIE-------------VAAGNRL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1326 QKAQRDCDLLRE---QYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAI-------------RL 1389
Cdd:TIGR02169 550 NNVVVEDDAVAKeaiELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPafkyvfgdtlvveDI 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1390 QEAAEAMGvaNARNASLE--------------RARHQLQlelGDALSDLGKVRSAAARLDQKQlqsgKALADWKQKHEES 1455
Cdd:TIGR02169 630 EAARRLMG--KYRMVTLEgelfeksgamtggsRAPRGGI---LFSRSEPAELQRLRERLEGLK----RELSSLQSELRRI 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1456 QALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLtnqvregtknltemekvkkliEEEKTEVQVT 1535
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL---------------------EQEIENVKSE 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1536 LEETEGALERNESKILHFQLELleakAELERKLS-EKDEEIENFRRKQQCTIDSLQSSLDSeaksrievtrlkkkMEEDL 1614
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEAL----NDLEARLShSRIPEIQAELSKLEEEVSRIEARLRE--------------IEQKL 821
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1615 NEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRS----LQEQ---T 1687
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKerdeLEAQlreL 901
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1688 ERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEE------VVQECQNAEEKAKKAAIEAANLSEEL 1761
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEelsledVQAELQRVEEEIRALEPVNMLAIQEY 981
|
890 900 910
....*....|....*....|....*....|....
gi 1981090065 1762 KKKQDTIAHLERTRENMEQTITDLQKRLAEAEQM 1795
Cdd:TIGR02169 982 EEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
839-1736 |
5.95e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 97.45 E-value: 5.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 839 EEVAGLKEECAQLQKALEKSEFQREELKAKQvSLTQEKNDLILQLQAEQETLanveEQCEWLIKSKIQLEARVKELSERv 918
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLD-LIIDEKRQQLERLRREREKA----ERYQALLKEKREYEGYELLKEKE- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 919 eeeeeinsELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISklnraakvvqeahqqt 998
Cdd:TIGR02169 234 --------ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---------------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 999 lddlhmeeeklsslskanLKLEQQVDELEGALEQerkarmncerelhkLEGNLKLNRESMENLESSQRHLAEELRKKELE 1078
Cdd:TIGR02169 290 ------------------LRVKEKIGELEAEIAS--------------LERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1079 LSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKK 1158
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1159 QETKFQKLHRDM---EEATLHFETTsaslKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLltrveqmtraka 1235
Cdd:TIGR02169 418 LSEELADLNAAIagiEAKINELEEE----KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV------------ 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1236 naeklctlyEERLHEATAKLDKvtqlandLAAQKTKLWSESGEFLRRLEEKEA-------LINQLSREKSNFTRQIEDLR 1308
Cdd:TIGR02169 482 ---------EKELSKLQRELAE-------AEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGSVGERYATAIEVAA 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1309 GQ------LEKETKSQSALAHALQ-KAQRDCDL-LREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENN---VIQRT-- 1375
Cdd:TIGR02169 546 GNrlnnvvVEDDAVAKEAIELLKRrKAGRATFLpLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAfkyVFGDTlv 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1376 -EDLEDAKK--------ELAIRLQEAAEAM-----------GVANARNASLERARHQLQlELGDALSDL-GKVRSAAARL 1434
Cdd:TIGR02169 626 vEDIEAARRlmgkyrmvTLEGELFEKSGAMtggsraprggiLFSRSEPAELQRLRERLE-GLKRELSSLqSELRRIENRL 704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1435 DQKQlqsgKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKN 1514
Cdd:TIGR02169 705 DELS----QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA 780
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1515 LTEMEkvKKLIEEEKTEVQVTLEETEGALERNESKILHFQLElLEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSSLD 1594
Cdd:TIGR02169 781 LNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK-LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1595 SEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQ 1674
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1981090065 1675 ----------SELEDLRSLQEQTERgrrlsEEELLEATERINLFYTQN-TSLLSQKKKLEADVARMQKEAEEV 1736
Cdd:TIGR02169 938 dpkgedeeipEEELSLEDVQAELQR-----VEEEIRALEPVNMLAIQEyEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
836-1577 |
1.83e-18 |
|
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: 92.81 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 836 EVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQekndlilQLQAEQETLANVEEQCEWLIKSKIQLEARVKELS 915
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEE-------QLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 916 ERVEEEEEINSELtaRGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAkvvqEAH 995
Cdd:TIGR02168 414 DRRERLQQEIEEL--LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL----AQL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 996 QQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQeRKARMNCERELHK-LEGNLklnRESMENLESsqrhlaeelRK 1074
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV-LSELISVDEGYEAaIEAAL---GGRLQAVVV---------EN 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1075 KELELSQMNSKVENEKGLVAQLqktvkeLQTQIKDlkEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLE 1154
Cdd:TIGR02168 555 LNAAKKAIAFLKQNELGRVTFL------PLDSIKG--TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVL 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1155 ITKKQETKFQKLHRDMEEATL-----------------HFETTSASLKKR-----HADSLAELEGQVENLQQVKQKLEKD 1212
Cdd:TIGR02168 627 VVDDLDNALELAKKLRPGYRIvtldgdlvrpggvitggSAKTNSSILERRreieeLEEKIEELEEKIAELEKALAELRKE 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1213 KSDLQLEVDDLLTRVEQMTRA-------KANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEE 1285
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQisalrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1286 KEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMvqwrm 1365
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI----- 861
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1366 kyennviqrtEDLEDAKKELAIRLQEAAEAMgvanarnASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKAL 1445
Cdd:TIGR02168 862 ----------EELEELIEELESELEALLNER-------ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1446 ADWKQKHEESQALLDASQKEVQAL-STELLKLKNTYEESIVGQETLRRENKNLQEEISNLtnqvreGTKNLTEMEKvkkl 1524
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL------GPVNLAAIEE---- 994
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1981090065 1525 IEEEKTEVQVTLEETEgalerneskilhfqlELLEAKAELERKLSEKDEEIEN 1577
Cdd:TIGR02168 995 YEELKERYDFLTAQKE---------------DLTEAKETLEEAIEEIDREARE 1032
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
835-1581 |
7.52e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 90.51 E-value: 7.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 835 SEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEK----NDLILQLQAEQE----TLANVEEQCEWLIKSKIQ 906
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvKEKIGELEAEIAslerSIAEKERELEDAEERLAK 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 907 LEARVKELSERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNR 986
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 987 AAKVVQEAHQQTLDDLHMEEEKLSSLskanlklEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQR 1066
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGI-------EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1067 HLAEELRKKELELSQ---------------------MNSKVENEKGLVAQLQKTVKELQTQI------------------ 1107
Cdd:TIGR02169 480 RVEKELSKLQRELAEaeaqaraseervrggraveevLKASIQGVHGTVAQLGSVGERYATAIevaagnrlnnvvveddav 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1108 -KDLKEKLEAERTTRA------KMERERADLTQ-----------DLADLNERLEE----VGGSSLA--QLEITKKQETKF 1163
Cdd:TIGR02169 560 aKEAIELLKRRKAGRAtflplnKMRDERRDLSIlsedgvigfavDLVEFDPKYEPafkyVFGDTLVveDIEAARRLMGKY 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1164 QKLHRDMEEATLHFETTSASLKKRHADSLA-ELEGQVENLQQVKQKLEKDKSDLQLEVDDLltrveqmtrakanaeklct 1242
Cdd:TIGR02169 640 RMVTLEGELFEKSGAMTGGSRAPRGGILFSrSEPAELQRLRERLEGLKRELSSLQSELRRI------------------- 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1243 lyEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALA 1322
Cdd:TIGR02169 701 --ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1323 HALQKAQRdcDLLREQYEEEQevkaelhRTLSKVNAEMVQWRmkyennviQRTEDLEDAKKELAIRLQEAAEAMGVANAR 1402
Cdd:TIGR02169 779 EALNDLEA--RLSHSRIPEIQ-------AELSKLEEEVSRIE--------ARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1403 NASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEE 1482
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1483 SIVGQETLRRENKnlqeEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQvTLEETEGALERNESKILHFQLELLEAKA 1562
Cdd:TIGR02169 922 LKAKLEALEEELS----EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIR-ALEPVNMLAIQEYEEVLKRLDELKEKRA 996
|
810
....*....|....*....
gi 1981090065 1563 ELERKLSEKDEEIENFRRK 1581
Cdd:TIGR02169 997 KLEEERKAILERIEEYEKK 1015
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
833-1397 |
1.32e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 833 KSSEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVK 912
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 913 ELSERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQ 992
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 993 EAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEEL 1072
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1073 RKKELELSQMNSKVENEKGLVAQLQktvkELQTQIKDLKEKLEAERTTRAkMERERADLTQDLADLNERLEEVGGSSLAQ 1152
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYE----GFLEGVKAALLLAGLRGLAGA-VAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1153 LEITKKQETKFQKLHRDmEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVeqmTR 1232
Cdd:COG1196 555 DDEVAAAAIEYLKAAKA-GRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV---AA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1233 AKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKlwsESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLE 1312
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE---LLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1313 KETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEmvqwrmkyennVIQRTEDLEDAKKELAiRLQEA 1392
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE-----------ELPEPPDLEELERELE-RLERE 775
|
....*
gi 1981090065 1393 AEAMG 1397
Cdd:COG1196 776 IEALG 780
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1187-1812 |
1.52e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1187 RHADSLAELEGQVENLQ-QVKQ-------KLEKDKSDLQL---EVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKL 1255
Cdd:COG1196 190 RLEDILGELERQLEPLErQAEKaeryrelKEELKELEAELlllKLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1256 DKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLL 1335
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1336 REQYEEEQEVKAELHRTLSKVNAEMVQWrmkyennviqrtedlEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQL 1415
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEA---------------EEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1416 ELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEEsIVGQETLRRENK 1495
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE-LLEELAEAAARL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1496 NLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELERKLSEKDEEI 1575
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGR 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1576 ENFrrkqqctidslqssldsEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEAtkslGQLQIQIKDLQMQLDDSTQL 1655
Cdd:COG1196 574 ATF-----------------LPLDKIRARAALAAALARGAIGAAVDLVASDLREAD----ARYYVLGDTLLGRTLVAARL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1656 NSDLKEQVAVAERRNSLLQsELEDLRSLQEQTERGRRLSEEELLEATERInlfytqntsllSQKKKLEADVARMQKEAEE 1735
Cdd:COG1196 633 EAALRRAVTLAGRLREVTL-EGEGGSAGGSLTGGSRRELLAALLEAEAEL-----------EELAERLAEEELELEEALL 700
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981090065 1736 VVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQIQKLESRVR 1812
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
836-1446 |
2.27e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 88.96 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 836 EVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEwlikskiQLEARVKELS 915
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE-------SLEAELEELE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 916 ERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRaakvvqEAH 995
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL------KEL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 996 QQTLDDLHMEEEKLSslsKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKK 1075
Cdd:TIGR02168 439 QAELEELEEELEELQ---EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1076 E-------LELSQMNSKVENEKGLVAQLQKT-----VKELQTQIKD---LKE-----------------KLEAERTTRAK 1123
Cdd:TIGR02168 516 SglsgilgVLSELISVDEGYEAAIEAALGGRlqavvVENLNAAKKAiafLKQnelgrvtflpldsikgtEIQGNDREILK 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1124 MERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKFQKLHRDMEEATL-----------------HFETTSASLKK 1186
Cdd:TIGR02168 596 NIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIvtldgdlvrpggvitggSAKTNSSILER 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1187 R-----HADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLC-------------------- 1241
Cdd:TIGR02168 676 RreieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLarleaeveqleeriaqlske 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1242 --------TLYEERLHEATAKLD-----------KVTQLANDLAAQKTKLWSESGEFLR---RLEEKEALINQLSREKSN 1299
Cdd:TIGR02168 756 lteleaeiEELEERLEEAEEELAeaeaeieeleaQIEQLKEELKALREALDELRAELTLlneEAANLRERLESLERRIAA 835
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1300 FTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQwRMKYENNVIQRTEDLE 1379
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE-LSEELRELESKRSELR 914
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1981090065 1380 DAKKELAIRLQEAAEAMGVANARNASL-ERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALA 1446
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1122-1898 |
4.05e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 88.20 E-value: 4.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1122 AKMERERADLTQDLADLNERLEEVG------GSSLAQLEITKKQETKFQKLHRDMEEATLhfeTTSASLKKRHADSLAEL 1195
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDliidekRQQLERLRREREKAERYQALLKEKREYEG---YELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1196 EGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMtrakanAEKLCTLYEERLHEATAKLDKVTqlandlaAQKTKLWSE 1275
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL------NKKIKDLGEEEQLRVKEKIGELE-------AEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1276 SGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSK 1355
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1356 VNAEMVQwrMKYENNVIQRTED-LEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQLELgdalsdlgkvrsaaARL 1434
Cdd:TIGR02169 390 YREKLEK--LKREINELKRELDrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI--------------KKQ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1435 DQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKn 1514
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1515 lTEMEKVKKLIEEEKTEVQVTLEETEG--------ALERNESKILHFQLELLEAKAELERKLSEK------------DEE 1574
Cdd:TIGR02169 533 -VGERYATAIEVAAGNRLNNVVVEDDAvakeaielLKRRKAGRATFLPLNKMRDERRDLSILSEDgvigfavdlvefDPK 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1575 IEN-FRRKQQCTI--DSLQS-----------SLDSE--------------AKSRIEVTRLKK----KMEEDLNEMELQLS 1622
Cdd:TIGR02169 612 YEPaFKYVFGDTLvvEDIEAarrlmgkyrmvTLEGElfeksgamtggsraPRGGILFSRSEPaelqRLRERLEGLKRELS 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1623 CANRQVSEATKSLGQLQIQIKDLQMQLddstqlnSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEAT 1702
Cdd:TIGR02169 692 SLQSELRRIENRLDELSQELSDASRKI-------GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1703 ERINLFYTQNTSLLSQKKKLEADVArmQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTI 1782
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1783 TDLQKRLAEAEQmALMGSRKQIQKLESRVrelegelegeirrsAEAQRGARRLERCIKELtyqaeedKKNLSRMQTQMDK 1862
Cdd:TIGR02169 843 IDLKEQIKSIEK-EIENLNGKKEELEEEL--------------EELEAALRDLESRLGDL-------KKERDELEAQLRE 900
|
810 820 830
....*....|....*....|....*....|....*.
gi 1981090065 1863 LQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEV 1898
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1286-1925 |
7.74e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.42 E-value: 7.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1286 KEALiNQLSREKSNFTRqIEDLRGQLEKETKSQSALAHALQKAQRdcdlLREQYEEEQ---------EVKAELHRTLSKV 1356
Cdd:TIGR02168 175 KETE-RKLERTRENLDR-LEDILNELERQLKSLERQAEKAERYKE----LKAELRELElallvlrleELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1357 NaEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQL---ELGDALSDLGKVRSAAAR 1433
Cdd:TIGR02168 249 K-EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIlreRLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1434 LDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTK 1513
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1514 NLTEMEK------------VKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELERKLSEKDEEIENFRRK 1581
Cdd:TIGR02168 408 RLERLEDrrerlqqeieelLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1582 QQcTIDSLQS---------------------------------SLDSEAKSRIEV------------------------- 1603
Cdd:TIGR02168 488 QA-RLDSLERlqenlegfsegvkallknqsglsgilgvlseliSVDEGYEAAIEAalggrlqavvvenlnaakkaiaflk 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1604 -----------------TRLKKKMEEDLNEMELQLSCANRQVSEATKS-------LGQLQIqIKDLQMQLDDSTQLNSDL 1659
Cdd:TIGR02168 567 qnelgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLrkalsylLGGVLV-VDDLDNALELAKKLRPGY 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1660 K------EQV--------AVAERRNSLL--QSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLE 1723
Cdd:TIGR02168 646 RivtldgDLVrpggvitgGSAKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1724 ADVARMQKEAEEVVQECQNAEEKAKKAAIEAANL-------SEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQmA 1796
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELeaeieelEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-A 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1797 LMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEV 1876
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1981090065 1877 AETQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQE 1925
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1192-1925 |
1.04e-16 |
|
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: 87.05 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1192 LAELEGQVENLQQVKQKLEKDKsDLQLEVDD-----LLTRVEQMTRAKANAEKlctlyeeRLHEATAKLDKVTQLANDLA 1266
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQ-ALLKEKREyegyeLLKEKEALERQKEAIER-------QLASLEEELEKLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1267 AqktklwsESGEFLRRLEEKEALINQLSREKSN-FTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEV 1345
Cdd:TIGR02169 265 K-------RLEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1346 KAELHRTLSKVNAEMVQWrmkyennvIQRTEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQLELGDALSDLG 1425
Cdd:TIGR02169 338 IEELEREIEEERKRRDKL--------TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1426 KVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELlklkntyEESIVGQETLRRENKNLQEEISNLT 1505
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL-------EQLAADLSKYEQELYDLKEEYDRVE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1506 NQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEEtegaLERNESKILHFQLELLEAKAELERKLsekdeEIENFRRKQQCT 1585
Cdd:TIGR02169 483 KELSKLQRELAEAEAQARASEERVRGGRAVEEV----LKASIQGVHGTVAQLGSVGERYATAI-----EVAAGNRLNNVV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1586 IDSlqsslDSEAKSRIEVTRLKK----------KMEE------------------DLNEMELQLSCANRQVSEATKSLGQ 1637
Cdd:TIGR02169 554 VED-----DAVAKEAIELLKRRKagratflplnKMRDerrdlsilsedgvigfavDLVEFDPKYEPAFKYVFGDTLVVED 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1638 LQIQiKDLQMQLDDSTqLNSDLKEQV------AVAERRNSLLQ-SELEDLRSLQEQTERGRRLSEEELLEATERINLFYt 1710
Cdd:TIGR02169 629 IEAA-RRLMGKYRMVT-LEGELFEKSgamtggSRAPRGGILFSrSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD- 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1711 qntSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLA 1790
Cdd:TIGR02169 706 ---ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1791 EAEQMALMGSRKQIQKLESRVRelegelegEIRRSAEAQrgARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNY 1870
Cdd:TIGR02169 783 DLEARLSHSRIPEIQAELSKLE--------EEVSRIEAR--LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1981090065 1871 KQQVEVAETQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQE 1925
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1115-1739 |
1.07e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.53 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1115 EAERttraKMERERADLTQdladLNERLEEVGgSSLAQLEITKKQETKFQKL-----HRDMEEATLHFETTSASLKK--- 1186
Cdd:COG1196 176 EAER----KLEATEENLER----LEDILGELE-RQLEPLERQAEKAERYRELkeelkELEAELLLLKLRELEAELEElea 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1187 ---RHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLAN 1263
Cdd:COG1196 247 eleELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1264 DLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQ 1343
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1344 EVKAELHRTLSKVNAEMVQWRMKyENNVIQRTEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQLELGDALSD 1423
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEA-LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1424 LGKVRSAAARLDQKQLQSGKALADWKQKHEESQ------------------------ALLDASQKEVQALSTELLKLKNT 1479
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGlrglagavavligveaayeaaleaALAAALQNIVVEDDEVAAAAIEY 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1480 YEESIVGQETLRRENK-NLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELL 1558
Cdd:COG1196 566 LKAAKAGRATFLPLDKiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1559 EAKAELERKLSEKDEEIENFRRKQQctidslQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQL 1638
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRREL------LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1639 QIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQ-SELEDLRSLQEQTERGRR----------LSEEELLEATERINL 1707
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEElPEPPDLEELERELERLEReiealgpvnlLAIEEYEELEERYDF 799
|
650 660 670
....*....|....*....|....*....|..
gi 1981090065 1708 FYTQNTSLLSQKKKLEADVARMQKEAEEVVQE 1739
Cdd:COG1196 800 LSEQREDLEEARETLEEAIEEIDRETRERFLE 831
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1054-1704 |
5.63e-16 |
|
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: 84.00 E-value: 5.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1054 NRESMENLESSQRHLAEELRK----KELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERa 1129
Cdd:pfam05483 72 NSEGLSRLYSKLYKEAEKIKKwkvsIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEN- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1130 DLTQDLADLNERLEEVGGSSLAQLEITKKQETK-FQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQK 1208
Cdd:pfam05483 151 NATRHLCNLLKETCARSAEKTKKYEYEREETRQvYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1209 LEKDKSDLQLEVDDLLTrveQMTRAKANAEKLCTLYEErlheataKLDKVTQLandlaAQKTKLWSESgeflrrleekea 1288
Cdd:pfam05483 231 YKKEINDKEKQVSLLLI---QITEKENKMKDLTFLLEE-------SRDKANQL-----EEKTKLQDEN------------ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1289 lINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYE 1368
Cdd:pfam05483 284 -LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1369 N---NVIQRTEDLEDAKKELAIRLQEAAEAMgvanarnASLERARHQLQLElgdaLSDLGKVRSAAARLDQKQLQSGKAL 1445
Cdd:pfam05483 363 EllrTEQQRLEKNEDQLKIITMELQKKSSEL-------EEMTKFKNNKEVE----LEELKKILAEDEKLLDEKKQFEKIA 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1446 ADWKQKHEESQALLDASQKEVQALSTELLKLKNTyeesivgQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLI 1525
Cdd:pfam05483 432 EELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS-------EEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1526 EEEKTEVQVTLEETEGALERNESKilhfQLELLEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTR 1605
Cdd:pfam05483 505 TQEASDMTLELKKHQEDIINCKKQ----EERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEY 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1606 LKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQ-LDDSTQLNSdLKEQVAVAERRNSLLQSELEDLRSLQ 1684
Cdd:pfam05483 581 EVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKgSAENKQLNA-YEIKVNKLELELASAKQKFEEIIDNY 659
|
650 660
....*....|....*....|
gi 1981090065 1685 EQTERGRRLSEEELLEATER 1704
Cdd:pfam05483 660 QKEIEDKKISEEKLLEEVEK 679
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1286-1918 |
1.99e-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: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1286 KEALiNQLSREKSNFTRqIEDLRGQLEK----------------------ETKSQSALAHALQKAQRDCDLLREQYEEEQ 1343
Cdd:COG1196 175 EEAE-RKLEATEENLER-LEDILGELERqleplerqaekaeryrelkeelKELEAELLLLKLRELEAELEELEAELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1344 EVKAELHRTLSKVNAEMvqwrmkyennviqrtEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQLELGDALSD 1423
Cdd:COG1196 253 AELEELEAELAELEAEL---------------EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1424 LGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISN 1503
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1504 LTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELERKLSEKDEEIENFRRKQQ 1583
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1584 CTIDSLQSSLDSEAKsrievtrlkkkmEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQV 1663
Cdd:COG1196 478 ALAELLEELAEAAAR------------LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1664 AVAERRNSLLQSELEDLRSLQEQTERGR----RLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQE 1739
Cdd:COG1196 546 AALQNIVVEDDEVAAAAIEYLKAAKAGRatflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1740 CQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMALmgSRKQIQKLESRVRELEGELE 1819
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE--LAERLAEEELELEEALLAEE 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1820 GEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSKYKKQ-------- 1891
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREiealgpvn 783
|
650 660 670
....*....|....*....|....*....|
gi 1981090065 1892 ---QHELNEVKERAEVAESQVNKLKiKARE 1918
Cdd:COG1196 784 llaIEEYEELEERYDFLSEQREDLE-EARE 812
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1453-1926 |
4.50e-15 |
|
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: 81.37 E-value: 4.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1453 EESQALLDASQKEVQALSTELLKLKNTYEESIVGqetLRRENKNLQEEISNLTNQV--REGTKNLTEMEKVKKLIEEEKT 1530
Cdd:pfam01576 60 EEMRARLAARKQELEEILHELESRLEEEEERSQQ---LQNEKKKMQQHIQDLEEQLdeEEAARQKLQLEKVTTEAKIKKL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1531 EVQVTLEETEGALERNESKILHfqlellEAKAELERKLSEKDEEIENF---RRKQQCTIDSLQSSLDSEAKSRIEVTRLK 1607
Cdd:pfam01576 137 EEDILLLEDQNSKLSKERKLLE------ERISEFTSNLAEEEEKAKSLsklKNKHEAMISDLEERLKKEEKGRQELEKAK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1608 KKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQT 1687
Cdd:pfam01576 211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1688 ERGRRLSEEELlEATeRINLFYTQNTSLLSQ--KKKLEADVARMQK--EAEEVVQECQnAEEKAKKAAIEAANLSEELKK 1763
Cdd:pfam01576 291 EKQRRDLGEEL-EAL-KTELEDTLDTTAAQQelRSKREQEVTELKKalEEETRSHEAQ-LQEMRQKHTQALEELTEQLEQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1764 KQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQiQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELT 1843
Cdd:pfam01576 368 AKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKR-KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVS 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1844 YQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEvAETQANQYLSKYKKQ--------QHELNEVKERAEVAESQVNKLKIK 1915
Cdd:pfam01576 447 SLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ-EETRQKLNLSTRLRQledernslQEQLEEEEEAKRNVERQLSTLQAQ 525
|
490
....*....|.
gi 1981090065 1916 AREFGKKVQEE 1926
Cdd:pfam01576 526 LSDMKKKLEED 536
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
838-1742 |
9.99e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 80.48 E-value: 9.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 838 GEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKnDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSER 917
Cdd:TIGR00606 199 GQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 918 VEEEEEINSELTargRKLEDECFELKKEIDDLETMlvkSEKEKRTTEHKVKNLTEEVEFLNEDISKLN--RAAKVVQEAH 995
Cdd:TIGR00606 278 KKQMEKDNSELE---LKMEKVFQGTDEQLNDLYHN---HQRTVREKERELVDCQRELEKLNKERRLLNqeKTELLVEQGR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 996 QQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKK 1075
Cdd:TIGR00606 352 LQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEI 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1076 ELELSQMNSKVENEKglvAQLQKTVKELQTQIKDLKeklEAERTTRAKMERERAdLTQDLADLNERLEEvggsslAQLEI 1155
Cdd:TIGR00606 432 RDEKKGLGRTIELKK---EILEKKQEELKFVIKELQ---QLEGSSDRILELDQE-LRKAERELSKAEKN------SLTET 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1156 TKKQETKFQKLHRDMEEaTLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLL---TRVEQMTR 1232
Cdd:TIGR00606 499 LKKEVKSLQNEKADLDR-KLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLgyfPNKKQLED 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1233 AKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSEsgefLRRLEEKeaLINQLSREksNFTRQIEDLRGQLE 1312
Cdd:TIGR00606 578 WLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQ----LSSYEDK--LFDVCGSQ--DEESDLERLKEEIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1313 KETKSQSALAHALQKAqrdcDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEA 1392
Cdd:TIGR00606 650 KSSKQRAMLAGATAVY----SQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRR 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1393 AEAMGVANARNASLERarhqLQLELGDALSDLGKVRSAAARLdQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTE 1472
Cdd:TIGR00606 726 DEMLGLAPGRQSIIDL----KEKEIPELRNKLQKVNRDIQRL-KNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQME 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1473 LLKLKNTYEE------SIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQvTLEETEGALERN 1546
Cdd:TIGR00606 801 LKDVERKIAQqaaklqGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTN-ELKSEKLQIGTN 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1547 ESKILHFQLELLEAKAELE---RKLSEKDEEI---ENFRRKQQCTIDSLQSSLDSEAK-SRIEVTRLKKKM--------- 1610
Cdd:TIGR00606 880 LQRRQQFEEQLVELSTEVQsliREIKDAKEQDsplETFLEKDQQEKEELISSKETSNKkAQDKVNDIKEKVknihgymkd 959
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1611 ---------EEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLR 1681
Cdd:TIGR00606 960 ienkiqdgkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQ 1039
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1981090065 1682 SLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEvvQECQN 1742
Cdd:TIGR00606 1040 HLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE--PQFRD 1098
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
844-1540 |
2.35e-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: 79.01 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 844 LKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIK-SKIQLEARVKELSERVEEEE 922
Cdd:pfam15921 108 LRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEdSNTQIEQLRKMMLSHEGVLQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 923 EINSELT----ARGRKLEDEcfelkkeiDDLETMLVKSEKEkrTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQT 998
Cdd:pfam15921 188 EIRSILVdfeeASGKKIYEH--------DSMSTMHFRSLGS--AISKILRELDTEISYLKGRIFPVEDQLEALKSESQNK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 999 LDDLhmeeeklssLSKANLKLEQQVDELE----GALEQERKARmnceRELHKLEGNLKLNRESMENLESS-QRHLAEelr 1073
Cdd:pfam15921 258 IELL---------LQQHQDRIEQLISEHEveitGLTEKASSAR----SQANSIQSQLEIIQEQARNQNSMyMRQLSD--- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1074 kKELELSQMNSKVENEKGLvaqLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDL----ADLNERLEEvggss 1149
Cdd:pfam15921 322 -LESTVSQLRSELREAKRM---YEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLqkllADLHKREKE----- 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1150 laqLEITKKQETKF-----------QKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKS-DLQ 1217
Cdd:pfam15921 393 ---LSLEKEQNKRLwdrdtgnsitiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSlTAQ 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1218 LEVDDLLTR--VEQMTRAKANAEK-------LCTLYEERLHEATAKLDKVTQLAN--DLAAQKTKLWSESGEFLRRLE-E 1285
Cdd:pfam15921 470 LESTKEMLRkvVEELTAKKMTLESsertvsdLTASLQEKERAIEATNAEITKLRSrvDLKLQELQHLKNEGDHLRNVQtE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1286 KEALINQLSREKsnftRQIEDLRGQLEKETK-----SQSALAHALQKAQRDCDLlREQYEEEQEVKA----------ELH 1350
Cdd:pfam15921 550 CEALKLQMAEKD----KVIEILRQQIENMTQlvgqhGRTAGAMQVEKAQLEKEI-NDRRLELQEFKIlkdkkdakirELE 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1351 RTLSKVNAEMVQW------RMKYENNVIQRTEDLEDAKKELAIRLQEAAEAMGV--ANARNAS--LERARHQLQLELGDA 1420
Cdd:pfam15921 625 ARVSDLELEKVKLvnagseRLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVlkRNFRNKSeeMETTTNKLKMQLKSA 704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1421 LSDLGKVRSAAARLD-------------QKQLQSGKALADWKQKHEE--SQALLDASQK------EVQALSTELLKLKnT 1479
Cdd:pfam15921 705 QSELEQTRNTLKSMEgsdghamkvamgmQKQITAKRGQIDALQSKIQflEEAMTNANKEkhflkeEKNKLSQELSTVA-T 783
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1981090065 1480 YEESIVGQ-ETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEE--KTEVQVTLEETE 1540
Cdd:pfam15921 784 EKNKMAGElEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQEsvRLKLQHTLDVKE 847
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
981-1925 |
3.40e-14 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 78.55 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 981 ISKLNRAAKVVQEaHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKlnreSMEN 1060
Cdd:TIGR00606 185 IKALETLRQVRQT-QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLK----EIEH 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1061 LESSQRHLAEELR---KKELELSQMNSKVEnekglvaqlQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLAD 1137
Cdd:TIGR00606 260 NLSKIMKLDNEIKalkSRKKQMEKDNSELE---------LKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1138 LNERleevggsslAQLEITKKQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGqvenlqqvkqkLEKDkSDLQ 1217
Cdd:TIGR00606 331 LNKE---------RRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDG-----------FERG-PFSE 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1218 LEVDDLLTRV-EQMTRAKANAEKLCTLYEERLHEATAKLDKvtqlandLAAQKTKLWSESGEFLRRLEEKEALINQLSRE 1296
Cdd:TIGR00606 390 RQIKNFHTLViERQEDEAKTAAQLCADLQSKERLKQEQADE-------IRDEKKGLGRTIELKKEILEKKQEELKFVIKE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1297 KSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEeeQEVKAELHRTLSKVNAEMVQwrMKYENNVIQRTE 1376
Cdd:TIGR00606 463 LQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSL--QNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQME 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1377 DLEDAKKE-----LAIRLQEAAEAMGVAN--ARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWK 1449
Cdd:TIGR00606 539 MLTKDKMDkdeqiRKIKSRHSDELTSLLGyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKE 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1450 QKH-------------EESQALLDASQKEVQALSTELLKL--KNTYEESIVGQETLRREN------------KNLQEEIS 1502
Cdd:TIGR00606 619 EQLssyedklfdvcgsQDEESDLERLKEEIEKSSKQRAMLagATAVYSQFITQLTDENQSccpvcqrvfqteAELQEFIS 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1503 NLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILhfqlELLEAKAELERKLSEKDEEIEnfrrKQ 1582
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP----ELRNKLQKVNRDIQRLKNDIE----EQ 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1583 QCTIDSLQSSLDSEAKSRIEVTRLKK-KMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKE 1661
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERfQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1662 QVAVAERRNSLLQSELEDLRS--LQEQTERGRRLS-EEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQ 1738
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNELKSekLQIGTNLQRRQQfEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1739 ECQnaeekakkaaieaanlsEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQIQKLESRVRELEgel 1818
Cdd:TIGR00606 931 SKE-----------------TSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECE--- 990
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1819 egeiRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEV 1898
Cdd:TIGR00606 991 ----KHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLI 1066
|
970 980
....*....|....*....|....*..
