|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
92-761 |
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: 1340.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASIAAIGDRKKEvANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 251
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKE-SGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 252 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYDYSYVSQGEVTVASIDDSEELLATDSAFDV 331
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 332 LGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 411
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 412 QVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 491
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 492 EEYKKEGIEWEFIDFGMDLQACIDLIEKP-MGIMSILEEECMFPKASDMTFKAKLFDNHLGKSANFGKPRnvKGKSEAHF 570
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPK--PKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 571 SLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYagadaGGDGGKGKGAKKKGSSFQTVSALHRENL 650
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDY-----EESGGGGGKKKKKGGSFRTVSQLHKEQL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 651 NKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTAIPEGQF 730
Cdd:cd01377 553 NKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFD 632
|
650 660 670
....*....|....*....|....*....|.
gi 2163567613 731 iDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd01377 633 -DGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
92-761 |
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: 1286.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASIAAIGDR-KKEVANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 250
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRsKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 251 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYDYSYVSQGEVTVASIDDSEELLATDSAFD 330
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 331 VLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 410
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 411 QQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 490
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 491 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHLGKSANFGKPRNVKGKSEAHF 570
Cdd:cd14916 401 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 571 SLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYaGADAGGDGGKGKGAKKKGSSFQTVSALHRENL 650
Cdd:cd14916 481 SLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-ASADTGDSGKGKGGKKKGSSFQTVSALHRENL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 651 NKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTAIPEGQF 730
Cdd:cd14916 560 NKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 639
|
650 660 670
....*....|....*....|....*....|.
gi 2163567613 731 IDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14916 640 IDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
92-761 |
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: 1278.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASIAAIGDRKKEVANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 251
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 252 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYDYSYVSQGEVTVASIDDSEELLATDSAFDV 331
Cdd:cd14913 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 332 LGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 411
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 412 QVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 491
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 492 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHLGKSANFGKPRNVKGKSEAHFS 571
Cdd:cd14913 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 572 LIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYagADAGGDGGKGKGAKKKGSSFQTVSALHRENLN 651
Cdd:cd14913 481 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATF--ATADADSGKKKVAKKKGSSFQTVSALFRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 652 KLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTAIPEGQFI 731
Cdd:cd14913 559 KLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 2163567613 732 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14913 639 DSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
92-761 |
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: 1237.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASIAAIGDRKKEVANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 251
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 252 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYDYSYVSQGEVTVASIDDSEELLATDSAFDV 331
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 332 LGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 411
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 412 QVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 491
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 492 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHLGKSANFGKPRNVKGKSEAHFS 571
Cdd:cd14917 401 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 572 LIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYagADAGGDGGKGKGAKKKGSSFQTVSALHRENLN 651
Cdd:cd14917 481 LIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANY--AGADAPIEKGKGKAKKGSSFQTVSALHRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 652 KLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTAIPEGQFI 731
Cdd:cd14917 559 KLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 2163567613 732 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14917 639 DSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
93-761 |
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: 1202.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGE 172
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 173 SGAGKTVNTKRVIQYFASIAAIGD--RKKEVANSSK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 248
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDgpGKKAQFLATKtgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 249 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYDYSYVSQGEVTVASIDDSEELLATDSA 328
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 329 FDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 408
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 409 SVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 488
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 489 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHLGKSANFGKPR-NVKGKSE 567
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRpDKKRKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 568 AHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAGADAGGD-GGKGKGAKKKGSSFQTVSALH 646
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEDpKSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 647 RENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTAIP 726
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 2163567613 727 EGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14927 642 DDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
92-761 |
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: 1150.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASIAAIGDRKKEVANSS-KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 250
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 251 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYDYSYVSQGEVTVASIDDSEELLATDSAFD 330
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 331 VLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 410
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 411 QQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 490
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 491 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHLGKSANFGKPRNVKGKSEAHF 570
Cdd:cd14923 401 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 571 SLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAGADAGGDGGKGKGAKKKGSSFQTVSALHRENL 650
Cdd:cd14923 481 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSGGSKKGGKKKGSSFQTVSAVFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 651 NKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTAIPEGQF 730
Cdd:cd14923 561 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 2163567613 731 IDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14923 641 IDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
92-761 |
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: 1141.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASIAAIGDRKKEVANSSK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 249
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 250 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYDYSYVSQGEVTVASIDDSEELLATDSAF 329
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 330 DVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 409
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 410 VQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 489
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 490 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHLGKSANFGKPRNVKGKSEAH 569
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 570 FSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNyAGADAGGDGGKGKGAKKKGSSFQTVSALHREN 649
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-GQTAEAEGGGGKKGGKKKGSSFQTVSALFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 650 LNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTAIPEGQ 729
Cdd:cd14915 560 LNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 2163567613 730 FIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14915 640 FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
92-761 |
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: 1141.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASIAAIGDRKKEVANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 251
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 252 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYDYSYVSQGEVTVASIDDSEELLATDSAFDV 331
Cdd:cd14918 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 332 LGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 411
Cdd:cd14918 241 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 412 QVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 491
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 492 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHLGKSANFGKPRNVKGKSEAHFS 571
Cdd:cd14918 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 572 LIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYagADAGGDGGKGKGAKKKGSSFQTVSALHRENLN 651
Cdd:cd14918 481 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--ASAEADSGAKKGAKKKGSSFQTVSALFRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 652 KLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTAIPEGQFI 731
Cdd:cd14918 559 KLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFI 638
|
650 660 670
....*....|....*....|....*....|
gi 2163567613 732 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14918 639 DSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
92-761 |
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: 1135.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASIAAIGDRKKEVANSSK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 249
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 250 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYDYSYVSQGEVTVASIDDSEELLATDSAF 329
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 330 DVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 409
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 410 VQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 489
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 490 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHLGKSANFGKPRNVKGKSEAH 569
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 570 FSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNyAGADAGGDGGKGKGAKKKGSSFQTVSALHREN 649
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSG-AAAAEAEEGGGKKGGKKKGSSFQTVSALFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 650 LNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTAIPEGQ 729
Cdd:cd14910 560 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 2163567613 730 FIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14910 640 FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
92-761 |
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: 1121.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASIAAIGDRKKEVANSSK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 249
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 250 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYDYSYVSQGEVTVASIDDSEELLATDSAF 329
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 330 DVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 409
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 410 VQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 489
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 490 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHLGKSANFGKPRNVKGKSEAH 569
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 570 FSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAGAD-AGGDGGKGKGAKKKGSSFQTVSALHRE 648
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEgASAGGGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 649 NLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTAIPEG 728
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 2163567613 729 QFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14912 641 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
80-761 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1082.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 80 IEDMAMLTFLHEPAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNML 159
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 160 TDRENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRKKEvansskGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGK 239
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV------GRLEEQILQSNPILEAFGNAKTVRNNNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 240 FIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITnNPYDYSYVSQ-GEVTVASIDD 318
Cdd:pfam00063 155 YIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLSQsGCYTIDGIDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 319 SEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVK 398
Cdd:pfam00063 234 SEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 399 VGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQ-PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEK 477
Cdd:pfam00063 314 TGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 478 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLFDNHlGKSANF 556
Cdd:pfam00063 394 LQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 557 GKPRNvkgKSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAGADAGGDGGKGKGA--KK 634
Cdd:pfam00063 472 QKPRL---QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTpkRT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 635 KGSSFQTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 714
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2163567613 715 QRYRILNPTAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:pfam00063 629 QRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
92-761 |
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: 1065.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASIAAIGDRKKEVansskGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 251
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL-----GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 252 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKpELLEMLLITNNPYDYSYVSQGEVTVASIDDSEELLATDSAFDV 331
Cdd:cd14929 156 SSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 332 LGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 411
Cdd:cd14929 235 LGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 412 QVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 491
Cdd:cd14929 315 QVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 492 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHLGKSANFGKPRNVKGKSEAHFS 571
Cdd:cd14929 395 EEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHFE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 572 LIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYagADAGGDGGKGKGAKKKGSSFQTVSALHRENLN 651
Cdd:cd14929 475 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY--ISTDSAIQFGEKKRKKGASFQTVASLHKENLN 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 652 KLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTAIPEGQFI 731
Cdd:cd14929 553 KLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFV 632
|
650 660 670
....*....|....*....|....*....|
gi 2163567613 732 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14929 633 SSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
73-773 |
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: 1024.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 73 NPPKFDRIEDMAMLTFLHEPAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISD 152
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 153 NAYQNMLTDRENQSILITGESGAGKTVNTKRVIQYFASIAAigdrkkevANSSKGTLEDQIIQANPALEAFGNAKTVRND 232
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG--------SNTEVGSVEDQILESNPILEAFGNAKTLRNN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 233 NSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNnPYDYSYVSQG-EV 311
Cdd:smart00242 153 NSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGgCL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 312 TVASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQA-EPDGTEDADKSAYLMGLNSADLLK 390
Cdd:smart00242 232 TVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 391 GLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLC 470
Cdd:smart00242 312 ALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 471 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLfDNH 549
Cdd:smart00242 392 INYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKL-NQH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 550 LGKSANFGKPRNvkgKSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYagadaggdggkg 629
Cdd:smart00242 470 HKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG------------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 630 KGAKKKGSSFQTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRIL 709
Cdd:smart00242 535 VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLP 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163567613 710 YGDFRQRYRILNPTAIPEGQFiDSRKGAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRD 773
Cdd:smart00242 615 FDEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
93-761 |
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: 1023.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGE 172
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 173 SGAGKTVNTKRVIQYFASIAAIGdrkkEVANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 252
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTG----KQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 253 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYDYSYVSQGEVTVASIDDSEELLATDSAFDVL 332
Cdd:cd14934 158 GADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 333 GFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQ 412
Cdd:cd14934 238 GFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 413 VYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 492
Cdd:cd14934 318 CNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 493 EYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHLGKSANFGKPRNVKGK-SEAHFS 571
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAHFE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 572 LIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFsnyagadAGGDGGKGKGAKKKGSSFQTVSALHRENLN 651
Cdd:cd14934 478 LVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLF-------KEEEAPAGSKKQKRGSSFMTVSNFYREQLN 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 652 KLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTAIPEGqFI 731
Cdd:cd14934 551 KLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FV 629
|
650 660 670
....*....|....*....|....*....|
gi 2163567613 732 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14934 630 DNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
92-761 |
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: 998.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASIAAigDRKKEVANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 251
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGA--SKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 252 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYDYSYVSQGEVTVASIDDSEELLATDSAFDV 331
Cdd:cd14909 159 AGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 332 LGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 411
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 412 QVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 491
Cdd:cd14909 319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 492 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHLGKSANFGKPRNVK-GKSEAHF 570
Cdd:cd14909 399 EEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAAHF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 571 SLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYaGADAGGDGGKGKGAKKKGSSFQTVSALHRENL 650
Cdd:cd14909 479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADH-AGQSGGGEQAKGGRGKKGGGFATVSSAYKEQL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 651 NKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTAIPEGQf 730
Cdd:cd14909 558 NSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE- 636
|
650 660 670
....*....|....*....|....*....|.
gi 2163567613 731 iDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14909 637 -DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
92-761 |
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: 841.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRT-EVPPHIFSISDNAYQNMLTDRENQSILIT 170
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 171 GESGAGKTVNTKRVIQYFASIAAIGDRKKevaNSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 250
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKS---SSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 251 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYDYSY----VSQGEVTVASIDDSEELLATD 326
Cdd:cd00124 158 LVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDDAEEFQELL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 327 SAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREE--QAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 404
Cdd:cd00124 238 DALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 405 TKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSL--ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 482
Cdd:cd00124 318 TKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 483 NHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLFDNHLGKSANFGKPRn 561
Cdd:cd00124 398 NQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 562 vkgKSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSalkllaslfsnyagadaggdggkgkgakkkgSSFqt 641
Cdd:cd00124 476 ---KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG-------------------------------SQF-- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 642 vsalhRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 721
Cdd:cd00124 520 -----RSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILA 594
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2163567613 722 PTAiPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd00124 595 PGA-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
30-1298 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 837.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 30 CFVPHPQLEFIRARVTARAGNGVTVTtEMGETLTVPEADVHPQ-------NPPKFDRIEDMAMLTFLHEPAVLYNLKERY 102
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVT-EEGKKEDGESVSVKKKvlgndriKLPKFDGVDDLTELSYLNEPAVLHNLEKRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 103 ASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGESGAGKTVNTK 182
Cdd:COG5022 91 NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 183 RVIQYFASIAAigdrkkeVANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLE 262
Cdd:COG5022 171 RIMQYLASVTS-------SSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 263 KSRVIFQLKAERNYHIFYQILSNKkPELLEMLLITNNPYDYSYVSQGEVT-VASIDDSEELLATDSAFDVLGFTAEEKAG 341
Cdd:COG5022 244 KSRVVHQNKNERNYHIFYQLLAGD-PEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 342 VYKLTGAIMHFGNMKFKqKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALA 421
Cdd:COG5022 323 IFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 422 KAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEW 501
Cdd:COG5022 402 KALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEW 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 502 EFIDFgMDLQACIDLIEK--PMGIMSILEEECMFPKASDMTFKAKLFDN-HLGKSANFGKPRnvkgKSEAHFSLIHYAGT 578
Cdd:COG5022 482 SFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSR----FRDNKFVVKHYAGD 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 579 VDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYagadaggdggkgkGAKKKGSSFQTVSALHRENLNKLMANLK 658
Cdd:COG5022 557 VEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE-------------ENIESKGRFPTLGSRFKESLNSLMSTLN 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 659 TTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTAIPEGQFI---DSRK 735
Cdd:COG5022 624 STQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDTKN 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 736 GAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSLIITRIQAQARGQLMRIEFKKILERRDALLVIQWNIRA 815
Cdd:COG5022 704 AVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRL 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 816 FMGVKNWPWMKLYFKIKPLLKSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMvsMLQEKNDLQLQVQAEQdnlad 895
Cdd:COG5022 784 RRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEF--SLKAEVLIQKFGRSLK----- 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 896 AEERCDQLIKNKIQLEAKvkemterleeeeemnAELAAKKRKLedecSELKKDIDDLE-LSLAKVEKEKHATENKVKNLT 974
Cdd:COG5022 857 AKKRFSLLKKETIYLQSA---------------QRVELAERQL----QELKIDVKSISsLKLVNLELESEIIELKKSLSS 917
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 975 EEMAGLDENITKLTKEKKILQEShqqalddlQAEEDKvnTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDL 1054
Cdd:COG5022 918 DLIENLEFKTELIARLKKLLNNI--------DLEEGP--SIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREG 987
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1055 KLAQESImdlendkqqleERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTgRAKVEKLRSEL 1134
Cdd:COG5022 988 NKANSEL-----------KNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSI-LKPLQKLKGLL 1055
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1135 LQELEETSERLEeaggatsvQLELNKKQEAEFQKLrrdleeaTLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEK 1214
Cdd:COG5022 1056 LLENNQLQARYK--------ALKLRRENSLLDDKQ-------LYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVA 1120
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1215 E--KSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQM-----NEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLE 1287
Cdd:COG5022 1121 QmiKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLfweanLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSEVN 1200
|
1290
....*....|.