gi 1981090065 1899 KERAEVAESQVNKLKIKAREFGKKVQE 1925
Cdd:TIGR00606 1067 KRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
937-1436 |
4.43e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.16 E-value: 4.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 937 DECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLnraakvvqeahqqtLDDLHMEEEKLSSLskan 1016
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL--------------LAEAGLDDADAEAV---- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1017 lklEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSqrhlAEELRKKELELsqmNSKVENEKGLVAQL 1096
Cdd:PRK02224 313 ---EARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER----AEELREEAAEL---ESELEEAREAVEDR 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1097 QKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVggsslaqleitkkqETKFQKLHRDMEEATLH 1176
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL--------------EATLRTARERVEEAEAL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1177 FE-----TTSASLKKR-HADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLyEERLHE 1250
Cdd:PRK02224 449 LEagkcpECGQPVEGSpHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDL-EELIAE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1251 ATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDL---RGQLEKETKSQSALAHALQK 1327
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELkerIESLERIRTLLAAIADAEDE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1328 AQRdcdlLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNviqRTEDLEDAKKELAIRLQEAAEAMgvanarnASLE 1407
Cdd:PRK02224 608 IER----LREKREALAELNDERRERLAEKRERKRELEAEFDEA---RIEEAREDKERAEEYLEQVEEKL-------DELR 673
|
490 500
....*....|....*....|....*....
gi 1981090065 1408 RARHQLQLELGDALSDLGKVRSAAARLDQ 1436
Cdd:PRK02224 674 EERDDLQAEIGAVENELEELEELRERREA 702
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
931-1790 |
6.98e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.87 E-value: 6.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 931 RGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQtlDDLHMEEEKLS 1010
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKA--EDARKAEEARK 1147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1011 SLSKANLKLEQQVDELEGAlEQERKARmncerELHKLEGNlklnRESMENLESSQRHLAEELRKKElELSQMNSKVENEK 1090
Cdd:PTZ00121 1148 AEDAKRVEIARKAEDARKA-EEARKAE-----DAKKAEAA----RKAEEVRKAEELRKAEDARKAE-AARKAEEERKAEE 1216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1091 GLVAQLQKTVKELQtQIKDLKEKleAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQlEITKKQETKFQKLHRDM 1170
Cdd:PTZ00121 1217 ARKAEDAKKAEAVK-KAEEAKKD--AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE-EARKADELKKAEEKKKA 1292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1171 EEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLE--KDKSDLQLEVDDLLTRVEQMTRAKAN-AEKLCTLYEER 1247
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADaaKKKAEEAKKAAEAAKAEAEAAADEAEaAEEKAEAAEKK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1248 LHEATAKLDKVTQLAN-----DLAAQKTKLWSESGEFLRRLEEKEALINQLsREKSNFTRQIEDLRGQLEKETKSQSALA 1322
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEekkkaDEAKKKAEEDKKKADELKKAAAAKKKADEA-KKKAEEKKKADEAKKKAEEAKKADEAKK 1451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1323 HALQKaqRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKElAIRLQEAAEAMGVANAR 1402
Cdd:PTZ00121 1452 KAEEA--KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK-ADEAKKAEEAKKADEAK 1528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1403 NAS----LERARHQLQLELGDALSDLGKVRSAAARldQKQLQSGKALAD---WKQKHEESQALLDASQKEVQALSTELLK 1475
Cdd:PTZ00121 1529 KAEeakkADEAKKAEEKKKADELKKAEELKKAEEK--KKAEEAKKAEEDknmALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1476 LK----NTYEESIVGQETLRREnknlQEEISNLTNQVREGTKNLTEMEKVKKliEEEKTEVQVTLEETEGALERNESKIL 1551
Cdd:PTZ00121 1607 MKaeeaKKAEEAKIKAEELKKA----EEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1552 HFQLELLEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDlnemelqlscaNRQVSEA 1631
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED-----------KKKAEEA 1749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1632 TKSLGQlqiQIKDLQMQLDDSTQLNSDLKEQVAVAERRnslLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQ 1711
Cdd:PTZ00121 1750 KKDEEE---KKKIAHLKKEEEKKAEEIRKEKEAVIEEE---LDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVIND 1823
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1712 NTSLLSQKKKLEADVARMQK-EAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLA 1790
Cdd:PTZ00121 1824 SKEMEDSAIKEVADSKNMQLeEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIP 1903
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
968-1860 |
9.76e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 77.32 E-value: 9.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 968 KNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKAnlklEQQVDELEGALEQERKARMNCERELHKL 1047
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLK----EQAKKALEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1048 egnLKLNRESMENLEssqrhlaEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERE 1127
Cdd:pfam02463 232 ---LKLNEERIDLLQ-------ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1128 RADLTQDLADLNERLEEvggsslAQLEITKKQEtkfqklhrdmeeatlhfettsaslkkrhadSLAELEGQVENLQQVKQ 1207
Cdd:pfam02463 302 LLKLERRKVDDEEKLKE------SEKEKKKAEK------------------------------ELKKEKEEIEELEKELK 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1208 KLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTklwSESGEFLRRLEEKE 1287
Cdd:pfam02463 346 ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ---LLLELARQLEDLLK 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1288 ALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTL----SKVNAEMVQW 1363
Cdd:pfam02463 423 EEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELllsrQKLEERSQKE 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1364 RMKYENN------VIQRTEDLEDAKKELAIRLQEAAEAMGVANarNASLERARHQLQLELGDALSDLGKVRSAAARLDQK 1437
Cdd:pfam02463 503 SKARSGLkvllalIKDGVGGRIISAHGRLGDLGVAVENYKVAI--STAVIVEVSATADEVEERQKLVRALTELPLGARKL 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1438 QLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKN-----TYEESIVGQETLRRENKNLQEEISNLTNQVREGT 1512
Cdd:pfam02463 581 RLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRakvveGILKDTELTKLKESAKAKESGLRKGVSLEEGLAE 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1513 KNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSS 1592
Cdd:pfam02463 661 KSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKL 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1593 LDSEAKSRIEV---TRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERR 1669
Cdd:pfam02463 741 LKQKIDEEEEEeekSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEE 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1670 NSLLQSELEDLRSLQEQ-------TERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQN 1742
Cdd:pfam02463 821 QLLIEQEEKIKEEELEElalelkeEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKK 900
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1743 AEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQIQKLESRVRELEGELEGEI 1822
Cdd:pfam02463 901 ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAI 980
|
890 900 910
....*....|....*....|....*....|....*...
gi 1981090065 1823 RRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQM 1860
Cdd:pfam02463 981 EEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQR 1018
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1022-1705 |
2.89e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.49 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1022 QVDELEGALEQERKARMNCERELHKLEGNLKlnreSMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVK 1101
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIK----RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1102 ELqtqiKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVggsslaqleitKKQETKFQKLHRDMEEAtlhfetts 1181
Cdd:PRK03918 232 EL----EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL-----------KKEIEELEEKVKELKEL-------- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1182 aslkKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEE------RLHEATAKL 1255
Cdd:PRK03918 289 ----KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekrleELEERHELY 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1256 DKVTQLANDLAAQKTKLWSESgeflrrLEEKEALINQLSREKSNFTRQIEDL---RGQLEKETKSQSALAHALQKAQRDC 1332
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLT------PEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAKGKC 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1333 DLLREQYEEEQ--EVKAELHRTLSKVNAEMvqwrmkyennvIQRTEDLEDAKKELairlqeaaeamgvanaRNASLERAR 1410
Cdd:PRK03918 439 PVCGRELTEEHrkELLEEYTAELKRIEKEL-----------KEIEEKERKLRKEL----------------RELEKVLKK 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1411 HQLQLELGDALSDLGKVRSAAARLDQKQLQsgkalADWKqKHEESQALLDASQKEVQALSTELLKLKNTYEESivgqETL 1490
Cdd:PRK03918 492 ESELIKLKELAEQLKELEEKLKKYNLEELE-----KKAE-EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL----AEL 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1491 RRENKNLQEEISNLTNQVRE-GTKNLTEMEKVKKLIEEEKTEVqVTLEETEGALERNESKILHFQLELLEAKAELErkls 1569
Cdd:PRK03918 562 EKKLDELEEELAELLKELEElGFESVEELEERLKELEPFYNEY-LELKDAEKELEREEKELKKLEEELDKAFEELA---- 636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1570 EKDEEIENFRRKqqctIDSLQSSLDSEAKSRIEVTRLKKKMEedLNEMELQLSCANRQVSEATKSLGQLQIQikdlqmql 1649
Cdd:PRK03918 637 ETEKRLEELRKE----LEELEKKYSEEEYEELREEYLELSRE--LAGLRAELEELEKRREEIKKTLEKLKEE-------- 702
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1981090065 1650 ddstqlnsdlKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERI 1705
Cdd:PRK03918 703 ----------LEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1196-1925 |
3.02e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.56 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1196 EGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMT--RAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKlw 1273
Cdd:PTZ00121 1057 EGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEAteEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEAR-- 1134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1274 seSGEFLRRLEEKEALINQlsrEKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQ--RDCDLLREQYEE---EQEVKAE 1348
Cdd:PTZ00121 1135 --KAEDARKAEEARKAEDA---KRVEIARKAEDARKAEEARKAEDAKKAEAARKAEevRKAEELRKAEDArkaEAARKAE 1209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1349 LHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEaaEAMGVANARNASLERARHQLQLELGDALSDLGKVR 1428
Cdd:PTZ00121 1210 EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE--EIRKFEEARMAHFARRQAAIKAEEARKADELKKAE 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1429 SAAARLDQKQLQSGKALADWKQKHEESQALlDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNlTNQV 1508
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA-AEEK 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1509 REGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKIlhfqlELLEAKAELERKLSEKDEEIENFRRKQQCTIDS 1588
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA-----DELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1589 LQSSLDSEAKSRIEVTR----LKKKMEEDLNEMELQLSCAN-RQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLK--E 1661
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKkaeeAKKKAEEAKKADEAKKKAEEaKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaeE 1520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1662 QVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERinlfytqntSLLSQKKKLEADVARMQKEAEEVVQ-EC 1740
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEK---------KKAEEAKKAEEDKNMALRKAEEAKKaEE 1591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1741 QNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQIQKLESRVRELEGELEG 1820
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1821 EIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQylskYKKQQHELNEVKE 1900
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE----AKKEAEEDKKKAE 1747
|
730 740
....*....|....*....|....*
gi 1981090065 1901 RAEVAESQVNKLKIKAREFGKKVQE 1925
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1527-1842 |
3.04e-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: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1527 EEKTEVQVTLEETEGALERNESKI--LHFQLELLEAKAELERKLSEKDEEIENFRrkqqctIDSLQSSLDSEAKSRIEVT 1604
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILneLERQLKSLERQAEKAERYKELKAELRELE------LALLVLRLEELREELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1605 RLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQ 1684
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1685 EQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKK 1764
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1765 QDTIAHLERTRENMEQTITDLQKRLAEAE----QMALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIK 1840
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAElkelQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
..
gi 1981090065 1841 EL 1842
Cdd:TIGR02168 486 QL 487
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
845-1734 |
4.14e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 75.01 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 845 KEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQL-QAEQETLANVEEqcewliksKIQLEARVKelserveeeee 923
Cdd:pfam02463 221 LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEiEKEEEKLAQVLK--------ENKEEEKEK----------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 924 inSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDdlh 1003
Cdd:pfam02463 282 --KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE--- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1004 mEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMN 1083
Cdd:pfam02463 357 -EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1084 SKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKF 1163
Cdd:pfam02463 436 EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLAL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1164 QKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEV--DDLLTRVEQMTRAKANAEKLC 1241
Cdd:pfam02463 516 IKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTElpLGARKLRLLIPKLKLPLKSIA 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1242 TLYEERLHEATAKldkvtQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSAL 1321
Cdd:pfam02463 596 VLEIDPILNLAQL-----DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSE 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1322 AHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYEnnviQRTEDLEDAKKELAIRLQEaaeamgvaNA 1401
Cdd:pfam02463 671 LTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL----EAEELLADRVQEAQDKINE--------EL 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1402 RNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYE 1481
Cdd:pfam02463 739 KLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1482 ESIvgqetlrrENKNLQEEISNLTNQvrEGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAK 1561
Cdd:pfam02463 819 EEQ--------LLIEQEEKIKEEELE--ELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDEL 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1562 AELERKLSEKDEEIENFRRkqqctIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELqLSCANRQVSEATKSLGQLQIQ 1641
Cdd:pfam02463 889 ESKEEKEKEEKKELEEESQ-----KLNLLEEKENEIEERIKEEAEILLKYEEEPEELL-LEEADEKEKEENNKEEEEERN 962
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1642 IKDLQMQLDDSTQLNSDLKEQVAVAERRNsllqSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKK 1721
Cdd:pfam02463 963 KRLLLAKEELGKVNLMAIEEFEEKEERYN----KDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFF 1038
|
890
....*....|...
gi 1981090065 1722 LEADVARMQKEAE 1734
Cdd:pfam02463 1039 YLELGGSAELRLE 1051
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
827-1272 |
1.09e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.56 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 827 KIKPLVKSSEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLqaeqETLANVEEQCEWLIKSKIQ 906
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 907 LEARVKELSERVeeeeeinsELTARGRKLEDECFELKK-----EIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDI 981
Cdd:PRK03918 350 LEKRLEELEERH--------ELYEEAKAKKEELERLKKrltglTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 982 SKLNRAAKVVQEAHQQ--TLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARmnceRELHKLEGNLKLNRESme 1059
Cdd:PRK03918 422 KELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLR----KELRELEKVLKKESEL-- 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1060 nleSSQRHLAEELRKKELELSQMN-SKVENEKGLVAQLQKTVKELQTQIKDLK---EKLEAERTTRAKMERERADLTQDL 1135
Cdd:PRK03918 496 ---IKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKkelEKLEELKKKLAELEKKLDELEEEL 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1136 ADLNERLEEVGGSSLAQLEITKKQETKFQKLHRDMEEATLHFEttsaSLKKRHADSLAELEGQVENLQQVKQKLEKDKSD 1215
Cdd:PRK03918 573 AELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELE----REEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1981090065 1216 L-QLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKL 1272
Cdd:PRK03918 649 LeELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1095-1853 |
1.34e-12 |
|
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: 73.23 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1095 QLQKTVKELQTQIKDLKEKLEAERTTRakmERERADLTQDLADLNERLEEVGGSSLAQLEItKKQETKFQKLHRDMEEAT 1174
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELH---EKQKFYLRQSVIDLQTKLQEMQMERDAMADI-RRRESQSQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1175 LHFETTSASLKKrhaDSLAELEGQVENLQQVKQKLEkdksDLQLEVDDLLTRVEQMTRAKA-NAEKLCTLYEERLHEATA 1253
Cdd:pfam15921 151 VHELEAAKCLKE---DMLEDSNTQIEQLRKMMLSHE----GVLQEIRSILVDFEEASGKKIyEHDSMSTMHFRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1254 KLdkVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNftrQIEDLRGQLEKET-----KSQSALAHAlQKA 1328
Cdd:pfam15921 224 KI--LRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQD---RIEQLISEHEVEItglteKASSARSQA-NSI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1329 QRDCDLLREQYEEEQEVK----AELHRTLSKVNAEMVQWRMKYENNViqrtedlEDAKKELAIRLQEAAEAmgvaNARNA 1404
Cdd:pfam15921 298 QSQLEIIQEQARNQNSMYmrqlSDLESTVSQLRSELREAKRMYEDKI-------EELEKQLVLANSELTEA----RTERD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1405 SLERARHQLQLELGDALSDLGKvRSAAARLDQKQlqsGKALadWKQKHEESQAL------LDASQKEVQALSTELLKLKN 1478
Cdd:pfam15921 367 QFSQESGNLDDQLQKLLADLHK-REKELSLEKEQ---NKRL--WDRDTGNSITIdhlrreLDDRNMEVQRLEALLKAMKS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1479 TYEESIVGQ-ETLRRENKNLqEEISNLTNQV---REGTKNLTEMEKVKKLIEE--EKT--EVQVTLEETEGALERNESKI 1550
Cdd:pfam15921 441 ECQGQMERQmAAIQGKNESL-EKVSSLTAQLestKEMLRKVVEELTAKKMTLEssERTvsDLTASLQEKERAIEATNAEI 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1551 L--------------HFQLE---LLEAKAE---LERKLSEKDEEIENFRRKqqctIDSLQSSLDSEAKSRIEVTRLKKKM 1610
Cdd:pfam15921 520 TklrsrvdlklqelqHLKNEgdhLRNVQTEceaLKLQMAEKDKVIEILRQQ----IENMTQLVGQHGRTAGAMQVEKAQL 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1611 EEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSD-LKEQVAVAERRNSLL------QSELEDLRSL 1683
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSErLRAVKDIKQERDQLLnevktsRNELNSLSED 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1684 QEQTERGRRLSEEELLEATERINLFYTQNTSLLSQK----KKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSE 1759
Cdd:pfam15921 676 YEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTrntlKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEE 755
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1760 ELKKKQDTIAHLERTRENMEQTITDLQkrlAEAEQMA--LMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLER 1837
Cdd:pfam15921 756 AMTNANKEKHFLKEEKNKLSQELSTVA---TEKNKMAgeLEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQ 832
|
810
....*....|....*.
gi 1981090065 1838 CIKELTYQAEEDKKNL 1853
Cdd:pfam15921 833 ESVRLKLQHTLDVKEL 848
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
844-1495 |
2.15e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 72.45 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 844 LKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKskiqlEARVKELSERVEEEEE 923
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLK-----EDHEKIQHLEEEYKKE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 924 INSElTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLH 1003
Cdd:pfam05483 235 INDK-EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1004 MEEEKLSSLSKANLKL----EQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELEL 1079
Cdd:pfam05483 314 ALEEDLQIATKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1080 SQMNSKVENEKGLVAQLQKTVKElqtqikdlKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQ 1159
Cdd:pfam05483 394 EEMTKFKNNKEVELEELKKILAE--------DEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1160 ETKFQKLHRDMEEatlhfETTSASLKKrhadslAELEGQVENLQQVKQKLEKDKSDLQLEvddLLTRVEQMTRAKANAEK 1239
Cdd:pfam05483 466 EEHYLKEVEDLKT-----ELEKEKLKN------IELTAHCDKLLLENKELTQEASDMTLE---LKKHQEDIINCKKQEER 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1240 LctlyeerLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQS 1319
Cdd:pfam05483 532 M-------LKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1320 ALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEAAEAMGVA 1399
Cdd:pfam05483 605 NKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIA 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1400 NARNASLERARHQLQLELGDALSDLGKVRSaaaRLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNT 1479
Cdd:pfam05483 685 DEAVKLQKEIDKRCQHKIAEMVALMEKHKH---QYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQ 761
|
650
....*....|....*.
gi 1981090065 1480 YEESIVGQETLRRENK 1495
Cdd:pfam05483 762 LEIEKEEKEKLKMEAK 777
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
934-1642 |
3.07e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 72.31 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 934 KLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAH--QQTLDDLHMEEEKLSS 1011
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1012 ----LSKANLKLEQQVDELEGALEQER---------------KARMNC-ERELHKLEGNLKLNRESMENLESSQRHLAEE 1071
Cdd:TIGR00618 275 qeavLEETQERINRARKAAPLAAHIKAvtqieqqaqrihtelQSKMRSrAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1072 LRKKELELSQMNSKVENEKGLvaQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERAdlTQDLADLNERLEEVggsSLA 1151
Cdd:TIGR00618 355 IHIRDAHEVATSIREISCQQH--TLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQA--TIDTRTSAFRDLQG---QLA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1152 QLEITKKQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSdlqlevddlltrvEQMT 1231
Cdd:TIGR00618 428 HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKA-------------VVLA 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1232 RAKANAEKLCTLYEERLHeatakldkvtqlandlAAQKTKLWSESGEFLRRLEEKEALINQLSREksnftrqIEDLRGQL 1311
Cdd:TIGR00618 495 RLLELQEEPCPLCGSCIH----------------PNPARQDIDNPGPLTRRMQRGEQTYAQLETS-------EEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1312 EKETKSQSALAHALQKAQRDCDLLREQYeeeQEVKAELHRTLSKVNaEMVQWRMKYENNVIQRTEDL--EDAKKELAIRL 1389
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCD---NRSKEDIPNLQNITV-RLQDLTEKLSEAEDMLACEQhaLLRKLQPEQDL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1390 QEAAEAMGVANARNASLERARHQLQLELgdaLSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQA-----LLDASQK 1464
Cdd:TIGR00618 628 QDVRLHLQQCSQELALKLTALHALQLTL---TQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkeMLAQCQT 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1465 EVQALSTELLKLKNTYEE----SIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETE 1540
Cdd:TIGR00618 705 LLRELETHIEEYDREFNEienaSSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLA 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1541 GALERNESKILHFQLELLEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMElQ 1620
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA-Q 863
|
730 740
....*....|....*....|....*
gi 1981090065 1621 LSCANRQVSEATKSLG---QLQIQI 1642
Cdd:TIGR00618 864 LTQEQAKIIQLSDKLNginQIKIQF 888
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1017-1575 |
3.08e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1017 LKLEQQVDELEGALEQERKARmncERELHKLEGNLKLNRESMENLESSQRHL---AEELRKKELELSQMNSKVENEKGLV 1093
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEV---LREINEISSELPELREELEKLEKEVKELeelKEEIEELEKELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1094 AQLQKTVKELQTQIKDLKEK--------------------LEAERTTRAKMERERADLTQDLADLNERLEEvGGSSLAQL 1153
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKvkelkelkekaeeyiklsefYEEYLDELREIEKRLSRLEEEINGIEERIKE-LEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1154 EITKKQETKFQKLHRDMEEATLHFETTSA------SLKKRHAD-SLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTR 1226
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEAKAkkeeleRLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1227 VEQMTRAKA---NAEKLCTLYEERLHEATAK--LDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNft 1301
Cdd:PRK03918 421 IKELKKAIEelkKAKGKCPVCGRELTEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL-- 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1302 RQIEDLRGQLEKETKSqsalaHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNaemvqwrmkyennviqRTEDLEDA 1381
Cdd:PRK03918 499 KELAEQLKELEEKLKK-----YNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE----------------KLEELKKK 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1382 KKELAIRLQEAAEAMGVANAR-----NASLERARHQLQlELGDALSDLGKVRSAAARLDQKQlqsgKALADWKQKHEESQ 1456
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKEleelgFESVEELEERLK-ELEPFYNEYLELKDAEKELEREE----KELKKLEEELDKAF 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1457 ALLDASQKEVQALSTELLKLKNTYEESivGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTL 1536
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYSEE--EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK 710
|
570 580 590
....*....|....*....|....*....|....*....
gi 1981090065 1537 EETEgALERNESKILHFQLELLEAKAELERKLSEKDEEI 1575
Cdd:PRK03918 711 KELE-KLEKALERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
954-1587 |
3.61e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.10 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 954 VKSEKEKRTTEHKVKnlTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQE 1033
Cdd:PTZ00121 1289 KKKADEAKKAEEKKK--ADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1034 RKARMNCERELHKLEGNLKLNRESMENLESSQRhlAEELRKK--ELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLK 1111
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK--AEEDKKKadELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1112 EKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKFQKLH--RDMEEATLHFETTSASLKKRHA 1189
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADeaKKAAEAKKKADEAKKAEEAKKA 1524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1190 DSL--AELEGQVENLQQV--KQKLEKDKSDLQLEVDDLLTRVEQMTRAKAN-------AEKLCTLYEERLHEATaKLDKV 1258
Cdd:PTZ00121 1525 DEAkkAEEAKKADEAKKAeeKKKADELKKAEELKKAEEKKKAEEAKKAEEDknmalrkAEEAKKAEEARIEEVM-KLYEE 1603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1259 TQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREq 1338
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK- 1682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1339 yEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEAA-----EAMGVANARNASLERAR-HQ 1412
Cdd:PTZ00121 1683 -AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKkeaeeDKKKAEEAKKDEEEKKKiAH 1761
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1413 LQLELGDALSDLGKVRSAAAR--LDQK----QLQSGKALADWKQKHE--------------ESQALLDASQKEVQALSTE 1472
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEeeLDEEdekrRMEVDKKIKDIFDNFAniieggkegnlvinDSKEMEDSAIKEVADSKNM 1841
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1473 LLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEktevqVTLEETEGALERNESKILH 1552
Cdd:PTZ00121 1842 QLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDD-----IEREIPNNNMAGKNNDIID 1916
|
650 660 670
....*....|....*....|....*....|....*
gi 1981090065 1553 FQLELLEAKaelERKLSEKDEEIENFRRKQQCTID 1587
Cdd:PTZ00121 1917 DKLDKDEYI---KRDAEETREEIIKISKKDMCIND 1948
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
964-1577 |
3.71e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 71.59 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 964 EHKVKNLTEEVEFLNEDISKLNRAAKVVQeahqqtlDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERE 1043
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLD-------KNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1044 LHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAK 1123
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1124 MERERADLTQDLADLNERL------EEVGGSSLAQLEITKKQ----ETKFQKLHRDMEEATLHFETTSASLK------KR 1187
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLLsnlkkkIQKNKSLESQISELKKQnnqlKDNIEKKQQEINEKTTEISNTQTQLNqlkdeqNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1188 HADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAK-----ANAEKLCTLYEERLHEATAKLDKVTQLA 1262
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKElkselKNQEKKLEEIQNQISQNNKIISQLNEQI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1263 NDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKS-------NFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLL 1335
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQsykqeikNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1336 REQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTE-----------------DLEDAKKELAIRLQEAAEamgv 1398
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESletqlkvlsrsinkikqNLEQKQKELKSKEKELKK---- 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1399 ANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKqlqsgkaLADWKQKHEESQALLDASQ--KEVQALSTELLKL 1476
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK-------ISDLEDELNKDDFELKKENleKEIDEKNKEIEEL 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1477 KNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLE 1556
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
650 660
....*....|....*....|.
gi 1981090065 1557 LLEAKAelerKLSEKDEEIEN 1577
Cdd:TIGR04523 654 IKEIRN----KWPEIIKKIKE 670
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1200-1900 |
7.79e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 70.77 E-value: 7.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1200 ENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLaNDLAAQKTKLWSESGEF 1279
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1280 LRRLEEKEALINQLS--REKSNFTRQIEDLrgqlekeTKSQSALAHALQKAQRDCDLLREQyeEEQEVKAELHRTLSKVN 1357
Cdd:TIGR00618 266 RARIEELRAQEAVLEetQERINRARKAAPL-------AAHIKAVTQIEQQAQRIHTELQSK--MRSRAKLLMKRAAHVKQ 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1358 AEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEAAEAMgvanarnaSLERARHQLQLELGdalSDLGKVRSAAARLDQK 1437
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQH--------TLTQHIHTLQQQKT---TLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1438 QLQSGKALADWKQKHEESQALLDA-SQKEVQALSTELLKL--KNTYEESIVGQETLRRENKNLQEEISNLTNqVREGTKN 1514
Cdd:TIGR00618 406 QREQATIDTRTSAFRDLQGQLAHAkKQQELQQRYAELCAAaiTCTAQCEKLEKIHLQESAQSLKEREQQLQT-KEQIHLQ 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1515 LTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQ------LELLEAKAELERKLSEKDEEIENFRRKQQCTIDS 1588
Cdd:TIGR00618 485 ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpltrrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1589 LQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAER 1668
Cdd:TIGR00618 565 MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1669 RNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERInLFYTQN--TSLLSQKKKLEADVARMQKEAEEVVQECQNAEEK 1746
Cdd:TIGR00618 645 LTALHALQLTLTQERVREHALSIRVLPKELLASRQLA-LQKMQSekEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEI 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1747 AKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQ---IQKLESRVRELEGELEGEIR 1823
Cdd:TIGR00618 724 ENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELshlAAEIQFFNRLREEDTHLLKT 803
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981090065 1824 RSAEAQRGARRLErciKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEVKE 1900
Cdd:TIGR00618 804 LEAEIGQEIPSDE---DILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
850-1272 |
1.20e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.05 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 850 QLQKALEKsefQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSERVEEEEEINSELT 929
Cdd:TIGR04523 211 QKNKSLES---QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 930 ARGRKLEDECFELKKE-----IDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHM 1004
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1005 EEEKLSSLSKAN-------LKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKEL 1077
Cdd:TIGR04523 368 KQNEIEKLKKENqsykqeiKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1078 ELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGG------SSLA 1151
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKkisslkEKIE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1152 QLEITKKQ-ETKFQKLHRDMEEatLHFETTSASLKKrhadSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQM 1230
Cdd:TIGR04523 528 KLESEKKEkESKISDLEDELNK--DDFELKKENLEK----EIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1981090065 1231 TRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKL 1272
Cdd:TIGR04523 602 IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1654-1926 |
1.32e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1654 QLNSdLKEQVAVAER-----------RNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKL 1722
Cdd:COG1196 201 QLEP-LERQAEKAERyrelkeelkelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1723 EADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQmALMGSRK 1802
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE-ELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1803 QIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQAN 1882
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1981090065 1883 QYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQEE 1926
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1281-1899 |
1.37e-11 |
|
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: 70.15 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1281 RRLEEKealiNQLSREKSNFTRQ-IEDLRGQLEKETKSQSALAhalqkaqrdcDLLREQYEEEQEVKAELHRTLSKVNAE 1359
Cdd:pfam15921 92 RRLNES----NELHEKQKFYLRQsVIDLQTKLQEMQMERDAMA----------DIRRRESQSQEDLRNQLQNTVHELEAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1360 --MVQWRMKYENNVIQRTEDL----EDAKKELAIRLQEAAEAMG--------VANARNASLERARHQLQLELGDALSDL- 1424
Cdd:pfam15921 158 kcLKEDMLEDSNTQIEQLRKMmlshEGVLQEIRSILVDFEEASGkkiyehdsMSTMHFRSLGSAISKILRELDTEISYLk 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1425 GKVRSAAARLDQKQLQSGKALADWKQKHEES-QALLDASQKEVQALsTELLKLKNTYEESI-----VGQETLRRENKNLQ 1498
Cdd:pfam15921 238 GRIFPVEDQLEALKSESQNKIELLLQQHQDRiEQLISEHEVEITGL-TEKASSARSQANSIqsqleIIQEQARNQNSMYM 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1499 EEISNLTNQVREGTKNLTEMEKV--KKLIEEEKTEVQVTLEETEGALERN----ESKILHFQLE-LLEAKAELERKLS-- 1569
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMyeDKIEELEKQLVLANSELTEARTERDqfsqESGNLDDQLQkLLADLHKREKELSle 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1570 -EKDEEIENFRRKQQCTIDSLQSSLDSEaksRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQlqiqIKDLQMQ 1648
Cdd:pfam15921 397 kEQNKRLWDRDTGNSITIDHLRRELDDR---NMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEK----VSSLTAQ 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1649 LDDSTQLNSDLKEQVAVaeRRNSLLQSE--LEDLRSLQEQTERGRRLSEEELLEATERINLFYTQntslLSQKKKLEADV 1726
Cdd:pfam15921 470 LESTKEMLRKVVEELTA--KKMTLESSErtVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQE----LQHLKNEGDHL 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1727 ARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDlqkRLAEAEQMALMGSRK--QI 1804
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIND---RRLELQEFKILKDKKdaKI 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1805 QKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQlkvQNYKQQVEVAETQANQY 1884
Cdd:pfam15921 621 RELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK---RNFRNKSEEMETTTNKL 697
|
650
....*....|....*
gi 1981090065 1885 LSKYKKQQHELNEVK 1899
Cdd:pfam15921 698 KMQLKSAQSELEQTR 712
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
29-74 |
3.46e-11 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 59.75 E-value: 3.46e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1981090065 29 DGKKKCWIPDGENAYIEAEVKgSEDDGTVIVETADGESLSIKEDKI 74
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIK-EEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1055-1620 |
3.99e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1055 RESMENLESSQRHLAEELRKKELeLSQMNSKVENEKGLVAQLQK--------TVKELQTQIKDLKEKLEAERTTRAKMER 1126
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIEL-LEPIRELAERYAAARERLAEleylraalRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1127 ERADLTQDLADLNERLEEV-------GGSSLAQLE--------ITKKQETKFQKLHRDMEEATLHFETTS---ASLKKRH 1188
Cdd:COG4913 310 ELERLEARLDALREELDELeaqirgnGGDRLEQLEreierlerELEERERRRARLEALLAALGLPLPASAeefAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1189 ADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANaeklctlYEERLHEATAKLDKVTQLAND---- 1264
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN-------IPARLLALRDALAEALGLDEAelpf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1265 ---------------------LAAQKTKL------WSESGEFLRRLEEKEAL-INQLSREKSNFTRQIEDLRGQLEK-ET 1315
Cdd:COG4913 463 vgelievrpeeerwrgaiervLGGFALTLlvppehYAAALRWVNRLHLRGRLvYERVRTGLPDPERPRLDPDSLAGKlDF 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1316 KSQSALAHALQKAQRDCDLLREQYEEEqevkaeLHRT--------LSKVNAEMVQ---WRMKYENNVIQRteDLEDAKKE 1384
Cdd:COG4913 543 KPHPFRAWLEAELGRRFDYVCVDSPEE------LRRHpraitragQVKGNGTRHEkddRRRIRSRYVLGF--DNRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1385 LAIRLQEAAEAMGVANARNASLERARHQLQlELGDALSDLGKVRSaaARLDQKQLQsgKALADWKQKHEEsqalLDASQK 1464
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSW--DEIDVASAE--REIAELEAELER----LDASSD 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1465 EVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVtLEETEGALE 1544
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF-AAALGDAVE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1545 RNESKILHFQLELLEAKAE-LERKLSEKdeeIENFRRKQQCTIDSLQSSLDSEAK-----SRIEVTRL---KKKMEEDLN 1615
Cdd:COG4913 765 RELRENLEERIDALRARLNrAEEELERA---MRAFNREWPAETADLDADLESLPEylallDRLEEDGLpeyEERFKELLN 841
|
....*
gi 1981090065 1616 EMELQ 1620
Cdd:COG4913 842 ENSIE 846
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1598-1913 |
7.12e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 7.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1598 KSRIEVTRLK-KKMEEDLN-------EMELQLSCANRQVSEATKSLgQLQIQIKDLQMQLddstQLNSD--LKEQVAVAE 1667
Cdd:COG1196 171 KERKEEAERKlEATEENLErledilgELERQLEPLERQAEKAERYR-ELKEELKELEAEL----LLLKLreLEAELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1668 RRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKA 1747
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1748 KKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQIQKLESRVRELEGELEGEIRRSAE 1827
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1828 AQRGARRLERcIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEVKERAEVAES 1907
Cdd:COG1196 406 EEAEEALLER-LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
....*.
gi 1981090065 1908 QVNKLK 1913
Cdd:COG1196 485 ELAEAA 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
926-1237 |
8.32e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 8.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 926 SELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHME 1005
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1006 EEKLSSLSKANLKLE-----QQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELS 1080
Cdd:TIGR02169 771 EEDLHKLEEALNDLEarlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1081 QMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLN---ERLEEVGGSSLAQLEITK 1157
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiEKKRKRLSELKAKLEALE 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1158 KQETKFQKLHRDMEE---ATLHFETTSASLKKRHADSLA----------ELEGQVENLQQVKQKLEKdksdLQLEVDDLL 1224
Cdd:TIGR02169 931 EELSEIEDPKGEDEEipeEELSLEDVQAELQRVEEEIRAlepvnmlaiqEYEEVLKRLDELKEKRAK----LEEERKAIL 1006
|
330
....*....|...
gi 1981090065 1225 TRVEQMTRAKANA 1237
Cdd:TIGR02169 1007 ERIEEYEKKKREV 1019
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
891-1531 |
8.79e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.40 E-value: 8.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 891 ANVEEQCEWLIKSKIQLEARVKELSERVEEEEEINSELTARGRKLEdecfELKKEIDDLETMLVKSEKEKRTTEHKVKNL 970
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 971 TEEVEFLNEDISKLNRAAKVVQEahqqtLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKarmNCERELHKLEGN 1050
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKELKE-----LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN---GIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1051 LKLNRESMENLESSQRHLaEELRKKELELSQMNSKVENEKGLVAQLQ-KTVKELQTQIKDLKEKLEAERTTRAKMERERA 1129
Cdd:PRK03918 337 EERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1130 DLTQDLADLNERLEEVggsslaqleitKKQETKFQKLHRDMEeatlhfETTSASLKKRHADSLAELEGQVENLQQVKQKL 1209
Cdd:PRK03918 416 ELKKEIKELKKAIEEL-----------KKAKGKCPVCGRELT------EEHRKELLEEYTAELKRIEKELKEIEEKERKL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1210 EKDKSdlqlEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEAL 1289
Cdd:PRK03918 479 RKELR----ELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1290 INQLsREKSNFTRQIEDLRGQLEKEtksqsalahalqkaqrdcdLLREQYEEEQEVKAELhRTLSKVNAEMVQWRmkyen 1369
Cdd:PRK03918 555 KKKL-AELEKKLDELEEELAELLKE-------------------LEELGFESVEELEERL-KELEPFYNEYLELK----- 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1370 NVIQRTEDLEDAKKELAIRLQEAAEAMGVANARnasLERARHQLQlELGDALSDlgkvrSAAARLDQKQLQSGKALADWK 1449
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKR---LEELRKELE-ELEKKYSE-----EEYEELREEYLELSRELAGLR 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1450 QKHEESQALLDASQKEVQALSTELLKLKNtYEESIVGQETLRRENKNLQEEISNLTNQVREGTknLTEMEKVKKLIEEEK 1529
Cdd:PRK03918 680 AELEELEKRREEIKKTLEKLKEELEEREK-AKKELEKLEKALERVEELREKVKKYKALLKERA--LSKVGEIASEIFEEL 756
|
..
gi 1981090065 1530 TE 1531
Cdd:PRK03918 757 TE 758
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1001-1741 |
1.05e-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: 67.30 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1001 DLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKArmNCERELHKLEGNLKLNRESMENLeSSQRHLAEELRKKELELS 1080
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQ--VLEKELKHLREALQQTQQSHAYL-TQKREAQEEQLKKQQLLK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1081 QMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTrakmereradltqdladlnerleevggsslaqlEITKKQE 1160
Cdd:TIGR00618 264 QLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVT---------------------------------QIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1161 TKFQKLHRDMEEATLHFETTSASLKKRhadslAELEGQVENLQQVKQKLEKdksdLQLEVDDLLTRVEQMTRAKANaekl 1240
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMKRAAHVKQQ-----SSIEEQRRLLQTLHSQEIH----IRDAHEVATSIREISCQQHTL---- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1241 ctlyEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQ---LEKETKS 1317
Cdd:TIGR00618 378 ----TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCaaaITCTAQC 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1318 QSALAHALQKAQRDcdlLREQYEEEQEVKaelhrTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEAAEAmG 1397
Cdd:TIGR00618 454 EKLEKIHLQESAQS---LKEREQQLQTKE-----QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNP-G 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1398 VANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLK 1477
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1478 ntyEESIVGQETLRRENKNLQEEISNLTNQVREGTKnltEMEKVKKLIEEEKTEVQVTLEETEGALERneskILHFQLEL 1557
Cdd:TIGR00618 605 ---EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQC---SQELALKLTALHALQLTLTQERVREHALS----IRVLPKEL 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1558 LEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLG- 1636
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARt 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1637 QLQIQIKDLQMQLDDST---QLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNT 1713
Cdd:TIGR00618 755 VLKARTEAHFNNNEEVTaalQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFL 834
|
730 740
....*....|....*....|....*...
gi 1981090065 1714 SLLSQKKKLEADVARMQKEAEEVVQECQ 1741
Cdd:TIGR00618 835 SRLEEKSATLGEITHQLLKYEECSKQLA 862
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
844-1115 |
2.30e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.81 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 844 LKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSERVEEEEE 923
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 924 INSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLH 1003
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1004 MEEEKLSSLSKANLKLEQQVDELEGALEQ--ERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQ 1081
Cdd:TIGR04523 521 SLKEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1981090065 1082 MNSKVENEKGLVAQLQKTV-------KELQTQIKDLKEKLE 1115
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEKELekakkenEKLSSIIKNIKSKKN 641
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1490-1925 |
4.35e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.04 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1490 LRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELE---- 1565
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnn 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1566 --------------RKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEA 1631
Cdd:TIGR04523 303 qkeqdwnkelkselKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1632 TKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQ 1711
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1712 NTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAE 1791
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1792 AEQMAL-MGSRKQIQKLESRVRelegELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRmqtQMDKLQLKVQNY 1870
Cdd:TIGR04523 543 LEDELNkDDFELKKENLEKEID----EKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK---EIEEKEKKISSL 615
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1981090065 1871 KQQVEVAETQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQE 1925
Cdd:TIGR04523 616 EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKE 670
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1559-1800 |
6.17e-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: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1559 EAKAELERKLSEKDEEIENfrrkqqctidsLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQL 1638
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAE-----------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1639 QIQIKDLQMQLDdstQLNSDLKEQVAVAERRNSllQSELEDLRSLQE--QTERGRRLSEEELLEATERINLFYTQNTSLL 1716
Cdd:COG4942 89 EKEIAELRAELE---AQKEELAELLRALYRLGR--QPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1717 SQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMA 1796
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
....
gi 1981090065 1797 LMGS 1800
Cdd:COG4942 244 PAAG 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1006-1482 |
9.36e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 9.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1006 EEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMNSK 1085
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1086 VENEkglvaQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKFQK 1165
Cdd:COG4717 132 QELE-----ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1166 LHRDMEEAtlhfettsaslkkrhadsLAELEGQVENLQQVKQKLEKDKSDLQLEvdDLLTRVEQMTRAKANAEKLCTLYE 1245
Cdd:COG4717 207 RLAELEEE------------------LEEAQEELEELEEELEQLENELEAAALE--ERLKEARLLLLIAAALLALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1246 ERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHAL 1325
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1326 QKAQRDCDLLREQYEE--EQEVKAELHRTLSKVNAEMV-QWRMKYENnvIQRTEDLEDAKKELAIRLQEAAEAMGVANAR 1402
Cdd:COG4717 347 EELQELLREAEELEEElqLEELEQEIAALLAEAGVEDEeELRAALEQ--AEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1403 N--ASLERARHQLQLELGDALSDLGKVRSAAARLDQ--KQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKN 1478
Cdd:COG4717 425 LdeEELEEELEELEEELEELEEELEELREELAELEAelEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEE 504
|
....
gi 1981090065 1479 TYEE 1482
Cdd:COG4717 505 AREE 508
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1092-1484 |
9.94e-10 |
|
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: 64.20 E-value: 9.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1092 LVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQEtkfqklhrDME 1171
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIERYQE--------DLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1172 EATLHFETTSASLKKRHaDSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRV---EQMTRAKANAEKLCTL----- 1243
Cdd:COG3096 358 ELTERLEEQEEVVEEAA-EQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiqyQQAVQALEKARALCGLpdltp 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1244 --YEERLHEATAKLDKVTQLANDLaAQKTKLWSES-GEFLRRLEEKEALINQLSREKSNFTRQiedlrgQLEKETKSQSA 1320
Cdd:COG3096 437 enAEDYLAAFRAKEQQATEEVLEL-EQKLSVADAArRQFEKAYELVCKIAGEVERSQAWQTAR------ELLRRYRSQQA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1321 LAHALQKAQRDCDLLREQYEEEQEVKAELHRtLSKvnaemvqwRMKYEnnvIQRTEDLEDAKKELAIRLQEAAEAMGVAN 1400
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQQQNAERLLEE-FCQ--------RIGQQ---LDAAEELEELLAELEAQLEELEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1401 ARNASLERARHQLQLELGdALSDLGKV-RSAAARLDQKQLQSGKALADWKQKHEESQALLDAsQKEVQALSTELLKLKNT 1479
Cdd:COG3096 578 EQRSELRQQLEQLRARIK-ELAARAPAwLAAQDALERLREQSGEALADSQEVTAAMQQLLER-EREATVERDELAARKQA 655
|
....*
gi 1981090065 1480 YEESI 1484
Cdd:COG3096 656 LESQI 660
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
863-1549 |
1.01e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 64.09 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 863 EELKAKQVSLTQEKNDLILQLQAEQETLANVEEQcewlIKSKIQLEARVKELSER-VEEEEEINSELTARGRKLEDECFE 941
Cdd:pfam12128 216 SRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQE----FNTLESAELRLSHLHFGyKSDETLIASRQEERQETSAELNQL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 942 LKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQ 1021
Cdd:pfam12128 292 LRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1022 QVDELEGALEQERKARmnCERELHKLEGNLKLNRES-----------MENLESSQRH-LAEELRKKELELSQMNSKVENE 1089
Cdd:pfam12128 372 DVTAKYNRRRSKIKEQ--NNRDIAGIKDKLAKIREArdrqlavaeddLQALESELREqLEAGKLEFNEEEYRLKSRLGEL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1090 KGLVAQLQKTvKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEvGGSSLAQLEI-TKKQETKFQKLHR 1168
Cdd:pfam12128 450 KLRLNQATAT-PELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQ-ASEALRQASRrLEERQSALDELEL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1169 DMEEAT---LHFETTSASLKKRHADSLAELE----------------GQVENLQQVKQKLEK-DKSDLQLEVDDLLTRVE 1228
Cdd:pfam12128 528 QLFPQAgtlLHFLRKEAPDWEQSIGKVISPEllhrtdldpevwdgsvGGELNLYGVKLDLKRiDVPEWAASEEELRERLD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1229 QMTRAKANAEKLCTLYEERLHEATAKLDKVtQLANDLAAQKTKlwsESGEFLRRL-EEKEALINQLSREKSNFTRQIEDL 1307
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQLVQANGELEKA-SREETFARTALK---NARLDLRRLfDEKQSEKDKKNKALAERKDSANER 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1308 RGQLEKETKsQSALAHALQKAQRDcDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLE-DAKKELA 1386
Cdd:pfam12128 684 LNSLEAQLK-QLDKKHQAWLEEQK-EQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALEtWYKRDLA 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1387 irlqeaaeAMGVANARNASLERARHqlqlELGDALSDLGKVRSAAARLDQKQLQSgkaladWKQKHEESQALLDASQKEV 1466
Cdd:pfam12128 762 --------SLGVDPDVIAKLKREIR----TLERKIERIAVRRQEVLRYFDWYQET------WLQRRPRLATQLSNIERAI 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1467 QALSTELLKLkntyeesivgQETLRRENKNLQEEISNLTNQVREGTKNLT----EMEKVKKLIEEEKTE-VQVTLEETEG 1541
Cdd:pfam12128 824 SELQQQLARL----------IADTKLRRAKLEMERKASEKQQVRLSENLRglrcEMSKLATLKEDANSEqAQGSIGERLA 893
|
....*...
gi 1981090065 1542 ALERNESK 1549
Cdd:pfam12128 894 QLEDLKLK 901
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1436-1913 |
1.05e-09 |
|
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: 63.98 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1436 QKQLQSGKALADwKQKHEESQALLDAsQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNL 1515
Cdd:pfam15921 91 QRRLNESNELHE-KQKFYLRQSVIDL-QTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1516 -TEMEKVKKL------IEEEKTEVQVTLEETEGA--LERNESKILHFQlellEAKAELERKLSEKDEEIENFRRKQQCTI 1586
Cdd:pfam15921 169 nTQIEQLRKMmlshegVLQEIRSILVDFEEASGKkiYEHDSMSTMHFR----SLGSAISKILRELDTEISYLKGRIFPVE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1587 DSLQSsLDSEAKSRIEV--TRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDStqlNSDLKEQVA 1664
Cdd:pfam15921 245 DQLEA-LKSESQNKIELllQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQ---NSMYMRQLS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1665 VAERRNSLLQSELEDLRSLQE----QTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEevVQEC 1740
Cdd:pfam15921 321 DLESTVSQLRSELREAKRMYEdkieELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS--LEKE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1741 QNAeekakkaaieaaNLSEELKKKQDTIAHLERTRE--NMEqtitdlqkrlaeaeqmalmgsrkqIQKLESRVRELEGEL 1818
Cdd:pfam15921 399 QNK------------RLWDRDTGNSITIDHLRRELDdrNME------------------------VQRLEALLKAMKSEC 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1819 EGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEV 1898
Cdd:pfam15921 443 QGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKL 522
|
490
....*....|....*
gi 1981090065 1899 KERAEVAESQVNKLK 1913
Cdd:pfam15921 523 RSRVDLKLQELQHLK 537
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
835-1246 |
1.13e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 835 SEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAeqetlanVEEQCEWLIKSKIQLEARVKel 914
Cdd:PRK02224 289 EELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA-------HNEEAESLREDADDLEERAE-- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 915 sERVEEEEEINSELTARGRKLED---ECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDI----SKLNRA 987
Cdd:PRK02224 360 -ELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREaeleATLRTA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 988 AKVVQEA--------------------HQQTLDDlhmEEEKLSSLSKANLKLEQQVDELEGALEQERKARmNCERELHKL 1047
Cdd:PRK02224 439 RERVEEAealleagkcpecgqpvegspHVETIEE---DRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1048 EGNLKLNRESMENLESS---QRHLAEELRKKELEL-SQMNSKVE--NEKGLVAQ-LQKTVKELQTQIKDLKEKLEAERTT 1120
Cdd:PRK02224 515 EERREDLEELIAERRETieeKRERAEELRERAAELeAEAEEKREaaAEAEEEAEeAREEVAELNSKLAELKERIESLERI 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1121 RAKMErERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKFQKLHRDMEEATLhfeTTSASLKKRHADSLAELEGQVE 1200
Cdd:PRK02224 595 RTLLA-AIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARI---EEAREDKERAEEYLEQVEEKLD 670
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1981090065 1201 NLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEE 1246
Cdd:PRK02224 671 ELREERDDLQAEIGAVENELEELEELRERREALENRVEALEALYDE 716
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1069-1282 |
1.75e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1069 AEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGS 1148
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1149 SLAQLEITKKQETKFQKLHR-DMEEATLHFETTSASLKKRH---------ADSLAELEGQVENLQQVKQKLEKDKSDLQL 1218
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRqPPLALLLSPEDFLDAVRRLQylkylaparREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1981090065 1219 EVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRR 1282
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
833-1239 |
2.15e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 62.73 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 833 KSSEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQ------EKNDLILQLQAEQETLANVEEQcEWLIKSKIQ 906
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkkikELEKQLNQLKSEISDLNNQKEQ-DWNKELKSE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 907 LEARVKELSERVEEEEEINSELTargrKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNR 986
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIIS----QLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLES 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 987 AAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLE---GNLKLNRESMEN--- 1060
Cdd:TIGR04523 392 QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEliiKNLDNTRESLETqlk 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1061 -LESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLN 1139
Cdd:TIGR04523 472 vLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1140 ERLeevggsslaqleitKKQETKFQKLHRDMEEATLHFETTSaslkkrhadslaeLEGQVENLQQVKQKLEKDKSDLQLE 1219
Cdd:TIGR04523 552 FEL--------------KKENLEKEIDEKNKEIEELKQTQKS-------------LKKKQEEKQELIDQKEKEKKDLIKE 604
|
410 420
....*....|....*....|
gi 1981090065 1220 VDDLLTRVEQMTRAKANAEK 1239
Cdd:TIGR04523 605 IEEKEKKISSLEKELEKAKK 624
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
839-1318 |
3.39e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 839 EEVAGLKEECAQLQKALEKSEFQREELK-------AKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARV 911
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAeevrdlrERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 912 KELSERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNE---DISKLNRAA 988
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgDAPVDLGNA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 989 KVVQEAHQQTLDDLHME----EEKLSSLSKANLKLEQQVDE---------LEG-----ALEQERKARMNCERELHKLEgn 1050
Cdd:PRK02224 411 EDFLEELREERDELREReaelEATLRTARERVEEAEALLEAgkcpecgqpVEGsphveTIEEDRERVEELEAELEDLE-- 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1051 lkLNRESMEN-LESsqrhlAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDL---KEKLEAE----RTTRA 1122
Cdd:PRK02224 489 --EEVEEVEErLER-----AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELrerAAELEAEaeekREAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1123 KMERERADLTQDLADLNERLEEVgGSSLAQLEITKKQETKFQKLHRDMEEatlhfettsasLKKRHADsLAELEGQVEnl 1202
Cdd:PRK02224 562 EAEEEAEEAREEVAELNSKLAEL-KERIESLERIRTLLAAIADAEDEIER-----------LREKREA-LAELNDERR-- 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1203 QQVKQKLEKdKSDLQLEVDDllTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKvtqLANDLAAQKTKLwsESGEFLRr 1282
Cdd:PRK02224 627 ERLAEKRER-KRELEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDD---LQAEIGAVENEL--EELEELR- 697
|
490 500 510
....*....|....*....|....*....|....*...
gi 1981090065 1283 lEEKEALINQLSREKS--NFTRQIEDLRGQLEKETKSQ 1318
Cdd:PRK02224 698 -ERREALENRVEALEAlyDEAEELESMYGDLRAELRQR 734
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1491-1848 |
4.40e-09 |
|
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: 61.68 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1491 RRENKNLQEEISNLTNQ--VREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELERKL 1568
Cdd:pfam17380 239 RKESFNLAEDVTTMTPEytVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1569 SEKdEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRL--KKKMEEDLNEMELQLSCanrqvsEATKSLGQLQIQIKDLQ 1646
Cdd:pfam17380 319 EEA-EKARQAEMDRQAAIYAEQERMAMERERELERIRQeeRKRELERIRQEEIAMEI------SRMRELERLQMERQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1647 MQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQT-ERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEAD 1725
Cdd:pfam17380 392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1726 VARMQKEAEEVVQECQNAEEKAKKAaieaanLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQ--MALMGSRKQ 1803
Cdd:pfam17380 472 RKRKKLELEKEKRDRKRAEEQRRKI------LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERrrEAEEERRKQ 545
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1981090065 1804 IQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEE 1848
Cdd:pfam17380 546 QEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
839-1384 |
4.70e-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: 61.57 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 839 EEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSERV 918
Cdd:TIGR04523 75 NKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 919 EEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKV----------KNLTEEVEFLNEDISKLNRAA 988
Cdd:TIGR04523 155 EKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlkkkiqknKSLESQISELKKQNNQLKDNI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 989 KVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLK-LNRESMEN----LES 1063
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdLNNQKEQDwnkeLKS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1064 SQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLE 1143
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1144 EVGGSSLAQLEITKKQETKFQKLHRDMEEatlhfettsasLKKRHADslaeLEGQVENLQQVKQKLEKDKSDLQLEVDDL 1223
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKEL-----------LEKEIER----LKETIIKNNSEIKDLTNQDSVKELIIKNL 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1224 LTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQ 1303
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1304 IEDLRGQLEK--ETKSQSALAHALQKAQRDCDLLREQYEE---EQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDL 1378
Cdd:TIGR04523 540 ISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSlkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL 619
|
....*.
gi 1981090065 1379 EDAKKE 1384
Cdd:TIGR04523 620 EKAKKE 625
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
941-1581 |
1.92e-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: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 941 ELKKEIDDLETMlvksEKEKRTTEHKVKNLTEEVEfLNEDISKLnRAAKVVQEAHQQTLDDLHmEEEKLSSLSKANLKLE 1020
Cdd:COG4913 229 ALVEHFDDLERA----HEALEDAREQIELLEPIRE-LAERYAAA-RERLAELEYLRAALRLWF-AQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1021 QQVDELEGALEQERKARMNCERELHKLEGNL-KLNRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKT 1099
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1100 VKELQTQIKDLKEKLEAERttrAKMERERADLTQDLADLNERLEEVggssLAQLEITKKQET----KFQKLHRDMEEATl 1175
Cdd:COG4913 382 FAALRAEAAALLEALEEEL---EALEEALAEAEAALRDLRRELREL----EAEIASLERRKSnipaRLLALRDALAEAL- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1176 hfettsaSLKKRHADSLAEL----------EGQVE---------------NLQQVKQKLE--KDKSDLQLEVDDLLTRVE 1228
Cdd:COG4913 454 -------GLDEAELPFVGELievrpeeerwRGAIErvlggfaltllvppeHYAAALRWVNrlHLRGRLVYERVRTGLPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1229 QMTRAKAN--AEKLctlyEERLHEATA-------------KLDKVTQLAN-DLAAQKTKLWSESGEF------------- 1279
Cdd:COG4913 527 ERPRLDPDslAGKL----DFKPHPFRAwleaelgrrfdyvCVDSPEELRRhPRAITRAGQVKGNGTRhekddrrrirsry 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1280 ------LRRLEEKEALINQLSREKSNFTRQIEDLRGQLEketksqsalahALQKAQRDCDLLREQYEEEQEVkAELHRTL 1353
Cdd:COG4913 603 vlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELD-----------ALQERREALQRLAEYSWDEIDV-ASAEREI 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1354 SKVNAEMvqwrmkyennviqrtEDLEDAKKELairlqeaaeamgvanarnASLERARHQLQLELGDALSDLGKVRSAAAR 1433
Cdd:COG4913 671 AELEAEL---------------ERLDASSDDL------------------AALEEQLEELEAELEELEEELDELKGEIGR 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1434 LDQKqlqsgkaLADWKQKHEESQALLDASQKEVQALSTELLklkNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTK 1513
Cdd:COG4913 718 LEKE-------LEQAEEELDELQDRLEAAEDLARLELRALL---EERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1981090065 1514 NLTE-MEKVKKLIEEEKTEVQVTLEETEGALERneskilHFQLE---LLEAKAELERKLSE-KDEEIENFRRK 1581
Cdd:COG4913 788 ELERaMRAFNREWPAETADLDADLESLPEYLAL------LDRLEedgLPEYEERFKELLNEnSIEFVADLLSK 854
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1525-1903 |
2.77e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1525 IEEEKTEVQVTLEETEGALERNESKILHFQLelleakAELERKLSEKDEEIENF---RRKQQCTIDSLQSSLDSEAKSRI 1601
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDLHERL------NGLESELAELDEEIERYeeqREQARETRDEADEVLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1602 EVTRLK---KKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDL--QMQLDDStqlnsdlkEQVAVAERRnsllqse 1676
Cdd:PRK02224 252 ELETLEaeiEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDA--------DAEAVEARR------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1677 lEDLRSLQEQTErgrrlseEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAAN 1756
Cdd:PRK02224 317 -EELEDRDEELR-------DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1757 LSEELKKKQDTIA-----------HLERTREN----------MEQTITDLQKRLAEAEQM-------------------- 1795
Cdd:PRK02224 389 LEEEIEELRERFGdapvdlgnaedFLEELREErdelrereaeLEATLRTARERVEEAEALleagkcpecgqpvegsphve 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1796 ALMGSRKQIQKLESR---VRELEGELEGEIRRSAEAQRGARRLERC----------IKELTYQAEEDKKNLSRMQTQMDK 1862
Cdd:PRK02224 469 TIEEDRERVEELEAEledLEEEVEEVEERLERAEDLVEAEDRIERLeerredleelIAERRETIEEKRERAEELRERAAE 548
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1981090065 1863 LQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEVKERAE 1903
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
987-1215 |
3.40e-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: 57.85 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 987 AAKVVQEAHQQTLDDLhmeEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQR 1066
Cdd:COG4942 17 AQADAAAEAEAELEQL---QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1067 HLAEELRKKELELS------QMNSKVENEKGLVAQ------------LQKTVKELQTQIKDLKEKLEAERTTRAKMERER 1128
Cdd:COG4942 94 ELRAELEAQKEELAellralYRLGRQPPLALLLSPedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1129 ADLTQDLADLNERLEEvggssLAQLEitKKQETKFQKLHRDmeeatlhfettsaslKKRHADSLAELEGQVENLQQVKQK 1208
Cdd:COG4942 174 AELEALLAELEEERAA-----LEALK--AERQKLLARLEKE---------------LAELAAELAELQQEAEELEALIAR 231
|
....*..