gi 2163567613 1288 EKEAFINQLTR 1298
Cdd:COG5022 1201 DLKNELIALFS 1211
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
93-761 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 797.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGE 172
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 173 SGAGKTVNTKRVIQYFASIAAIGDRKKEVANSSK-------GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF 245
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAvnpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 246 GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLItNNPYDYSYVSQGEVTVASIDDSEELLAT 325
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 326 DSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 404
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNTV-AQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 405 TKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 483
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 484 HHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHLgksanfGKPRNVK 563
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 564 G--KSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAGADAGGDGGKGKG--AKKKGSSF 639
Cdd:cd14911 474 TdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQfgARTRKGMF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 640 QTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 719
Cdd:cd14911 554 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2163567613 720 LNPTAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14911 634 LTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
93-761 |
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: 764.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGE 172
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 173 SGAGKTVNTKRVIQYFASIAAigDRKKEVANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 252
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVAS--SHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 253 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLItnNPYD-YSYVSQGEVTVASIDDSEELLATDSAFDV 331
Cdd:cd14920 160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL--EGFNnYRFLSNGYIPIPGQQDKDNFQETMEAMHI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 332 LGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 410
Cdd:cd14920 238 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENTV-AQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 411 QQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQpRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 488
Cdd:cd14920 317 EQADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 489 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLFdNHLGKSANFGKPRNVKGk 565
Cdd:cd14920 396 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKD- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 566 sEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAGADAGGDGGKGKGA------KKKGSSF 639
Cdd:cd14920 474 -KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETafgsayKTKKGMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 640 QTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 719
Cdd:cd14920 553 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2163567613 720 LNPTAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14920 633 LTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
93-761 |
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: 719.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGE 172
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 173 SGAGKTVNTKRVIQYFASIAAIGDRKKEVANS--SKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 250
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 251 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPyDYSYVSQGEVTVASIDDSEELLATDSAFD 330
Cdd:cd14932 162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYS-KYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 331 VLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 409
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDTA-AQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 410 VQQVYYSIGALAKAVYEKMFNWMVVRINNSLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 488
Cdd:cd14932 320 QEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 489 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLFdNHLGKSANFGKPRnvKGK 565
Cdd:cd14932 400 LEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPK--KLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 566 SEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAG-----ADAGGDGGKGKGAKKKGSSFQ 640
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRivgldKVAGMGESLHGAFKTRKGMFR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 641 TVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 720
Cdd:cd14932 557 TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 636
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2163567613 721 NPTAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14932 637 TPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
92-761 |
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: 698.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYA-SWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILIT 170
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 171 GESGAGKTVNTKRVIQYFASIAAigdrkkevANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 250
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGG--------SSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 251 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNK-KPELLEMLLITNNpyDYSYVSQGE-VTVASIDDSEELLATDSA 328
Cdd:cd01380 153 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKELHLGSAE--DFFYTNQGGsPVIDGVDDAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 329 FDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 408
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 409 SVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQP--RQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 486
Cdd:cd01380 311 TLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 487 FVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHLGK-SANFGKPRNVKGK 565
Cdd:cd01380 391 FKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 566 seahFSLIHYAGTVDYNIIGWLEKNKDPLNEtvvglyqkSALKLLASlfsnyagadaggdggkgkgakkkgSSF--QTVS 643
Cdd:cd01380 470 ----FIVKHFADDVEYQVEGFLEKNRDTVSE--------EHLNVLKA------------------------SKNrkKTVG 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 644 ALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPT 723
Cdd:cd01380 514 SQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPS 593
|
650 660 670
....*....|....*....|....*....|....*...
gi 2163567613 724 AipEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd01380 594 K--EWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
93-761 |
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: 691.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGE 172
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 173 SGAGKTVNTKRVIQYFASIAAIGDRKKEvaNSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 252
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVASSHKGKKD--TSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 253 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPyDYSYVSQGEVTVASIDDSEELLATDSAFDVL 332
Cdd:cd14921 160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFN-NYTFLSNGFVPIPAAQDDEMFQETLEAMSIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 333 GFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 411
Cdd:cd14921 239 GFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNTA-AQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 412 QVYYSIGALAKAVYEKMFNWMVVRINNSLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 490
Cdd:cd14921 318 QADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 491 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLFDNHlGKSANFGKPRNVKGKSE 567
Cdd:cd14921 398 QEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLKDKTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 568 ahFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAGADAGGDGGKGKGAKKKGSS------FQT 641
Cdd:cd14921 477 --FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASktkkgmFRT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 642 VSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 721
Cdd:cd14921 555 VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2163567613 722 PTAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14921 635 ANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
93-761 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 684.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGE 172
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 173 SGAGKTVNTKRVIQYFASIAAIGDRKKEvanssKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 252
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVASSHKSKKD-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 253 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLItnNPYD-YSYVSQGEVTVASIDDSEELLATDSAFDV 331
Cdd:cd14919 157 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 332 LGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 410
Cdd:cd14919 235 MGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNTA-AQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 411 QQVYYSIGALAKAVYEKMFNWMVVRINNSLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 489
Cdd:cd14919 314 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 490 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLFDNHlGKSANFGKPRNVKGKs 566
Cdd:cd14919 394 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 567 eAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSN------YAGADAGGDGGKGKGAKKKGSSFQ 640
Cdd:cd14919 472 -ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDvdriigLDQVAGMSETALPGAFKTRKGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 641 TVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 720
Cdd:cd14919 551 TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2163567613 721 NPTAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14919 631 TPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
93-761 |
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: 684.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGE 172
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 173 SGAGKTVNTKRVIQYFASIAAIGDRKKEVAN--SSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 250
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVASSHKTKKDQNSlaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 251 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPyDYSYVSQGEVTVASIDDSEELLATDSAFD 330
Cdd:cd15896 162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYN-NYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 331 VLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 409
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASmPDNTA-AQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 410 VQQVYYSIGALAKAVYEKMFNWMVVRINNSLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 488
Cdd:cd15896 320 QEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 489 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLFDNHlGKSANFGKPRnvKGK 565
Cdd:cd15896 400 LEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKPK--KLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 566 SEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAG----ADAGGDGGKGKGAKKKGSSFQT 641
Cdd:cd15896 477 DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRivglDKVSGMSEMPGAFKTRKGMFRT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 642 VSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 721
Cdd:cd15896 557 VGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 636
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2163567613 722 PTAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd15896 637 PNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
93-761 |
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: 665.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGE 172
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 173 SGAGKTVNTKRVIQYFASIAAIGDRKKEVAnsSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 252
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVASSPKGRKEPG--VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 253 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYdYSYVSQGEVTVASiDDSEELLATDSAFDVL 332
Cdd:cd14930 160 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 333 GFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 411
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNTA-AQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 412 QVYYSIGALAKAVYEKMFNWMVVRINNSLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 489
Cdd:cd14930 317 QADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 490 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLFDNHlGKSANFGKPRNVkgKS 566
Cdd:cd14930 396 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHL--RD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 567 EAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAGADAGGDGGKGKG----AKKKGSSFQTV 642
Cdd:cd14930 473 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDgppgGRPRRGMFRTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 643 SALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP 722
Cdd:cd14930 553 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 632
|
650 660 670
....*....|....*....|....*....|....*....
gi 2163567613 723 TAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14930 633 NAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
93-761 |
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: 650.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGE 172
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 173 SGAGKTVNTKRVIQYFASIAaiGDRKKEVansskGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 252
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVS--GGSESEV-----ERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 253 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYDYSYVSQGEVTVASIDDSEELLATDSAFDVL 332
Cdd:cd01378 155 GGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 333 GFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEY---VTKGQS 409
Cdd:cd01378 235 GFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISDTSV-LDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 410 VQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQ-YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHhmFV 488
Cdd:cd01378 314 VEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE--LT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 489 L--EQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFP-KASDMTFKAKLfDNHLGKSANFGKPRNVKG 564
Cdd:cd01378 392 LkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 565 KSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAGADAGGDGGkgkgakkkgssfqTVSA 644
Cdd:cd01378 470 LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSKKRPP-------------TAGT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 645 LHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTA 724
Cdd:cd01378 537 KFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKT 616
|
650 660 670
....*....|....*....|....*....|....*..
gi 2163567613 725 IPEGQFIDsRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd01378 617 WPAWDGTW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
93-761 |
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: 638.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGE 172
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 173 SGAGKTVNTKRVIQYFASIAAigdrkkevansSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 252
Cdd:cd01381 82 SGAGKTESTKLILQYLAAISG-----------QHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 253 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITnNPYDYSYVSQGE-VTVASIDDSEELLATDSAFDV 331
Cdd:cd01381 151 GAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELG-DASDYYYLTQGNcLTCEGRDDAAEFADIRSAMKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 332 LGFTAEEKAGVYKLTGAIMHFGNMKFKQKQRE--EQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 409
Cdd:cd01381 230 LMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 410 VQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYF---IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 486
Cdd:cd01381 310 AEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 487 FVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLFDNHlGKSANFGKPRNvkgK 565
Cdd:cd01381 390 FKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKPKS---D 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 566 SEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAGADAGGDGGKgkgakkkgssfQTVSAL 645
Cdd:cd01381 465 LNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKS-----------PTLSSQ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 646 HRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPtAI 725
Cdd:cd01381 534 FRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP-GI 612
|
650 660 670
....*....|....*....|....*....|....*.
gi 2163567613 726 PEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd01381 613 PPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
92-761 |
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: 637.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRgkKRTEVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASIAAIGDRkkevansskgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 251
Cdd:cd01383 79 ESGAGKTETAKIAMQYLAALGGGSSG-----------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 252 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITnNPYDYSYVSQGE-VTVASIDDSEELLATDSAFD 330
Cdd:cd01383 148 CGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLK-SASEYKYLNQSNcLTIDGVDDAKKFHELKEALD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 331 VLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 410
Cdd:cd01383 227 TVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 411 QQVYYSIGALAKAVYEKMFNWMVVRINNSLET-KQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 489
Cdd:cd01383 307 QQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 490 EQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLfDNHLGKSANFgkprnvKGKSEA 568
Cdd:cd01383 387 EQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGERGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 569 HFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNyaGADAGGDGGKGKGAKKKGSSFQTVSALHRE 648
Cdd:cd01383 459 AFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASK--MLDASRKALPLTKASGSDSQKQSVATKFKG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 649 NLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTAIPEG 728
Cdd:cd01383 537 QLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSAS 616
|
650 660 670
....*....|....*....|....*....|...
gi 2163567613 729 QFIDSRKGAekLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd01383 617 QDPLSTSVA--ILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
93-761 |
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: 623.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGE 172
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 173 SGAGKTVNTKRVIQYfasIAAIGDRKKEVansskgtlEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 252
Cdd:cd14883 82 SGAGKTETTKLILQY---LCAVTNNHSWV--------EQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 253 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKK--PELLEmLLITNNPYDYSYVSQ-GEVTVASIDDSEELLATDSAF 329
Cdd:cd14883 151 GAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKE-KLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRLAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 330 DVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAE-PDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 408
Cdd:cd14883 230 NVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 409 SVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 488
Cdd:cd14883 310 KVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 489 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKASDMTFKAKLFDNHlGKSANFGKPRnvKGKSE 567
Cdd:cd14883 390 LEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPD--RRRWK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 568 AHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFS---NYAGADAGGDGGKGKGAKKKGSSFQTVSA 644
Cdd:cd14883 466 TEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTypdLLALTGLSISLGGDTTSRGTSKGKPTVGD 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 645 LHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP-- 722
Cdd:cd14883 546 TFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPra 625
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 2163567613 723 -TAIPEGQFIDSRkgaeKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14883 626 rSADHKETCGAVR----ALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
92-761 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 589.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILIT 170
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 171 GESGAGKTVNTKRVIQYfasIAAIGDRkkevANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 250
Cdd:cd01384 81 GESGAGKTETTKMLMQY---LAYMGGR----AVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 251 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLItNNPYDYSYVSQGE-VTVASIDDSEELLATDSAF 329
Cdd:cd01384 154 ISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKL-KDPKQFHYLNQSKcFELDGVDDAEEYRATRRAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 330 DVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEP--DGTEDADK-SAYLMGLNSADLLKGLCHPRVKVGNEYVTK 406
Cdd:cd01384 233 DVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPkdEKSEFHLKaAAELLMCDEKALEDALCKRVIVTPDGIITK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 407 GQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 486
Cdd:cd01384 313 PLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 487 FVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLFDNhLGKSANFGKPRnvkgK 565
Cdd:cd01384 393 FKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPK----L 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 566 SEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFsnyagadaggdGGKGKGAKKKGSSFQTVSAL 645
Cdd:cd01384 467 SRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF-----------PPLPREGTSSSSKFSSIGSR 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 646 HRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTAI 725
Cdd:cd01384 536 FKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVL 615
|
650 660 670
....*....|....*....|....*....|....*.