gi 1981090065 1209 LEKDKSD 1215
Cdd:COG4942 232 LEAEAAA 238
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1226-1913 |
3.61e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1226 RVEQMTRAKA--NAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSES--GEFLRRLEEkealinqlSREKSNFT 1301
Cdd:PTZ00121 1171 KAEDAKKAEAarKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAkkAEAVKKAEE--------AKKDAEEA 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1302 RQIEDLRGQLEKETKSQSALAH-----ALQKAQ--RDCDLLREQyeEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQR 1374
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHfarrqAAIKAEeaRKADELKKA--EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1375 TEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQLELGDALSDLGKVRSAaarldQKQLQSGKALADWKQKHEE 1454
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA-----KKKADAAKKKAEEKKKADE 1395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1455 SQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTevqv 1534
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK---- 1471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1535 TLEETEGALERNESKILHFQLELLEAKAELERKLSEKDEEIENFRRKQQC-TIDSLQSSLDSEAKSRIEVTRLKKKMEED 1613
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAkKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1614 LNEMELQLSCANRQVSEATK-------SLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQE- 1685
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKaeedknmALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEe 1631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1686 --QTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADvarmQKEAEEVVQEcqnaEEKAKKAAIEAANLSEELKK 1763
Cdd:PTZ00121 1632 kkKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED----KKKAEEAKKA----EEDEKKAAEALKKEAEEAKK 1703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1764 KQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLErciKELT 1843
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE---KEAV 1780
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1844 YQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEvAETQANQYLSKYKkqQHELNEVKERAEVAESQVNKLK 1913
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDKKIKDIFDNFANIIE-GGKEGNLVINDSK--EMEDSAIKEVADSKNMQLEEAD 1847
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1166-1807 |
4.28e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1166 LHRDMEEAtlhfettsaslkKRHADSLAELEGQVENLQQVKQKLEkdksdlqlEVDDLLTRVEQMTRAKANAeklctLYE 1245
Cdd:COG4913 240 AHEALEDA------------REQIELLEPIRELAERYAAARERLA--------ELEYLRAALRLWFAQRRLE-----LLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1246 ERLHEATAKLDKVTQLANDLAAQKTKLwsesgeflrrLEEKEALINQLSrekSNFTRQIEDLRGQLEKETKSQSALAHAL 1325
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDAL----------REELDELEAQIR---GNGGDRLEQLEREIERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1326 QKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEAAEAMGVANARNAS 1405
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1406 LERARHQLQLELGDALSDL---------------------GKVRSAAARL--DQKQLqsgKALADW----KQKH------ 1452
Cdd:COG4913 442 LLALRDALAEALGLDEAELpfvgelievrpeeerwrgaieRVLGGFALTLlvPPEHY---AAALRWvnrlHLRGrlvyer 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1453 -EESQALLDASQKEVQALSTELLKLKNTYE---ESIVGQ----------ETLRRENKNLQEE--IS--------NLTNQV 1508
Cdd:COG4913 519 vRTGLPDPERPRLDPDSLAGKLDFKPHPFRawlEAELGRrfdyvcvdspEELRRHPRAITRAgqVKgngtrhekDDRRRI 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1509 RE----GTKNLtemEKVKKLiEEEKTEVQVTLEETEGALERNESkilhfQLELLEAKAELERKLSEKDEEIENFRRKQQc 1584
Cdd:COG4913 599 RSryvlGFDNR---AKLAAL-EAELAELEEELAEAEERLEALEA-----ELDALQERREALQRLAEYSWDEIDVASAER- 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1585 TIDSLQSSLDSEAKSRIEVTRLKKKMEE---DLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDD-----STQLN 1656
Cdd:COG4913 669 EIAELEAELERLDASSDDLAALEEQLEEleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedlaRLELR 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1657 SDLKEQVAVAERRNSlLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSqkkkleADVArmqkEAEEV 1736
Cdd:COG4913 749 ALLEERFAAALGDAV-ERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLD------ADLE----SLPEY 817
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1981090065 1737 VQECQNAEekakkaaieaanlSEELKKKQDTIAhlERTRENMEQTITDLQKRLAEAEQMAlmgsRKQIQKL 1807
Cdd:COG4913 818 LALLDRLE-------------EDGLPEYEERFK--ELLNENSIEFVADLLSKLRRAIREI----KERIDPL 869
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
833-1203 |
4.57e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 833 KSSEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVK 912
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 913 ELSERVEEeeeiNSELTARGRKLE-----------DECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDI 981
Cdd:PRK02224 437 TARERVEE----AEALLEAGKCPEcgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 982 SKLNRAAKVVQ--EAHQQTLDDlhmEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESME 1059
Cdd:PRK02224 513 RLEERREDLEEliAERRETIEE---KRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1060 NLESSqRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERA-----DLTQD 1134
Cdd:PRK02224 590 SLERI-RTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAeeyleQVEEK 668
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1981090065 1135 LADLNER----LEEVGG--SSLAQLEITKKQETKFQKLHRDMEeaTLHFETTsaSLKKRHADSLAELEGQ-VENLQ 1203
Cdd:PRK02224 669 LDELREErddlQAEIGAveNELEELEELRERREALENRVEALE--ALYDEAE--ELESMYGDLRAELRQRnVETLE 740
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1246-1875 |
5.89e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1246 ERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKetksqsalahaL 1325
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK-----------L 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1326 QKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRmKYENNVIQRTEDLEDAKKELAiRLQEAAEAMGVANARNAS 1405
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE-ERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1406 LERARHQLQLELGD----------ALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLdASQKEVQALSTELL- 1474
Cdd:PRK03918 305 YLDELREIEKRLSRleeeingieeRIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTg 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1475 ----KLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVqvTLEETEGALERNESKI 1550
Cdd:PRK03918 384 ltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL--TEEHRKELLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1551 LHFQLELLEAKaELERKLSEKDEEIENFRRKQqctidslqssldSEAKSRIEVTRLKKKMEEDLNEMELQ-LSCANRQVS 1629
Cdd:PRK03918 462 KRIEKELKEIE-EKERKLRKELRELEKVLKKE------------SELIKLKELAEQLKELEEKLKKYNLEeLEKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1630 EATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEqvavAERRNSLLQSELEDLrsLQEQTERGRRlSEEELLEATERINLFY 1709
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAE----LEKKLDELEEELAEL--LKELEELGFE-SVEELEERLKELEPFY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1710 TQNTSLLSQKKKLEADVARMQKEAEEvvqecqnaeekakkaaieaanlseelkkkqdtiahLERTRENMEQTITDLQKRL 1789
Cdd:PRK03918 602 NEYLELKDAEKELEREEKELKKLEEE-----------------------------------LDKAFEELAETEKRLEELR 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1790 AEAEQMALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKK------NLSRMQTQMDKL 1863
Cdd:PRK03918 647 KELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKakkeleKLEKALERVEEL 726
|
650
....*....|..
gi 1981090065 1864 QLKVQNYKQQVE 1875
Cdd:PRK03918 727 REKVKKYKALLK 738
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1071-1278 |
8.48e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1071 ELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEE------ 1144
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1145 VGGSSLAQLE--------------------ITKKQETKFQKLHRDMEEAtlhfettsASLKKRHADSLAELEGQVENLQQ 1204
Cdd:COG3883 97 RSGGSVSYLDvllgsesfsdfldrlsalskIADADADLLEELKADKAEL--------EAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1981090065 1205 VKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGE 1278
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
966-1173 |
9.91e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 966 KVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELH 1045
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1046 KLEGNL--------KLNRESMENLESSQRHLAEELRKKELelsqMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAE 1117
Cdd:COG4942 101 AQKEELaellralyRLGRQPPLALLLSPEDFLDAVRRLQY----LKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1981090065 1118 RTTRAKMERERADLTQDLADLNERLEEVGG---SSLAQLEITKKQETKFQKLHRDMEEA 1173
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKelaELAAELAELQQEAEELEALIARLEAE 235
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
839-1265 |
9.94e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 9.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 839 EEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDL--ILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSE 916
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 917 RVEEEEEINSELTARGRKLEDEC----FELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQ 992
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 993 EAHQ-----------------QTLDDLHMEEEK----------------LSSLSKANLKLEQQVDELEGALEQERKARMN 1039
Cdd:COG4717 241 LEERlkearlllliaaallalLGLGGSLLSLILtiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1040 CERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQmnskvenekglvAQLQKTVKELQTQIKDLKEKLEAERT 1119
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE------------LQLEELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1120 TRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQ--ETKFQKLHRDMEEAtlhfettsASLKKRHADSLAELEG 1197
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEEL--------EEELEELREELAELEA 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1981090065 1198 QVENLQQvkqklEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEAT-AKLDKVTQLANDL 1265
Cdd:COG4717 461 ELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYReERLPPVLERASEY 524
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1607-1834 |
1.22e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1607 KKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLR-SLQE 1685
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRaELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1686 QTER-GRRLSEEELLEATERINLFYTQNTSLLSQK--KKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELK 1762
Cdd:COG4942 102 QKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1981090065 1763 KKQDTIAHLERTRENMEQTITDLQKRLAEAEQmALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARR 1834
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAA-ELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1019-1258 |
1.80e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1019 LEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRH--LAEELRKKELELSQmnskVENEKGLVAQL 1096
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELER----LDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1097 QKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSS-----------LAQLEITKKQETKFQK 1165
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelralleerFAAALGDAVERELREN 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1166 LHRDMEEATLHFETTSASL-------KKRHADSLAELEGQVENLQQVKQKLEkdksdlQLEVDDLLTRVEQMTRAKANAE 1238
Cdd:COG4913 771 LEERIDALRARLNRAEEELeramrafNREWPAETADLDADLESLPEYLALLD------RLEEDGLPEYEERFKELLNENS 844
|
250 260
....*....|....*....|....*
gi 1981090065 1239 K-----LCTLYEERLHEATAKLDKV 1258
Cdd:COG4913 845 IefvadLLSKLRRAIREIKERIDPL 869
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
833-1222 |
2.11e-07 |
|
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: 56.23 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 833 KSSEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVK 912
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 913 ELSERveeeeeinsELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISklnraakvvq 992
Cdd:TIGR02169 790 HSRIP---------EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK---------- 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 993 eahqqtlddlhMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEgnlklnrESMENLESSQRHLAEEL 1072
Cdd:TIGR02169 851 -----------SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE-------AQLRELERKIEELEAQI 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1073 RKKELELSQMNSKVENEKGLVAQLQKTVKELQtqiKDLKEKLEAErttraKMERERADLTQDLadlnERLEEVGGSSLAQ 1152
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEIEDPKGEDE---EIPEEELSLE-----DVQAELQRVEEEI----RALEPVNMLAIQE 980
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1981090065 1153 LEITKKQETKFQ-KLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDD 1222
Cdd:TIGR02169 981 YEEVLKRLDELKeKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELSGGTGELILENPD 1051
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1041-1239 |
2.28e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1041 ERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTT 1120
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1121 RAKM--------ERERADL---TQDLADLNERLEEVGGSSLAQLEITKKQETKFQKLHRDMEEATLHFETTSAsLKKRHA 1189
Cdd:COG4942 106 LAELlralyrlgRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA-LLAELE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1190 DSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEK 1239
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1298-1704 |
2.54e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1298 SNFTRQIEDLRGQLEKETKSQSALAHA---LQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEM--VQWRMKYENNVI 1372
Cdd:PRK04863 272 ADYMRHANERRVHLEEALELRRELYTSrrqLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlVQTALRQQEKIE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1373 QRTEDLEdakkELAIRLQEAAEAMGVANARNASLERarhqlqlelgdalsdlgkvRSAAARLDQKQLQSGkaLADWKQKH 1452
Cdd:PRK04863 352 RYQADLE----ELEERLEEQNEVVEEADEQQEENEA-------------------RAEAAEEEVDELKSQ--LADYQQAL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1453 EESQALLDASQKEVQAL--STELLKLKNTYEESIVG-QETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLI---- 1525
Cdd:PRK04863 407 DVQQTRAIQYQQAVQALerAKQLCGLPDLTADNAEDwLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVrkia 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1526 -EEEKTEVQVTLEETEGALErnESKILHFQLELLEAK-AELERKLSEKDEEIENFRRKQQctidSLQSSLDSEAksriEV 1603
Cdd:PRK04863 487 gEVSRSEAWDVARELLRRLR--EQRHLAEQLQQLRMRlSELEQRLRQQQRAERLLAEFCK----RLGKNLDDED----EL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1604 TRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQ------MQLDDS-TQLNSDLKEQVAVAERRNSLLQSE 1676
Cdd:PRK04863 557 EQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAarapawLAAQDAlARLREQSGEEFEDSQDVTEYMQQL 636
|
410 420
....*....|....*....|....*...
gi 1981090065 1677 LEDLRSLQEQTERGRRlSEEELLEATER 1704
Cdd:PRK04863 637 LERERELTVERDELAA-RKQALDEEIER 663
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
845-1496 |
2.69e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.13 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 845 KEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQcEWLIKSKIQLEARVKELSERVEEEEEI 924
Cdd:TIGR00618 292 AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-RRLLQTLHSQEIHIRDAHEVATSIREI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 925 NS---ELTARGRKLEDEcfelkKEIDDLETMLVKSEKEKRTTE-HKVKNLTEEVEFLNEDISKLN-------RAAKVVQE 993
Cdd:TIGR00618 371 SCqqhTLTQHIHTLQQQ-----KTTLTQKLQSLCKELDILQREqATIDTRTSAFRDLQGQLAHAKkqqelqqRYAELCAA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 994 AHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQerkarmncERELHKLEGNLKlnresmENLESSQRHLAEELR 1073
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ--------ETRKKAVVLARL------LELQEEPCPLCGSCI 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1074 KKELELSQMNSKVENEKgLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGgsslAQL 1153
Cdd:TIGR00618 512 HPNPARQDIDNPGPLTR-RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSK----EDI 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1154 EITKKQETKFQKL--HRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEvddlLTRVEQMT 1231
Cdd:TIGR00618 587 PNLQNITVRLQDLteKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT----LTQERVRE 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1232 RAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLwsesgEFLRRLEEKEALINQLSREKSNFTR-QIEDLRGQ 1310
Cdd:TIGR00618 663 HALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQ-----TLLRELETHIEEYDREFNEIENASSsLGSDLAAR 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1311 LEketksqsALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQ 1390
Cdd:TIGR00618 738 ED-------ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQ 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1391 EAAEAMGVANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALS 1470
Cdd:TIGR00618 811 EIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDG 890
|
650 660 670
....*....|....*....|....*....|....*...
gi 1981090065 1471 TELLK------------LKNTYEESIVGQETLRRENKN 1496
Cdd:TIGR00618 891 DALIKflheitlyanvrLANQSEGRFHGRYADSHVNAR 928
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
960-1175 |
2.71e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 960 KRTTEHKVKNLTEEVEFLNEdisKLNRAAKVVQEAhQQTLDDLhMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMN 1039
Cdd:COG3206 163 EQNLELRREEARKALEFLEE---QLPELRKELEEA-EAALEEF-RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1040 CERELHKLEGNLKLNRESMENLESSQ--RHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAE 1117
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1981090065 1118 -RTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETK---FQKLHRDMEEATL 1175
Cdd:COG3206 318 lEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVArelYESLLQRLEEARL 379
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1062-1230 |
3.38e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.39 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1062 ESSQRHLaEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNER 1141
Cdd:COG1579 3 PEDLRAL-LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1142 LEEVggSSLAQLEITKKQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVD 1221
Cdd:COG1579 82 LGNV--RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
....*....
gi 1981090065 1222 DLLTRVEQM 1230
Cdd:COG1579 160 ELEAEREEL 168
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1307-1707 |
5.21e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.96 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1307 LRGQLEKETKSQSALAhaLQKAQRDCdllREQYEEEQEVKAELHRTLSKVNA----------------EMVQWRMKYENN 1370
Cdd:COG3096 274 MRHANERRELSERALE--LRRELFGA---RRQLAEEQYRLVEMARELEELSAresdleqdyqaasdhlNLVQTALRQQEK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1371 VIQRTEDLEdakkELAIRLQEAAEAmgvanARNASLERARHQLQLElgdalsdlgkvrsaAARLDQKQLQSGkaLADWKQ 1450
Cdd:COG3096 349 IERYQEDLE----ELTERLEEQEEV-----VEEAAEQLAEAEARLE--------------AAEEEVDSLKSQ--LADYQQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1451 KHEESQALLDASQKEVQAL--STELLKLKNTYEESIVG-QETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEE 1527
Cdd:COG3096 404 ALDVQQTRAIQYQQAVQALekARALCGLPDLTPENAEDyLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCK 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1528 EKTEVqvtleETEGALER--------NESKILHFQLELLEAK-AELERKLSEKdeeiENFRRKQQctidSLQSSLDSEAK 1598
Cdd:COG3096 484 IAGEV-----ERSQAWQTarellrryRSQQALAQRLQQLRAQlAELEQRLRQQ----QNAERLLE----EFCQRIGQQLD 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1599 SRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQ----LDDSTQLNSdLKEQVAVAerrnsllq 1674
Cdd:COG3096 551 AAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawLAAQDALER-LREQSGEA-------- 621
|
410 420 430
....*....|....*....|....*....|....*....
gi 1981090065 1675 seLEDLRSLQE------QTERGRRLSEEELLEATERINL 1707
Cdd:COG3096 622 --LADSQEVTAamqqllEREREATVERDELAARKQALES 658
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
934-1525 |
7.07e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.52 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 934 KLEDECFELKKEIDDLE---TMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEE--- 1007
Cdd:PRK01156 163 SLERNYDKLKDVIDMLRaeiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSaln 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1008 KLSSLSKANLKLEQQVDELEGALEQErkarmncERELHKLEGnlkLNRESMENLESSQRHLAEELRKKELELSQMNSKVE 1087
Cdd:PRK01156 243 ELSSLEDMKNRYESEIKTAESDLSME-------LEKNNYYKE---LEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1088 NEKGLVAQLQKtvkeLQTQIKDLKEkLEAERTTRAKMERERADLTQDLADLNERLEEVGG--SSLAQLEITKKQETKFQK 1165
Cdd:PRK01156 313 ILSNIDAEINK----YHAIIKKLSV-LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSylKSIESLKKKIEEYSKNIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1166 LHRDMEEATLHFETTSAS-LKKRHAD---SLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTR----VEQMTRAKANA 1237
Cdd:PRK01156 388 RMSAFISEILKIQEIDPDaIKKELNEinvKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpVCGTTLGEEKS 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1238 EKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSesgeFLRRLEEKEAlinqlsREKSNFTRQIEDLRGQLEKETKS 1317
Cdd:PRK01156 468 NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKK----RKEYLESEEI------NKSINEYNKIESARADLEDIKIK 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1318 QSALAHALQKAQR--------DCDLLREQYEEEQEVKAELhrtlSKVNAEMVQWRmkyENNVIQRTEDLEDAKKELAIRL 1389
Cdd:PRK01156 538 INELKDKHDKYEEiknrykslKLEDLDSKRTSWLNALAVI----SLIDIETNRSR---SNEIKKQLNDLESRLQEIEIGF 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1390 QEaaeamgVANARNASLERARHQLQLeLGDALSDLGKVRSAAARLdQKQLQSGKALADWKQKHEESQALLDASQKEVQal 1469
Cdd:PRK01156 611 PD------DKSYIDKSIREIENEANN-LNNKYNEIQENKILIEKL-RGKIDNYKKQIAEIDSIIPDLKEITSRINDIE-- 680
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1981090065 1470 sTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLI 1525
Cdd:PRK01156 681 -DNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1294-1926 |
7.85e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1294 SREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQ 1373
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1374 RTEDLEDAKKELAIRLQEAAEAMGVANARnaSLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHE 1453
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEVRKAE--ELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAE 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1454 ESQalldaSQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEisnltnqvregtknLTEMEKVKKLIEEEKTEVQ 1533
Cdd:PTZ00121 1241 EAK-----KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE--------------LKKAEEKKKADEAKKAEEK 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1534 VTLEETEG-ALERNESKILHFQLELLEAKAE-LERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRLKKKME 1611
Cdd:PTZ00121 1302 KKADEAKKkAEEAKKADEAKKKAEEAKKKADaAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1612 EDLNEMElqlscANRQVSEATKSLGQLQIQIKDLQMQldDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERG- 1690
Cdd:PTZ00121 1382 AAKKKAE-----EKKKADEAKKKAEEDKKKADELKKA--AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAe 1454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1691 -RRLSEEELLEATERinlfytQNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIA 1769
Cdd:PTZ00121 1455 eAKKAEEAKKKAEEA------KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1770 HLERTRENMEQTITDLQKRLAEAEQMALMGSRKQIQKLESRvRELEGELEGEIRRSAEAQRGArrlERCIKELTYQAEED 1849
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA-KKAEEDKNMALRKAEEAKKAE---EARIEEVMKLYEEE 1604
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981090065 1850 KKNLSRMQTQMDKLQLKVQNYKQQVEVAEtqanqylsKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQEE 1926
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKK--------KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1582-1795 |
9.22e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 9.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1582 QQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLddstqlnSDLKE 1661
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------AELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1662 QVAVAERRNSLLQSELED-LRSLQEQTERGR---RLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVV 1737
Cdd:COG4942 91 EIAELRAELEAQKEELAElLRALYRLGRQPPlalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1981090065 1738 QECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQM 1795
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1317-1686 |
9.35e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.15 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1317 SQSALAHALQKA--------QRDCDLLREQYEEEQEVKA---ELHRTLS------KVNAEMVQwrmkYENNVIQRTEDLE 1379
Cdd:PRK11281 22 LSSAFARAASNGdlpteadvQAQLDALNKQKLLEAEDKLvqqDLEQTLAlldkidRQKEETEQ----LKQQLAQAPAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1380 DAKKELAiRLQEAAEAMGVANARNASLErarhQLQLELGDALSDLGKVRSAAARLDQKqlqsgkaLADWKQKHEESQALL 1459
Cdd:PRK11281 98 QAQAELE-ALKDDNDEETRETLSTLSLR----QLESRLAQTLDQLQNAQNDLAEYNSQ-------LVSLQTQPERAQAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1460 DASQKEVQALSTELLKLKntyeesiVGQETLRRENKN-LQEEISNLTNQVREGTKNLtemekvkklieEEKTEVQVTLEE 1538
Cdd:PRK11281 166 YANSQRLQQIRNLLKGGK-------VGGKALRPSQRVlLQAEQALLNAQNDLQRKSL-----------EGNTQLQDLLQK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1539 tegalerneskilhfQLELLEAK-AELERKLSEKDEEIENFRRKQ-QCTIDSLQSSldsEAKSRIEVTRLKKKmEEDLNe 1616
Cdd:PRK11281 228 ---------------QRDYLTARiQRLEHQLQLLQEAINSKRLTLsEKTVQEAQSQ---DEAARIQANPLVAQ-ELEIN- 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1617 meLQLSCANRQVSEATKSLGQLQIQIKDlqmQLDDSTQLNSDLKEQVAVAerRNSLLQSeledlRSLQEQ 1686
Cdd:PRK11281 288 --LQLSQRLLKATEKLNTLTQQNLRVKN---WLDRLTQSERNIKEQISVL--KGSLLLS-----RILYQQ 345
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
844-1143 |
1.06e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.97 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 844 LKEECAQLQKALEKSEFQREELKAKQVSLTQEKndlilQLQAEQETLAnVEEQCEWlikSKIQLEARVKELSERVEEEEE 923
Cdd:pfam17380 301 LRQEKEEKAREVERRRKLEEAEKARQAEMDRQA-----AIYAEQERMA-MEREREL---ERIRQEERKRELERIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 924 INSEltaRGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEveflnedISKLNRAAKVVQEAHQQTLDDLH 1003
Cdd:pfam17380 372 MEIS---RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQ-------KVEMEQIRAEQEEARQREVRRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1004 MEEEK-LSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMEN-LESSQRHLAEELRK-----KE 1076
Cdd:pfam17380 442 EERAReMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKeLEERKQAMIEEERKrklleKE 521
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1981090065 1077 LELSQMNSKVENEKGLVAQLQKTVKELQT--QIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLE 1143
Cdd:pfam17380 522 MEERQKAIYEEERRREAEEERRKQQEMEErrRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1281-1908 |
1.07e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.07 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1281 RRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSAlahALQKAQRDCDLLREQYEEEQEVKAELHrtlsKVNAEM 1360
Cdd:pfam12128 276 SRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADA---AVAKDRSELEALEDQHGAFLDADIETA----AADQEQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1361 V-QWRMKYENnVIQRTEDLEDAKKELAIRLQEAAEAMGVANAR-----NASLERARHQLQLELGDALSDLGKVRSAAarl 1434
Cdd:pfam12128 349 LpSWQSELEN-LEERLKALTGKHQDVTAKYNRRRSKIKEQNNRdiagiKDKLAKIREARDRQLAVAEDDLQALESEL--- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1435 dQKQLQSGKA-LADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKnlqeEISNLTNQVREGTK 1513
Cdd:pfam12128 425 -REQLEAGKLeFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANA----EVERLQSELRQARK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1514 NLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHF----------QLELLEAKAELERklSEKDEEIENFRRKQQ 1583
Cdd:pfam12128 500 RRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFlrkeapdweqSIGKVISPELLHR--TDLDPEVWDGSVGGE 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1584 CTIDSLQssLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQL--NSDLKE 1661
Cdd:pfam12128 578 LNLYGVK--LDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTAlkNARLDL 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1662 QVAVAERRNSLLQseledlrsLQEQTERGRRLSEEEL--LEATERINLFYTQNTSLLSQKKKLEADVARMQK----EAEE 1735
Cdd:pfam12128 656 RRLFDEKQSEKDK--------KNKALAERKDSANERLnsLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYwqvvEGAL 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1736 VVQECQNAEEKAKKAAIEAANLSE-------ELKKK---QDTIAHLERTRENMEQTITDLQKRLAEAEQMalmgsRKQIQ 1805
Cdd:pfam12128 728 DAQLALLKAAIAARRSGAKAELKAletwykrDLASLgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRY-----FDWYQ 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1806 KLESRVRELEGELEGEIRRSAEAQRGarrlercikELTYQAEEDKKNLSRMQTQMDKLQlkvqnyKQQVEvaetqANQYL 1885
Cdd:pfam12128 803 ETWLQRRPRLATQLSNIERAISELQQ---------QLARLIADTKLRRAKLEMERKASE------KQQVR-----LSENL 862
|
650 660
....*....|....*....|...
gi 1981090065 1886 SKYKKQQHELNEVKERAEVAESQ 1908
Cdd:pfam12128 863 RGLRCEMSKLATLKEDANSEQAQ 885
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1097-1348 |
1.11e-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: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1097 QKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVggsslaqleitkkqetkfQKLHRDMEEATLH 1176
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL------------------ARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1177 FETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEvddLLTRVEQMTRAKANAEKLCTLYEERLheatAKLD 1256
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLA---LLLSPEDFLDAVRRLQYLKYLAPARR----EQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1257 KVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSnftrQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLR 1336
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|..
gi 1981090065 1337 EQYEEEQEVKAE 1348
Cdd:COG4942 230 ARLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
841-1195 |
1.43e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 841 VAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDL--ILQLQAEQETLANVEEQCEwlikskiQLEARVKELSERv 918
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIA-------ELEAELERLDAS- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 919 eeeeeiNSELTARGRKLEdecfELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEdisKLNRAAKVVQEAHQQT 998
Cdd:COG4913 684 ------SDDLAALEEQLE----ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD---RLEAAEDLARLELRAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 999 LDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLN-RESMENLESSQRHLaEELRKKEL 1077
Cdd:COG4913 751 LEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADlDADLESLPEYLALL-DRLEEDGL 829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1078 ElsqmnskvenekglvaqlqktvkELQTQIKDLKEKLEAERTTR--AKMERERADLTQDLADLNERLEEV---GGSSLaQ 1152
Cdd:COG4913 830 P-----------------------EYEERFKELLNENSIEFVADllSKLRRAIREIKERIDPLNDSLKRIpfgPGRYL-R 885
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1981090065 1153 LEITKKQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAEL 1195
Cdd:COG4913 886 LEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRL 928
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1076-1320 |
1.44e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1076 ELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEvggsslaqlei 1155
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1156 tkkQETKFQKLHRDMEEATLHFETTSASLKkrhADSLAELEGQVENLQQV----KQKLEKDKSDlQLEVDDLLTRVEQmt 1231
Cdd:COG3883 84 ---RREELGERARALYRSGGSVSYLDVLLG---SESFSDFLDRLSALSKIadadADLLEELKAD-KAELEAKKAELEA-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1232 rAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQL 1311
Cdd:COG3883 155 -KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
....*....