gi 2163567613 726 peGQFIDSRKGAEKLLGSLDIdhNQYKFGHTKVFFK 761
Cdd:cd01384 616 --KGSDDEKAACKKILEKAGL--KGYQIGKTKVFLR 647
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
92-761 |
5.15e-175 |
|
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: 546.68 E-value: 5.15e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFAsiaaigdrkkEVANSSKGtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 251
Cdd:cd14872 81 ESGAGKTEATKQCLSFFA----------EVAGSTNG-VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 252 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLlitNNPYDYSYVSQGE-VTVASIDDSEELLATDSAFD 330
Cdd:cd14872 150 CGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGW---GSSAAYGYLSLSGcIEVEGVDDVADFEEVVLAME 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 331 VLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKS---AYLMGLNSADLLKGLCHPRVKVgneyvtKG 407
Cdd:cd14872 227 QLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLkevATLLGVDAATLEEALTSRLMEI------KG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 408 Q-------SVQQVYYSIGALAKAVYEKMFNWMVVRINNSLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQ 479
Cdd:cd14872 301 CdptriplTPAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 480 QFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKASDMTFKAKLfDNHLGKSANFGk 558
Cdd:cd14872 381 QHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAA-NQTHAAKSTFV- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 559 pRNVKGKSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSnyagadaggdggkgKGAKKKGSS 638
Cdd:cd14872 458 -YAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFP--------------PSEGDQKTS 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 639 FQTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 718
Cdd:cd14872 523 KVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYR 602
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2163567613 719 ILnPTAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14872 603 FL-VKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
95-761 |
3.61e-170 |
|
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: 533.75 E-value: 3.61e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 95 LYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGES 173
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 174 GAGKTVNTKRVIQYFAsiaaigdrkkEVANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 253
Cdd:cd01382 84 GAGKTESTKYILRYLT----------ESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 254 ADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLitnnpydysyvsqgevTVASIDDSEELLATDSAFDVLG 333
Cdd:cd01382 154 GFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 334 FTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKS----AYLMGLNSADLLKGLCHpRVKVGNEYVTKGQS 409
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKSEQSleyaAELLGLDQDELRVSLTT-RVMQTTRGGAKGTV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 410 ------VQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQpRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 483
Cdd:cd01382 297 ikvplkVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 484 HHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLFDNHLgKSANFGKPRnv 562
Cdd:cd01382 376 ERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK-NHFRLSIPR-- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 563 KGKSEAH--------FSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFsnyagaDAGGDGGKGKGAKK 634
Cdd:cd01382 452 KSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLF------ESSTNNNKDSKQKA 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 635 KGSSFQTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 714
Cdd:cd01382 526 GKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLY 605
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2163567613 715 QRYRILNPTAIPEgqfIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd01382 606 NMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
92-761 |
2.96e-169 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 531.66 E-value: 2.96e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILIT 170
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 171 GESGAGKTVNTKRVIQYFASIAaigdrkkevansskGTLED----QIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 246
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA--------------GGLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 247 ATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLlitnnPYDYSYVSQGEVTVASID---DSEELL 323
Cdd:cd14903 147 KNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFL-----DSANECAYTGANKTIKIEgmsDRKHFA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 324 ATDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAE--PDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGN 401
Cdd:cd14903 222 RTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 402 EYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 481
Cdd:cd14903 302 DVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 482 FNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHLGKSANFGKPRN 561
Cdd:cd14903 382 FTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRT 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 562 vkgkSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAGADAGGDGGKGKGAKKKGS---S 638
Cdd:cd14903 461 ----SRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGgalT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 639 FQTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 718
Cdd:cd14903 537 TTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFW 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2163567613 719 ILNPTAipEGQFIDSRKGAEKLLGSLDIDH-NQYKFGHTKVFFK 761
Cdd:cd14903 617 LFLPEG--RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
93-761 |
5.26e-167 |
|
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: 525.50 E-value: 5.26e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRTEVPPHIFSISDNAY----QNMLTDRENQSI 167
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtqliQSGVLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 168 LITGESGAGKTVNTKRVIQYFASIA---AIGDRKKEVANSSK-----GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGK 239
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARITsgfAQGASGEGEAASEAieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 240 FIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNnPYDYSYVSQGEVTVASIDDS 319
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 320 EELLATDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGT-EDADKSAYLMGLNSADLLKGLCHPRVK 398
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 399 VGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 478
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 479 QQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILE--EECMFPKAS--DMTFKAKLFDNHLGKS 553
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgKVNGKPGIFItlDDCWRFKGEeaNKKFVSQLHASFGRKS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 554 ANFGKPRNVKGK---------SEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASlfsnyagadagg 624
Cdd:cd14890 480 GSGGTRRGSSQHphfvhpkfdADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSIREV------------ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 625 dggkgkgakkkgssfqTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGF 704
Cdd:cd14890 548 ----------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGF 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2163567613 705 PNRILYGDFRQRYRILNPTAIPEGQFIdsrkgaEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14890 612 ALREEHDSFFYDFQVLLPTAENIEQLV------AVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
92-761 |
1.06e-164 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 517.98 E-value: 1.06e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASIAAIGDRkkevansskgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 251
Cdd:cd01379 81 ESGAGKTESANLLVQQLTVLGKANNR----------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 252 ASADIETYLLEKSRVIFQLKAERNYHIFYQIL----SNKKpeLLEMLLITNNPYDYSYVSQGEVTVASIDDS--EELLAT 325
Cdd:cd01379 151 TGARISEYLLEKSRVVHQAIGERNFHIFYYIYaglaEDKK--LAKYKLPENKPPRYLQNDGLTVQDIVNNSGnrEKFEEI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 326 DSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQ----AEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGN 401
Cdd:cd01379 229 EQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 402 EYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSL---ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 478
Cdd:cd01379 309 ETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpdRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 479 QQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACID-LIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHlgKSANFG 557
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYYW 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 558 KPRNVkgksEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLAslfsnyagadaggdggkgkgakkkgs 637
Cdd:cd01379 466 RPKSN----ALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR-------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 638 sfQTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRY 717
Cdd:cd01379 516 --QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRY 593
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2163567613 718 RIL--NPTAIPEGqfidSRKGAEKLLGSLDIDHnqYKFGHTKVFFK 761
Cdd:cd01379 594 YFLafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
841-1918 |
2.15e-164 |
|
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: 532.83 E-value: 2.15e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 841 EKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTER 920
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 921 LEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQESHQQ 1000
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1001 ALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDF 1080
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1081 ELNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEEAGGATSVQLELNK 1160
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1161 KQEAEFQKLRRDLEEATLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNL 1240
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1241 EKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKA 1320
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1321 KNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQEAEEAVE 1400
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1401 AVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLK 1480
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1481 NAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLEF 1560
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1561 NQVKADYERKLAEKDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKA 1640
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1641 LQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLIN 1720
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1721 QKKKMEADISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLAL 1800
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1801 KGGKKQLQKLEVRVRELENELEAEQKRNAESIKGLRKSERRVKELSYQTEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEA 1880
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 2163567613 1881 EEQANSNLAKFRKVQHELDEAEERADMAESQVNKLRAR 1918
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
92-759 |
5.64e-164 |
|
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: 517.03 E-value: 5.64e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY------RGKKRTEVPPHIFSISDNAYQNMLTDRE-- 163
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 164 --NQSILITGESGAGKTVNTKRVIQYFASIAAIgdRKKEVANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFI 241
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSA--TTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 242 RIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPyDYSYVSQGEVTVA--SIDDS 319
Cdd:cd14901 159 RLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVE-EYKYLNSSQCYDRrdGVDDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 320 EELLATDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTE-DADKSAYLMGLNSADLLKGLCHPRVK 398
Cdd:cd14901 238 VQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLaNVRAACDLLGLDMDVLEKTLCTREIR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 399 VGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQP--RQYFIGVLDIAGFEIFDFNSFEQLCINFTNE 476
Cdd:cd14901 318 AGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFANE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 477 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDlQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLFDNhLGKSAN 555
Cdd:cd14901 398 KLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHAS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 556 FGKPRNVKGKSEahFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASlfsnyagadaggdggkgkgakkk 635
Cdd:cd14901 476 FSVSKLQQGKRQ--FVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 636 gssfqTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ 715
Cdd:cd14901 531 -----TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVH 605
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2163567613 716 RYRILNPTAIPEGQFIDSRKGAEKLLGSLDI----DHNQYKFGHTKVF 759
Cdd:cd14901 606 TYSCLAPDGASDTWKVNELAERLMSQLQHSElnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
93-761 |
6.76e-163 |
|
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: 514.30 E-value: 6.76e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGE 172
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 173 SGAGKTVNTKRVIQYFASiaaigdrkkeVANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGKLA 252
Cdd:cd01387 82 SGSGKTEATKLIMQYLAA----------VNQRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 253 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKkPELLEMLLITNNPYDYSYVSQG-EVTVASIDDSEELLATDSAFDV 331
Cdd:cd01387 151 GAITSQYLLEKSRIVTQAKNERNYHVFYELLAGL-PAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAMQV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 332 LGFTAEEKAGVYKLTGAIMHFGNMKFKQKQRE---EQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 408
Cdd:cd01387 230 LGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 409 SVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 488
Cdd:cd01387 310 TIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 489 LEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLFDNHlGKSANFGKPRnvkgKSE 567
Cdd:cd01387 390 LEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPR----MPL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 568 AHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYagadagGDGGKGKGAKKKGSSF-------Q 640
Cdd:cd01387 464 PEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH------RAQTDKAPPRLGKGRFvtmkprtP 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 641 TVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 720
Cdd:cd01387 538 TVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 2163567613 721 NPTAIPEGQFIDSRkgaEKLLGSLD--IDHNQYKFGHTKVFFK 761
Cdd:cd01387 618 VALKLPRPAPGDMC---VSLLSRLCtvTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
92-761 |
4.60e-162 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 512.32 E-value: 4.60e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRgKKRTEVPPHIFSISDNAYQNMLTDRENQSILIT 170
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 171 GESGAGKTVNTKRVIQYFASiAAIGDRKKevanssKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF----- 245
Cdd:cd14888 80 GESGAGKTESTKYVMKFLAC-AGSEDIKK------RSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklks 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 246 ----GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILS-NKKPELLEMLLITNNPYD------------------ 302
Cdd:cd14888 153 krmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaAREAKNTGLSYEENDEKLakgadakpisidmssfep 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 303 ---YSYVSQ-GEVTVASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQA---EPDGTEDAD 375
Cdd:cd14888 233 hlkFRYLTKsSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTDDLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 376 KSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLE-TKQPRQYFIGVLD 454
Cdd:cd14888 313 KVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGVLD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 455 IAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLI-EKPMGIMSILEEECMF 533
Cdd:cd14888 393 IFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 534 PKASDMTFKAKLFDNHLGKSaNFGKprnVKGKSEAhFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASL 613
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKGHK-RFDV---VKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 614 FSNYAGADAGGDGGKGKgakkkgssFQTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGV 693
Cdd:cd14888 547 FSAYLRRGTDGNTKKKK--------FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGV 618
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2163567613 694 LEGIRICRKGFPNRILYGDFRQRYRILNPtaipegqfidsrkgaekllGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14888 619 LQAVQVSRAGYPVRLSHAEFYNDYRILLN-------------------GEGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
95-761 |
1.24e-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: 498.44 E-value: 1.24e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 95 LYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGESG 174
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 175 AGKTVNTKRVIQYFASIaaigdrkkevanSSKGT---LEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 251
Cdd:cd01385 84 SGKTESTNFLLHHLTAL------------SQKGYgsgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 252 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITnNPYDYSYVSQGE-VTVASIDDSEELLATDSAFD 330
Cdd:cd01385 152 RGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLK-QPEDYHYLNQSDcYTLEGEDEKYEFERLKQAME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 331 VLGFTAEEKAGVYKLTGAIMHFGNMKFKQK--QREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 408
Cdd:cd01385 231 MVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPY 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 409 SVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQ----PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 484
Cdd:cd01385 311 KLPEAIATRDAMAKCLYSALFDWIVLRINHALLNKKdleeAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 485 HMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKlFDNHLGKSANFGKPRnvk 563
Cdd:cd01385 391 HIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 564 gKSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSAL-----------------KLLASLFSNYAGADAGGDG 626
Cdd:cd01385 466 -VMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSafvreligidpvavfrwAVLRAFFRAMAAFREAGRR 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 627 GKGKGAKKKGSSFQ----------------TVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRC 690
Cdd:cd01385 545 RAQRTAGHSLTLHDrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRY 624
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163567613 691 NGVLEGIRICRKGFPNRILYGDFRQRYRILnptaIPEGQfIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd01385 625 TGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
93-761 |
8.68e-153 |
|
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: 486.22 E-value: 8.68e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASIAAIGDRKKEVANSSKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 251
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISQQSLELSLKEKTSC--VEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 252 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITnNPYDYSYVSQ-GEVTVASIDDSEELLATDSAFD 330
Cdd:cd14873 160 QGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLNQsGCVEDKTISDQESFREVITAME 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 331 VLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDadkSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 410
Cdd:cd14873 239 VMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTALGR---SAELLGLDPTQLTDALTQRSMFLRGEEILTPLNV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 411 QQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQyFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 490
Cdd:cd14873 316 QQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 491 QEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHlGKSANFGKPRnvkgKSEAHF 570
Cdd:cd14873 395 QLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPR----VAVNNF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 571 SLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAGADAGGDGGKGKGAKKkgssfQTVSALHRENL 650
Cdd:cd14873 469 GVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRR-----PTVSSQFKDSL 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 651 NKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP-TAIPEgq 729
Cdd:cd14873 544 HSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRnLALPE-- 621
|
650 660 670
....*....|....*....|....*....|..
gi 2163567613 730 fiDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14873 622 --DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
98-761 |
1.07e-151 |
|
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: 483.49 E-value: 1.07e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 98 LKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRTEV--PPHIFSISDNAYQNMLTDR----ENQSILIT 170
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKEEATASspPPHVFSIAERAYRAMKGVGkgqgTPQSIVVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 171 GESGAGKTVNTKRVIQYFASIAAIGDRKKEVANSSKG--TLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 248
Cdd:cd14892 87 GESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 249 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILS----NKKPEL-LEMLLitnnpyDYSYVSQGE-VTVASIDDSEEL 322
Cdd:cd14892 167 GRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAgldaNENAALeLTPAE------SFLFLNQGNcVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 323 LATDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQ--KQREEQAEPDGTEDADKSAYLMGLNSADLLKGLC-----HP 395
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVtqttsTA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 396 RVKVGNEYVTKGQSVQqvyySIGALAKAVYEKMFNWMVVRINNS----------LETKQPRQYFIGVLDIAGFEIFDFNS 465
Cdd:cd14892 321 RGSVLEIKLTAREAKN----ALDALCKYLYGELFDWLISRINAChkqqtsgvtgGAASPTFSPFIGILDIFGFEIMPTNS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 466 FEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEK-PMGIMSILEEECMFP-KASDMTFKA 543
Cdd:cd14892 397 FEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 544 KLFDNHLGKSANFGKPRNvkgkSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSalkllaslfsnyagadag 623
Cdd:cd14892 476 IYHQTHLDKHPHYAKPRF----ECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSS------------------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 624 gdggkgkgakkkgSSFqtvsalhRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKG 703
Cdd:cd14892 534 -------------SKF-------RTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREG 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2163567613 704 FPNRILYGDFRQRYRIL-------NPTAIPEGQFIDSRKGAEKLLGSLdiDHNQYKFGHTKVFFK 761
Cdd:cd14892 594 FPIRRQFEEFYEKFWPLarnkagvAASPDACDATTARKKCEEIVARAL--ERENFQLGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
94-761 |
1.23e-148 |
|
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: 474.18 E-value: 1.23e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 94 VLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKK-RTEVPPHIFSISDNAYQNMLTDRENQSILITGE 172
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 173 SGAGKTVNTKRVIQYFASIAAigdrkkevanSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 252
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKLSP----------SDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 253 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLItNNPYDYSYVSQGEVTVASIDDSEELLATDSAFDVL 332
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELEYYRQMFHDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 333 -------GFTAEEKAGVYKLTGAIMHFGNMKFkqkqrEEQAEPDGTEDADK-----SAYLMGLNSADLLKGLCHPRVKVG 400
Cdd:cd14897 232 tnimkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVNTIR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 401 NEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYF-----IGVLDIAGFEIFDFNSFEQLCINFTN 475
Cdd:cd14897 307 GERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCINLSN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 476 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLfDNHLGKSA 554
Cdd:cd14897 387 ERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 555 NFGKPrnVKGKSEahFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYagadaggdggkgkgakk 634
Cdd:cd14897 465 RYVAS--PGNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY----------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 635 kgssfqtvsalHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 714
Cdd:cd14897 524 -----------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFV 592
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 2163567613 715 QRYRILNPTAIPegqfidSRKGAE-KLLGSLDIDHNQ-YKFGHTKVFFK 761
Cdd:cd14897 593 KRYKEICDFSNK------VRSDDLgKCQKILKTAGIKgYQFGKTKVFLK 635
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
92-761 |
2.85e-144 |
|
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: 462.87 E-value: 2.85e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILIT 170
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 171 GESGAGKTVNTKRVIQYFASIAaiGDRKKEVAnsskgtleDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 250
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA--GGRKDKTI--------AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 251 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSN-KKPELLEMLLITNNPYDYSYVSQGEVTVASIDDSEELLATDSAF 329
Cdd:cd14904 151 LIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 330 DVLGFTAEEKAGVYKLTGAIMHFGNMKFkQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 409
Cdd:cd14904 231 SLIGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 410 VQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQY-FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 488
Cdd:cd14904 310 PVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 489 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHLGKSAN----FGKPRNVKg 564
Cdd:cd14904 390 TVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTKKDNesidFPKVKRTQ- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 565 kseahFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNyagaDAGGDGGKGKGAKKKGSSFQTVSA 644
Cdd:cd14904 468 -----FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGS----SEAPSETKEGKSGKGTKAPKSLGS 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 645 LHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTA 724
Cdd:cd14904 539 QFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPS 618
|
650 660 670
....*....|....*....|....*....|....*...
gi 2163567613 725 IPEGqfiDSRKGAEKLLGSLDIDHN-QYKFGHTKVFFK 761
Cdd:cd14904 619 MHSK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
94-726 |
2.17e-143 |
|
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: 459.39 E-value: 2.17e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 94 VLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAY-----------RGKKRTEVPPHIFSISDNAYQNM--- 158
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 159 -LTDRENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRKKEVANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRF 237
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 238 GKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMllitnnpydysyvsqgevtvasiD 317
Cdd:cd14900 163 GKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKR-----------------------D 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 318 DSEELLAtdsAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDA-------DKSAYLMGLNSADLLK 390
Cdd:cd14900 220 MYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 391 GLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSL-----ETKQPRQYFIGVLDIAGFEIFDFNS 465
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 466 FEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAK 544
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLASK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 545 LFdNHLGKSANFGKPRNVKGKseAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQksalkllaslfsnyagadagg 624
Cdd:cd14900 456 LY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV--------------------- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 625 dggkgkgakkkgSSFQtvsalHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGF 704
Cdd:cd14900 512 ------------YGLQ-----FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGF 574
|
650 660
....*....|....*....|..