gi 1981090065 1312 EKETKSQSA 1320
Cdd:COG3883 234 AAAAAAAAA 242
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1047-1907 |
1.63e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1047 LEGNLKLNRESMENLESSQRHlaEELRKKELELSQMNS-----KVENEK----GLVAQLQKTVKELQTQIKDLKEKLEAE 1117
Cdd:PRK04863 235 MEAALRENRMTLEAIRVTQSD--RDLFKHLITESTNYVaadymRHANERrvhlEEALELRRELYTSRRQLAAEQYRLVEM 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1118 RTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQEtkfqklhrDMEEATLHFETtSASLKKRHADSLAELEG 1197
Cdd:PRK04863 313 ARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQA--------DLEELEERLEE-QNEVVEEADEQQEENEA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1198 QVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKA---NAEKLCTL-------YEERLHEATAKLDKVTQLANDLA- 1266
Cdd:PRK04863 384 RAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQaleRAKQLCGLpdltadnAEDWLEEFQAKEQEATEELLSLEq 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1267 ------------AQKTKL-------------WSESGEFLRRLEEKEALINQLSREKsnftRQIEDLRGQLEKETKSQSAL 1321
Cdd:PRK04863 464 klsvaqaahsqfEQAYQLvrkiagevsrseaWDVARELLRRLREQRHLAEQLQQLR----MRLSELEQRLRQQQRAERLL 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1322 AHALQKAQRDCDL--LREQYEEEQEVKAElhrTLSKVNAEMVQWRMkyennviqrteDLEDAKKELAIRLQeaaeamgva 1399
Cdd:PRK04863 540 AEFCKRLGKNLDDedELEQLQEELEARLE---SLSESVSEARERRM-----------ALRQQLEQLQARIQ--------- 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1400 naRNASLERARHQLQlelgDALSDLGKvrsaaarldqkqlQSGKALADwkqkheesqalldaSQKEVQALSTELLKLKNT 1479
Cdd:PRK04863 597 --RLAARAPAWLAAQ----DALARLRE-------------QSGEEFED--------------SQDVTEYMQQLLEREREL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1480 YEESivgqETLRRENKNLQEEISNLTNqvREGTknltEMEKVKKLIE----EEKTEV--QVTLEE---TEGALERNESKI 1550
Cdd:PRK04863 644 TVER----DELAARKQALDEEIERLSQ--PGGS----EDPRLNALAErfggVLLSEIydDVSLEDapyFSALYGPARHAI 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1551 LHFQLELLEAK----------------------------AELER----KLSEKDEEIENF-------RRKQQCTIDSLQS 1591
Cdd:PRK04863 714 VVPDLSDAAEQlagledcpedlyliegdpdsfddsvfsvEELEKavvvKIADRQWRYSRFpevplfgRAAREKRIEQLRA 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1592 SLDSE----AKSRIEVTRLKKkMEEDLNEM-------------ELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDdstq 1654
Cdd:PRK04863 794 EREELaeryATLSFDVQKLQR-LHQAFSRFigshlavafeadpEAELRQLNRRRVELERALADHESQEQQQRSQLE---- 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1655 lnsDLKEQVavaerrnSLLQsELEDLRSLQEQTERGRRLSE-EELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEA 1733
Cdd:PRK04863 869 ---QAKEGL-------SALN-RLLPRLNLLADETLADRVEEiREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQF 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1734 EEVVQECQNAEEKAKKAAIEAANLSEELKKK-----QDTIAHLERTRENMEQtitdLQKRLAEAEQMALMgSRKQIQKLE 1808
Cdd:PRK04863 938 EQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEMLAKNSDLNEK----LRQRLEQAEQERTR-AREQLRQAQ 1012
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1809 SRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKnlSRMQTQMDKLQlkvqnykQQVEVAETQANQYLSKY 1888
Cdd:PRK04863 1013 AQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAE--ERARARRDELH-------ARLSANRSRRNQLEKQL 1083
|
970
....*....|....*....
gi 1981090065 1889 KKQQHELNEVKERAEVAES 1907
Cdd:PRK04863 1084 TFCEAEMDNLTKKLRKLER 1102
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
954-1152 |
2.04e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 954 VKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQE 1033
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1034 RKARMNCERELHKLE-----GNLK--LNR-ESMENLESSQRHLAEELRKKELELSQMNSKVENEKG----LVAQLQKTVK 1101
Cdd:COG3883 92 ARALYRSGGSVSYLDvllgsESFSdfLDRlSALSKIADADADLLEELKADKAELEAKKAELEAKLAeleaLKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1981090065 1102 ELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQ 1152
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1514-1695 |
2.41e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1514 NLTEMEKVKKLIEEEKTEVQVTLEETEGALE--RNESKILHFQLE---LLEAKAELERKLSEKDEEIENFRRKqqctIDS 1588
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEaklLLQQLSELESQLAEARAELAEAEAR----LAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1589 LQSSLDS--EAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQ-LNSDLKEQVAV 1665
Cdd:COG3206 245 LRAQLGSgpDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQrILASLEAELEA 324
|
170 180 190
....*....|....*....|....*....|.
gi 1981090065 1666 AERRNSLLQSELEDLRS-LQEQTERGRRLSE 1695
Cdd:COG3206 325 LQAREASLQAQLAQLEArLAELPELEAELRR 355
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1267-1913 |
2.65e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1267 AQKTKLWSESGEFLRR-----LEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLRE---- 1337
Cdd:pfam05483 87 AEKIKKWKVSIEAELKqkenkLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKEtcar 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1338 ------QYEEEQEVKAELHRTLSKVNAEMVqwrMKYENNVIQRtedlEDAKKELAIRLQEAAEAMG-VANARNASLERAR 1410
Cdd:pfam05483 167 saektkKYEYEREETRQVYMDLNNNIEKMI---LAFEELRVQA----ENARLEMHFKLKEDHEKIQhLEEEYKKEINDKE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1411 HQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEEsqalLDASQKEVQALSTELLKLKNTYEESIVGQETL 1490
Cdd:pfam05483 240 KQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDEN----LKELIEKKDHLTKELEDIKMSLQRSMSTQKAL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1491 RRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEE----TEGALERNESKILHFQLELLEAKAELEr 1566
Cdd:pfam05483 316 EEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEllrtEQQRLEKNEDQLKIITMELQKKSSELE- 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1567 klsekdeEIENFRRKQQCTIDSLQSSLdSEAKSRIEVTRLKKKMEEDLNEMELQLscanrqvseatksLGQLQIQIKDLQ 1646
Cdd:pfam05483 395 -------EMTKFKNNKEVELEELKKIL-AEDEKLLDEKKQFEKIAEELKGKEQEL-------------IFLLQAREKEIH 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1647 mqlddstqlnsDLKEQVAVAERRNSLLQSELEDLRSLQEQtergRRLSEEELLEATERINL----FYTQNTSLLSQKKKL 1722
Cdd:pfam05483 454 -----------DLEIQLTAIKTSEEHYLKEVEDLKTELEK----EKLKNIELTAHCDKLLLenkeLTQEASDMTLELKKH 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1723 EADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTI-AHLERTRENmeqtitdlqkrlAEAEQMALMGSR 1801
Cdd:pfam05483 519 QEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVkCKLDKSEEN------------ARSIEYEVLKKE 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1802 KQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERcikeltyQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQA 1881
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKK-------KGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNY 659
|
650 660 670
....*....|....*....|....*....|..
gi 1981090065 1882 NQYLSKYKKQQHELNEVKERAEVAESQVNKLK 1913
Cdd:pfam05483 660 QKEIEDKKISEEKLLEEVEKAKAIADEAVKLQ 691
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
906-1144 |
3.21e-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: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 906 QLEARVKelserveeeeeinsELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLN 985
Cdd:COG4942 24 EAEAELE--------------QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 986 RAAKVVQEahqqtldDLHMEEEKLSSLSKANLKLEQQvDELEGALEQERKARMncERELHKLEGNLKLNRESMENLESSQ 1065
Cdd:COG4942 90 KEIAELRA-------ELEAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLDA--VRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1981090065 1066 RHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEE 1144
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1190-1580 |
3.44e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1190 DSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEklctlYEERLHEATAKLDkvtqlandlaaqk 1269
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-----LYQELEALEAELA------------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1270 tklwsESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAH-ALQKAQRDCDLLREQYEEEQEVKAE 1348
Cdd:COG4717 143 -----ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1349 LHRTLSKVNAEMVQWRMKYENNVIQRT----------------------------------------------EDLEDAK 1382
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERlkearlllliaaallallglggsllsliltiagvlflvlgllallfLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1383 KELAIRLQEAAEAMGVANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQsgkaladwkQKHEESQALLDAS 1462
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE---------AEELEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1463 QKEVQALsteLLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKV--KKLIEEEKTEVQVTLEETE 1540
Cdd:COG4717 369 EQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELE 445
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1981090065 1541 GALERNESKI--LHFQLELLEAKAELERKLSEKDEEIENFRR 1580
Cdd:COG4717 446 EELEELREELaeLEAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1426-1913 |
4.60e-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: 51.89 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1426 KVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTyEESIVGQETLRRENKNLQEEISNLT 1505
Cdd:TIGR00618 188 KKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQS-HAYLTQKREAQEEQLKKQQLLKQLR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1506 NQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETegALERNESKILHFQLELLEAKAELERKLSEKDEEIENfRRKQQCT 1585
Cdd:TIGR00618 267 ARIEELRAQEAVLEETQERINRARKAAPLAAHIK--AVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ-QSSIEEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1586 IDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMEL-----QLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLK 1660
Cdd:TIGR00618 344 RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLtqhihTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQ 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1661 EQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERinlfYTQNTSLLSQKKKLEADVARMQKEAEEVVQEC 1740
Cdd:TIGR00618 424 GQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQS----LKEREQQLQTKEQIHLQETRKKAVVLARLLEL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1741 QNAE---EKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLqkrlaEAEQMALMGSRKQIQKLESRVRELEGE 1817
Cdd:TIGR00618 500 QEEPcplCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDV-----YHQLTSERKQRASLKEQMQEIQQSFSI 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1818 LEGEIRRSAEAQRGARRL-ERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELN 1896
Cdd:TIGR00618 575 LTQCDNRSKEDIPNLQNItVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT 654
|
490
....*....|....*..
gi 1981090065 1897 EVKERAEVAESQVNKLK 1913
Cdd:TIGR00618 655 LTQERVREHALSIRVLP 671
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1562-1794 |
5.10e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1562 AELERKLSEKDEEIENFRRKQQctidslqsSLDSEAKSRIEVTRLKKkMEEDLNEMELQLSCANRQVSEATKSLGQLQIQ 1641
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNG--------LVDLSEEAKLLLQQLSE-LESQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1642 IKDLQmqlddSTQLNSDLKEQVAVAERRNSLLQSEL----EDLRSLQEQTERGRRLSEEELLEATERINlfyTQNTSLLS 1717
Cdd:COG3206 256 LPELL-----QSPVIQQLRAQLAELEAELAELSARYtpnhPDVIALRAQIAALRAQLQQEAQRILASLE---AELEALQA 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981090065 1718 QKKKLEADVARMQKEAEEvvqecqnaeekakkaaieaanlseeLKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQ 1794
Cdd:COG3206 328 REASLQAQLAQLEARLAE-------------------------LPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1218-1843 |
5.56e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1218 LEVDDLLTRVEQMtraKANAEKLctlyeERLHEATAKL-DKVTQLA--NDLAAQKTKLWsesgeflRRLEEKEALINQLS 1294
Cdd:COG4913 218 LEEPDTFEAADAL---VEHFDDL-----ERAHEALEDArEQIELLEpiRELAERYAAAR-------ERLAELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1295 REKSnfTRQIEDLRGQLEketksqsALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNaemvqwrmkyennviqr 1374
Cdd:COG4913 283 LWFA--QRRLELLEAELE-------ELRAELARLEAELERLEARLDALREELDELEAQIRGNG----------------- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1375 TEDLEDAKKELAirlqeaaeamgvanarnaslerarhQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALAdwkqkhee 1454
Cdd:COG4913 337 GDRLEQLEREIE-------------------------RLERELEERERRRARLEALLAALGLPLPASAEEFA-------- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1455 sqALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLtnqvREGTKNLT-EMEKVKKLIEEE--KTE 1531
Cdd:COG4913 384 --ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL----ERRKSNIPaRLLALRDALAEAlgLDE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1532 ---------VQVTLEET--EGALERneskILH-FQLELLeAKAELERKLSEKdeeIENFRRKQQCTIDSLQSSLDSEAKS 1599
Cdd:COG4913 458 aelpfvgelIEVRPEEErwRGAIER----VLGgFALTLL-VPPEHYAAALRW---VNRLHLRGRLVYERVRTGLPDPERP 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1600 RIEVTRLKKKMEEDLN------EMEL-------------QLSCANRQVSEA--TKSLGQLQiqikdlqmQLDDSTQLNSD 1658
Cdd:COG4913 530 RLDPDSLAGKLDFKPHpfrawlEAELgrrfdyvcvdspeELRRHPRAITRAgqVKGNGTRH--------EKDDRRRIRSR 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1659 -------------LKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNT--SLLSQKKKLE 1723
Cdd:COG4913 602 yvlgfdnraklaaLEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaELEAELERLD 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1724 A---DVARMQKEAEEVVQEcqnaeekakkaaieAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGS 1800
Cdd:COG4913 682 AssdDLAALEEQLEELEAE--------------LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1981090065 1801 RkqiQKLESRVRELEG-ELEGEIRRSAEAQRGA--RRLERCIKELT 1843
Cdd:COG4913 748 R---ALLEERFAAALGdAVERELRENLEERIDAlrARLNRAEEELE 790
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1404-1905 |
5.79e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 51.36 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1404 ASLERARHQLQLELgDALSDLGKVRSAAARLDQKQLQSGKALADW-KQKHEESQALLDASQKEVQALSTELLKLKNTYEE 1482
Cdd:pfam10174 243 SSLERNIRDLEDEV-QMLKTNGLLHTEDREEEIKQMEVYKSHSKFmKNKIDQLKQELSKKESELLALQTKLETLTNQNSD 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1483 SI----VGQETLRRENKN---LQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILhfql 1555
Cdd:pfam10174 322 CKqhieVLKESLTAKEQRaaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKIN---- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1556 eLLEAKAE-LERKLSEKDEEIENFRRKQQ------CTIDSLQSSLDsEA---KSRIeVTRLKKKME-EDLNEMElqlsca 1624
Cdd:pfam10174 398 -VLQKKIEnLQEQLRDKDKQLAGLKERVKslqtdsSNTDTALTTLE-EAlseKERI-IERLKEQRErEDRERLE------ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1625 nrQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLR-SLQEQTERGRRLseEELLEATE 1703
Cdd:pfam10174 469 --ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEiAVEQKKEECSKL--ENQLKKAH 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1704 RINLFYTQNTSLLSQKKKLEADVARMQKEAeevvqecqnaeekakkaaieaanlseelKKKQDTIAHLERTRENMEQTIT 1783
Cdd:pfam10174 545 NAEEAVRTNPEINDRIRLLEQEVARYKEES----------------------------GKAQAEVERLLGILREVENEKN 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1784 DLQKRLAEAEQMALmgsrKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKE--LTYQAEEDKKNLSRMQTQMD 1861
Cdd:pfam10174 597 DKDKKIAELESLTL----RQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADnsQQLQLEELMGALEKTRQELD 672
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1981090065 1862 KLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEVKERAEVA 1905
Cdd:pfam10174 673 ATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLA 716
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
576-667 |
5.82e-06 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 48.50 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 576 GVVPY---NISGWLEKNKDLLNETVVAVFQKSSNRLLAslfenymstdsAIPFGEKKR-----------KKGASFQTVAS 641
Cdd:cd01363 71 GVIPYlasVAFNGINKGETEGWVYLTEITVTLEDQILQ-----------ANPILEAFGnakttrnenssRFGKFIEILLD 139
|
90 100 110
....*....|....*....|....*....|.
gi 1981090065 642 L-----HKENLNKLMTNLKSTAPHFVRCINP 667
Cdd:cd01363 140 IagfeiINESLNTLMNVLRATRPHFVRCISP 170
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1380-1912 |
6.69e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 51.36 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1380 DAKKELAIRLQEAAEAMGVANARNASLERARHqLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALL 1459
Cdd:pfam10174 40 ELKKERALRKEEAARISVLKEQYRVTQEENQH-LQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1460 DASQKEVQALSTELLKLKNTYEE---SIVGQ--------ETLRRENKNLQ---------EEISNLTNQVREGTKNLTEME 1519
Cdd:pfam10174 119 RRLQSEHERQAKELFLLRKTLEEmelRIETQkqtlgardESIKKLLEMLQskglpkksgEEDWERTRRIAEAEMQLGHLE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1520 KVKKLIEEEKTEVQVTLE-ETEGALERNESKILHFQLELLEAK-AELERKLSEKDEEIEnfrrkqqctidSLQSSLDSEA 1597
Cdd:pfam10174 199 VLLDQKEKENIHLREELHrRNQLQPDPAKTKALQTVIEMKDTKiSSLERNIRDLEDEVQ-----------MLKTNGLLHT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1598 KSRievtrlkkkmEEDLNEMELQLSCAN---RQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSD-------LKEQVAVAE 1667
Cdd:pfam10174 268 EDR----------EEEIKQMEVYKSHSKfmkNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqhievLKESLTAKE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1668 RRNSLLQSELEDLRS--------LQEQTERGRRLSEE------------ELLEATER-INLFYTQNTSLLSQKKkleaDV 1726
Cdd:pfam10174 338 QRAAILQTEVDALRLrleekesfLNKKTKQLQDLTEEkstlageirdlkDMLDVKERkINVLQKKIENLQEQLR----DK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1727 ARMQKEAEEVVQECQnaeekakkaaIEAANLSEELKKKQDTIAHLERTRENM-EQTITDLQKRLAEAEQMalmgsRKQIQ 1805
Cdd:pfam10174 414 DKQLAGLKERVKSLQ----------TDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESL-----KKENK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1806 KLESRVRELEGELEG--------EIRRSAEAQRGARRLERcIKELTYQAEEDKKNLSRMQTQMDKlqlkvqnyKQQVEVA 1877
Cdd:pfam10174 479 DLKEKVSALQPELTEkesslidlKEHASSLASSGLKKDSK-LKSLEIAVEQKKEECSKLENQLKK--------AHNAEEA 549
|
570 580 590
....*....|....*....|....*....|....*
gi 1981090065 1878 ETQANQYLSKYKKQQHELNEVKERAEVAESQVNKL 1912
Cdd:pfam10174 550 VRTNPEINDRIRLLEQEVARYKEESGKAQAEVERL 584
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1000-1288 |
6.86e-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: 50.84 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1000 DDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELEL 1079
Cdd:pfam19220 27 ADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1080 SQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQ 1159
Cdd:pfam19220 107 EELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1160 ETKFQKLHRDMEEatlhFETTSASLKKRhadsLAELEGQVENLQQVKQK----LEKDKSDLQLEVDDLLTRVEQMTRAKA 1235
Cdd:pfam19220 187 AAELAELTRRLAE----LETQLDATRAR----LRALEGQLAAEQAERERaeaqLEEAVEAHRAERASLRMKLEALTARAA 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1981090065 1236 NAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLwsesgefLRRLEEKEA 1288
Cdd:pfam19220 259 ATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTL-------ERRLAGLEA 304
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1450-1669 |
7.95e-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: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1450 QKHEESQALLDASQKEVQALSTELLKLKNTyeesivgQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEK 1529
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-------EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1530 TEVQVTLEETEGALERNESKI----LHFQLELL---EAKAELERKLsEKDEEIENFRRKQqctIDSLQSSLDSEAKSRIE 1602
Cdd:COG4942 93 AELRAELEAQKEELAELLRALyrlgRQPPLALLlspEDFLDAVRRL-QYLKYLAPARREQ---AEELRADLAELAALRAE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981090065 1603 VTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERR 1669
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1245-1468 |
1.18e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1245 EERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHA 1324
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1325 LQKaqrdcdLLREQYEEEQEVKAELhrTLSKVNAEMVQWRMKYENNVIQ----RTEDLEDAKKELAIRLQEAAEAMGVAN 1400
Cdd:COG4942 106 LAE------LLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAParreQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1981090065 1401 ARNASLERARHQLQLELGDAlsdlgkvRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQA 1468
Cdd:COG4942 178 ALLAELEEERAALEALKAER-------QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1730-1925 |
1.41e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1730 QKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEqmalmgsrKQIQKLES 1809
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE--------KEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1810 RVRELEGELEGEIRR------------------SAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYK 1871
Cdd:COG4942 98 ELEAQKEELAELLRAlyrlgrqpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1981090065 1872 QQVEVAETQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQE 1925
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
839-1113 |
1.51e-05 |
|
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: 50.02 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 839 EEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSERV 918
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 919 EEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQT 998
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 999 LDDLHMEEEKL--SSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKE 1076
Cdd:TIGR04523 544 EDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
250 260 270
....*....|....*....|....*....|....*..
gi 1981090065 1077 LELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEK 1113
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1029-1794 |
2.08e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1029 ALEQERKARMNceRELHKLEGnlklnRESM--ENLESSQRHLA---------EELRKKELELSQMNSKVENEKGLVAQL- 1096
Cdd:COG3096 302 AEEQYRLVEMA--RELEELSA-----RESDleQDYQAASDHLNlvqtalrqqEKIERYQEDLEELTERLEEQEEVVEEAa 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1097 -------------QKTVKELQTQIKDLKEKLEAERT------------TRAKMERERADLTQD-----LADLNERLEEVG 1146
Cdd:COG3096 375 eqlaeaearleaaEEEVDSLKSQLADYQQALDVQQTraiqyqqavqalEKARALCGLPDLTPEnaedyLAAFRAKEQQAT 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1147 gSSLAQLEitkkqetkfQKLhRDMEEATLHFETTSASLKKrhadslaeLEGQVENLQ--QVKQKLEKDKSDLQLevddLL 1224
Cdd:COG3096 455 -EEVLELE---------QKL-SVADAARRQFEKAYELVCK--------IAGEVERSQawQTARELLRRYRSQQA----LA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1225 TRVEQMTRAKANAEKLctlyEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQI 1304
Cdd:COG3096 512 QRLQQLRAQLAELEQR----LRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1305 EDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQwrmkyENNVIQRTEDLEDAKKE 1384
Cdd:COG3096 588 EQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVE-----RDELAARKQALESQIER 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1385 LA-------IRLQEAAEAMG----------------------VANARNA----SLERARHQLQlELGDALSDL----GKV 1427
Cdd:COG3096 663 LSqpggaedPRLLALAERLGgvllseiyddvtledapyfsalYGPARHAivvpDLSAVKEQLA-GLEDCPEDLylieGDP 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1428 RSAAARLDQKQLQSGKALA-----DWKQKHEESQALLD--ASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEE 1500
Cdd:COG3096 742 DSFDDSVFDAEELEDAVVVklsdrQWRYSRFPEVPLFGraAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQF 821
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1501 ISNLTNQVREGtknltEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHF--QLELLEAKAELERKLSEKD--EEIE 1576
Cdd:COG3096 822 VGGHLAVAFAP-----DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLkeQLQLLNKLLPQANLLADETlaDRLE 896
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1577 NFRRKQQCTIDSlQSSLDSEAKSRIEVTRLKKKMEED-LNEMELQLscanrQVSEATKSLGQLQIQIKDLQ--MQ----- 1648
Cdd:COG3096 897 ELREELDAAQEA-QAFIQQHGKALAQLEPLVAVLQSDpEQFEQLQA-----DYLQAKEQQRRLKQQIFALSevVQrrphf 970
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1649 -LDDSTQL---NSDLKEQvavaerrnsllqseledLRSLQEQTERGRRLSEEELLEATERinlfYTQNTSLLSQKKKLEA 1724
Cdd:COG3096 971 sYEDAVGLlgeNSDLNEK-----------------LRARLEQAEEARREAREQLRQAQAQ----YSQYNQVLASLKSSRD 1029
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1981090065 1725 DVARMQKEAEEVVQE--CQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQ 1794
Cdd:COG3096 1030 AKQQTLQELEQELEElgVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAER 1101
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1110-1873 |
2.24e-05 |
|
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: 49.36 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1110 LKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQ-LEITKKQetkFQKLHRDMEEATLHFETTsaslkkrh 1188
Cdd:pfam07111 21 LERRLDTQRPTVTMWEQDVSGDGQGPGRRGRSLELEGSQALSQqAELISRQ---LQELRRLEEEVRLLRETS-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1189 adslaelegqvenLQQvKQKLEKDKSDLqlevdDLLTRVEQMTRAKAnaeklctlyeERLHEATAKLDKVTQlanDLAAQ 1268
Cdd:pfam07111 90 -------------LQQ-KMRLEAQAMEL-----DALAVAEKAGQAEA----------EGLRAALAGAEMVRK---NLEEG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1269 KTKlwsESGEFLRRLEEKEALINQLSREK-SNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQY---EEEQE 1344
Cdd:pfam07111 138 SQR---ELEEIQRLHQEQLSSLTQAHEEAlSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLsktQEELE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1345 VKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAK--KELAIRLQEAAEAMGVanaRNASLErarHQLQLElgdals 1422
Cdd:pfam07111 215 AQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQhlQEDRADLQATVELLQV---RVQSLT---HMLALQ------ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1423 dlgkvrsaAARLDQKQLQSGKALADWKQKheeSQALLDASQKEVQALSTELLKLKNTYEESIvgqetlrrenKNLQEEIS 1502
Cdd:pfam07111 283 --------EEELTRKIQPSDSLEPEFPKK---CRSLLNRWREKVFALMVQLKAQDLEHRDSV----------KQLRGQVA 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1503 NLTNQVregTKNLTEMEKVKKLIEEEKTEVQVtleetegalERNESKILHFQL-ELLEAKAELERKLSEKDEEIENFRRK 1581
Cdd:pfam07111 342 ELQEQV---TSQSQEQAILQRALQDKAAEVEV---------ERMSAKGLQMELsRAQEARRRQQQQTASAEEQLKFVVNA 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1582 QQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVseatkSLGQLQIQIKDLQmqlDDSTQLNSDLKE 1661
Cdd:pfam07111 410 MSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKV-----ALAQLRQESCPPP---PPAPPVDADLSL 481
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1662 QVAVAERRNSLLQSELE-DLRSLQEQTERGRRLSEEELLEaterinlfytqntsLLSQKKKLEADVARMQKEAEEVVQEC 1740
Cdd:pfam07111 482 ELEQLREERNRLDAELQlSAHLIQQEVGRAREQGEAERQQ--------------LSEVAQQLEQELQRAQESLASVGQQL 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1741 QNAEEKAKKAAIEAANLSEELKKKQDTI--AHLERTRE---NMEQTITDLQKRLAEA--EQMALMGSRKQIQK--LESRV 1811
Cdd:pfam07111 548 EVARQGQQESTEEAASLRQELTQQQEIYgqALQEKVAEvetRLREQLSDTKRRLNEArrEQAKAVVSLRQIQHraTQEKE 627
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1981090065 1812 RELEGELEGEIRRSAEAQRGARRLercikeltyQAEEDKKNLSRMQTQMDKLqlkVQNYKQQ 1873
Cdd:pfam07111 628 RNQELRRLQDEARKEEGQRLARRV---------QELERDKNLMLATLQQEGL---LSRYKQQ 677
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
840-1120 |
2.73e-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: 49.33 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 840 EVAGLKEECAQLQKAL-EKSEFQR--EELKAKQvsltqekNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSE 916
Cdd:pfam05483 406 ELEELKKILAEDEKLLdEKKQFEKiaEELKGKE-------QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKT 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 917 RVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQ 996
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFI 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 997 QTLDD----LHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKL-EGNLKLNRESmeNLESSQRHLAE- 1070
Cdd:pfam05483 559 QKGDEvkckLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELhQENKALKKKG--SAENKQLNAYEi 636
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1071 ELRKKELELSQMNSKVENekgLVAQLQKTVKELQTQIKDLKEKLEAERTT 1120
Cdd:pfam05483 637 KVNKLELELASAKQKFEE---IIDNYQKEIEDKKISEEKLLEEVEKAKAI 683
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
933-1256 |
2.88e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 49.08 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 933 RKLEDECFELKKEIDDLETMLVKS---------EKEKRTTEHKVKN------LTEEVEFLNEDISKLNRAAKVVQEAHQQ 997
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPselalnemiEKLKKEIDLEYTEaviamgLQERLENLREEFSKANSQDQLMHPVLME 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 998 TLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLnRESMENLESSQRHlaeELRKKEL 1077
Cdd:PLN03229 512 KIEKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKF-KEVMDRPEIKEKM---EALKAEV 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1078 ELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEK--LEAERTTRAKMERERADLTQDLADLNERLEEvggsslaqlEI 1155
Cdd:PLN03229 588 ASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSmgLEVIGVTKKNKDTAEQTPPPNLQEKIESLNE---------EI 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1156 TKKQE--TKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEgqvenlQQVKQKLEK--DKSDLQLEVDDLltRVEQMT 1231
Cdd:PLN03229 659 NKKIErvIRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALE------QQIKQKIAEalNSSELKEKFEEL--EAELAA 730
|
330 340
....*....|....*....|....*
gi 1981090065 1232 RAKANAEKLCTLYEERLHEATAKLD 1256
Cdd:PLN03229 731 ARETAAESNGSLKNDDDKEEDSKED 755
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1492-1906 |
2.91e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1492 RENKNLQEEISNLTNQVREgtknLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFqlELLEAKAELERKLSEK 1571
Cdd:COG4717 71 KELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEKLLQLL--PLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1572 DEEIENFRRKQQctidslqssldseakSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSlgqlqiQIKDLQMQLDD 1651
Cdd:COG4717 145 PERLEELEERLE---------------ELRELEEELEELEAELAELQEELEELLEQLSLATEE------ELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1652 STQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEE-LLEATERINLFYTQNTSLLSQKKKLEADVA--- 1727
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlLLLIAAALLALLGLGGSLLSLILTIAGVLFlvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1728 -----------RMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQD-TIAHLERTRENMEQTITDLQKRLAEAEQM 1795
Cdd:COG4717 284 gllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1796 ALMGSRKQIQKLesrVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDK--LQLKVQNYKQQ 1873
Cdd:COG4717 364 QLEELEQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEE 440
|
410 420 430
....*....|....*....|....*....|...
gi 1981090065 1874 VEVAETQANQYLSKYKKQQHELNEVKERAEVAE 1906
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1618-1794 |
3.33e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1618 ELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRS-LQEQTER-GRRLSE 1695
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeIEERREElGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1696 -----------EELLEAT---------ERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQNaeeKAKKAAIEAA 1755
Cdd:COG3883 95 lyrsggsvsylDVLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA---LKAELEAAKA 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1981090065 1756 NLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQ 1794
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1385-1600 |
3.43e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1385 LAIRLQEAAEAMGVANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQK 1464
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1465 EVQALSTELLKLKNTYEESIVGQETLRREN------------------KNLQEEISNLTNQVREGTKNLTEMEKVKKLIE 1526
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPplalllspedfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1981090065 1527 EEKTEVQVTLEETEGALERNESKilhfQLELLEAKAELERKLSEKDEEIENFRRKQQcTIDSLQSSLDSEAKSR 1600
Cdd:COG4942 171 AERAELEALLAELEEERAALEAL----KAERQKLLARLEKELAELAAELAELQQEAE-ELEALIARLEAEAAAA 239
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1093-1414 |
4.04e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.58 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1093 VAQLQKTVKELQTQIKdlKEKLEAERTTRAKMERERAdltqdlADLNERLEEVGGSSLAQLEitkKQETKFQKLHRDMEE 1172
Cdd:pfam17380 277 IVQHQKAVSERQQQEK--FEKMEQERLRQEKEEKARE------VERRRKLEEAEKARQAEMD---RQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1173 ATLHFETTSASLKKRHADSLAELEGQVEnLQQVKQkLEKdksdLQLEVDDLLTRVEQMTRAkanAEKLCTLYEERLHeat 1252
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEEIAME-ISRMRE-LER----LQMERQQKNERVRQELEA---ARKVKILEEERQR--- 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1253 akldKVTQLANDLAAQKTKLWSESGEFLRRLEEKEAL-INQLSREKSNFTRQIEDLRGQLEKETKSQSalahALQKAQRD 1331
Cdd:pfam17380 414 ----KIQQQKVEMEQIRAEQEEARQREVRRLEEERAReMERVRLEEQERQQQVERLRQQEEERKRKKL----ELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1332 CDLLREQYEE--EQEVKAELHRTLSKVNA-EMVQWRMKYENNVI----QRTEDLEDAKKELAI----RLQEAAEAMGVAN 1400
Cdd:pfam17380 486 RKRAEEQRRKilEKELEERKQAMIEEERKrKLLEKEMEERQKAIyeeeRRREAEEERRKQQEMeerrRIQEQMRKATEER 565
|
330
....*....|....
gi 1981090065 1401 ARNASLERARHQLQ 1414
Cdd:pfam17380 566 SRLEAMEREREMMR 579
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1279-1697 |
6.53e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1279 FLRRLE-EKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRdcdlLREQYEEEQEVKAELHRTLSKVN 1357
Cdd:COG4717 47 LLERLEkEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1358 AEMVQWRmkyennVIQRTEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQlELGDALSDLGKVRSAAARLDQK 1437
Cdd:COG4717 123 KLLQLLP------LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA-ELQEELEELLEQLSLATEEELQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1438 QLQsgKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEE------------------SIVGQETLRRENKNLQE 1499
Cdd:COG4717 196 DLA--EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAaaleerlkearlllliaaALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1500 EISNL------------TNQVREGTKNLTEMEKVKKLIEEEKTEvQVTLEETEGALERNESKILHFQLELLEAKAELERK 1567
Cdd:COG4717 274 TIAGVlflvlgllallfLLLAREKASLGKEAEELQALPALEELE-EEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1568 LSEKDE-----EIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSE--ATKSLGQLQI 1640
Cdd:COG4717 353 LREAEEleeelQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEE 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1981090065 1641 QIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEE 1697
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1624-1848 |
6.93e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1624 ANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLrslqeqtERGRRLSEEELLEATE 1703
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-------EQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1704 RINlfyTQNTSLLSQKKKLEADVARMQKEAE----------EVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLER 1773
Cdd:COG4942 91 EIA---ELRAELEAQKEELAELLRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1981090065 1774 TRENMEQTITDLQKRLaEAEQMALMGSRKQIQKLESRVRELEGELEGEIrrsAEAQRGARRLERCIKELTYQAEE 1848
Cdd:COG4942 168 ELEAERAELEALLAEL-EEERAALEALKAERQKLLARLEKELAELAAEL---AELQQEAEELEALIARLEAEAAA 238
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1515-1611 |
7.56e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1515 LTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEA-KAELERKLSEKDEEIENFRRKqqctIDSLQSSL 1593
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAeVEELEAELEEKDERIERLERE----LSEARSEE 457
|
90
....*....|....*...
gi 1981090065 1594 DSEAKSRIEVTRLKKKME 1611
Cdd:COG2433 458 RREIRKDREISRLDREIE 475
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
957-1123 |
8.64e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 957 EKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAkvvqEAHQQTLDDLHMEEEKLSSLSKAnlkLEQQVDELEGALEQERKA 1036
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARL----EAAKTELEDLEKEIKRLELEIEE---VEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1037 RmncerELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEA 1116
Cdd:COG1579 89 K-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*..
gi 1981090065 1117 ERTTRAK 1123
Cdd:COG1579 164 EREELAA 170
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
844-1322 |
1.26e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.12 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 844 LKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEwlikskiQLEARVKELSERVEEEEE 923
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAA-------ILQTEVDALRLRLEEKES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 924 INSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLH 1003
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALT 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1004 MEEEKLSSLSKANLKLEQQVDELEGA----LEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELEL 1079
Cdd:pfam10174 440 TLEEALSEKERIIERLKEQREREDRErleeLESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKL 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1080 SQMNSKVENEKglvaqlqKTVKELQTQIKDLKEKLEAERTTRAKMERERAdLTQDLAdlneRLEEVGGSSLAQLEitkkq 1159
Cdd:pfam10174 520 KSLEIAVEQKK-------EECSKLENQLKKAHNAEEAVRTNPEINDRIRL-LEQEVA----RYKEESGKAQAEVE----- 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1160 etKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVddlltRVEQMTRAKANAEK 1239
Cdd:pfam10174 583 --RLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEA-----RRREDNLADNSQQL 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1240 lctlyeeRLHEATAKLDKVTQlanDLAAQKTKLWSESgeflRRLEEKEALINQLSREKsnftrqiedlRGQLEK--ETKS 1317
Cdd:pfam10174 656 -------QLEELMGALEKTRQ---ELDATKARLSSTQ----QSLAEKDGHLTNLRAER----------RKQLEEilEMKQ 711
|
....*
gi 1981090065 1318 QSALA 1322
Cdd:pfam10174 712 EALLA 716
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1303-1912 |
1.26e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1303 QIEDLRGQLE-KETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRmkyennviQRTEDLEDA 1381
Cdd:PRK02224 188 SLDQLKAQIEeKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR--------EELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1382 KKELAIRLQEAAEAMGVANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDA 1461
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1462 SQKEVQALSTELLKLKNTYEEsivgqetLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEG 1541
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEE-------LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAED 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1542 ALE--RNESKILHFQLELLEAKAELERKLSEKDEEIENFRRKQQCTidslQSSLDSEAKSRIEVTRLKK-KMEEDLNEME 1618
Cdd:PRK02224 413 FLEelREERDELREREAELEATLRTARERVEEAEALLEAGKCPECG----QPVEGSPHVETIEEDRERVeELEAELEDLE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1619 LQLSCANRQVSEAtKSLGQLQIQIKDLQMQLDDSTQLnsdlkeqvaVAERRNSLlqseledlrslQEQTERGRRLSEEel 1698
Cdd:PRK02224 489 EEVEEVEERLERA-EDLVEAEDRIERLEERREDLEEL---------IAERRETI-----------EEKRERAEELRER-- 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1699 leaterinlfytqntsllsqKKKLEADVARMQKEAEEVVQECQnaeekakKAAIEAANLSEELKKKQDTIAHLER----- 1773
Cdd:PRK02224 546 --------------------AAELEAEAEEKREAAAEAEEEAE-------EAREEVAELNSKLAELKERIESLERirtll 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1774 -TRENMEQTITDLQKRLaeaEQMALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLErcikelTYQAEEDKKn 1852
Cdd:PRK02224 599 aAIADAEDEIERLREKR---EALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAE------EYLEQVEEK- 668
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1853 LSRMQTQMDKLQLKVQNYKQQVEvaetqanqylskykkqqhELNEVKERAEVAESQVNKL 1912
Cdd:PRK02224 669 LDELREERDDLQAEIGAVENELE------------------ELEELRERREALENRVEAL 710
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
851-1343 |
1.39e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 851 LQKALEKsefQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKelserveeeeeinsELTA 930
Cdd:COG4717 47 LLERLEK---EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE--------------ELEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 931 RGRKLEDECFELKKEIDDLETMLVKSEKEKRTTE--HKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQ----TLDDLHM 1004
Cdd:COG4717 110 ELEELREELEKLEKLLQLLPLYQELEALEAELAElpERLEELEERLEELRELEEELEELEAELAELQEEleelLEQLSLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1005 EEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMNS 1084
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1085 KVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQdlADLNERLEEVGGSSLAQLEITKKQETKFQ 1164
Cdd:COG4717 270 SLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1165 KLHRDMEEAT---------LHFETTSASLKKRHADSLAELEGQVENLQQvKQKLEKDKSDLQLEVDDLLTRVEQMtRAKA 1235
Cdd:COG4717 348 ELQELLREAEeleeelqleELEQEIAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEEL-LEAL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1236 NAEKLctlyEERLHEATAKLDKVTQLANDLAAQKTKLWSEsgefLRRLEEKEALinqlsrekSNFTRQIEDLRGQLEKET 1315
Cdd:COG4717 426 DEEEL----EEELEELEEELEELEEELEELREELAELEAE----LEQLEEDGEL--------AELLQELEELKAELRELA 489
|
490 500
....*....|....*....|....*...
gi 1981090065 1316 KSQSALAHALQKAQRdcdlLREQYEEEQ 1343
Cdd:COG4717 490 EEWAALKLALELLEE----AREEYREER 513
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1282-1790 |
1.45e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.66 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1282 RLEEKEALINQLSREKSNftRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLL-REQYEEEQEVKAElhrTLSKVNAEM 1360
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQ--MELEHKRARIELEKKASALKRQLDRESDRNQELQkRIRLLEKREAEAE---EALREQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1361 VQWRMKYENNVIQRTEDLEDakkelaiRLQEAAEAMGVANARNASLERARHQLQLELGDALSDLGKVRsaaarlDQKQLQ 1440
Cdd:pfam05557 78 NRLKKKYLEALNKKLNEKES-------QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQ------ERLDLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1441 SGKAladwkQKHEESQALLDASQKEvqaLSTELLKLKnTYEESIVGQETLRRENKNLQEEISNLTN------QVREGTKN 1514
Cdd:pfam05557 145 KAKA-----SEAEQLRQNLEKQQSS---LAEAEQRIK-ELEFEIQSQEQDSEIVKNSKSELARIPElekeleRLREHNKH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1515 LTEMEKVKKLIEEEKTEVQVTLEETEGAlerneskilhfqlelLEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSsld 1594
Cdd:pfam05557 216 LNENIENKLLLKEEVEDLKRKLEREEKY---------------REEAATLELEKEKLEQELQSWVKLAQDTGLNLRS--- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1595 SEAKSRievtRLKKKMEEDLNEMElQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQ 1674
Cdd:pfam05557 278 PEDLSR----RIEQLQQREIVLKE-ENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLT 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1675 SELEDLRSLQE-------QTERGRRLSeEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKA 1747
Cdd:pfam05557 353 KERDGYRAILEsydkeltMSNYSPQLL-ERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQE 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1981090065 1748 KKAAIEAANLS-EELKKKQDtiaHLERTRENMEQTITDLQKRLA 1790
Cdd:pfam05557 432 SLADPSYSKEEvDSLRRKLE---TLELERQRLREQKNELEMELE 472
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1189-1433 |
1.57e-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: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1189 ADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQ 1268
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1269 KTKLWSESGEFLR---RLEEKEALINQLSREKSNftrQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEV 1345
Cdd:COG4942 99 LEAQKEELAELLRalyRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1346 KAELhrtlskvnaemvqwrmkyENNVIQRTEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQlelgDALSDLG 1425
Cdd:COG4942 176 LEAL------------------LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE----ALIARLE 233
|
....*...
gi 1981090065 1426 KVRSAAAR 1433
Cdd:COG4942 234 AEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1556-1908 |
1.66e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1556 ELLEAKAELERKLSEKDEEIENFRRKQQctidslqssldsEAKSRIEVTRLK-KKMEEDLNEMELQLSCANRQVSEATKS 1634
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAGISKYKERRK------------ETERKLERTRENlDRLEDILNELERQLKSLERQAEKAERY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1635 LgQLQIQIKDLQMQLddstqLNSDLKEQVAVAERrnslLQSELEDLRSLQEQTERGRRLSEEELLEaterinlfytqnts 1714
Cdd:TIGR02168 216 K-ELKAELRELELAL-----LVLRLEELREELEE----LQEELKEAEEELEELTAELQELEEKLEE-------------- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1715 LLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEq 1794
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK- 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1795 malmgsrkqiqklesrvreleGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQV 1874
Cdd:TIGR02168 351 ---------------------EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
330 340 350
....*....|....*....|....*....|....
gi 1981090065 1875 EvaetQANQYLSKYKKQQHELNEVKERAEVAESQ 1908
Cdd:TIGR02168 410 E----RLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1714-1911 |
1.78e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1714 SLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAE-- 1791
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEll 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1792 --------AEQMALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKL 1863
Cdd:COG4942 111 ralyrlgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1981090065 1864 QLKVQNYKQQVEVAETQANQY---LSKYKKQQHELNEVKERAEVAESQVNK 1911
Cdd:COG4942 191 EALKAERQKLLARLEKELAELaaeLAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1419-1609 |
1.79e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1419 DALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESivgqETLRRENKNLQ 1498
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV----EARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1499 EEISNlTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELERKLSEKDEEIENF 1578
Cdd:COG1579 83 GNVRN-NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170 180 190
....*....|....*....|....*....|.
gi 1981090065 1579 RRKqqctIDSLQSSLDSEAKSRIEVTRLKKK 1609
Cdd:COG1579 162 EAE----REELAAKIPPELLALYERIRKRKN 188
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1025-1165 |
1.98e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1025 ELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGL------------ 1092
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeyea 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981090065 1093 ----VAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKFQK 1165
Cdd:COG1579 94 lqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1462-1926 |
1.99e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1462 SQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEG 1541
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1542 aLERNESKILHFQLELLEAKAELERKLSEKDEEIENFRRKQQCTidslqSSLDSEAKSRIEVTRLKKKMEEDLNEMELQL 1621
Cdd:PRK03918 243 -LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----KELKEKAEEYIKLSEFYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1622 SCANRQVSEatkslgqLQIQIKDLQmqlDDSTQLNSDLKEQVAVAERRNSLLQS--ELEDLRSLQEQTERGR-RLSEEEL 1698
Cdd:PRK03918 317 SRLEEEING-------IEERIKELE---EKEERLEELKKKLKELEKRLEELEERheLYEEAKAKKEELERLKkRLTGLTP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1699 LEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEE-----LKKKQDTIAHLER 1773
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1774 TRENMEQTITDLQKRLAEAEQMALMGSR--------KQIQKLESR------------------VRELEGELEGEIRRSAE 1827
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESEliklkelaEQLKELEEKlkkynleelekkaeeyekLKEKLIKLKGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1828 AQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLK-VQNYKQQVEVAETQANQYLS-------------KYKKQQH 1893
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPFYNEYLElkdaekelereekELKKLEE 626
|
490 500 510
....*....|....*....|....*....|...
gi 1981090065 1894 ELNEVKERAEVAESQVNKLKIKAREFGKKVQEE 1926
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEE 659
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
878-1381 |
2.03e-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: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 878 DLILQLQAEQETLANVEEQCEWLIKSKIQLEA--RVKELSERVEEEEEINsELTARGRKLEDECFELKKEIDDLETMLVK 955
Cdd:COG4913 242 EALEDAREQIELLEPIRELAERYAAARERLAEleYLRAALRLWFAQRRLE-LLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 956 SEKEKRTTEHKVKNL-TEEVEFLNEDISKLNRAAKVVQEAH---QQTLDDLHMEE-------EKLSSLSKANL------- 1017
Cdd:COG4913 321 LREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRarlEALLAALGLPLpasaeefAALRAEAAALLealeeel 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1018 -KLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLessQRHLAEELRKKEL------ELSQMNSKVENEK 1090
Cdd:COG4913 401 eALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL---RDALAEALGLDEAelpfvgELIEVRPEEERWR 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1091 G-------------LV-----AQLQKTVKELqtqikDLKEKL--EAERTTRAKMERERADlTQDLAD------------L 1138
Cdd:COG4913 478 GaiervlggfaltlLVppehyAAALRWVNRL-----HLRGRLvyERVRTGLPDPERPRLD-PDSLAGkldfkphpfrawL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1139 NERLEEVGG----SSLAQLE-----IT-----KKQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQ 1204
Cdd:COG4913 552 EAELGRRFDyvcvDSPEELRrhpraITragqvKGNGTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEE 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1205 VKQKLEKDKSDLQlEVDDLLTRVEQMTRAKANAEKLctlyEERLHEATAKLDKVTQLANDLAA---QKTKLWSESGEFLR 1281
Cdd:COG4913 632 RLEALEAELDALQ-ERREALQRLAEYSWDEIDVASA----EREIAELEAELERLDASSDDLAAleeQLEELEAELEELEE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1282 RLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSA---------LAHALQKAQRdcDLLREQYEEEQEV-KAELHR 1351
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralleerFAAALGDAVE--RELRENLEERIDAlRARLNR 784
|
570 580 590
....*....|....*....|....*....|
gi 1981090065 1352 TLSKVNAEMVQWRMKYENNVIQRTEDLEDA 1381
Cdd:COG4913 785 AEEELERAMRAFNREWPAETADLDADLESL 814
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1435-1634 |
2.17e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1435 DQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVRE---- 1510
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1511 ---------------GTKNLTE----MEKVKKLIEEEKTEVQvTLEETEGALERNESKILHFQLELLEAKAELERKLSEK 1571
Cdd:COG3883 95 lyrsggsvsyldvllGSESFSDfldrLSALSKIADADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1981090065 1572 DEEIEnfrrKQQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKS 1634
Cdd:COG3883 174 EAQQA----EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
925-1308 |
2.54e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.10 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 925 NSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLT--------EEVEFLNEDISKLNRAAKVVQEAHQ 996
Cdd:COG5185 156 VETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGtvnsikesETGNLGSESTLLEKAKEIINIEEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 997 QTLDDLHMEEEKLsslskanlklEQQVDELEGALEQERKARMNCERELHKLEGNLKLNREsmeNLESSQRHLAEELRKKE 1076
Cdd:COG5185 236 KGFQDPESELEDL----------AQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENAN---NLIKQFENTKEKIAEYT 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1077 LELSQMNSKVENEK-----GLVAQLQKTVKELQTQIKDLKEKLE------AERTTRAKMERERADLTQDLADLNERLEEV 1145
Cdd:COG5185 303 KSIDIKKATESLEEqlaaaEAEQELEESKRETETGIQNLTAEIEqgqeslTENLEAIKEEIENIVGEVELSKSSEELDSF 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1146 GgsslAQLEITKKqetKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENL-------QQVKQKLEKDKSDLQL 1218
Cdd:COG5185 383 K----DTIESTKE---SLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQAtssneevSKLLNELISELNKVMR 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1219 EVDDLLTRVEQMTRAKANAEKLCTLYEerlheataKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKS 1298
Cdd:COG5185 456 EADEESQSRLEEAYDEINRSVRSKKED--------LNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLK 527
|
410
....*....|
gi 1981090065 1299 NFTRQIEDLR 1308
Cdd:COG5185 528 DFMRARGYAH 537
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1393-1583 |
2.88e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1393 AEAMGVANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTE 1472
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1473 LLKLKNTYEESIVG-QETLRREN--------KNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEektevqvtLEETEGAL 1543
Cdd:COG3883 81 IEERREELGERARAlYRSGGSVSyldvllgsESFSDFLDRLSALSKIADADADLLEELKADKAE--------LEAKKAEL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1981090065 1544 ERNESKILHFQLELLEAKAELERKLSEKDEEIENFRRKQQ 1583
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
907-1170 |
3.48e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 907 LEARVKELSERVEEEEEINSELTARGRKLEDECFELKKEIddletmlvKSEKEKRTTEhkVKNLTEEVEFLNEDISKLNR 986
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTI--------KAEIEELTDE--LLNLVMDIEDPSAALNKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 987 AAKVVQEAHQQTLDDLHMEEE---------KLSSLSKANLKLEQQVDELEGALEQERKARMNcerelhklegnlklnres 1057
Cdd:PHA02562 263 AAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDE------------------ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1058 menlESSQRHLAEELRKKELELsqmNSKVENEKGLVAQLQKTVKELQTQIKDLKEkleaerttrakmerERADLTQDLAD 1137
Cdd:PHA02562 325 ----LEEIMDEFNEQSKKLLEL---KNKISTNKQSLITLVDKAKKVKAAIEELQA--------------EFVDNAEELAK 383
|
250 260 270
....*....|....*....|....*....|...
gi 1981090065 1138 LNERLEEVggsslaqleITKKQETKFQKLHRDM 1170
Cdd:PHA02562 384 LQDELDKI---------VKTKSELVKEKYHRGI 407
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1190-1795 |
3.49e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1190 DSLAELEGQVENLQQVKQKLEKDKSDL-----QLEVD-----DLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVT 1259
Cdd:PRK01156 173 DVIDMLRAEISNIDYLEEKLKSSNLELenikkQIADDekshsITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1260 QLANDLAAQKTKL---------WSESGEFLRRLEEKEALINQLS-REKSNFTRQIEDLRgQLEKETKSQSALAHALQKAQ 1329
Cdd:PRK01156 253 RYESEIKTAESDLsmeleknnyYKELEERHMKIINDPVYKNRNYiNDYFKYKNDIENKK-QILSNIDAEINKYHAIIKKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1330 RDCDLLREQYEEEQEVKAELHRTLSkvnaEMVQWRMKYE---NNVIQRTEDLEDAKKELAIRLQEAAEAMGVANARNASL 1406
Cdd:PRK01156 332 SVLQKDYNDYIKKKSRYDDLNNQIL----ELEGYEMDYNsylKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1407 ERARHQLQLELGDALSDLGKVRsaaarldqkqlQSGKALADWKQKHEESQALLDAsQKEVQALSTELlklkntyeesivG 1486
Cdd:PRK01156 408 KKELNEINVKLQDISSKVSSLN-----------QRIRALRENLDELSRNMEMLNG-QSVCPVCGTTL------------G 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1487 QETLRRENKNLQEEISNLTNQVREgtknlteMEKVKKLIEEEKTEVQVTLEETEGalerneskilhfqlELLEAKAELER 1566
Cdd:PRK01156 464 EEKSNHIINHYNEKKSRLEEKIRE-------IEIEVKDIDEKIVDLKKRKEYLES--------------EEINKSINEYN 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1567 KLSEKDEEIENFRrkqqctiDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSeatkslgqlQIQIKDLQ 1646
Cdd:PRK01156 523 KIESARADLEDIK-------IKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVIS---------LIDIETNR 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1647 MQLDDstqlnsdLKEQVAVAERRNSLLQSELEDLRSLqeqTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLE--- 1723
Cdd:PRK01156 587 SRSNE-------IKKQLNDLESRLQEIEIGFPDDKSY---IDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDnyk 656
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1981090065 1724 ---ADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQM 1795
Cdd:PRK01156 657 kqiAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKI 731
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1456-1687 |
3.61e-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: 45.27 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1456 QALLDASQKE----VQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIE----- 1526
Cdd:pfam07888 33 QNRLEECLQEraelLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSassee 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1527 --EEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELERkLSEKDEEIENFRRKQQCTIDSLQSSLDSeakSRIEVT 1604
Cdd:pfam07888 113 lsEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER-MKERAKKAGAQRKEEEAERKQLQAKLQQ---TEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1605 RLKKKMEEDLNEMELQLSCANRQVSEATKsLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQ 1684
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITT-LTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQR 267
|
...
gi 1981090065 1685 EQT 1687
Cdd:pfam07888 268 DRT 270
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1661-1925 |
4.01e-04 |
|
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: 45.44 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1661 EQVAVAERRNSLLQSE----LEDLRSLQEQTERGRRLSEE-ELLEATERINlfytQNTSLLSQKKKLEADVARMQKEAEE 1735
Cdd:TIGR02169 180 EEVEENIERLDLIIDEkrqqLERLRREREKAERYQALLKEkREYEGYELLK----EKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1736 VVQECQNAEEKAKKAAIEAANLSEELKKK--------QDTIAHLERTRENMEQTITDLQKRLAEAEQmALMGSRKQIQKL 1807
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDAEE-RLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1808 ESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSK 1887
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270
....*....|....*....|....*....|....*...
gi 1981090065 1888 YKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQE 1925
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1022-1580 |
4.03e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1022 QVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLE---SSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQK 1098
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRaeiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1099 TVKELQTQIKDLKEK----------LEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETK------ 1162
Cdd:PRK01156 219 EIERLSIEYNNAMDDynnlksalneLSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKnrnyin 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1163 -FQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDksDLQLEVDDLLTRVEQMTRAKANAEKLC 1241
Cdd:PRK01156 299 dYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYD--DLNNQILELEGYEMDYNSYLKSIESLK 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1242 TLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLE--------- 1312
Cdd:PRK01156 377 KKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcp 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1313 ------KETKSQSALAHALQKAQR---DCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKK 1383
Cdd:PRK01156 457 vcgttlGEEKSNHIINHYNEKKSRleeKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKI 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1384 ELAiRLQEAAEAMGVANARNASLErarhqlqleLGDalsdlgkvrsaaarLDQKQLQSGKALAdwkqkhEESQALLDASQ 1463
Cdd:PRK01156 537 KIN-ELKDKHDKYEEIKNRYKSLK---------LED--------------LDSKRTSWLNALA------VISLIDIETNR 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1464 KEVQALSTELLKLKNTYEESIVGQETLRRENKN----LQEEISNLTNQVREGTKNLTEMEKVKKLIE------------- 1526
Cdd:PRK01156 587 SRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKsireIENEANNLNNKYNEIQENKILIEKLRGKIDnykkqiaeidsii 666
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1981090065 1527 EEKTEVQVTLEETEGALERNESKILHFQLELLEAKA----------ELERKLSEKDEEIENFRR 1580
Cdd:PRK01156 667 PDLKEITSRINDIEDNLKKSRKALDDAKANRARLEStieilrtrinELSDRINDINETLESMKK 730
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1759-1866 |
4.07e-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: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1759 EELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQmalmgsrkQIQKLESRVRELEGELEGEIRRSAEAQRGAR---RL 1835
Cdd:COG2433 406 RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE--------RIERLERELSEARSEERREIRKDREISRLDReieRL 477
|
90 100 110
....*....|....*....|....*....|.
gi 1981090065 1836 ERCIKELTYQAEEDKKNLSRMQtQMDKLQLK 1866
Cdd:COG2433 478 ERELEEERERIEELKRKLERLK-ELWKLEHS 507
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1655-1889 |
4.12e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1655 LNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRR--LSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKE 1732
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1733 AEEVvqecqNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAeqmalmgsRKQIQKLESRVR 1812
Cdd:COG3206 242 LAAL-----RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL--------RAQIAALRAQLQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981090065 1813 ELEGELEGEIRRSAEAqrgARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQlkvqnykQQVEVAETQANQYLSKYK 1889
Cdd:COG3206 309 QEAQRILASLEAELEA---LQAREASLQAQLAQLEARLAELPELEAELRRLE-------REVEVARELYESLLQRLE 375
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
833-1066 |
4.16e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 833 KSSEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQ--VSLTQEKNDLILQLQAEQETLANVEEQcewliksKIQLEAR 910
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAE-------LAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 911 VKELSERVEEEEEINSELTArgrklEDECFELKKEIDDLETMLvkSEKEKRTTEH--KVKNLTEEVEFLNEDISKlnRAA 988
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAEL--AELSARYTPNhpDVIALRAQIAALRAQLQQ--EAQ 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1981090065 989 KVVQEAHQQtlddlhmeeekLSSLSKANLKLEQQVDELEGALEQERKArmncERELHKLEGNLKLNRESMENLESSQR 1066
Cdd:COG3206 313 RILASLEAE-----------LEALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYESLLQRLE 375
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1245-1472 |
4.18e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1245 EERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHA 1324
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1325 LQKAQRDCDLLrEQYEEEQEVKAELHRtlskvnAEMVQWRMKYENNVIQRT----EDLEDAKKELAIRLQEAAEAMGVAN 1400
Cdd:COG3883 95 LYRSGGSVSYL-DVLLGSESFSDFLDR------LSALSKIADADADLLEELkadkAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1981090065 1401 ARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTE 1472
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
835-1145 |
4.62e-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: 44.89 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 835 SEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEA----- 909
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETelerm 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 910 --RVKELSERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEV------EFLNEDI 981
Cdd:pfam07888 156 keRAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLttahrkEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 982 SKLNRAAKVVQEAHQQTLDDLHMEEEKLSS--------LSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKL 1053
Cdd:pfam07888 236 LEELRSLQERLNASERKVEGLGEELSSMAAqrdrtqaeLHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1054 NRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGL-VAQLQKTVKELQtqikDLKEKLEAERTTRAKMERERADLT 1132
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCnRVQLSESRRELQ----ELKASLRVAQKEKEQLQAEKQELL 391
|
330
....*....|...