gi 2163567613 705 PNRILYGDFRQRYRILNPTAIP 726
Cdd:cd14900 575 PIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
94-761 |
5.63e-140 |
|
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: 451.28 E-value: 5.63e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 94 VLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNML----TDRENQSILI 169
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 170 TGESGAGKTVNTKRVIQYFASIAAigdrkkevANSSkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATG 249
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCR--------GNSQ---LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 250 KLASADIETYLLEKSRVIFQLKAERNYHIFYQI---LSNKKPELLEMLlitnNPYDYSYVSQG---EVTVASIDDSEELL 323
Cdd:cd14889 151 HVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLL----DPGKYRYLNNGagcKREVQYWKKKYDEV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 324 AtdSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREE-QAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNE 402
Cdd:cd14889 227 C--NAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 403 YVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQY---FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQ 479
Cdd:cd14889 305 QIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVelrEIGILDIFGFENFAVNRFEQACINLANEQLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 480 QFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDL-IEKPMGIMSILEEECMFPKASDMTFKAKLfDNHLGKSANFGK 558
Cdd:cd14889 385 YFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYGK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 559 PRNvkgKSEAhFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLF----SNYAGADAGGDGGKGKGAKK 634
Cdd:cd14889 463 SRS---KSPK-FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFtatrSRTGTLMPRAKLPQAGSDNF 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 635 KGSSFQTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 714
Cdd:cd14889 539 NSTRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFA 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2163567613 715 QRYRILNPTAIPEGqfidSRKGAEKLLGSLDIdhNQYKFGHTKVFFK 761
Cdd:cd14889 619 ERYKILLCEPALPG----TKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
94-761 |
9.22e-140 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 451.02 E-value: 9.22e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 94 VLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGK--------KRTEVPPHIFSISDNAYQNMLTDREN 164
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 165 QSILITGESGAGKTVNTKRVIQYFASIAAIGDRKKEV---------ANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSS 235
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVltltssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 236 RFGKFIRIHFG-ATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNP--YDYSYVSQGE-V 311
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLsgDRYDYLKKSNcY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 312 TVASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQ--REEQAEPDGTEDADKSAYLMGLNSADLL 389
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 390 KGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSL--------ETKQPRQYFIGVLDIAGFEIF 461
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 462 DFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF--IDFgMDLQACIDLIEK-PMGIMSILEEECMFPKASD 538
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 539 MTFKAKLFDNHlgksANFGKPRNVKGKSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSnya 618
Cdd:cd14907 482 EKLLNKIKKQH----KNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFS--- 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 619 gADAGGDGGKGKGAKKKGSSFQTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIR 698
Cdd:cd14907 555 -GEDGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIR 633
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2163567613 699 ICRKGFPNRILYGDFRQRYRILNptaipegqfidsrkgaekllgsldidhNQYKFGHTKVFFK 761
Cdd:cd14907 634 VRKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
92-727 |
1.11e-134 |
|
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: 437.42 E-value: 1.11e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYR--GKKRTE-------VPPHIFSISDNAYQNMLTD- 161
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 162 RENQSILITGESGAGKTVNTKRVIQYFASIAAIGDR-KKEVANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 240
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGaPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 241 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQIL------SNKKPELLEMLLITNN-PYDYSYVSQGEV-T 312
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggdeeEHEKYEFHDGITGGLQlPNEFHYTGQGGApD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 313 VASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAY---LMGLNSADLL 389
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 390 KGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSL--ETKQPRQYFIGVLDIAGFEIFDFNSFE 467
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 468 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFP-KASDMTFKAKL 545
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 546 FDNHL-------GKSANFGKPRNVKGKSeaHFSLIHYAGTVDYNI-IGWLEKNKDPLNETVVGLYQKSalkllaslfsny 617
Cdd:cd14908 480 YETYLpeknqthSENTRFEATSIQKTKL--IFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFESG------------ 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 618 agadaggdggkgkgakkkgSSFqtvsalhRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGI 697
Cdd:cd14908 546 -------------------QQF-------KAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAV 599
|
650 660 670
....*....|....*....|....*....|
gi 2163567613 698 RICRKGFPNRILYGDFRQRYRILNPTaIPE 727
Cdd:cd14908 600 RVARSGYPVRLPHKDFFKRYRMLLPL-IPE 628
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
92-761 |
2.22e-134 |
|
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: 435.24 E-value: 2.22e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYAS--WMIYTYSGLFCVTVNPYKWLPvyNAEVvAAYRGKKRTEVPPHIFSISDNAYQNMLTDRE---NQS 166
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 167 ILITGESGAGKTVNTKRVIQYFASIAAIGD--RKKEVANSSKG------TLEDQIIQANPALEAFGNAKTVRNDNSSRFG 238
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKkaSGQDIEQSSKKrklsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 239 KFIRIHFGATG-KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITnNPYDYSYVSQ-GEVTVASI 316
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLL-SPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 317 DDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREE----QAEPDGTEDADKSAYLMGLNSADLLKGL 392
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 393 CHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFD-FNSFEQLCI 471
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 472 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLFDNHl 550
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 551 GKSANFGKPRNvKGKSEAhFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSAlkllasLFSNyagadaggdggkgk 630
Cdd:cd14891 475 KRHPCFPRPHP-KDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSA------KFSD-------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 631 gakkkgsSFQTvsalhrenlnkLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILY 710
Cdd:cd14891 533 -------QMQE-----------LVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTY 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2163567613 711 GDFRQRYRILNPTAI------PEGQFIdsrkgaEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14891 595 AELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
92-722 |
4.25e-130 |
|
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: 425.85 E-value: 4.25e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYR--------GKKRTEVPPHIFSISDNAYQNML-TD 161
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 162 RENQSILITGESGAGKTVNTKRVIQYFASIAAIGDR-KKEVANSSKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 240
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSStEQEGSDAVE--IGKRILQTNPILESFGNAQTIRNDNSSRFGKF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 241 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNpYDYSYVSQGEVTVA-----S 315
Cdd:cd14902 159 IKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKG-GKYELLNSYGPSFArkravA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 316 IDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDA---DKSAYLMGLNSADLLKGL 392
Cdd:cd14902 238 DKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLETLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 393 CHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINN-------SLETKQPRQYF--IGVLDIAGFEIFDF 463
Cdd:cd14902 318 SSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDeinyfdsAVSISDEDEELatIGILDIFGFESLNR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 464 NSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLqACIDLIE-KPMGIMSILEEECMFPKASDMTFK 542
Cdd:cd14902 398 NGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNA-ACLALFDdKSNGLFSLLDQECLMPKGSNQALS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 543 AKLFDNHLGksanfgkprnvkgksEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAGADA 622
Cdd:cd14902 477 TKFYRYHGG---------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSP 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 623 GGDGGKGKGAKKKGSSFQTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRK 702
Cdd:cd14902 542 GADNGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARH 621
|
650 660
....*....|....*....|
gi 2163567613 703 GFPNRILYGDFRQRYRILNP 722
Cdd:cd14902 622 GYSVRLAHASFIELFSGFKC 641
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
54-814 |
8.26e-126 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 417.12 E-value: 8.26e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 54 VTTEMGETLTVPEADV----HPQNPPKFDrieDMAMLTFLHEPAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNA 129
Cdd:PTZ00014 71 IDPPTNSTFEVKPEHAfnanSQIDPMTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 130 EVVAAYR-GKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGESGAGKTVNTKRVIQYFASiaaigdrkkevanSSKGT 208
Cdd:PTZ00014 148 DWIRRYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS-------------SKSGN 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 209 LeDQIIQ-----ANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQIL 283
Cdd:PTZ00014 215 M-DLKIQnaimaANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 284 SNKKPELLEMLLITNNPyDYSYVSQGEVTVASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKqrE 363
Cdd:PTZ00014 294 KGANDEMKEKYKLKSLE-EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGK--E 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 364 EQAEPDGTEDADKS-------AYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRI 436
Cdd:PTZ00014 371 EGGLTDAAAISDESlevfneaCELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 437 NNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDL 516
Cdd:PTZ00014 451 NATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLL 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 517 IEKPMGIMSILEEECMFPKASDMTFKAKLFdNHLGKSANFGKPRNVKGKSeahFSLIHYAGTVDYNIIGWLEKNKDPLNE 596
Cdd:PTZ00014 531 CGKGKSVLSILEDQCLAPGGTDEKFVSSCN-TNLKNNPKYKPAKVDSNKN---FVIKHTIGDIQYCASGFLFKNKDVLRP 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 597 TVVGLYQKSALKLLASLFSNyagadaggdggkGKGAKKKGSSFQTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEP 676
Cdd:PTZ00014 607 ELVEVVKASPNPLVRDLFEG------------VEVEKGKLAKGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKP 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 677 GVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNpTAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHT 756
Cdd:PTZ00014 675 LDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD-LAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKT 753
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2163567613 757 KVFFKAGLLGLLEEMRDERLSL---IITRIQAqargQLMRIEFKKILERRDALLV-IQWNIR 814
Cdd:PTZ00014 754 MVFLKKDAAKELTQIQREKLAAwepLVSVLEA----LILKIKKKRKVRKNIKSLVrIQAHLR 811
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
92-761 |
3.20e-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: 406.47 E-value: 3.20e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASIAAIGDRKKEVansskgtledQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGKL 251
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDRLR----------QPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 252 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLItNNPYDYSYVSQGEV-TVASIDDSEELLATDSAFD 330
Cdd:cd14896 150 VGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 331 VLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDAD--KSAYLMGLnSADLLKGLCHPRVKVGN-EYVTKG 407
Cdd:cd14896 229 GLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQV-PPERLEGAVTHRVTETPyGRVSRP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 408 QSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYF--IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 485
Cdd:cd14896 308 LPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 486 MFVLEQEEYKKEGIEWEFIDfGMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLFDNHlGKSANFGKPRNvkg 564
Cdd:cd14896 388 LLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQL--- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 565 kSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFsnyagADAGGDGGKGKGAKKKGSSFQtvsa 644
Cdd:cd14896 463 -PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLF-----QEAEPQYGLGQGKPTLASRFQ---- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 645 lhrENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTA 724
Cdd:cd14896 533 ---QSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSER 609
|
650 660 670
....*....|....*....|....*....|....*..
gi 2163567613 725 IPEgqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14896 610 QEA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
92-761 |
7.54e-123 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 404.72 E-value: 7.54e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNaevVAAYRGK--KRTEVPPHIFSISDNAYQNMLT-------D 161
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 162 RENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRKKEvANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFI 241
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSS-SKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 242 RIHFG-----ATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPE-LLEMLLITNNPYDYSYVSQGEVTVAS 315
Cdd:cd14895 157 RMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmKLELQLELLSAQEFQYISGGQCYQRN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 316 --IDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDA------------------D 375
Cdd:cd14895 237 dgVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqhlD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 376 KSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQY------- 448
Cdd:cd14895 317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnkaank 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 449 ----FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGI 523
Cdd:cd14895 397 dttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRPSGI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 524 MSILEEECMFPKASDMTFKAKLFdNHLGKSANFGKPRnvKGKSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQ 603
Cdd:cd14895 476 FSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLG 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 604 KSALKLLASLFSNYAGADAGGDGGKGKGAKKKGSSFQTV--SALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDN 681
Cdd:cd14895 553 KTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVgiGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDM 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 682 TLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILnpTAIPEGQFIDsrkgAEKLLGSLDIDHNQykFGHTKVFFK 761
Cdd:cd14895 633 AKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLL--VAAKNASDAT----ASALIETLKVDHAE--LGKTRVFLR 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
92-761 |
2.52e-117 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 387.04 E-value: 2.52e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRG-KKRTEVPPHIFSISDNAYQNMLTDRENQSILIT 170
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 171 GESGAGKTVNTKRVIQYFASiaaigdRKKEVANSSkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 250
Cdd:cd14876 81 GESGAGKTEATKQIMRYFAS------AKSGNMDLR---IQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 251 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLE--MLLITNnpyDYSYVSQGEVTVASIDDSEELLATDSA 328
Cdd:cd14876 152 IRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSkyHLLGLK---EYKFLNPKCLDVPGIDDVADFEEVLES 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 329 FDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQReeqaepDGTEDA-----------DKSAYLMGLNSADLLKGLCHPRV 397
Cdd:cd14876 229 LKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTE------QGVDDAaaisneslevfKEACSLLFLDPEALKRELTVKVT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 398 KVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEK 477
Cdd:cd14876 303 KAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEM 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 478 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDmtfkAKLFDNHLGKSANFG 557
Cdd:cd14876 383 LQKNFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSD----EKFVSACVSKLKSNG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 558 KPRNVKGKSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNyagadaggdggkGKGAKKKGS 637
Cdd:cd14876 459 KFKPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG------------VVVEKGKIA 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 638 SFQTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRY 717
Cdd:cd14876 527 KGSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQF 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2163567613 718 RILNPtAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14876 607 KFLDL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
94-722 |
1.03e-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: 371.49 E-value: 1.03e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 94 VLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRTE-VPPHIFSISDNAYQNMLTDRE--NQSILI 169
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQkLKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 170 TGESGAGKTVNTKRVIQYFASIAAigDRKKEVANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 249
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAA--SPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 250 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSN-KKPELLEMLLITNNpyDYSYVSQGEVTVASiDDSEellATDSA 328
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGaSADERLQWHLPEGA--AFSWLPNPERNLEE-DCFE---VTREA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 329 FDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQA---EPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVT 405
Cdd:cd14880 235 MLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 406 --KGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPR-QYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 482
Cdd:cd14880 315 fkKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 483 NHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDmtfkAKLFDNHLgKSANFGKP-- 559
Cdd:cd14880 395 VAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSS----AAQLQTRI-ESALAGNPcl 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 560 -RNvKGKSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSnyagaDAGGDGGKGKGAKKKGSS 638
Cdd:cd14880 469 gHN-KLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFP-----ANPEEKTQEEPSGQSRAP 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 639 FQTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 718
Cdd:cd14880 543 VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
|
....
gi 2163567613 719 ILNP 722
Cdd:cd14880 623 LLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
94-721 |
4.65e-108 |
|
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: 362.76 E-value: 4.65e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 94 VLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKR-TEVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASIAAIGDRKKEVANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT-GK 250
Cdd:cd14906 83 ESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdGK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 251 LASADIETYLLEKSRVIFQL-KAERNYHIFYQILSNKKPELLEMLLITNNPYDYSYVSQGEVTVASI------------- 316
Cdd:cd14906 163 IDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsnhnn 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 317 --DDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQ---REEQAEPDGTEDADKSAYLMGLNSADLLKG 391
Cdd:cd14906 243 ktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFKQA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 392 LCHPRVKVGNE--YVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRIN-----------NSLETKQPRQYFIGVLDIAGF 458
Cdd:cd14906 323 LLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINrkfnqntqsndLAGGSNKKNNLFIGVLDIFGF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 459 EIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKAS 537
Cdd:cd14906 403 ENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPKGS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 538 DMTFKAKLfdNHLGKSANFGKPRNVkgkSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSny 617
Cdd:cd14906 482 EQSLLEKY--NKQYHNTNQYYQRTL---AKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ-- 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 618 agadagGDGGKGKGAKKKGSSFQTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGI 697
Cdd:cd14906 555 ------QQITSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTI 628
|
650 660
....*....|....*....|....
gi 2163567613 698 RICRKGFPNRILYGDFRQRYRILN 721
Cdd:cd14906 629 KVRKMGYSYRRDFNQFFSRYKCIV 652
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
93-718 |
1.79e-106 |
|
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: 358.25 E-value: 1.79e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYR-------GKKRTEV---PPHIFSISDNAYQNMLTD 161
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 162 RENQSILITGESGAGKTVNTKRVIQYFA-------SIAAIGDRKKEVANSSKGTLEDQIIQANPALEAFGNAKTVRNDNS 234
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAvhcgtgnNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 235 SRFGKFIRIHF-GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNK----KPELLEMLLITNNPYDYSYVSQG 309
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 310 EVTVA--SIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQ--KQREEQAEPDGTEDA----------D 375
Cdd:cd14899 242 LCSKRrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 376 KSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQY------- 448
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 449 --------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDlQACIDLIE-K 519
Cdd:cd14899 402 ddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 520 PMGIMSILEEECMFPKASDMTFKAKLFDNHLGKSANFGKPRNVKGKSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVV 599
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 600 GLYQKSALKLLASLFSNYAGADAGGDGGKGKGAKKKGSSFQT------VSALHRENLNKLMANLKTTHPHFVRCLIPNER 673
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSaiaavsVGTQFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2163567613 674 KEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 718
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
94-761 |
1.84e-104 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 351.23 E-value: 1.84e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 94 VLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGES 173
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 174 GAGKTVNTKRVIQYFASIaaigdrkkevANSSKGTLEDQIIQA-NPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 252
Cdd:cd01386 83 GSGKTTNCRHILEYLVTA----------AGSVGGVLSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 253 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLIT-----NNPYDYSYVSQGEVTvasiDDSEELLATDS 327
Cdd:cd01386 153 SASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNqlaesNSFGIVPLQKPEDKQ----KAAAAFSKLQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 328 AFDVLGFTAEEKAGVYKLTGAIMHFGN---MKFKQKQREEQAEPdgtEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 404
Cdd:cd01386 229 AMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 405 T---------------KGQSVQQvyySIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFN----- 464
Cdd:cd01386 306 TtssgqesparsssggPKLTGVE---ALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrg 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 465 -SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEK---------------PMGIMSILE 528
Cdd:cd01386 383 aTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLLD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 529 EECMFPKASDMTFKAKLFdNHLGKSaNFGKPRNVKGKSEA--HFSLIHYAGT--VDYNIIGWLEKNK-DPLNETVVGLYQ 603
Cdd:cd01386 463 EEALYPGSSDDTFLERLF-SHYGDK-EGGKGHSLLRRSEGplQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQ 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 604 KSALKLLA----SLFSNYagadaggdggkgkgakkkgsSFQtvsalhrenLNKLMANLKTTHPHFVRCLIPNERKEPGV- 678
Cdd:cd01386 541 ESQKETAAvkrkSPCLQI--------------------KFQ---------VDALIDTLRRTGLHFVHCLLPQHNAGKDEr 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 679 -----------MDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP----TAIPEGQFIDSRKGAEKLLGS 743
Cdd:cd01386 592 stsspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPpltkKLGLNSEVADERKAVEELLEE 671
|
730
....*....|....*...
gi 2163567613 744 LDIDHNQYKFGHTKVFFK 761
Cdd:cd01386 672 LDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
98-761 |
1.93e-103 |
|
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: 347.26 E-value: 1.93e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 98 LKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRT-----EVPPHIFSISDNAYQNMLTDRENQSILITG 171
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASIAAIGDRKkevansskgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 251
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTD----------VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 252 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYdYSYVSQGEV-TVASIDDSEELLATDSAFD 330
Cdd:cd14886 157 KGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASKCyDAPGIDDQKEFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 331 VLgFTAEEKAGVYKLTGAIMHFGNMKFKQKQR---EEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKG 407
Cdd:cd14886 236 KL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 408 QSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 487
Cdd:cd14886 315 VTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 488 VLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKP-MGIMSILEEECMFPKASDMTFKAKLfDNHLgKSANFgkprnVKGK- 565
Cdd:cd14886 395 KSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSF-----IPGKg 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 566 SEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAGADAGGDGgkgkgakkkgssfQTVSAL 645
Cdd:cd14886 467 SQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKG-------------KFLGST 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 646 HRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL---NP 722
Cdd:cd14886 534 FQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 2163567613 723 TAIPEGQfiDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14886 614 SSQNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
94-761 |
3.14e-102 |
|
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: 344.10 E-value: 3.14e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 94 VLYNLKERYASWMI-YTYSGLFCVTVNPYKWLPvYNAEVvaaYRGKKRTE-----VPPHIFSISDNAY-QNMLTDRENQS 166
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMP-FNSEE---ERKKYLALpdprlLPPHIWQVAHKAFnAIFVQGLGNQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 167 ILITGESGAGKTVNTKRVIQYFASIAAIgdrkkEVANSSKGTLEDQIIQ----ANPALEAFGNAKTVRNDNSSRFGKFIR 242
Cdd:cd14875 79 VVISGESGSGKTENAKMLIAYLGQLSYM-----HSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 243 IHF-GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYDYSYVSQGE------VTVAS 315
Cdd:cd14875 154 LYFdPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNtfvrrgVDGKT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 316 IDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDAdKSAYLMGLNSADLLKGLChp 395
Cdd:cd14875 234 LDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLRECFL-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 396 rVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLetkQPRQ-----YFIGVLDIAGFEIFDFNSFEQLC 470
Cdd:cd14875 311 -VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASI---TPQGdcsgcKYIGLLDIFGFENFTRNSFEQLC 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 471 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLFDNH 549
Cdd:cd14875 387 INYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQW 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 550 LGKSANFGKPrnvKGKSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAGADAGGdggkg 629
Cdd:cd14875 466 ANKSPYFVLP---KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRK----- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 630 kgakkkgssfQTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRIL 709
Cdd:cd14875 538 ----------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRP 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2163567613 710 YGDF-RQRYRILNPTAIPEGQFIDSRKGAEKLLGSLDIDHN----QYKFGHTKVFFK 761
Cdd:cd14875 608 IEQFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYYQRLYGwakpNYAVGKTKVFLR 664
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
93-736 |
2.80e-99 |
|
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: 332.63 E-value: 2.80e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKwlPVYNAEVVAAYRgKKRTEVPPHIFSISDNAYQNMLTdRENQSILITGE 172
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 173 SGAGKTVNTKRVIQYFASiaaigdrkkevANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgaTGKLA 252
Cdd:cd14898 78 SGSGKTENAKLVIKYLVE-----------RTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKIT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 253 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKpellemLLITNNPYDYSYVSQGEVTVasIDDSEELLATDSAFDVL 332
Cdd:cd14898 145 GAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMTCSAMKSL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 333 GFTAEEKagVYKLTGAIMHFGNMKFKQkqrEEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQ 412
Cdd:cd14898 217 GIANFKS--IEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 413 VYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQyfIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 492
Cdd:cd14898 292 ARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 493 EYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFP--KASDMTFKAKLFDNHlgksanfgkprNVKGKSEAHF 570
Cdd:cd14898 370 MYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAwgNVKNLLVKIKKYLNG-----------FINTKARDKI 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 571 SLIHYAGTVDYNIIGWLEKNKdplnetvvglyQKSALKLLASLFSNyagadaggdggkgkgakkKGSSFQTVSALHRENL 650
Cdd:cd14898 438 KVSHYAGDVEYDLRDFLDKNR-----------EKGQLLIFKNLLIN------------------DEGSKEDLVKYFKDSM 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 651 NKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPTAIpegQF 730
Cdd:cd14898 489 NKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLF---EV 565
|
....*.
gi 2163567613 731 IDSRKG 736
Cdd:cd14898 566 VDYRKG 571
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
93-729 |
5.20e-96 |
|
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: 325.62 E-value: 5.20e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYR---GKKRTEVPPHIFSISDNAYQNMLTDRENQSILI 169
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 170 TGESGAGKTVNTKRVIQYFASIAAigdrkkevanSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 249
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTCRAS----------SSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 250 K-LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLItNNPYDYSYVSQGE----VTVASIDDSEELLA 324
Cdd:cd14878 152 KhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHL-NNLCAHRYLNQTMredvSTAERSLNREKLAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 325 TDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 404
Cdd:cd14878 231 LKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 405 TKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQ 480
Cdd:cd14878 311 IRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 481 FFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACID-LIEKPMGIMSILEEECMFPKASDMTFKAKLfdNHLGKSANFGKP 559
Cdd:cd14878 391 YINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPSGFLSLLDEESQMIWSVEPNLPKKL--QSLLESSNTNAV 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 560 R--------NVKGKSE-AHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFsnyagadaggdggkgk 630
Cdd:cd14878 469 YspmkdgngNVALKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF---------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 631 gakkkGSSFQTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILY 710
Cdd:cd14878 533 -----QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSF 607
|
650
....*....|....*....
gi 2163567613 711 GDFRQRYRILNPTAIPEGQ 729
Cdd:cd14878 608 SDFLSRYKPLADTLLGEKK 626
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
92-761 |
1.01e-91 |
|
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: 315.43 E-value: 1.01e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYAS--------WMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRE 163
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 164 NQSILITGESGAGKTVNTKRVIQYfasIAAIGDRKKevaNSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 243
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTY---LAAVSDRRH---GADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 244 HFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPElLEMLLITNNPYDYSYvsqgevtvasiddseELL 323
Cdd:cd14887 155 HFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAA-ATQKSSAGEGDPEST---------------DLR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 324 ATDSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEP-----------DGTEDADKSAYLMGLNS------- 385
Cdd:cd14887 219 RITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKrkltsvsvgceETAADRSHSSEVKCLSSglkvtea 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 386 -----ADLLKGLCHPRVKVGNEYV------------TKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQY 448
Cdd:cd14887 299 srkhlKTVARLLGLPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPSE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 449 --------------FIGVLDIAGFEIF---DFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFI--DFGMD 509
Cdd:cd14887 379 sdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPFS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 510 LQACIDLIEKP------------------------MGIMSILEEE-CMFPKASDMTFKAKLFDNHLGK----SANFGKPR 560
Cdd:cd14887 459 FPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAKYKNIT 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 561 NVKGKSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETvvglyqksalklLASLFSNYAGADAGGDGGKGKGAKKKGSSFQ 640
Cdd:cd14887 539 PALSRENLEFTVSHFACDVTYDARDFCRANREATSDE------------LERLFLACSTYTRLVGSKKNSGVRAISSRRS 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 641 TVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 720
Cdd:cd14887 607 TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETK 686
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 2163567613 721 NPTAIPEgqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 761
Cdd:cd14887 687 LPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
94-761 |
1.24e-89 |
|
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: 306.56 E-value: 1.24e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 94 VLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEvvaaYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGES 173
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 174 GAGKTVNTKRVIQYFASiaaiGDRKKevaNSSKGTLEDqiiqANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 253
Cdd:cd14937 79 GSGKTEASKLVIKYYLS----GVKED---NEISNTLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 254 ADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPyDYSYVSQGEVTVASIDDSEELLATDSAFDVLG 333
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDKMN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 334 FTAEEKAGVYKLTGAIMhFGNMKFKQ-----KQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 408
Cdd:cd14937 227 MHDMKDDLFLTLSGLLL-LGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 409 SVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 488
Cdd:cd14937 306 SVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 489 LEQEEYKKEGIEWEFIDFGMDlQACIDLIEKPMGIMSILEEECMFPKASDMTFkAKLFDNHLGKSANFGKPRNVKGKSea 568
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYASTKKDINKN-- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 569 hFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYAGADAGGDGgkgkgakkkgssfQTVSALHRE 648
Cdd:cd14937 462 -FVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRK-------------NLITFKYLK 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 649 NLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRIcRKGFPNRILYGDFRQRYRILNPTAIPEG 728
Cdd:cd14937 528 NLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDS 606
|
650 660 670
....*....|....*....|....*....|...
gi 2163567613 729 QFIDSRKGAEKLLGSLDIDhnQYKFGHTKVFFK 761
Cdd:cd14937 607 SLTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
98-760 |
3.47e-85 |
|
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: 293.69 E-value: 3.47e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 98 LKERYASWMIYTY---SGLfcVTVNPYKWLPVYNAEVVAAYR-------GKKRTEVPPHIFSISDNAYQNMLTDRENQSI 167
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 168 LITGESGAGKTVNTKRVIQYFASIAAigdrkkevaNSSKGT-LEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 246
Cdd:cd14879 88 VFLGETGSGKSESRRLLLRQLLRLSS---------HSKKGTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 247 ATGKLASADIETYLLEKSRVIfQLKA-ERNYHIFYQILSNKKPELLEMLLItNNPYDY----SYVSQGEVTVASIDDSE- 320
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQHLGL-DDPSDYallaSYGCHPLPLGPGSDDAEg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 321 -ELLATdsAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQkqreeqaEPDGTEDA---------DKSAYLMGLNSADLLK 390
Cdd:cd14879 237 fQELKT--ALKTLGFKRKHVAQICQLLAAILHLGNLEFTY-------DHEGGEESavvkntdvlDIVAAFLGVSPEDLET 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 391 GLCHPRVKVGNEYVT-----KGQSVQQvyysiGALAKAVYEKMFNWMVVRINNSL-ETKQPRQYFIGVLDIAGFEIFD-- 462
Cdd:cd14879 308 SLTYKTKLVRKELCTvfldpEGAAAQR-----DELARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSst 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 463 -FNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEEC-MFPKASDM 539
Cdd:cd14879 383 gGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTDE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 540 TFKAKLfDNHLGKSANFGKPRNVKGKSEAH-FSLIHYAGTVDYNIIGWLEKNKDPLNETVVglyqksalkllaSLFSNya 618
Cdd:cd14879 462 QMLEAL-RKRFGNHSSFIAVGNFATRSGSAsFTVNHYAGEVTYSVEGFLERNGDVLSPDFV------------NLLRG-- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 619 gadaggdggkgkgakkkgssfqtvSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIR 698
Cdd:cd14879 527 ------------------------ATQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAA 582
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2163567613 699 ICRKGFPNRILYGDFRQRYrilnptaIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFF 760
Cdd:cd14879 583 RLRVEYVVSLEHAEFCERY-------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
92-709 |
2.70e-76 |
|
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: 269.08 E-value: 2.70e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRTE-------VPPHIFSISDNAYQNMLTDRE 163
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 164 NQSILITGESGAGKTVNTKRVIQYFASIAAigdrkkevaNSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 243
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQT---------DSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 244 HF---------GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYDY----------- 303
Cdd:cd14884 152 IFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYgllnpdeshqk 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 304 -SYVSQGEVTVASIDDSEELLATDSA-----FDVLGFTAEEKAGV---YKLTGAIMHFGNMKFKQkqreeqaepdgteda 374
Cdd:cd14884 232 rSVKGTLRLGSDSLDPSEEEKAKDEKnfvalLHGLHYIKYDERQInefFDIIAGILHLGNRAYKA--------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 375 dkSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRIN-NSLETKQPRQY----- 448
Cdd:cd14884 297 --AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrNVLKCKEKDESdnedi 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 449 ------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEW--EFIDFGMDLQACIDLIEKP 520
Cdd:cd14884 375 ysineaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICcsDVAPSYSDTLIFIAKIFRR 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 521 MGIMSILEEECMfpKASDMTFKAKLFDN----HLGKSANFGK--PRNVKGKSEAH------FSLIHYAGTVDYNIIGWLE 588
Cdd:cd14884 455 LDDITKLKNQGQ--KKTDDHFFRYLLNNerqqQLEGKVSYGFvlNHDADGTAKKQnikkniFFIRHYAGLVTYRINNWID 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 589 KNKDPLNETVVGLYQKSALKLLASLFSNyagadaggdggkgkgakKKGSSFQTVSALHRENLNKLMANLKTTHPHFVRCL 668
Cdd:cd14884 533 KNSDKIETSIETLISCSSNRFLREANNG-----------------GNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2163567613 669 IPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRIL 709
Cdd:cd14884 596 LPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
93-729 |
2.94e-72 |
|
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: 255.57 E-value: 2.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYrgkkrtevppHIFSISDNAYQNMLTDREN-QSILITG 171
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 172 ESGAGKTVNTKRVIQYFASiaaigDRKKEVANSSKGTLEDQIiqanpalEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 251
Cdd:cd14874 72 ESGSGKSYNAFQVFKYLTS-----QPKSKVTTKHSSAIESVF-------KSFGCAKTLKNDEATRFGCSIDLLYKRNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 252 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNpYDYSYVSQGEVTVASIDDSEELLATDSAFDV 331
Cdd:cd14874 140 GLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL-QKFFYINQGNSTENIQSDVNHFKHLEDALHV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 332 LGFTAEEKAGVYKLTGAIMHFGNMKFKQKQR---EEQAEPDGTEDADK-SAYLMGLNSADLLKGLChPRVKVGNEYvtkg 407
Cdd:cd14874 219 LGFSDDHCISIYKIISTILHIGNIYFRTKRNpnvEQDVVEIGNMSEVKwVAFLLEVDFDQLVNFLL-PKSEDGTTI---- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 408 qSVQQVYYSIGALAKAVYEKMFNWMVVRInnSLETKQPRQY-FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 486
Cdd:cd14874 294 -DLNAALDNRDSFAMLIYEELFKWVLNRI--GLHLKCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 487 FVLEQEEYKKEGIEwefIDFGMdlQACID-------LIEKPMGIMSILEEECMFPKASDMTFKAKLFDNHLGKSAnFGKP 559
Cdd:cd14874 371 FHDQLVDYAKDGIS---VDYKV--PNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGKA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 560 RNvkgKSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNYagadaggdggKGKGAKKKGSSF 639
Cdd:cd14874 445 RN---KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY----------SSNTSDMIVSQA 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 640 QTVSALHRENLNKlmanLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 719
Cdd:cd14874 512 QFILRGAQEIADK----INGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRC 587
|
650
....*....|
gi 2163567613 720 LNPTAIPEGQ 729
Cdd:cd14874 588 LLPGDIAMCQ 597
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
93-741 |
4.81e-72 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 255.04 E-value: 4.81e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 93 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPvyNAEVVAAYRGKKRTevpPHIFSISDNAYQNMLTDRENQSILITGE 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 173 SGAGKTVNTKRVIQYFASIAAIG---DRKKEVAnsskgtledqiiQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATG 249
Cdd:cd14881 77 SGSGKTYASMLLLRQLFDVAGGGpetDAFKHLA------------AAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 250 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITN-NPYDYSYVSQGEVTVASIDDSEELLATDSA 328
Cdd:cd14881 144 ALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGySPANLRYLSHGDTRQNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 329 FDVLG--FTaeekaGVYKLTGAIMHFGNMKFKQKQrEEQAEPDGTEDADKSAYLMGLNSADLLKGL---CHprvkvgney 403
Cdd:cd14881 224 LGILGipFL-----DVVRVLAAVLLLGNVQFIDGG-GLEVDVKGETELKSVAALLGVSGAALFRGLttrTH--------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 404 VTKGQ---SVQQVYYSIG---ALAKAVYEKMFNWMVVRIN-----NSLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCIN 472
Cdd:cd14881 289 NARGQlvkSVCDANMSNMtrdALAKALYCRTVATIVRRANslkrlGSTLGTHATDGFIGILDMFGFEDPKPSQLEHLCIN 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 473 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-IDFgMDLQACIDLIEK-PMGIMSILEEECMfPKASDMTFKAKLFDNHL 550
Cdd:cd14881 369 LCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHR 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 551 GkSANFGKPRNVKGKSeahFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLlasLFSNYagadaggdggkgk 630
Cdd:cd14881 447 Q-NPRLFEAKPQDDRM---FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF---GFATH------------- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 631 gakkkGSSFQTvsalhreNLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILY 710
Cdd:cd14881 507 -----TQDFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRF 574
|
650 660 670
....*....|....*....|....*....|.