gi 1981090065 1133 QDLADLNERLEEV 1145
Cdd:pfam07888 392 EYIRQLEQRLETV 404
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1443-1656 |
5.59e-04 |
|
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: 43.98 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1443 KALADWKQKHE---ESQALLDASQKEVQALSTELLKLKNTYEESIVGQET--LRRENKNLQEEISNLTNQVRE-GTKNLT 1516
Cdd:pfam09787 7 QELADYKQKAArilQSKEKLIASLKEGSGVEGLDSSTALTLELEELRQERdlLREEIQKLRGQIQQLRTELQElEAQQQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1517 EMEKVKKLIEEEKTEVQVTL---EETEGALERNESKILHFQLELLEAKAELERKLSEKDEEIEnfRRKQQCTIDSLQSSL 1593
Cdd:pfam09787 87 EAESSREQLQELEEQLATERsarREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIE--KLRNQLTSKSQSSSS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1981090065 1594 DSEAKSRIevtrlkKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLN 1656
Cdd:pfam09787 165 QSELENRL------HQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKELQGEGSNGTSIN 221
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
833-1420 |
7.17e-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: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 833 KSSEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKndlILQLQAEQETLANVEEQCEWLIKS-KIQLEARV 911
Cdd:pfam12128 295 LDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDAD---IETAAADQEQLPSWQSELENLEERlKALTGKHQ 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 912 KELSERVEEEEEINSELTARGRKLEDECFELKKEIDDL----ETMLVKSEKEKRTT-EHKVKNLTEEVEFLNEDISKLnr 986
Cdd:pfam12128 372 DVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQlavaEDDLQALESELREQlEAGKLEFNEEEYRLKSRLGEL-- 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 987 aaKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKL-EGNLKLNR------ESME 1059
Cdd:pfam12128 450 --KLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALrQASRRLEErqsaldELEL 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1060 NLESSQRHLAEELRKKELELSQMNSKV--------------ENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKME 1125
Cdd:pfam12128 528 QLFPQAGTLLHFLRKEAPDWEQSIGKVispellhrtdldpeVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLD 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1126 RERADLtQDLADLNERLEEVGGSSLAQLEITKKQET-----------KFQKLHRDMEEATLHFETTSASLKKRHADSLAE 1194
Cdd:pfam12128 608 KAEEAL-QSAREKQAAAEEQLVQANGELEKASREETfartalknarlDLRRLFDEKQSEKDKKNKALAERKDSANERLNS 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1195 LEGQVENL----QQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKvTQLANDLAAqkt 1270
Cdd:pfam12128 687 LEAQLKQLdkkhQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE-TWYKRDLAS--- 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1271 klwsesgeflrrLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHA-LQKAQRDCDLLREQYEEEQEVKAEL 1349
Cdd:pfam12128 763 ------------LGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETwLQRRPRLATQLSNIERAISELQQQL 830
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1981090065 1350 HRTLSKV---NAEMVQWRMKYENNVIQRTEDLEDAKKELA----IRL-QEAAEAMGVANARNASLERARHQLQLELGDA 1420
Cdd:pfam12128 831 ARLIADTklrRAKLEMERKASEKQQVRLSENLRGLRCEMSklatLKEdANSEQAQGSIGERLAQLEDLKLKRDYLSESV 909
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1095-1352 |
7.67e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1095 QLQKTVKELQ----TQIKDLKEKLEAERTTrakmereraDLTQDLADLNERLEEVGG-SSLAQLEITKKQETKFQKLhrd 1169
Cdd:PRK05771 17 YKDEVLEALHelgvVHIEDLKEELSNERLR---------KLRSLLTKLSEALDKLRSyLPKLNPLREEKKKVSVKSL--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1170 mEEATLHFETTSASLkkrhADSLAELEGQVENLQQVKQKLEKDKSDLQ------LEVDDLLTR-----------VEQMTR 1232
Cdd:PRK05771 85 -EELIKDVEEELEKI----EKEIKELEEEISELENEIKELEQEIERLEpwgnfdLDLSLLLGFkyvsvfvgtvpEDKLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1233 AKANAEKLCTLYEERLHE------ATAK--LDKVTQLANDLAAQKTKLwSESGEFLRRLEEKEALINQLSREksnftrqI 1304
Cdd:PRK05771 160 LKLESDVENVEYISTDKGyvyvvvVVLKelSDEVEEELKKLGFERLEL-EEEGTPSELIREIKEELEEIEKE-------R 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1981090065 1305 EDLRGQLEKETKSqsalahaLQKAQRDCDLLREQYEEEQEVKAELHRT 1352
Cdd:PRK05771 232 ESLLEELKELAKK-------YLEELLALYEYLEIELERAEALSKFLKT 272
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
934-1892 |
9.56e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.66 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 934 KLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKN-----LTEEVEFLNEDISK-LNRaakvvqeahqqTLDDLHMEEE 1007
Cdd:TIGR01612 697 KLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNelldiIVEIKKHIHGEINKdLNK-----------ILEDFKNKEK 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1008 KLSSLSKANLKLEQQVDELEGALeQERKARMNCERELHklegNLKlNRESMENLESSQRHLaEELRKKELELSQMNSKVE 1087
Cdd:TIGR01612 766 ELSNKINDYAKEKDELNKYKSKI-SEIKNHYNDQINID----NIK-DEDAKQNYDKSKEYI-KTISIKEDEIFKIINEMK 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1088 NEKGLVaqLQKTVKELQTQiKDLKEKLEAERTTRAKMERE-RADLTQDlaDLNERLEEVGGSSLAQLEITKKQETKFQKL 1166
Cdd:TIGR01612 839 FMKDDF--LNKVDKFINFE-NNCKEKIDSEHEQFAELTNKiKAEISDD--KLNDYEKKFNDSKSLINEINKSIEEEYQNI 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1167 H--RDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAkanaeklctLY 1244
Cdd:TIGR01612 914 NtlKKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKA---------FK 984
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1245 EERLHEATAKLDKVTQLANDLaaqKTKLWSESGEFL-RRLEEKEALINQLSREKSNFTRQIEDLrgQLEKETKSQSALAH 1323
Cdd:TIGR01612 985 DASLNDYEAKNNELIKYFNDL---KANLGKNKENMLyHQFDEKEKATNDIEQKIEDANKNIPNI--EIAIHTSIYNIIDE 1059
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1324 ALQKAQRDCDLLREQYEEEQEVkaelhrtlSKVNAEMVQWRMKYENnviqrtedLEDAKKELAIRLQEaaeamgvanarn 1403
Cdd:TIGR01612 1060 IEKEIGKNIELLNKEILEEAEI--------NITNFNEIKEKLKHYN--------FDDFGKEENIKYAD------------ 1111
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1404 aslerarhqlqlelgdalsDLGKVRSAAARLDQKQLQSGKALADWKQKHE----ESQALLDASQKEV-QALSTELLKLKN 1478
Cdd:TIGR01612 1112 -------------------EINKIKDDIKNLDQKIDHHIKALEEIKKKSEnyidEIKAQINDLEDVAdKAISNDDPEEIE 1172
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1479 TYEESIVgqeTLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKL-IEEEKTEVQVTLEETEGALERNESKIlhfqlEL 1557
Cdd:TIGR01612 1173 KKIENIV---TKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGInLSYGKNLGKLFLEKIDEEKKKSEHMI-----KA 1244
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1558 LEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRLKKKME--EDLNEMELQLSCANRQVSEATksl 1635
Cdd:TIGR01612 1245 MEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDEniSDIREKSLKIIEDFSEESDIN--- 1321
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1636 gqlQIQiKDLQMQLDDSTQLNSDLKEQVA-VAERRNSL----LQSELEDLRSLQEQTERGRRLSEEElLEATERINLFYT 1710
Cdd:TIGR01612 1322 ---DIK-KELQKNLLDAQKHNSDINLYLNeIANIYNILklnkIKKIIDEVKEYTKEIEENNKNIKDE-LDKSEKLIKKIK 1396
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1711 QNTSLLSQKKKLEADVarmqkeAEEVVQEC-QNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRL 1789
Cdd:TIGR01612 1397 DDINLEECKSKIESTL------DDKDIDECiKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHIL 1470
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1790 AEAEQMALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELT-----YQAEEDKKNLSRMQTQMDKLQ 1864
Cdd:TIGR01612 1471 KIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTellnkYSALAIKNKFAKTKKDSEIII 1550
|
970 980
....*....|....*....|....*...
gi 1981090065 1865 LKVQNYKQQVEVAETQANQYLSKYKKQQ 1892
Cdd:TIGR01612 1551 KEIKDAHKKFILEAEKSEQKIKEIKKEK 1578
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
972-1118 |
9.62e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 9.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 972 EEV--EFLNEDISKLNRAAKVVQEAHQQTLDDlhmEEEKLSSLSKANLKLEQQVDELEGALEQerkarmnCERELHKLEG 1049
Cdd:COG2433 379 EEAleELIEKELPEEEPEAEREKEHEERELTE---EEEEIRRLEEQVERLEAEVEELEAELEE-------KDERIERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1981090065 1050 NLKLNRESMEnlessqrhlaEELRKKElELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKE--KLEAER 1118
Cdd:COG2433 449 ELSEARSEER----------REIRKDR-EISRLDREIERLERELEEERERIEELKRKLERLKElwKLEHSG 508
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1455-1712 |
1.09e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1455 SQALLDASQKEVQA-LSTELLKLKNTyeesivgqETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEvQ 1533
Cdd:PRK11281 50 KQKLLEAEDKLVQQdLEQTLALLDKI--------DRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLS-T 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1534 VTLEETEGALERNESKILHFQLELLEAKAEL-------ERKLSEKDEeieNFRRKQQctIDSLQSSLDSEAKSRIEVTRL 1606
Cdd:PRK11281 121 LSLRQLESRLAQTLDQLQNAQNDLAEYNSQLvslqtqpERAQAALYA---NSQRLQQ--IRNLLKGGKVGGKALRPSQRV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1607 KKKMEE-------DLNEMELQ-----LSCANRQVSEATKSLGQLQIQIKDLQ-----MQLDDSTQLNSDLKE-QVAVAER 1668
Cdd:PRK11281 196 LLQAEQallnaqnDLQRKSLEgntqlQDLLQKQRDYLTARIQRLEHQLQLLQeainsKRLTLSEKTVQEAQSqDEAARIQ 275
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1981090065 1669 RNSLLQSELEdlrslqeqteRGRRLSEEeLLEATERINLFYTQN 1712
Cdd:PRK11281 276 ANPLVAQELE----------INLQLSQR-LLKATEKLNTLTQQN 308
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1019-1545 |
1.23e-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: 44.17 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1019 LEQQVDELEGALEQERKARmnceRELHKLEGNLKLNRESMENLEssqrHLAEELRKKELELSQmnsKVENEKGLVAQLQK 1098
Cdd:COG3096 517 LRAQLAELEQRLRQQQNAE----RLLEEFCQRIGQQLDAAEELE----ELLAELEAQLEELEE---QAAEAVEQRSELRQ 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1099 TVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVggSSLAQLE---ITKKQETKFQKLHRDMEEATL 1175
Cdd:COG3096 586 QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAM--QQLLEREreaTVERDELAARKQALESQIERL 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1176 H-----FETTSASLKK-----------------------------RHADSLAELEGQVENLQQvkqkLEKDKSDLQL--- 1218
Cdd:COG3096 664 SqpggaEDPRLLALAErlggvllseiyddvtledapyfsalygpaRHAIVVPDLSAVKEQLAG----LEDCPEDLYLieg 739
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1219 ---EVDDLLTRVEQMTRA-----------------------KANAEKLCTLYEER--LHEATA-------KLDKVTQLAN 1263
Cdd:COG3096 740 dpdSFDDSVFDAEELEDAvvvklsdrqwrysrfpevplfgrAAREKRLEELRAERdeLAEQYAkasfdvqKLQRLHQAFS 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1264 DLAAQKTKLWSEsgeflrrlEEKEALINQLSREKSNFTRQIEDLRGQlekETKSQSALAHA------LQK---------- 1327
Cdd:COG3096 820 QFVGGHLAVAFA--------PDPEAELAALRQRRSELERELAQHRAQ---EQQLRQQLDQLkeqlqlLNKllpqanllad 888
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1328 ---AQRdCDLLREQYEEEQEVKAELHR---TLSKVnAEMVQwrmkyennVIQRT--------EDLEDAKKELAiRLQEAA 1393
Cdd:COG3096 889 etlADR-LEELREELDAAQEAQAFIQQhgkALAQL-EPLVA--------VLQSDpeqfeqlqADYLQAKEQQR-RLKQQI 957
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1394 EAMGVANARNASLERARHQLQLELGDALSDlgKVRSAAARLDQKQLQSGKALADWKQKHEESQALL-------DASQKEV 1466
Cdd:COG3096 958 FALSEVVQRRPHFSYEDAVGLLGENSDLNE--KLRARLEQAEEARREAREQLRQAQAQYSQYNQVLaslkssrDAKQQTL 1035
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1467 QALSTELLKLKNTYEESIVgqETLRRENKNLQEEISNLTNQVREGTKNLT----EMEKVKKLIEEEKTEVQVTLEETEGA 1542
Cdd:COG3096 1036 QELEQELEELGVQADAEAE--ERARIRRDELHEELSQNRSRRSQLEKQLTrceaEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
...
gi 1981090065 1543 LER 1545
Cdd:COG3096 1114 KAG 1116
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1625-1878 |
1.35e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1625 NRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQ---VAVAERRNSLLQsELEDLRSLQEQTERGRRLSEEELLEA 1701
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglVDLSEEAKLLLQ-QLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1702 TERINLFYTQNTSLLS--QKKKLEADVARMQKEAEEvvqecqnaeekakkaaieaanLSEELKKKQDTIAHLERTRENME 1779
Cdd:COG3206 246 RAQLGSGPDALPELLQspVIQQLRAQLAELEAELAE---------------------LSARYTPNHPDVIALRAQIAALR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1780 QTITDLQKRLAEAEQMALMGSRKQIQKLESRVRelegELEGEIRRSAEAQRGARRLERcikeltyQAEEDKKNLSRMQTQ 1859
Cdd:COG3206 305 AQLQQEAQRILASLEAELEALQAREASLQAQLA----QLEARLAELPELEAELRRLER-------EVEVARELYESLLQR 373
|
250
....*....|....*....
gi 1981090065 1860 MDKLQLKVQNYKQQVEVAE 1878
Cdd:COG3206 374 LEEARLAEALTVGNVRVID 392
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1042-1173 |
1.37e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1042 RELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMnskveneKGLVAQLQKTVKELQTQIKDLKEKLEAERTTR 1121
Cdd:PRK09039 60 SQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRL-------QALLAELAGAGAAAEGRAGELAQELDSEKQVS 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1981090065 1122 AKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKFQKLHRDMEEA 1173
Cdd:PRK09039 133 ARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVA 184
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
851-1121 |
1.54e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.74 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 851 LQKALEKSEFQREELKAKQVSLTqeKNDLILQLQAEQEtlANVEEQCEWLIKSKIQLEARVKELSERVEEEEEINSELTA 930
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLS--ETDARIKLAAQEK--IHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 931 RGRKLEDECFELKKEID---DLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRA------AKVvqEAHQQTLDD 1001
Cdd:PLN02939 234 ENMLLKDDIQFLKAELIevaETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLqydcwwEKV--ENLQDLLDR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1002 LHMEEEKLSSLSKANLKLEQQVDELEGALEqerkarmncerelhklEGNL-KLNRESMENLESSQRHLAEELRKKELEls 1080
Cdd:PLN02939 312 ATNQVEKAALVLDQNQDLRDKVDKLEASLK----------------EANVsKFSSYKVELLQQKLKLLEERLQASDHE-- 373
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1981090065 1081 qMNSKVEnekglvaQLQKTVKELQTQIKDLKEklEAERTTR 1121
Cdd:PLN02939 374 -IHSYIQ-------LYQESIKEFQDTLSKLKE--ESKKRSL 404
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1611-1924 |
1.64e-03 |
|
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: 43.63 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1611 EEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSlqeqterg 1690
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELES-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1691 rRLSEEElleatERinlfytqNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAH 1770
Cdd:pfam01576 83 -RLEEEE-----ER-------SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1771 LERTRENMEQTITDLQKRLAEAEQMALMGSrKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDK 1850
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLS-KLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1981090065 1851 KNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQ 1924
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELE 302
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1040-1152 |
1.89e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1040 CERELHKLEGNL-KLNRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKtvkelqtqikdLKEKLEAER 1118
Cdd:COG0542 416 LERRLEQLEIEKeALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQE-----------LKEELEQRY 484
|
90 100 110
....*....|....*....|....*....|....*
gi 1981090065 1119 TTRAKMERERADLTQDLADLNERL-EEVGGSSLAQ 1152
Cdd:COG0542 485 GKIPELEKELAELEEELAELAPLLrEEVTEEDIAE 519
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1443-1792 |
2.04e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.50 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1443 KALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETlrrenKNLQEEISNLTNQVR--------EGTKN 1514
Cdd:TIGR01612 620 KKAIDLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIYSTIKSELS-----KIYEDDIDALYNELSsivkenaiDNTED 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1515 LTEMEKVKKLIEEEKTEVQ----VTLEETEGALERNESKILHFqleLLEAKAELERKLS-EKDEEIENFRRKQQctidSL 1589
Cdd:TIGR01612 695 KAKLDDLKSKIDKEYDKIQnmetATVELHLSNIENKKNELLDI---IVEIKKHIHGEINkDLNKILEDFKNKEK----EL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1590 QSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLK----EQVAV 1665
Cdd:TIGR01612 768 SNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKfmkdDFLNK 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1666 AERRNSLLQSELEDLRSLQEQ-TERGRRLSEEElleATERINLF---YTQNTSLLSQ-KKKLEADVARMQ--KEAEEVVQ 1738
Cdd:TIGR01612 848 VDKFINFENNCKEKIDSEHEQfAELTNKIKAEI---SDDKLNDYekkFNDSKSLINEiNKSIEEEYQNINtlKKVDEYIK 924
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1981090065 1739 ECQNAEEKAKKAAIEAANLSEELKKKQDTIAH---LERTREN-MEQTITDLQKRLAEA 1792
Cdd:TIGR01612 925 ICENTKESIEKFHNKQNILKEILNKNIDTIKEsnlIEKSYKDkFDNTLIDKINELDKA 982
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
962-1114 |
2.12e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 42.72 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 962 TTEHKVKNLTEEVEFLNEDISKLNRAAKVVqeA----HQQTLDDLHmeeeklsslSKANLKLEQQVDELEGALEQERKAR 1037
Cdd:smart00435 232 TLQEQLKELTAKDGNVAEKILAYNRANREV--AilcnHQRTVSKTH---------EKSMEKLQEKIKALKYQLKRLKKMI 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1981090065 1038 MNCERElhklegnlklnRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDlKEKL 1114
Cdd:smart00435 301 LLFEMI-----------SDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEKKKKQIERLEERIEKLEVQATD-KEEN 365
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
924-1299 |
2.30e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 924 INSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEhkvKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDdlH 1003
Cdd:pfam12128 630 ANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKN---KALAERKDSANERLNSLEAQLKQLDKKHQAWLE--E 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1004 MEEEKLSSLSKANLKL----------EQQVDELEGALEQERKARMN-CERELHKLEGNLKLNRESMENLESSQRHLA--- 1069
Cdd:pfam12128 705 QKEQKREARTEKQAYWqvvegaldaqLALLKAAIAARRSGAKAELKaLETWYKRDLASLGVDPDVIAKLKREIRTLErki 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1070 EELRKKELELSQ----MNSKVENEK-GLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEE 1144
Cdd:pfam12128 785 ERIAVRRQEVLRyfdwYQETWLQRRpRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRG 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1145 VggsslaQLEITKkqeTKFQKLHRDMEEATLHFETTSASLKkrhaDSLAELEGQVEnlqQVKQKLEKDKSDLQLEVDDLL 1224
Cdd:pfam12128 865 L------RCEMSK---LATLKEDANSEQAQGSIGERLAQLE----DLKLKRDYLSE---SVKKYVEHFKNVIADHSGSGL 928
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1225 TRVEQMTRAKA---NAEKLCTLYEERLheatakLDKVTQLANDLAAQKTKLWSESG--------EFLRRLEEKEALINQL 1293
Cdd:pfam12128 929 AETWESLREEDhyqNDKGIRLLDYRKL------VPYLEQWFDVRVPQSIMVLREQVsilgvdltEFYDVLADFDRRIASF 1002
|
....*.
gi 1981090065 1294 SREKSN 1299
Cdd:pfam12128 1003 SRELQR 1008
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
1485-1704 |
2.30e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 42.32 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1485 VGQETLRReNKNLQEEISNLTNQVREGTKNLT----EMEKVKKLI-------EEEKTEvqvtlEETEGALERNESKILHF 1553
Cdd:pfam04849 88 IGQSLLKQ-NSVLTERNEALEEQLGSAREEILqlrhELSKKDDLLqiysndaEESETE-----SSCSTPLRRNESFSSLH 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1554 QLELLEAkaeLERKLSEKDEEIEnfrrkqqctidslqsSLDSEA-KSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEAT 1632
Cdd:pfam04849 162 GCVQLDA---LQEKLRGLEEENL---------------KLRSEAsHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1633 KSLG--------------QLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEEL 1698
Cdd:pfam04849 224 EELArkmeenlrqqeeitSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEEL 303
|
....*.
gi 1981090065 1699 LEATER 1704
Cdd:pfam04849 304 KELRKK 309
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
840-1390 |
2.48e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 840 EVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDL---ILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSE 916
Cdd:PRK01156 198 ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLksaLNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 917 RVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLvksekekrttehkvKNLTEEVeflnedisklnraakvvqeahq 996
Cdd:PRK01156 278 LEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQIL--------------SNIDAEI---------------------- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 997 QTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKE 1076
Cdd:PRK01156 322 NKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1077 LELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRA------------------KMERERADLTQDLADL 1138
Cdd:PRK01156 402 IDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlgeeKSNHIINHYNEKKSRL 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1139 NERLEEVggsslaQLEITKKQETKFQ--KLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDL 1216
Cdd:PRK01156 482 EEKIREI------EIEVKDIDEKIVDlkKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRY 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1217 Q-LEVDDLLTRVEQMTRAKANAEKL-CTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLS 1294
Cdd:PRK01156 556 KsLKLEDLDSKRTSWLNALAVISLIdIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKY 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1295 REKSNFTRQIEDLRGQLEkETKSQSALAHALQKAQRDcdlLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNvIQR 1374
Cdd:PRK01156 636 NEIQENKILIEKLRGKID-NYKKQIAEIDSIIPDLKE---ITSRINDIEDNLKKSRKALDDAKANRARLESTIEIL-RTR 710
|
570
....*....|....*.
gi 1981090065 1375 TEDLEDAKKELAIRLQ 1390
Cdd:PRK01156 711 INELSDRINDINETLE 726
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
834-1203 |
2.71e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 43.01 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 834 SSEVGE-EVAGLKEECaqlqKALEKSEFQREelkaKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQL--EAR 910
Cdd:pfam15818 86 ATEIKEkEIEGLKETL----KALQVSKYSLQ----KKVSEMEQKLQLHLLAKEDHHKQLNEIEKYYATITGQFGLvkENH 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 911 VKELSERVEEEEeINSELTARGRKLEDECFELKKEIDDLETMLVKSekeKRTTEHKVK----NLTEEVEFLNEDISKLNR 986
Cdd:pfam15818 158 GKLEQNVQEAIQ-LNKRLSALNKKQESEICSLKKELKKVTSDLIKS---KVTCQYKMGeeniNLTIKEQKFQELQERLNM 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 987 AAKVVQEAHQQTLddlHMEEEK---LSSLSKANLKLEQQVD---ELEGALEQERKARMNCERELHKLEGNLKLNRESMEN 1060
Cdd:pfam15818 234 ELELNKKINEEIT---HIQEEKqdiIISFQHMQQLLQQQTQantEMEAELKALKENNQTLERDNELQREKVKENEEKFLN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1061 LESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERttrakmereradlTQDLADLNe 1140
Cdd:pfam15818 311 LQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKK-------------FQNVPEVN- 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1981090065 1141 rlEEVGGSSLAQLEITKKQetKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQ 1203
Cdd:pfam15818 377 --NENSEMSTEKSENLIIQ--KYNSEQEIREENTKSFCSDTEYRETEKKKGPPVEEIIIEDLQ 435
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
760-1217 |
2.88e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.82 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 760 GFLGQLEAIRDERLSKVFTLFQARAQGKLMRIKFQKILEERDALILIQWNIRAFMAVKNWPWmrlFFKIKPLVKSSEVGE 839
Cdd:pfam07111 173 GLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQVPPE---VHSQTWELERQELLD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 840 EVAGLKEECAQLQKALEKSEFQREELKAKqvsLTQEKNDLILQLQAEQETLANVEEQCEWLIKSkiqlearvkelseRVE 919
Cdd:pfam07111 250 TMQHLQEDRADLQATVELLQVRVQSLTHM---LALQEEELTRKIQPSDSLEPEFPKKCRSLLNR-------------WRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 920 EEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTL 999
Cdd:pfam07111 314 KVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1000 DDLHMEEEKL----SSLSKANLKLEQQVDELEGALEQ--ERKARMN-CERELHKLEGnLKLNRESMENLESSQRHLAEEL 1072
Cdd:pfam07111 394 QQTASAEEQLkfvvNAMSSTQIWLETTMTRVEQAVARipSLSNRLSyAVRKVHTIKG-LMARKVALAQLRQESCPPPPPA 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1073 RKKELELS-QMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAK----MERERADLTQDLADLNERLEEV-- 1145
Cdd:pfam07111 473 PPVDADLSlELEQLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEvaqqLEQELQRAQESLASVGQQLEVArq 552
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1981090065 1146 -------GGSSLAQlEITKKQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQ 1217
Cdd:pfam07111 553 gqqesteEAASLRQ-ELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQ 630
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
839-1127 |
2.93e-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: 42.44 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 839 EEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQaeqetlanveeqcEWLIKSKIQLEARVKELSERV 918
Cdd:pfam09731 173 AEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAP-------------ETPPKLPEHLDNVEEKVEKAQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 919 EEEEEIN--SELTARGRKLEDEcfELKKEIDDLETMLVKSEKEKRTTEHK-VKNLTEEVEFLNEDISKLNRAAkvvQEAH 995
Cdd:pfam09731 240 SLAKLVDqyKELVASERIVFQQ--ELVSIFPDIIPVLKEDNLLSNDDLNSlIAHAHREIDQLSKKLAELKKRE---EKHI 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 996 QQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKarmncerelhklegnLKLNRESMENL---------ESSQR 1066
Cdd:pfam09731 315 ERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFERE---------------REEIRESYEEKlrtelerqaEAHEE 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1981090065 1067 HLAEELRKKELEL-----SQMNSKVENEKGLvaqLQKTVKELQTQIKDLKEKLEAerttRAKMERE 1127
Cdd:pfam09731 380 HLKDVLVEQEIELqreflQDIKEKVEEERAG---RLLKLNELLANLKGLEKATSS----HSEVEDE 438
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1317-1542 |
3.14e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1317 SQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRmKYENNVIQRTEDLEDAKKELAIRLQEAAEAM 1396
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1397 GVANARNASLERARHQLQL--------ELGDALSDLGKVRSAAARlDQKQLQSGKALadwKQKHEESQALLDASQKEVQA 1468
Cdd:COG3883 86 EELGERARALYRSGGSVSYldvllgseSFSDFLDRLSALSKIADA-DADLLEELKAD---KAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1981090065 1469 LSTELLKLKNTYEESIVGQE----TLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGA 1542
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEallaQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
1427-1526 |
3.34e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 41.64 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1427 VRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTN 1506
Cdd:COG4026 112 IKNAIIRAGLKSLQNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKS 191
|
90 100
....*....|....*....|
gi 1981090065 1507 QVREGTKNLTEMEKvKKLIE 1526
Cdd:COG4026 192 EYSDLKSRFEELLK-KRLLE 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1320-1549 |
3.57e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1320 ALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQwrmkYENNVIQRTEDLEDAKKELAIRLQEAAEAMGVA 1399
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1400 NARNASLERARHQLQlELGDALSDLGKVRSAAARLDQKQ-LQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKN 1478
Cdd:COG4942 93 AELRAELEAQKEELA-ELLRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1981090065 1479 TYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESK 1549
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
839-1118 |
3.63e-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: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 839 EEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEArvkelserv 918
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA--------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 919 eeeeeinseltargrkledecfELKKEIDDLETMLVKSEKEKRTTEHKVKnlteeveFLNEDISKLNRAAKVVQEAHQQT 998
Cdd:COG4942 98 ----------------------ELEAQKEELAELLRALYRLGRQPPLALL-------LSPEDFLDAVRRLQYLKYLAPAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 999 LDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQerkarmncerelhklegnlklnresmenLESSQRHLAEELRKKELE 1078
Cdd:COG4942 149 REQAEELRADLAELAALRAELEAERAELEALLAE----------------------------LEEERAALEALKAERQKL 200
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1981090065 1079 LSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAER 1118
Cdd:COG4942 201 LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
986-1145 |
3.67e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 986 RAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQ 1065
Cdd:COG1196 651 LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1066 RHLAEELRKKELELSQMNSKVENEKGL----VAQLQKTVKELQTQIKDL-------KEKLEAERTTRAKMERERADLTQD 1134
Cdd:COG1196 731 EAEREELLEELLEEEELLEEEALEELPeppdLEELERELERLEREIEALgpvnllaIEEYEELEERYDFLSEQREDLEEA 810
|
170
....*....|.