gi 2163567613 711 GDFRQRYRILNPTAiPEGQFIDSRKGAEKLL 741
Cdd:cd14881 575 KAFNARYRLLAPFR-LLRRVEEKALEDCALI 604
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
98-713 |
7.07e-67 |
|
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: 240.76 E-value: 7.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 98 LKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYrgKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGESGAG 176
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 177 KTVNTKRVIQYFASIAAigdrkkevanSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADI 256
Cdd:cd14905 85 KSENTKIIIQYLLTTDL----------SRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 257 ETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLItNNPYDYSYVSQ-GEVTVASIDDSEELLATDSAFDVLGFT 335
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQL-GDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFDFP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 336 AEEKAGVYKLTGAIMHFGNMKFKQKQREeqaepdgTEDADKSaylmglnsadLLKGLCH----PRVKVGNEYVT-KGQSV 410
Cdd:cd14905 234 SEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDRT----------LIESLSHnitfDSTKLENILISdRSMPV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 411 QQVYYSIGALAKAVYEKMFNWMVVRINNSLetkQPRQY--FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 488
Cdd:cd14905 297 NEAVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 489 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKpmgIMSILEEECMFPKASDMTFKAKLfDNHLGKSANFGKPRNvkgksea 568
Cdd:cd14905 374 QEQREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL-QNFLSRHHLFGKKPN------- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 569 HFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLAS---LFsNYAGADAGGDGGKGKGAKKKGSSFQTVSAL 645
Cdd:cd14905 443 KFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSrdgVF-NINATVAELNQMFDAKNTAKKSPLSIVKVL 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 646 ------HRENLNKLMAN-------------------LKTTHP-------------HFVRCLIPNERKEPGVMDNTLVMHQ 687
Cdd:cd14905 522 lscgsnNPNNVNNPNNNsgggggggnsgggsgsggsTYTTYSstnkainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQ 601
|
650 660 670
....*....|....*....|....*....|
gi 2163567613 688 LRCNGVLEGIRICRKGFP----NRILYGDF 713
Cdd:cd14905 602 IKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
95-760 |
1.92e-62 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 229.09 E-value: 1.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 95 LYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKR----------TEVPPHIFSISDNAYQNMLTDREN 164
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 165 QSILITGESGAGKTVNTKRVIQYFASIA--AIGDRKKEVANSSKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIR 242
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGdeTEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 243 IHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKK--PELLEMLLITNNPYDYSYVSQG--EVTVASID- 317
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQAdpLATNFALDa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 318 -DSEELLatdSAFDVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREEQAEPDGTEDADKSAYLMGLN-------SADLL 389
Cdd:cd14893 244 rDYRDLM---SSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTVSDAQSCALKdpaqillAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 390 KglCHPRV------------KVGNEYVT--KGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETKQPR--------- 446
Cdd:cd14893 321 E--VEPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksnivin 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 447 QYFIGVLDIAGFEIFD--FNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWE-------FIDFGMDLQACIDLI 517
Cdd:cd14893 399 SQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVEnrltvnsNVDITSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 518 E-KPMGIMSILEEECMFPKASDMTFKAKLFDnhlGKSANFGKPRNVKGKSEAH------------FSLIHYAGTVDYNII 584
Cdd:cd14893 479 EdKPFGIFDLLTENCKVRLPNDEDFVNKLFS---GNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNGK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 585 GWLEKNKDPLNETVVGLYQKSALKLLASL-FSNYAGADAGGDGGKGKGAKKKGSSFQTVSALHRENLN------------ 651
Cdd:cd14893 556 GLSSKNMLSISSTCAAIMQSSKNAVLHAVgAAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynq 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 652 --KLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRilnptaipegQ 729
Cdd:cd14893 636 adALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK----------N 705
|
730 740 750
....*....|....*....|....*....|....*
gi 2163567613 730 FIDSRKGAEKLLGSLD----IDHNQYKFGHTKVFF 760
Cdd:cd14893 706 VCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
114-243 |
4.60e-61 |
|
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: 206.81 E-value: 4.60e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 114 FCVTVNPYKWLPVYNAEVV-AAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGESGAGKTVNTKRVIQYFASIA 192
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2163567613 193 AIGDRKKEVANSS-----KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 243
Cdd:cd01363 81 FNGINKGETEGWVylteiTVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
94-720 |
8.27e-60 |
|
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: 218.84 E-value: 8.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 94 VLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTEVPPHIFSISDNAYQNMLTDRENQSILITGES 173
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 174 GAGKTVNTKRVIQYfasIAAIGDRKKEVAnsskgtleDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 253
Cdd:cd14882 83 YSGKTTNARLLIKH---LCYLGDGNRGAT--------GRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 254 ADIETYLLEKSRVIFQLKAERNYHIFYQILS--NKKPELLEMLLITNNPYDYSYVSQG-------------EVTVASIDD 318
Cdd:cd14882 152 AIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEvppsklkyrrddpEGNVERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 319 SEELLAtdsafdVLGFTAEEKAGVYKLTGAIMHFGNMKFKQKQREeqAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVK 398
Cdd:cd14882 232 FEEILK------DLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 399 VGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRINNSLETkqPR-----QYFIGVLDIAGFEIFDFNSFEQLCINF 473
Cdd:cd14882 304 KGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMVNT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 474 TNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEecmfpkAS-DMTFKAKLFDNHLGK 552
Cdd:cd14882 382 LNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD------ASrSCQDQNYIMDRIKEK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 553 SANFgkprnVKGKSEAHFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKSALKLLASLFSNyagadaggdggkgkga 632
Cdd:cd14882 456 HSQF-----VKKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN---------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 633 kKKGSSFQTVSALHR----ENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICRKGFPNRI 708
Cdd:cd14882 515 -SQVRNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRI 593
|
650
....*....|..
gi 2163567613 709 LYGDFRQRYRIL 720
Cdd:cd14882 594 PFQEFLRRYQFL 605
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
92-759 |
4.78e-51 |
|
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: 194.28 E-value: 4.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 92 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRTE-VPPHIFSISDNAYQNMLTDRENQSILIT 170
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 171 GESGAGKTVNTKRVIQYFA------------SIAAIGDRKKEVANSS-KGTLEDQIIQANPALEAFGNAKTVRNDNSSRF 237
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAyqvkgsrrlptnLNDQEEDNIHNEENTDyQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 238 GKFIRIHFgATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLEMLLITNNPYdYSYVSQGEVTVASID 317
Cdd:cd14938 161 SKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIEN-YSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 318 DSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHFGN-------------MKFKQKQRE----------EQAEPDGTEDA 374
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 375 DKSAYL----MGLNSADLLKGLCHPRVkVGNEYVTKGQSVQQVYYSIGALAKAVYEKMFNWMVVRIN---NSLETKQPRQ 447
Cdd:cd14938 319 VKNLLLacklLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINekcTQLQNININT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 448 YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM--GIMS 525
Cdd:cd14938 398 NYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 526 ILEEECMfPKASDMTFKAKLFDNHLGKSANFGKPRNVKGKSEAhFSLIHYAGTVDYNIIGWLEKNKDPLNETVVGLYQKS 605
Cdd:cd14938 478 LLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 606 ALKLLASL--FSNYAGADAGGDGGKGKGAKKKGSSF--------QTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKE 675
Cdd:cd14938 556 ENEYMRQFcmFYNYDNSGNIVEEKRRYSIQSALKLFkrrydtknQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESKR 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 676 P-GVMDNTLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPtaipegqfiDSRKGAEKLLGSLDIDHNQYKFG 754
Cdd:cd14938 636 ElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMIG 706
|
....*
gi 2163567613 755 HTKVF 759
Cdd:cd14938 707 NNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
958-1766 |
1.25e-34 |
|
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: 145.58 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 958 KVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQESHQQALD--DLQAEEDKVN--TLAKAKVKLEQQVDDLESSL 1033
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykELKAELRELElaLLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1034 EQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEEL 1113
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1114 EEELEAERTGRAKVEKLRSELLQELEETSERLEEAGGATSVQLELNKKQEAEFQKLRRDLEEATLQHEATAATLRkkhad 1193
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE----- 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1194 svaELSEQLDNLQRVKQKLEKEKSELKLELDdvnsnteqlikaktnlekmcrttEDQMNEHRSKLEEAQRTVTDLSTQRA 1273
Cdd:TIGR02168 404 ---RLEARLERLEDRRERLQQEIEELLKKLE-----------------------EAELKELQAELEELEEELEELQEELE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1274 KLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAK----AKNALAHALQSAQHDcDLLREQYEEEMEAK 1349
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegVKALLKNQSGLSGIL-GVLSELISVDEGYE 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1350 TELQRALSKANSEVAqwrTKYETDAIQRTEELEEAKK--------------KLAQRLQEAEEAVEAVNAKCSSLEKTKHR 1415
Cdd:TIGR02168 537 AAIEAALGGRLQAVV---VENLNAAKKAIAFLKQNELgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPK 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1416 LQNEIEDLMA------DVERSNAAAAALDKKQRNF----DKILSEW----------------KQKFEESQTELEASQKEA 1469
Cdd:TIGR02168 614 LRKALSYLLGgvlvvdDLDNALELAKKLRPGYRIVtldgDLVRPGGvitggsaktnssilerRREIEELEEKIEELEEKI 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1470 RSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHE 1549
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1550 EGKILRAQLEFNQVKADYERKLAEKDEEIEQskrnhlrvVDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANR 1629
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREA--------LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1630 TAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQELIEASERVq 1709
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL- 924
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 2163567613 1710 llhsqnTSLINQKKKMEADISQLQTEV-EEAIQECRNAEEKAKKAITDAAMMAEELKK 1766
Cdd:TIGR02168 925 ------AQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1139-1922 |
1.65e-33 |
|
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: 141.73 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1139 EETSERLEEAGGATsvqlelnkkqeaefqKLRRDLEEATLQHEATAATLrKKHADSVAELSEQLDNLQRVKQKLEKEKsE 1218
Cdd:TIGR02168 155 EERRAIFEEAAGIS---------------KYKERRKETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERYK-E 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1219 LKLELDDVnsnteQLIKAKtnlekmcrtteDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTr 1298
Cdd:TIGR02168 218 LKAELREL-----ELALLV-----------LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1299 gkltytQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQRt 1378
Cdd:TIGR02168 281 ------EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL- 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1379 EELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEES 1458
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1459 qtELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAA 1538
Cdd:TIGR02168 434 --ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1539 LEEAEaslehEEGKILRAQLEFNQVKADYERKLaekdEEIEQSKRNHLrVVDSLQTSLDA-ETRSRNEALRLKKKMEGDL 1617
Cdd:TIGR02168 512 LKNQS-----GLSGILGVLSELISVDEGYEAAI----EAALGGRLQAV-VVENLNAAKKAiAFLKQNELGRVTFLPLDSI 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1618 NEMEIQLSHANRTAA------------EAQKQVKALQGYLKDTQLQLDDVVRANEDLKE---NIAIV------------- 1669
Cdd:TIGR02168 582 KGTEIQGNDREILKNiegflgvakdlvKFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrpGYRIVtldgdlvrpggvi 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1670 -----ERRNNLL--QSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQE 1742
Cdd:TIGR02168 662 tggsaKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1743 CRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlalkggkkQLQKLEVRVRELENELE 1822
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE--------ELKALREALDELRAELT 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1823 AEQKRNAESIKGLRKSERRVKELSYQTEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKVQHELDEAE 1902
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
810 820
....*....|....*....|
gi 2163567613 1903 ERADMAESQVNKLRARSRDI 1922
Cdd:TIGR02168 894 SELEELSEELRELESKRSEL 913
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
838-1603 |
1.86e-28 |
|
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: 125.17 E-value: 1.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 838 AETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEM 917
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 918 TERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQES 997
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 998 HQQALDDLQAEEDKVNTL-----AKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLE 1072
Cdd:TIGR02168 402 IERLEARLERLEDRRERLqqeieELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1073 ERLKKKDFELNTLNA---RIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQEL--------EET 1141
Cdd:TIGR02168 482 RELAQLQARLDSLERlqeNLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVvvenlnaaKKA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1142 SERLEEAGGATSVQLELNKKQEAEFQKLRRDLEEATLQHEATAATLRKKHADSVAELSEQLDNL---QRVKQKLEKEKSE 1218
Cdd:TIGR02168 562 IAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvDDLDNALELAKKL 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1219 LKLE----LDDVNSNTEQLI---KAKTNLEKMCRTTEdqMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEA 1291
Cdd:TIGR02168 642 RPGYrivtLDGDLVRPGGVItggSAKTNSSILERRRE--IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1292 FINQLTRgkltytqQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYE 1371
Cdd:TIGR02168 720 ELEELSR-------QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1372 TDAIQRT------EELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFD 1445
Cdd:TIGR02168 793 QLKEELKalrealDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1446 KILSEWKQKFEESQ-------TELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQK-S 1517
Cdd:TIGR02168 873 SELEALLNERASLEealallrSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlT 952
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1518 IHELEKVRKQLDAEKLELQAALEEAEASLEhEEGKI-LRAQLEFNQVKADYERKLAEKdEEIEQSKRNHLRVVDslqtSL 1596
Cdd:TIGR02168 953 LEEAEALENKIEDDEEEARRRLKRLENKIK-ELGPVnLAAIEEYEELKERYDFLTAQK-EDLTEAKETLEEAIE----EI 1026
|
....*..
gi 2163567613 1597 DAETRSR 1603
Cdd:TIGR02168 1027 DREARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1306-1927 |
1.21e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 122.86 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1306 QLEDLKRQLEeeaKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETdAIQRTEELEEAK 1385
Cdd:TIGR02168 201 QLKSLERQAE---KAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1386 KKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEAS 1465
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1466 QKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEAS 1545
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1546 LEHEEGKILRAQLEFNQVK-ADYERKLAEKDEEIE-------------QSKRNHLRVVDSLQTSLDAETRSRNEALRLKK 1611
Cdd:TIGR02168 437 ELQAELEELEEELEELQEElERLEEALEELREELEeaeqaldaaerelAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1612 KMEG-----------------------------------------------------------DLNEMEIQLSHANRTAA 1632
Cdd:TIGR02168 517 GLSGilgvlselisvdegyeaaieaalggrlqavvvenlnaakkaiaflkqnelgrvtflpldSIKGTEIQGNDREILKN 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1633 ------------EAQKQVKALQGYLKDTQLQLDDVVRANEDLKE---NIAIV------------------ERRNNLL--Q 1677
Cdd:TIGR02168 597 iegflgvakdlvKFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrpGYRIVtldgdlvrpggvitggsaKTNSSILerR 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1678 SELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEK---AKKAI 1754
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqLSKEL 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1755 TDA----AMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlALKGGKKQLQKLEVRVRELENELEAEQKRNAE 1830
Cdd:TIGR02168 757 TELeaeiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-ALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1831 SIKGLRKSERRVKELSYQTEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKVQHELDEAEERADMAES 1910
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
730
....*....|....*..
gi 2163567613 1911 QVNKLRARSRDIGAKKG 1927
Cdd:TIGR02168 916 ELEELREKLAQLELRLE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
855-1738 |
1.81e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 122.09 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 855 KEALEKSEARRKELEEKMVSmlqekndLQLQVQAEQDNLA-DAEERCDQLIKNKIQLEAKVKEMTERLEEEEEMNAELAA 933
Cdd:TIGR02168 185 RENLDRLEDILNELERQLKS-------LERQAEKAERYKElKAELRELELALLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 934 KKRKLEdecsELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQESHQQALDDLQAEEDKVN 1013
Cdd:TIGR02168 258 LTAELQ----ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1014 TLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEdeq 1093
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE--- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1094 aisaQLQKKLKELQARIEELeeeleaertGRAKVEKLRSELLQELEETSERLEEAGGATSVQLELNKKQEAEFQKLRRDL 1173
Cdd:TIGR02168 411 ----RLEDRRERLQQEIEEL---------LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1174 EEATLQHEATAATLrkkhaDSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNsnteQLIKAKTNLEKMCRTT-----E 1248
Cdd:TIGR02168 478 DAAERELAQLQARL-----DSLERLQENLEGFSEGVKALLKNQSGLSGILGVLS----ELISVDEGYEAAIEAAlggrlQ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1249 DQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEeeaKAKNAL---- 1324
Cdd:TIGR02168 549 AVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLR---KALSYLlggv 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1325 --AHALQSAQHdcdlLREQYEEEMEAKTeLQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAV 1402
Cdd:TIGR02168 626 lvVDDLDNALE----LAKKLRPGYRIVT-LDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKAL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1403 NAkcssLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELfklkna 1482
Cdd:TIGR02168 701 AE----LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL------ 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1483 yEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLEFNQ 1562
Cdd:TIGR02168 771 -EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1563 VKADYErKLAEKDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQ 1642
Cdd:TIGR02168 850 LSEDIE-SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1643 GYLKDTQLQLDDVV-RANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARK-------LAEQELIEASERVQLLHSQ 1714
Cdd:TIGR02168 929 LRLEGLEVRIDNLQeRLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlAAIEEYEELKERYDFLTAQ 1008
|
890 900
....*....|....*....|....
gi 2163567613 1715 NTSLINQKKKMEADISQLQTEVEE 1738
Cdd:TIGR02168 1009 KEDLTEAKETLEEAIEEIDREARE 1032
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1305-1924 |
2.11e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 121.58 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1305 QQLEDLKRQ---------LEEEAKAK--NALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVaqwrtkyetd 1373
Cdd:COG1196 200 RQLEPLERQaekaeryreLKEELKELeaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL---------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1374 aiqrtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQ 1453
Cdd:COG1196 270 -----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1454 KFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKL 1533
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1534 ELQAALEEAEASLEHEEGKILRAQLEFNQVKADyERKLAEKDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKM 1613
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEE-EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1614 EGDLNemeiqlshanrtAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNllqseleelramVEQSERA 1693
Cdd:COG1196 504 EGFLE------------GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIV------------VEDDEVA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1694 RKLAEQELIEASERVQLLHSqntSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAItdaamMAEELKKEQDTSAH 1773
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPL---DKIRARAALAAALARGAIGAAVDLVASDLREADARYYV-----LGDTLLGRTLVAAR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1774 LERMKKNMEQTVKDLQLRLDEAEQLALKGGKK--QLQKLEVRVRELENELEAEQKRNAESIKGLRKSERRVKELSYQTEE 1851
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTggSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2163567613 1852 DRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQANSNLAkfrKVQHELDEAEERADMAESQVNKLRARSRDIGA 1924
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE---EEALEELPEPPDLEELERELERLEREIEALGP 781
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1211-1823 |
1.82e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 118.50 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1211 KLEKEKSELKLE--------LDDVnsnTEQLIKAKTNLEKMCRTTEdQMNEHRSKLEEAQRTVT-----DLSTQRAKLQT 1277
Cdd:COG1196 171 KERKEEAERKLEateenlerLEDI---LGELERQLEPLERQAEKAE-RYRELKEELKELEAELLllklrELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1278 ENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALS 1357
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1358 KANSEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQEAEEAVEAvnakcssLEKTKHRLQNEIEDLMADVERSNAAAAAL 1437
Cdd:COG1196 327 ELEEELEE--------LEEELEELEEELEEAEEELEEAEAELAE-------AEEALLEAEAELAEAEEELEELAEELLEA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1438 DKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKS 1517
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1518 IHELEKVRKQLDAEKLELQA---ALEEAEASLEHEEGKILRAQLEFNQVKADYERKLAEKDEEIEQSKRNHLRVVDSLQT 1594
Cdd:COG1196 472 AALLEAALAELLEELAEAAArllLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1595 SLDAETRSRNEALRLKKKMEGDLNemEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNN 1674
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRAT--FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1675 LLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAI 1754
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163567613 1755 TDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQLQKLEVRVRELENELEA 1823
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1094-1904 |
1.55e-25 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 115.94 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1094 AISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEeaggatsvQLELNKKQEAEFQKLRRDL 1173
Cdd:TIGR02169 149 SMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLE--------RLRREREKAERYQALLKEK 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1174 EEAtlqhEATAATLRKKHAD-SVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKaktnleKMCRTTEDQMN 1252
Cdd:TIGR02169 221 REY----EGYELLKEKEALErQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK------KIKDLGEEEQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1253 EHRSKLEEaqrtvtdLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHALQSAQ 1332
Cdd:TIGR02169 291 RVKEKIGE-------LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1333 HDCDLLREQYEEEMEAKTELQRALSKANSEVAQwrTKYETDAIQRTEE-LEEAKKKLAQRLQEAEEAVEAVNAKCSSLEK 1411
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYREKLEK--LKREINELKRELDrLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1412 TKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLST----------------- 1474
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEErvrggraveevlkasiq 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1475 -------ELFKLKNAYEESLE-----HLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVR-KQLDAEKLELQAALEE 1541
Cdd:TIGR02169 522 gvhgtvaQLGSVGERYATAIEvaagnRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRdERRDLSILSEDGVIGF 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1542 AEASLEHEE------GKILRAQLEFNQVKA-----------DYERKLAEKDEEIEQSKRNhLRVVDSLQTSLDAETRSRN 1604
Cdd:TIGR02169 602 AVDLVEFDPkyepafKYVFGDTLVVEDIEAarrlmgkyrmvTLEGELFEKSGAMTGGSRA-PRGGILFSRSEPAELQRLR 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1605 EALrlkKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELR 1684
Cdd:TIGR02169 681 ERL---EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1685 AmvEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEEL 1764
Cdd:TIGR02169 758 S--ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1765 KKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlalkggkkQLQKLEVRVRELENELEAEQKRNAESIKGLRKSERRVKE 1844
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEE--------ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1845 LSYQTEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQAnSNLAKFRKVQHELDEAEER 1904
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP-EEELSLEDVQAELQRVEEE 966
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1069-1742 |
1.76e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.95 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1069 QQLEERLKKKD-----FELNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSE 1143
Cdd:COG1196 216 RELKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1144 RLEEAGGATSVQLELNKKQEAEFQKLRRDLEEATLQHEATAATLrkkhadsvAELSEQLDNLQRVKQKLEKEKSELKLEL 1223
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL--------EELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1224 DDVNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTrgklty 1303
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE------ 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1304 tQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQRTEELEE 1383
Cdd:COG1196 442 -EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1384 AKKKLAQRLQEAEEAVEAVnakcsslektkhrLQNEIEDLMADVERSNAAAAAldkKQRNFDKILSEWKQKFEESQTELE 1463
Cdd:COG1196 521 GLAGAVAVLIGVEAAYEAA-------------LEAALAAALQNIVVEDDEVAA---AAIEYLKAAKAGRATFLPLDKIRA 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1464 ASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAE 1543
Cdd:COG1196 585 RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1544 ASLEHEEGKILRAQLEfnqvkadyERKLAEKDEEIEQSkrnhlrvvdsLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQ 1623
Cdd:COG1196 665 GSRRELLAALLEAEAE--------LEELAERLAEEELE----------LEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1624 LSHANRTAAEAQKQvkalqgyLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRA--MveqserarkLAEQEL 1701
Cdd:COG1196 727 EEQLEAEREELLEE-------LLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnL---------LAIEEY 790
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2163567613 1702 IEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQE 1742
Cdd:COG1196 791 EELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLE 831
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
838-1798 |
3.97e-24 |
|
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: 111.31 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 838 AETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLqlqvqaeqdnladaeERCDQLIKNKIQLEAKvkem 917
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA---------------ERYQALLKEKREYEGY---- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 918 terleeeeemnaELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKkilQES 997
Cdd:TIGR02169 227 ------------ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE---QLR 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 998 HQQALDDLQAEedkvntLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGdlklAQESIMDLENDKQQLEERLKK 1077
Cdd:TIGR02169 292 VKEKIGELEAE------IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE----LEREIEEERKRRDKLTEEYAE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1078 KDFELNTLNARIEDEQAISAQLQKKLKELQarieeleeeleaertgrakveklrsellQELEETSERLEEAGGATSVQLE 1157
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYR----------------------------EKLEKLKREINELKRELDRLQE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1158 LNKKQEAEFQKLRRDLEEATLQHEATAATLRKKhADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNsnteqlikak 1237
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDK-ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE---------- 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1238 tnlekmcrttedqmnehrSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFInqltRGKLTYTQQLEDLKRQ--LE 1315
Cdd:TIGR02169 483 ------------------KELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASI----QGVHGTVAQLGSVGERyaTA 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1316 EEAKAKNALAHAL----QSAQHDCDLLREQYE--------EEMEAKTELQRALSKANS-----EVAQWRTKYETD---AI 1375
Cdd:TIGR02169 541 IEVAAGNRLNNVVveddAVAKEAIELLKRRKAgratflplNKMRDERRDLSILSEDGVigfavDLVEFDPKYEPAfkyVF 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1376 QRT---EELEEAKK--------KLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNF 1444
Cdd:TIGR02169 621 GDTlvvEDIEAARRlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRI 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1445 DKILSEWKQKFEESQTELEASQKEArslstelfklknayEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKV 1524
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEI--------------EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1525 RKQLDAEKLELQAALEEAEASLEHEEGKILRAQLefnqvkadyeRKLAEKDEEIEQskrnhlrVVDSLQTSLDAETRSRN 1604
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL----------SKLEEEVSRIEA-------RLREIEQKLNRLTLEKE 829
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1605 EALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKEniaivERRNnlLQSELEELR 1684
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK-----ERDE--LEAQLRELE 902
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1685 AMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISqlQTEVEEAIQECRNAEEKAKKAITDAAMMA-EE 1763
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE--EELSLEDVQAELQRVEEEIRALEPVNMLAiQE 980
|
970 980 990
....*....|....*....|....*....|....*
gi 2163567613 1764 LKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQL 1798
Cdd:TIGR02169 981 YEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
834-1424 |
7.22e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.03 E-value: 7.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 834 LLKSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAK 913
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 914 VKEMTERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKI 993
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 994 LQESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEE 1073
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1074 RLKKKDFELNTLNARIEDEQAISAQLQ--KKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEEAGGA 1151
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLeaEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1152 TSVQLELNKKQEAEFQKLRRDLEEATLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTE 1231
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1232 QLIKAKtnlekmcrtteDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLK 1311
Cdd:COG1196 631 RLEAAL-----------RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1312 RQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAqwrtKYETDAIQRTEELEEAKKKLAQR 1391
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA----LEELPEPPDLEELERELERLERE 775
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2163567613 1392 LQE-------AEEAVEAVNAKCSSLEKTKHRLQNEIEDLM 1424
Cdd:COG1196 776 IEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLE 815
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
834-1584 |
3.87e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 107.85 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 834 LLKSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDL-----------QLQVQAE------------- 889
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgeeeQLRVKEKigeleaeiasler 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 890 -----QDNLADAEERCDQLIKNKIQLEAKVKEMTERLeeeeemnAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKH 964
Cdd:TIGR02169 309 siaekERELEDAEERLAKLEAEIDKLLAEIEELEREI-------EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 965 ATENKVKNLTEEMAGLDENITKLTKEKKILQESHQQALDDLqaeEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLE 1044
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL---ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1045 RAKRklegDLKLAQESIMDLENDKQQLEERLKKKDFELntlnariedeqaisAQLQKKLKELQARIEELEEELEAERTGR 1124
Cdd:TIGR02169 459 QLAA----DLSKYEQELYDLKEEYDRVEKELSKLQREL--------------AEAEAQARASEERVRGGRAVEEVLKASI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1125 AKVEKLRSELLQELEETSERLEEAGG----ATSVQLELNKKQEAEFQKLRR----------------------------- 1171
Cdd:TIGR02169 521 QGVHGTVAQLGSVGERYATAIEVAAGnrlnNVVVEDDAVAKEAIELLKRRKagratflplnkmrderrdlsilsedgvig 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1172 ---------------------------DLEEA----------TLQHE-------ATAATLRKKHADSVA-ELSEQLDNLQ 1206
Cdd:TIGR02169 601 favdlvefdpkyepafkyvfgdtlvveDIEAArrlmgkyrmvTLEGElfeksgaMTGGSRAPRGGILFSrSEPAELQRLR 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1207 RVKQKLEKEKSELKLELddvnsnteqlikaktnlekmcRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQL 1286
Cdd:TIGR02169 681 ERLEGLKRELSSLQSEL---------------------RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1287 EEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHALQsaqhdcDLLREQYEEEMEaktELQRALSKANSEVAQW 1366
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN------DLEARLSHSRIP---EIQAELSKLEEEVSRI 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1367 RtkyetdaiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDK 1446
Cdd:TIGR02169 811 E--------ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1447 ILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKnlqeEILDLTEQLGASQKSIHELEKVRK 1526
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGEDEEIPEEELSLEDVQA 958
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163567613 1527 QLDAEKLELQaALEEAE--ASLEHEEGKILRAQLEFNQVKADYERK-LAEKDEEIEQSKRN 1584
Cdd:TIGR02169 959 ELQRVEEEIR-ALEPVNmlAIQEYEEVLKRLDELKEKRAKLEEERKaILERIEEYEKKKRE 1018
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
991-1844 |
5.79e-23 |
|
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: 107.51 E-value: 5.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 991 KKILQE-SHQqaLDDLQAEEDKVNTL-AKAKVKLEQQVDDLESSLEQ---EKKIRMDLERAKRKLEGDLK-LAQESIMDL 1064
Cdd:pfam15921 77 ERVLEEySHQ--VKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLRnQLQNTVHEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1065 ENDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAK-VEKLRSELLQELEETSE 1143
Cdd:pfam15921 155 EAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRsLGSAISKILRELDTEIS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1144 RLEEAGGATSVQLELNK-----KQEAEFQKLRRDLEEATLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSE 1218
Cdd:pfam15921 235 YLKGRIFPVEDQLEALKsesqnKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1219 LKLELDDVNSNTEQLikaKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLE---------EK 1289
Cdd:pfam15921 315 YMRQLSDLESTVSQL---RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQklladlhkrEK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1290 EAFINQLTRGKL-----TYTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCdllREQYEEEMEAKTELQRALSKANSEVA 1364
Cdd:pfam15921 392 ELSLEKEQNKRLwdrdtGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEC---QGQMERQMAAIQGKNESLEKVSSLTA 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1365 QWRTKYE---------TDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMAD---VERSNA 1432
Cdd:pfam15921 469 QLESTKEmlrkvveelTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQT 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1433 AAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFK--RENKNLQeeildlteq 1510
Cdd:pfam15921 549 ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilKDKKDAK--------- 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1511 lgasqksIHELEKVRKQLDAEKLELQAALEE---AEASLEHEEGKILR----AQLEFNQVKADYE---RKLAEKDEEIEQ 1580
Cdd:pfam15921 620 -------IRELEARVSDLELEKVKLVNAGSErlrAVKDIKQERDQLLNevktSRNELNSLSEDYEvlkRNFRNKSEEMET 692
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1581 SKRNHLRVVDSLQTSLDaetRSRNEalrlkkkmegdLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQL----DDVV 1656
Cdd:pfam15921 693 TTNKLKMQLKSAQSELE---QTRNT-----------LKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIqfleEAMT 758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1657 RANED----------LKENIAIVERRNNLLQSELEELRAmvEQSERARKLAEQELIEASERVQLLHSQNtslINQKKKME 1726
Cdd:pfam15921 759 NANKEkhflkeeknkLSQELSTVATEKNKMAGELEVLRS--QERRLKEKVANMEVALDKASLQFAECQD---IIQRQEQE 833
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1727 ADISQLQ--TEVEEAIQECRNAEEKAKKAITDAAMMAE---ELKKEQDTSAHL-----------ERMKKNMEQTVKDLQL 1790
Cdd:pfam15921 834 SVRLKLQhtLDVKELQGPGYTSNSSMKPRLLQPASFTRthsNVPSSQSTASFLshhsrktnalkEDPTRDLKQLLQELRS 913
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163567613 1791 RLDEAEQLAL-----KGGKKQLQKLEVRVRELENELE-----AEQKRNAESIKGLRKSERRVKE 1844
Cdd:pfam15921 914 VINEEPTVQLskaedKGRAPSLGALDDRVRDCIIESSlrsdiCHSSSNSLQTEGSKSSETCSRE 977
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
835-1597 |
9.75e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 106.69 E-value: 9.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 835 LKSAETEKEMQTMKEEfghlKEALEKSEARRKELEEKMVS-MLQEKNDLQLQVQAEQDNLADAEERCDQLiknKIQLEAK 913
Cdd:TIGR02169 191 LIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYeLLKEKEALERQKEAIERQLASLEEELEKL---TEEISEL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 914 VKEMTERLEEEEEMNAELaakKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKI 993
Cdd:TIGR02169 264 EKRLEEIEQLLEELNKKI---KDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 994 LQEShqqaLDDLQAEEDKV-NTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGdlklAQESIMDLENDKQQLE 1072
Cdd:TIGR02169 341 LERE----IEEERKRRDKLtEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK----LKREINELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1073 ERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEEAggat 1152
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL---- 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1153 svQLELNKKqEAEFQKLRRDLEEATLQHEATAATLRKKHAdSVAELSEQldnlqrvkqkleKEKSELKLE------LDDV 1226
Cdd:TIGR02169 489 --QRELAEA-EAQARASEERVRGGRAVEEVLKASIQGVHG-TVAQLGSV------------GERYATAIEvaagnrLNNV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1227 NSNTEQLIKAKTNL---EKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRA--------------------KLQTENSELS 1283
Cdd:TIGR02169 553 VVEDDAVAKEAIELlkrRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAvdlvefdpkyepafkyvfgdTLVVEDIEAA 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1284 RQLE-------------EKEAFI----NQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAhALQSAQHDCDLLREQYEEEM 1346
Cdd:TIGR02169 633 RRLMgkyrmvtlegelfEKSGAMtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELS-SLQSELRRIENRLDELSQEL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1347 EAKTELQRALSKANSEVAQwrtkYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMAD 1426
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQ----EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1427 VERSnaaaaaldkkqrnfdkilsewkqKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILD 1506
Cdd:TIGR02169 788 LSHS-----------------------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1507 LTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLEFNQVkadyERKLAEKDEEIEQSKRNHL 1586
Cdd:TIGR02169 845 LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL----ERKIEELEAQIEKKRKRLS 920
|
810
....*....|.