gi 1981090065 1135 LADLNERLEEV 1145
Cdd:COG1196 811 RETLEEAIEEI 821
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1673-1910 |
3.83e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1673 LQSELEDLRSLQEQTERGRRlsEEELLEATERINLFYTQNTSLLSQKKKLEA--DVARMQKEAEEVVQECQNaeekakka 1750
Cdd:COG4913 230 LVEHFDDLERAHEALEDARE--QIELLEPIRELAERYAAARERLAELEYLRAalRLWFAQRRLELLEAELEE-------- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1751 aieaanLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQmalmgsrKQIQKLEsrvreleGELEGEIRRSAEAQR 1830
Cdd:COG4913 300 ------LRAELARLEAELERLEARLDALREELDELEAQIRGNGG-------DRLEQLE-------REIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1831 GARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEvkERAEVAESQVN 1910
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA--EIASLERRKSN 437
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1654-1926 |
4.25e-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: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1654 QLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATErinlfyTQNTSLLSQKKKLEADVARMQKEA 1733
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAE------KARQAEMDRQAAIYAEQERMAMER 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1734 EEVVQECQNAEEKAKKAAIEAANLSEELKKkqdtIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQiqklesRVRE 1813
Cdd:pfam17380 347 ERELERIRQEERKRELERIRQEEIAMEISR----MRELERLQMERQQKNERVRQELEAARKVKILEEERQ------RKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1814 LEGELEGEIRRSAEA--QRGARRLErcikeltyqaEEDKKNLSRMQTQMDKLQLKVQNYKQQvEVAETQANQYLSKYKKQ 1891
Cdd:pfam17380 417 QQKVEMEQIRAEQEEarQREVRRLE----------EERAREMERVRLEEQERQQQVERLRQQ-EEERKRKKLELEKEKRD 485
|
250 260 270
....*....|....*....|....*....|....*
gi 1981090065 1892 QHELNEVKERAEVAESQVNKLKIKAREFGKKVQEE 1926
Cdd:pfam17380 486 RKRAEEQRRKILEKELEERKQAMIEEERKRKLLEK 520
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1124-1341 |
4.52e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1124 MERERADLTQDLADLNERLEEVGgsslAQLEITKKQETKFQKLHR--DMEEATLHFETTSASLKKRHADSLAELEGQVEN 1201
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELR----KELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1202 LQQVKQKLEKDKSDLQLEVDDllTRVEQMTRAKANAEKLCTLYEERLheaTAKLDKVTQLANDLAAQKTKLWSESGeflR 1281
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARY---TPNHPDVIALRAQIAALRAQLQQEAQ---R 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1282 RLEEKEALINQLSREKSNFTRQIEDLRGQLeketKSQSALAHALQKAQRDCDLLREQYEE 1341
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYES 369
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1416-1926 |
4.56e-03 |
|
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: 41.96 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1416 ELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTEL------------LKLKNTYEES 1483
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLeldgfergpfseRQIKNFHTLV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1484 IVGQEtlrRENKNLQEEISNLTNQVREGTKNLTEmekvkklIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAE 1563
Cdd:TIGR00606 400 IERQE---DEAKTAAQLCADLQSKERLKQEQADE-------IRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGS 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1564 LERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKS----RIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQ 1639
Cdd:TIGR00606 470 SDRILELDQELRKAERELSKAEKNSLTETLKKEVKSlqneKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDE 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1640 iQIKDLQMQLDDS----------TQLNSD----LKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEateri 1705
Cdd:TIGR00606 550 -QIRKIKSRHSDEltsllgyfpnKKQLEDwlhsKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSS----- 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1706 nlfYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDL 1785
Cdd:TIGR00606 624 ---YEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDL 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1786 QKRLAEAEQmalmgsrkQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQL 1865
Cdd:TIGR00606 701 QSKLRLAPD--------KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET 772
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1981090065 1866 KVQNYKQQVEVAET-QANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQEE 1926
Cdd:TIGR00606 773 LLGTIMPEEESAKVcLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEK 834
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
839-1285 |
4.61e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 839 EEVAGLKEECAQLQKALEKSEFQREELKAKQ--------VSLTQEKNDLILQLQAEQETLANVEEQCEWL----IKSKIQ 906
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARLEALLAALglplPASAEE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 907 LEARVKELSERVEEEEEINSELTARGRKLEDECFELKKEIDDLetmlvksEKEKRTTEHKVKNLTEEVEF----LNEDIS 982
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL-------EAEIASLERRKSNIPARLLAlrdaLAEALG 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 983 KLNRAAKVVQEAHQQTLDD----------LH-------MEEEKLSSLSKA--NLKLEQQVDELEGALEQERKARMNCERE 1043
Cdd:COG4913 455 LDEAELPFVGELIEVRPEEerwrgaiervLGgfaltllVPPEHYAAALRWvnRLHLRGRLVYERVRTGLPDPERPRLDPD 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1044 --LHKLEG---------NLKLNR-------ESMENLESSQRHLAEE-LRKKELELSQMNSKVENEKGLV---------AQ 1095
Cdd:COG4913 535 slAGKLDFkphpfrawlEAELGRrfdyvcvDSPEELRRHPRAITRAgQVKGNGTRHEKDDRRRIRSRYVlgfdnraklAA 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1096 LQKTVKELQTQIKDLKEKLEAERTTRAKMeRERADLTQDLADLNERLEEVGGsslAQLEITKKQETKfqklhRDMEEATL 1175
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDAL-QERREALQRLAEYSWDEIDVAS---AEREIAELEAEL-----ERLDASSD 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1176 HFETtsasLKKRhadsLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLY-----EERLHE 1250
Cdd:COG4913 686 DLAA----LEEQ----LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElrallEERFAA 757
|
490 500 510
....*....|....*....|....*....|....*...
gi 1981090065 1251 ATAKL---DKVTQLANDLAAQKTKLWSESGEFLRRLEE 1285
Cdd:COG4913 758 ALGDAverELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1056-1355 |
4.73e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 41.60 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1056 ESMENLESSQRHLAEELRKKELELSQMNSKVENekgLVAQLQKTVKELQTQIKDLKEKLEaerttraKMERERADLTQDL 1135
Cdd:pfam04108 3 SSAQDLCRWANELLTDARSLLEELVVLLAKIAF---LRRGLSVQLANLEKVREGLEKVLN-------ELKKDFKQLLKDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1136 ADLNERLEEVggsslaqLEITKKQETKFQKLHRDMEEATLH-F--ETTSASLKKRHADSLAELEGQVENLQQVKQKLEKD 1212
Cdd:pfam04108 73 DAALERLEET-------LDKLRNTPVEPALPPGEEKQKTLLdFidEDSVEILRDALKELIDELQAAQESLDSDLKRFDDD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1213 KSDLQLEVDDLLTRveqmTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQ 1292
Cdd:pfam04108 146 LRDLQKELESLSSP----SESISLIPTLLKELESLEEEMASLLESLTNHYDQCVTAVKLTEGGRAEMLEVLENDARELDD 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1981090065 1293 LSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSK 1355
Cdd:pfam04108 222 VVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSALQLIAEIQSRLPEYLAALKEFEERWEE 284
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1061-1376 |
4.78e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1061 LESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERadltQDLADLNE 1140
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKY----KELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1141 RLEEVGGSSLAQLEitkkqetkfqklhrDMEEATLHFETTSASLKKRHADSLAELE---GQVENLQQVKQKLEKDKSDLQ 1217
Cdd:pfam07888 112 ELSEEKDALLAQRA--------------AHEARIRELEEDIKTLTQRVLERETELErmkERAKKAGAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1218 LEvddLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKtklwsesgeflRRLEEKEALINQLS--R 1295
Cdd:pfam07888 178 AK---LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH-----------RKEAENEALLEELRslQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1296 EKSNFT-RQIEDLRGQLEkETKSQSALAHA------LQKAQRDCDL--LREQYEEEQEVKAELHRTLSKvNAEMVQWRMK 1366
Cdd:pfam07888 244 ERLNASeRKVEGLGEELS-SMAAQRDRTQAelhqarLQAAQLTLQLadASLALREGRARWAQERETLQQ-SAEADKDRIE 321
|
330
....*....|
gi 1981090065 1367 YENNVIQRTE 1376
Cdd:pfam07888 322 KLSAELQRLE 331
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1019-1156 |
5.08e-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: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1019 LEQQVDELEGALEQERKARMNCERE---LHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMNS----------- 1084
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAEldrLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIdlarrrvlapi 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1981090065 1085 ------KVENEKGLVAQLQKTVKELQTQI-KDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVgGSSLAQLEIT 1156
Cdd:pfam00529 136 ggisreSLVTAGALVAQAQANLLATVAQLdQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLA-KLDLERTEIR 213
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1255-1570 |
5.14e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.06 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1255 LDKVTQLANDLAAQKTKLwsesgeflRRLEEKEAliNQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDL 1334
Cdd:pfam00038 17 IDKVRFLEQQNKLLETKI--------SELRQKKG--AEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1335 LREQYEEE----QEVKAELHrTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKelaIRLQEAAEAMGVANARNASLERaR 1410
Cdd:pfam00038 87 FRQKYEDElnlrTSAENDLV-GLRKDLDEATLARVDLEAKIESLKEELAFLKK---NHEEEVRELQAQVSDTQVNVEM-D 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1411 HQLQLELGDALSDLGKVRSAAARLDQKQLQsgkalADWKQKHEESQALLDASQKEVQALSTELLKLKNTYeesivgqETL 1490
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAAKNREEAE-----EWYQSKLEELQQAAARNGDALRSAKEEITELRRTI-------QSL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1491 RRENKNLQEEISNLTNQVREgtknltemekvkklieeektevqvtLEET-EGALERNESKILHFQLELLEAKAELERKLS 1569
Cdd:pfam00038 230 EIELQSLKKQKASLERQLAE-------------------------TEERyELQLADYQELISELEAELQETRQEMARQLR 284
|
.
gi 1981090065 1570 E 1570
Cdd:pfam00038 285 E 285
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1373-1601 |
5.26e-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: 41.29 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1373 QRTEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQLELGDALSDL----GKVRSAAARLDQKQLQSGKALADW 1448
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIraleQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1449 KQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEE 1528
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1981090065 1529 KTEVQVTLEETEGALERNESKILHFQLELLEAK---AELERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRI 1601
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAaelAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1373-1724 |
5.35e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.65 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1373 QRTEDLEDAKKElaiRLQEAAEAMGVANARNASLERARHQLQLELGdalsdlgkvRSAAARLDQKQLQSGKALADWKQKH 1452
Cdd:pfam17380 288 QQQEKFEKMEQE---RLRQEKEEKAREVERRRKLEEAEKARQAEMD---------RQAAIYAEQERMAMERERELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1453 EESQALLDASQKEVQALST------ELLKLKNTYEESIVGQETLRRENKNLQEEisnltNQVREGTKNLTEMEKVKKLIE 1526
Cdd:pfam17380 356 EERKRELERIRQEEIAMEIsrmrelERLQMERQQKNERVRQELEAARKVKILEE-----ERQRKIQQQKVEMEQIRAEQE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1527 EEKT-EVQVTLEETEGALE--RNESKILHFQLELL-EAKAELERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIE 1602
Cdd:pfam17380 431 EARQrEVRRLEEERAREMErvRLEEQERQQQVERLrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1603 VTRLKKKMEEdlnEMElqlscanrqvseatkslgqlqiqikdlqmqlDDSTQLNSDLKEQVAVAERRNsllQSELEDLRS 1682
Cdd:pfam17380 511 EERKRKLLEK---EME-------------------------------ERQKAIYEEERRREAEEERRK---QQEMEERRR 553
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1981090065 1683 LQEQTergRRLSEEE-LLEATERINLFYTQNTSLLSQKKKLEA 1724
Cdd:pfam17380 554 IQEQM---RKATEERsRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1190-1362 |
5.56e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1190 DSLAELEGQVENLQQvKQKLEKD-KSDLQLEVDDLLTRVEQmtrAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQ 1268
Cdd:PRK09039 53 SALDRLNSQIAELAD-LLSLERQgNQDLQDSVANLRASLSA---AEAERSRLQALLAELAGAGAAAEGRAGELAQELDSE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1269 KTklwsESGEFLRRLEekeaLINQlsreksnftrQIEDLRGQLeketksqSALAHALQKAqrdcdllrEQYEEEQEVK-A 1347
Cdd:PRK09039 129 KQ----VSARALAQVE----LLNQ----------QIAALRRQL-------AALEAALDAS--------EKRDRESQAKiA 175
|
170
....*....|....*
gi 1981090065 1348 ELHRTLSKVNAEMVQ 1362
Cdd:PRK09039 176 DLGRRLNVALAQRVQ 190
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
874-1230 |
5.72e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 874 QEKNDLilqLQAEQETLANVEEQCEWLIKSKIQLEARVKELSERVEEEEEI-------NSELTARGRKLEDECFELKKEI 946
Cdd:pfam07888 41 QERAEL---LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEElrqsrekHEELEEKYKELSASSEELSEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 947 DDLETMLVKSEKEKRTTEHKVKNLTE-------EVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKL 1019
Cdd:pfam07888 118 DALLAQRAAHEARIRELEEDIKTLTQrvleretELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQEL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1020 EQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKEL---ELSQMNSKVENEKGLVAQL 1096
Cdd:pfam07888 198 RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGlgeELSSMAAQRDRTQAELHQA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1097 QKTVKELQTQIKDLKEKLEAERTTRAKmerERADLTQDLADLNERLEevggsslaqleitkKQETKFQKLHRDMEEATLH 1176
Cdd:pfam07888 278 RLQAAQLTLQLADASLALREGRARWAQ---ERETLQQSAEADKDRIE--------------KLSAELQRLEERLQEERME 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1981090065 1177 FETTSASLKKRHADSLAELEGQVENLQQVKQKL---EKDKSDLQLEVDDLLTRVEQM 1230
Cdd:pfam07888 341 REKLEVELGREKDCNRVQLSESRRELQELKASLrvaQKEKEQLQAEKQELLEYIRQL 397
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
952-1657 |
6.03e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.71 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 952 MLVKSEKEKRTTEHKVKNLTEEVEFLNED-ISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANlKLEQQVDELEGAL 1030
Cdd:PRK10246 188 MVFEQHKSARTELEKLQAQASGVALLTPEqVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLD-ELQQEASRRQQAL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1031 EQERKARMNCERELHKLEgnLKLNRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQL----QKTVKELQTQ 1106
Cdd:PRK10246 267 QQALAAEEKAQPQLAALS--LAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIrhhaAKQSAELQAQ 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1107 IKDLKEKLEAE-------------RTTRAKMERERADL---TQDLADLNERLEEVGGSSL--------AQLEITKKQETK 1162
Cdd:PRK10246 345 QQSLNTWLAEHdrfrqwnnelagwRAQFSQQTSDREQLrqwQQQLTHAEQKLNALPAITLtltadevaAALAQHAEQRPL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1163 FQKLhrdmeeATLHfeTTSASLKKRhadsLAELEGQVENLQQVKQKLE----------KDKSDLQLEVDDLLTRVEQMT- 1231
Cdd:PRK10246 425 RQRL------VALH--GQIVPQQKR----LAQLQVAIQNVTQEQTQRNaalnemrqryKEKTQQLADVKTICEQEARIKd 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1232 ----RAKANAEKLCTLYEERLHEATAKLDKVTQLAN----DLAAQKTKLWSESGEFLRrlEEKEALINQLSREKSNFTRQ 1303
Cdd:PRK10246 493 leaqRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNqsrlDALEKEVKKLGEEGAALR--GQLDALTKQLQRDESEAQSL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1304 IEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVK--AELHRTLSKVNAEMVQWRmKYENNVIQRTEDLEDA 1381
Cdd:PRK10246 571 RQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRllSQRHELQGQIAAHNQQII-QYQQQIEQRQQQLLTA 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1382 KKELAIRLQEAAEAMGVANAR--NASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALAD-WKQKHEESQAL 1458
Cdd:PRK10246 650 LAGYALTLPQEDEEASWLATRqqEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDnWRQVHEQCLSL 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1459 ldasQKEVQALSTELLKLKNTYEESIVgQETLRRENKNLQEEISNLTNQVREGTknLTEMEKVKKLIEEEKTEVQVTLEE 1538
Cdd:PRK10246 730 ----HSQLQTLQQQDVLEAQRLQKAQA-QFDTALQASVFDDQQAFLAALLDEET--LTQLEQLKQNLENQRQQAQTLVTQ 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1539 TEGALERNeskilhfqlelleakaelerklsekdeeienfrrkQQCTIDSLQSSLDSEaKSRIEVTRLKKKMEEDLN--- 1615
Cdd:PRK10246 803 TAQALAQH-----------------------------------QQHRPDGLDLTVTVE-QIQQELAQLAQQLRENTTrqg 846
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1981090065 1616 EMELQLscanRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNS 1657
Cdd:PRK10246 847 EIRQQL----KQDADNRQQQQALMQQIAQATQQVEDWGYLNS 884
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1369-1617 |
6.36e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1369 NNVIQRTEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQLELGDAL----SDLGKVRSAAARLD--------- 1435
Cdd:PLN02939 159 EKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLirgaTEGLCVHSLSKELDvlkeenmll 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1436 QKQLQSGKALADWKQKHEES-------QALLDASQKEVQ----ALSTELLKLkntyeeSIVGQETLRRENKNLQEEISNL 1504
Cdd:PLN02939 239 KDDIQFLKAELIEVAETEERvfklekeRSLLDASLRELEskfiVAQEDVSKL------SPLQYDCWWEKVENLQDLLDRA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1505 TNQVREGTKNLTEMEKVKKLIEEektevqvtLEETEGalERNESKILHFQLELLEAKAE-LERKLSEKDEEIENFRRKQQ 1583
Cdd:PLN02939 313 TNQVEKAALVLDQNQDLRDKVDK--------LEASLK--EANVSKFSSYKVELLQQKLKlLEERLQASDHEIHSYIQLYQ 382
|
250 260 270
....*....|....*....|....*....|....
gi 1981090065 1584 CTIDSLQSSLdseaKSRIEVTRlKKKMEEDLNEM 1617
Cdd:PLN02939 383 ESIKEFQDTL----SKLKEESK-KRSLEHPADDM 411
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
839-1204 |
6.50e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 839 EEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANV------EEQCEWLIKSKIQLEARVK 912
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVqtalrqQEKIERYQADLEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 913 ELSERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLvkSEKEKRTTE-HKVKNLTEEVEFLNEDISKLNRAAKVV 991
Cdd:PRK04863 366 EQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQAL--DVQQTRAIQyQQAVQALERAKQLCGLPDLTADNAEDW 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 992 QE---AHQQTLDD-LHMEEEKLSSLSKANlkleqqvDELEGALEQERKARMNCERELHKLEGnlklnRESMENLESsQRH 1067
Cdd:PRK04863 444 LEefqAKEQEATEeLLSLEQKLSVAQAAH-------SQFEQAYQLVRKIAGEVSRSEAWDVA-----RELLRRLRE-QRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1068 LAEELRKKELELSQMNSKVENEKGLVAQLQKTVK-----------------ELQTQIKDLKEKLEAERTTRAKMERERAD 1130
Cdd:PRK04863 511 LAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKrlgknlddedeleqlqeELEARLESLSESVSEARERRMALRQQLEQ 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1131 LTQDLADL----------NERLEEVGGSSLAQLEITKKQETKFQKLHRDMEEATLHfettsaslKKRHADSLAELEGQVE 1200
Cdd:PRK04863 591 LQARIQRLaarapawlaaQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVE--------RDELAARKQALDEEIE 662
|
....
gi 1981090065 1201 NLQQ 1204
Cdd:PRK04863 663 RLSQ 666
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1445-1691 |
6.72e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1445 LADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKL 1524
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1525 IEEEKTEVQVTL--EETEGALERNE--SKILHFQLELLEAKAELERKLSEKDEEIENfrrkqqctidslqssldseaksr 1600
Cdd:COG3883 98 SGGSVSYLDVLLgsESFSDFLDRLSalSKIADADADLLEELKADKAELEAKKAELEA----------------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1601 ievtrLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDdstqlnsDLKEQVAVAERRNSLLQSELEDL 1680
Cdd:COG3883 155 -----KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA-------ELEAELAAAEAAAAAAAAAAAAA 222
|
250
....*....|.
gi 1981090065 1681 RSLQEQTERGR 1691
Cdd:COG3883 223 AAAAAAAAAAA 233
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1235-1395 |
7.23e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1235 ANAEKLCTLYEerLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKE 1314
Cdd:COG1579 1 AMPEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1315 TKSQS---------ALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKEL 1385
Cdd:COG1579 79 EEQLGnvrnnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|
gi 1981090065 1386 AIRLQEAAEA 1395
Cdd:COG1579 159 EELEAEREEL 168
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1701-1908 |
7.32e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1701 ATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQdtiAHLERTRENMEQ 1780
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1781 TITDLQKRLAEAEQM-ALMGSrKQIQKLESRVrelegeleGEIRRSAEAQRgaRRLERcIKELTYQAEEDKKNLSRMQTQ 1859
Cdd:COG3883 91 RARALYRSGGSVSYLdVLLGS-ESFSDFLDRL--------SALSKIADADA--DLLEE-LKADKAELEAKKAELEAKLAE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1981090065 1860 MDKLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEVKERAEVAESQ 1908
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1056-1211 |
7.52e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 40.97 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1056 ESMENLESSQRHLA--EELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQ----------IKDLKEKLEAERTTRAK 1123
Cdd:pfam15066 302 QSFESLQPLEEDMAlnEVLQKLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKitkqqvfvdiINKLKENVEELIEDKYN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1124 MERERADLTQDLADLNE-------RLEEVGGSSLA-QLEItKKQETKFQKLH-RDMEEatLHFETTSASLKKRHADSLAE 1194
Cdd:pfam15066 382 VILEKNDINKTLQNLQEilantqkHLQESRKEKETlQLEL-KKIKVNYVHLQeRYITE--MQQKNKSVSQCLEMDKTLSK 458
|
170
....*....|....*..
gi 1981090065 1195 LEGQVENLQQVKQKLEK 1211
Cdd:pfam15066 459 KEEEVERLQQLKGELEK 475
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
927-1538 |
7.55e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.58 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 927 ELTARGRKLEDECFELKKEIDDLETMLVKS-------EKEKR-----TTEHKVKNLTEEVEFLNEDISKLNRAAKVVQE- 993
Cdd:TIGR01612 1133 ALEEIKKKSENYIDEIKAQINDLEDVADKAisnddpeEIEKKienivTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEv 1212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 994 -----AHQQTLDDLHME---EEKLSS--LSKANLKLEQQVDELEGAlEQERKARMNCERELHKLEGNLKL-NRESMENLE 1062
Cdd:TIGR01612 1213 kginlSYGKNLGKLFLEkidEEKKKSehMIKAMEAYIEDLDEIKEK-SPEIENEMGIEMDIKAEMETFNIsHDDDKDHHI 1291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1063 SSQRH--LAEELRKKELELSQMNS----------------------------------------KVENEKGLVAQLQKTV 1100
Cdd:TIGR01612 1292 ISKKHdeNISDIREKSLKIIEDFSeesdindikkelqknlldaqkhnsdinlylneianiynilKLNKIKKIIDEVKEYT 1371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1101 KELQTQIKDLKEKLEAERTTRAKME--------RERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKFQKLHRDMEE 1172
Cdd:TIGR01612 1372 KEIEENNKNIKDELDKSEKLIKKIKddinleecKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNEN 1451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1173 ATLHFETTS-ASLKKRHADSLAELEGQVE---NLQQVKQKLEKDKSdLQLEVDdlltrveqmtRAKANAEKLCTLYEERL 1248
Cdd:TIGR01612 1452 VLLLFKNIEmADNKSQHILKIKKDNATNDhdfNINELKEHIDKSKG-CKDEAD----------KNAKAIEKNKELFEQYK 1520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1249 HEATAKLDKVTQLANDLAAQKTKlwsesgeflrrlEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKa 1328
Cdd:TIGR01612 1521 KDVTELLNKYSALAIKNKFAKTK------------KDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAK- 1587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1329 qrdcdllreqyeEEQEVKAELHRTLSKVNAEMVQWRM----KYENNVIQRTEDLEDAKKELAIRLQEAAEAmgvanarna 1404
Cdd:TIGR01612 1588 ------------NDKSNKAAIDIQLSLENFENKFLKIsdikKKINDCLKETESIEKKISSFSIDSQDTELK--------- 1646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1405 slerarhqlqlELGDALSDLgkvrsaaarldQKQLQSgkaLADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESI 1484
Cdd:TIGR01612 1647 -----------ENGDNLNSL-----------QEFLES---LKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGI 1701
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1981090065 1485 VgqETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKL--------IEEEKTEVQVTLEE 1538
Cdd:TIGR01612 1702 I--EKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLegidpnekLEEYNTEIGDIYEE 1761
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
868-1233 |
7.84e-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: 41.21 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 868 KQVSLTQEKNDLILQ----LQAEQETLANVEEQCEWLIKSKIQLEARVKELSERVEEEEEINSELTARGRKLEDECFELK 943
Cdd:pfam05622 21 QQVSLLQEEKNSLQQenkkLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 944 KEIDDL-----ETMLVKSEKEK-RTTEHKVKNLTEEVEFLN---EDISKLNRAAKVVQEAH----QQTLDdlHMEEEKLS 1010
Cdd:pfam05622 101 HRNEELtslaeEAQALKDEMDIlRESSDKVKKLEATVETYKkklEDLGDLRRQVKLLEERNaeymQRTLQ--LEEELKKA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1011 SLSKANLKL-EQQVDELEGALEQERKARMNCERELHKLEGN---LKLNRESMENLESSQRHLAEELRKKELELSQMNSKV 1086
Cdd:pfam05622 179 NALRGQLETyKRQVQELHGKLSEESKKADKLEFEYKKLEEKleaLQKEKERLIIERDTLRETNEELRCAQLQQAELSQAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1087 ENEKGLVAQLQKTVKELQ-TQIKDLKEKLEAE----RTTRAKMERER-ADLTQDLADLNERLEEVGGSSLAQLEITKKQE 1160
Cdd:pfam05622 259 ALLSPSSDPGDNLAAEIMpAEIREKLIRLQHEnkmlRLGQEGSYRERlTELQQLLEDANRRKNELETQNRLANQRILELQ 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1981090065 1161 TKFQKLHRDMEEATLHFETTSASLKK--RHADSLAELEGQVENLQQVKQKLEKD-KSDLQLEVDDL---LTRVEQMTRA 1233
Cdd:pfam05622 339 QQVEELQKALQEQGSKAEDSSLLKQKleEHLEKLHEAQSELQKKKEQIEELEPKqDSNLAQKIDELqeaLRKKDEDMKA 417
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
934-1090 |
8.85e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 934 KLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAK----------VVQEAhqQTLDDLH 1003
Cdd:COG3883 41 ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsggsvsyldVLLGS--ESFSDFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1004 MEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMN 1083
Cdd:COG3883 119 DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
....*..
gi 1981090065 1084 SKVENEK 1090
Cdd:COG3883 199 AELEAEL 205
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
996-1213 |
9.03e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.50 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 996 QQTLDDLHMeeeKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKK 1075
Cdd:pfam15619 17 QNELAELQS---KLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1076 ELELSQMNSKVenekglvAQLQKTVKElqtqiKDLkekleaerttrakmeRERADLTQDLADLNERLEEvggsslaqlei 1155
Cdd:pfam15619 94 EAELLRLRDQL-------KRLEKLSED-----KNL---------------AEREELQKKLEQLEAKLED----------- 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1981090065 1156 tkkQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKL-EKDK 1213
Cdd:pfam15619 136 ---KDEKIQDLERKLELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKLkEKER 191
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
898-1925 |
9.24e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.19 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 898 EWLIKSKI--QLEARVKELSERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKE-------KRTTEHKVK 968
Cdd:TIGR01612 531 DQNIKAKLykEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEiiyinklKLELKEKIK 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 969 NLTEEVEFLNEDISklnraAKVVQEAHQQTLDDL----------HME-EEKLSSLSKANLK--LEQQVDELEGALEQERK 1035
Cdd:TIGR01612 611 NISDKNEYIKKAID-----LKKIIENNNAYIDELakispyqvpeHLKnKDKIYSTIKSELSkiYEDDIDALYNELSSIVK 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1036 armncERELHKLEGNLKLnresmENLESSQRHLAEELRKKELELSQMN-SKVENEKGlvaQLQKTVKELQTQI-----KD 1109
Cdd:TIGR01612 686 -----ENAIDNTEDKAKL-----DDLKSKIDKEYDKIQNMETATVELHlSNIENKKN---ELLDIIVEIKKHIhgeinKD 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1110 LKEKLEAERTTRAKMERERADLTQDLADLN---ERLEEVGGSSLAQLEI--TKKQETKfqklhRDMEEATLHFETTSASl 1184
Cdd:TIGR01612 753 LNKILEDFKNKEKELSNKINDYAKEKDELNkykSKISEIKNHYNDQINIdnIKDEDAK-----QNYDKSKEYIKTISIK- 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1185 kkrhADSLAELEGQVENLQqvkqklekdksdlqlevDDLLTRVEQMTrakaNAEKLCTLYEERLHEATAKLdkVTQLAND 1264
Cdd:TIGR01612 827 ----EDEIFKIINEMKFMK-----------------DDFLNKVDKFI----NFENNCKEKIDSEHEQFAEL--TNKIKAE 879
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1265 LAAQKTKLWSesgeflRRLEEKEALINQLSREKSNFTRQIEDLRgQLEKETKSQSALAHALQKAQRDCDLLREQYeeEQE 1344
Cdd:TIGR01612 880 ISDDKLNDYE------KKFNDSKSLINEINKSIEEEYQNINTLK-KVDEYIKICENTKESIEKFHNKQNILKEIL--NKN 950
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1345 VKaelhrTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEaaeamgvanARNASLERARHQLQLELGDalsdl 1424
Cdd:TIGR01612 951 ID-----TIKESNLIEKSYKDKFDNTLIDKINELDKAFKDASLNDYE---------AKNNELIKYFNDLKANLGK----- 1011
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1425 GKVRSAAARLDQKQlqsgKALADWKQKHEESQAllDASQKEVqALSTELLKLKNTYEESIvgQETLRRENKNLQEEIS-N 1503
Cdd:TIGR01612 1012 NKENMLYHQFDEKE----KATNDIEQKIEDANK--NIPNIEI-AIHTSIYNIIDEIEKEI--GKNIELLNKEILEEAEiN 1082
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1504 LT--NQVREGTKNLTEMEKVKklieEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELERKLSEKDEEIENFRRK 1581
Cdd:TIGR01612 1083 ITnfNEIKEKLKHYNFDDFGK----EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDV 1158
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1582 QQCTIdSLQSSLDSEAKSRIEVTRLKKKmEEDLNEMELQLScanrQVSEATKSLGQLQiQIKDLQMQLDDStqLNSDLKE 1661
Cdd:TIGR01612 1159 ADKAI-SNDDPEEIEKKIENIVTKIDKK-KNIYDEIKKLLN----EIAEIEKDKTSLE-EVKGINLSYGKN--LGKLFLE 1229
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1662 QVAVAERRNS----LLQSELEDLRSLQEQTERGRRLSEEELLEATER--INLFYTQNTSLLSQKKKLEADVARMQKEAEE 1735
Cdd:TIGR01612 1230 KIDEEKKKSEhmikAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMetFNISHDDDKDHHIISKKHDENISDIREKSLK 1309
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1736 VVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTR--------ENMEQTITDLQKRLAEAEQM------ALMGSR 1801
Cdd:TIGR01612 1310 IIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIAniynilklNKIKKIIDEVKEYTKEIEENnknikdELDKSE 1389
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 1802 KQIQKLESRVrelegeLEGEIRRSAEAQRGARRLERCIKELTY-----------------QAEEDKKNLSRMQTQMDKLQ 1864
Cdd:TIGR01612 1390 KLIKKIKDDI------NLEECKSKIESTLDDKDIDECIKKIKElknhilseesnidtyfkNADENNENVLLLFKNIEMAD 1463
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1981090065 1865 LKVQN-YKQQVEVAETQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQE 1925
Cdd:TIGR01612 1464 NKSQHiLKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTE 1525
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
985-1115 |
9.81e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1981090065 985 NRAAKVVQEAHQQtlddlhMEEEKlsslSKANLKLEQQVDELEGALEQERKARmncERELHKLEGNLKlNREsmENLESS 1064
Cdd:PRK12704 38 EEAKRILEEAKKE------AEAIK----KEALLEAKEEIHKLRNEFEKELRER---RNELQKLEKRLL-QKE--ENLDRK 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1981090065 1065 QrhlaEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQikdLKEKLE 1115
Cdd:PRK12704 102 L----ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE---QLQELE 145
|
|
| |