gi 2163567613 1587 RVVDSLQTSLD 1597
Cdd:TIGR02169 921 ELKAKLEALEE 931
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
839-1541 |
1.69e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.79 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 839 ETEKEMQTMKEEfghlkeaLEKSEARRKELEEKMVSmlqekndlqLQVQAEQ----DNLADAEERCD-QLIKNKIQ-LEA 912
Cdd:COG1196 176 EAERKLEATEEN-------LERLEDILGELERQLEP---------LERQAEKaeryRELKEELKELEaELLLLKLReLEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 913 KVKEMTERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKK 992
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 993 ILQESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLE 1072
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1073 ERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEEtsERLEEAGGAT 1152
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE--LLEEAALLEA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1153 SVQLELNKKQEAEfQKLRRDLEEATLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEK--EKSELKLELDDVNSNT 1230
Cdd:COG1196 478 ALAELLEELAEAA-ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAalEAALAAALQNIVVEDD 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1231 EQLIKAKtnlekmcrttedqmnEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRgkltytqQLEDL 1310
Cdd:COG1196 557 EVAAAAI---------------EYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR-------EADAR 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1311 KRQLEEEAKAKNALAHALQSAQHdcdlLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQ 1390
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALR----RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1391 RLQEAEEAVEAvnakcssLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEAR 1470
Cdd:COG1196 691 EELELEEALLA-------EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163567613 1471 SLSTELFKLKNAYEE-------SLEHLETFKRENKNLQEEILDLTEqlgasqkSIHELEKVRKQLDAEKLE-LQAALEE 1541
Cdd:COG1196 764 ELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEE-------ARETLEEAIEEIDRETRErFLETFDA 835
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1235-1906 |
7.09e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 104.07 E-value: 7.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1235 KAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTE--NSELSRQLEEK---EAFINQLTRGKLTYTQQLED 1309
Cdd:PTZ00121 1119 EAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDarKAEEARKAEDAkkaEAARKAEEVRKAEELRKAED 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1310 LK-----RQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQralSKANSEVAQWRTKYETDAIQRTEELEEA 1384
Cdd:PTZ00121 1199 ARkaeaaRKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEE---ERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1385 KKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDlmadversNAAAAALDKKQRNFDKILSEWKQKFEESQTELEA 1464
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE--------AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEA 1347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1465 SQKEARSLSTELfklkNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEA 1544
Cdd:PTZ00121 1348 AKAEAEAAADEA----EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1545 SLEHEEGKilraqlefnqvKADYERKLAEKDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQL 1624
Cdd:PTZ00121 1424 KKKAEEKK-----------KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA 1492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1625 SHANRTAAEAQKQVKALQgylKDTQLQLDDVVRANEDLK---ENIAIVERRNNLLQSELEELRAM--VEQSERARKlAEQ 1699
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKK---KADEAKKAEEAKKADEAKkaeEAKKADEAKKAEEKKKADELKKAeeLKKAEEKKK-AEE 1568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1700 ELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAitdaammaEELKKEQDTSAHLERMKK 1779
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--------EELKKAEEEKKKVEQLKK 1640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1780 NMEQTVKDL-QLRLDEAEQLALKGGKKQLQKLEVRVRELENELEAEQKRNAESIKGLRKSERRVKELSYQTEEDRKNMVR 1858
Cdd:PTZ00121 1641 KEAEEKKKAeELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2163567613 1859 LQDLVDKLQLKVKAYKRQAEEAE---EQANSNLAKFRKVQHELDEAEERAD 1906
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
967-1678 |
7.53e-21 |
|
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: 99.71 E-value: 7.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 967 ENKVKNLTEEMAGLDENITKLTKEKKILQESHQQALDDLQAEEDKVNtlakakvKLEQQVDDLESSLEQEKKIRMDLERA 1046
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIK-------ILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1047 KRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIeeleeeleaertgrak 1126
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQK---------------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1127 vEKLRSELLQELEETSERLEEaggatsvqLELNKKQEAEFQKLRRDLEEATLQHeataatlrKKHADSVAELSEQLDNLQ 1206
Cdd:TIGR04523 169 -EELENELNLLEKEKLNIQKN--------IDKIKNKLLKLELLLSNLKKKIQKN--------KSLESQISELKKQNNQLK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1207 RVKQKLEKEKSELKLELddvNSNTEQLIKAKTNLEKmcrtTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQl 1286
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEI---SNTQTQLNQLKDEQNK----IKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1287 eeKEAFINQLTRGKLTYTQ-QLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQ 1365
Cdd:TIGR04523 304 --KEQDWNKELKSELKNQEkKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1366 WRtkyetdaiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFD 1445
Cdd:TIGR04523 382 YK--------QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1446 KILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVR 1525
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1526 KQLDAEKLELQAALEEaeasleheegkilraqLEFNQVKADYERKLAEKDEEIEQSKRNhlrvvdslQTSLDAETRSRNE 1605
Cdd:TIGR04523 534 KEKESKISDLEDELNK----------------DDFELKKENLEKEIDEKNKEIEELKQT--------QKSLKKKQEEKQE 589
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2163567613 1606 ALRLKKKMEGDLN----EMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENI-AIVERRNNLLQS 1678
Cdd:TIGR04523 590 LIDQKEKEKKDLIkeieEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIkEIRNKWPEIIKK 667
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1078-1878 |
8.72e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 100.60 E-value: 8.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1078 KDFELNTLNARIEDEQaiSAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEEAGGATSVQLE 1157
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEA--TEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1158 --LNKKQEAEFQKLRRDLEEATLQHEA-------TAATLRKKHADSVAELSEQLDNLQRVKqklEKEKSELKLELDDVNS 1228
Cdd:PTZ00121 1155 eiARKAEDARKAEEARKAEDAKKAEAArkaeevrKAEELRKAEDARKAEAARKAEEERKAE---EARKAEDAKKAEAVKK 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1229 NTEqlikAKTNLEKMCRTTEDQMNEHRSKLEEAQrtVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLE 1308
Cdd:PTZ00121 1232 AEE----AKKDAEEAKKAEEERNNEEIRKFEEAR--MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD 1305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1309 DLKRQLEEEAKAKNALAHAlQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQRTEELE--EAKK 1386
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKkaDAAK 1384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1387 KLAQRLQEAEEA---VEAVNAKCSSLEKtKHRLQNEIEDLMADVERSNAAAAAldKKQRNFDKILSEWKQKFEESQTELE 1463
Cdd:PTZ00121 1385 KKAEEKKKADEAkkkAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKAEE 1461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1464 ASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQlgasQKSIHELEKVRKQLDAEKLElqaaleEAE 1543
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA----KKKADEAKKAEEAKKADEAK------KAE 1531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1544 ASLEHEEGKILRAQLEFNQVKADYERKLAEKDEEIEQSKRNHLRVVDSLQTsldAETRSRNEALRLKKKMEGDLNEMEIQ 1623
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK---AEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1624 LSHANRtaaEAQKQVKALQgylkdtqlqlddvVRANEDLKENIaiverrNNLLQSELEELRamveQSERARKLAEQELIE 1703
Cdd:PTZ00121 1609 AEEAKK---AEEAKIKAEE-------------LKKAEEEKKKV------EQLKKKEAEEKK----KAEELKKAEEENKIK 1662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1704 ASErvqllhsqntslinQKKKMEADisqlqtevEEAIQECRNAEEKAKKAitdaammAEELKKEQDTSAHLERMKKNMEQ 1783
Cdd:PTZ00121 1663 AAE--------------EAKKAEED--------KKKAEEAKKAEEDEKKA-------AEALKKEAEEAKKAEELKKKEAE 1713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1784 TVKdlqlrldEAEQLalkggKKQLQKLEVRVRELENELEaEQKRNAESIKGLRKSERRVKELSYQTEEDRKNMVRLQDLV 1863
Cdd:PTZ00121 1714 EKK-------KAEEL-----KKAEEENKIKAEEAKKEAE-EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
810
....*....|....*
gi 2163567613 1864 DKLQLKVKAYKRQAE 1878
Cdd:PTZ00121 1781 IEEELDEEDEKRRME 1795
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
213-701 |
2.51e-20 |
|
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: 98.28 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 213 IIQANPALEAFGNAKTVRNDNSSRFGKF--IRIHFGATG---KLASADIETYLLEKSRVIFQL------KAERNYHIFYQ 281
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 282 ILSNKKPELLEMLLITNNPYD------YSYVSQGEVTVASIDDSEELLATD--------SAFDVLGFTAEEKAGVYKLTG 347
Cdd:cd14894 329 MVAGVNAFPFMRLLAKELHLDgidcsaLTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 348 AIMHFGNMKFKQKQREEQAEPDGT---EDADKSAYLMGLNSADLLKGLCHPR---VKVGNEYVTKGQSVQQVYYSIGALA 421
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 422 KAVYEKMFNWMVVRIN-----NSLETKQPRQY------------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 484
Cdd:cd14894 489 RLLYQLAFNYVVFVMNeatkmSALSTDGNKHQmdsnasapeavsLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYAREEQ 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 485 HMFVLEQEEYKKEGIEWEfidfgmdlQACIDLIEKPMGIMSILEEECMFPKASDMTF-----KAKLFDNHL--GKSANFG 557
Cdd:cd14894 569 VIAVAYSSRPHLTARDSE--------KDVLFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIydRNSSRLP 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 558 KPRNVKGKSEAH---------FSLIHYAGTVDYNIIGWLEKNKDPLNETV-VGLYQKSALKLLASLF-SNYAGADAGGDG 626
Cdd:cd14894 641 EPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLlVGLKTSNSSHFCRMLNeSSQLGWSPNTNR 720
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2163567613 627 GKGKGAKKKGSSFQTVSALHRENLNKLMANLKTTHPHFVRCLIPNERKEPGVMDNTLVMHQLRCNGVLEGIRICR 701
Cdd:cd14894 721 SMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
836-1423 |
2.90e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 98.59 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 836 KSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVK 915
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 916 EMTERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQ 995
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 996 ESHQQAldDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEER- 1074
Cdd:TIGR02168 428 KKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFs 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1075 -----LKKKDFELNTLNARI--------EDEQAISA-------------------------------------------Q 1098
Cdd:TIGR02168 506 egvkaLLKNQSGLSGILGVLselisvdeGYEAAIEAalggrlqavvvenlnaakkaiaflkqnelgrvtflpldsikgtE 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1099 LQKKLKELQARIEELEEELEAERTGRAKVEKLRSELL------------------------------------------- 1135
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLggvlvvddldnalelakklrpgyrivtldgdlvrpggvitggs 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1136 -----------QELEETSERLEEAGG-ATSVQLELNKKQ------EAEFQKLRRDLEEATLQHEATAATLRK------KH 1191
Cdd:TIGR02168 666 aktnssilerrREIEELEEKIEELEEkIAELEKALAELRkeleelEEELEQLRKELEELSRQISALRKDLARleaeveQL 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1192 ADSVAELSEQLDNLQRVKQKLEKEKSELKLELD-------DVNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRT 1264
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAeaeaeieELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1265 VTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEE 1344
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163567613 1345 EMEAKTELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDL 1423
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1197-1926 |
1.85e-19 |
|
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: 96.01 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1197 ELSEQLDNLQRVKQKLEKEKSELKleldDVNSNTEQLIKAKTNLEkmcrtteDQMNEHRSKLEEAQRTVTDLSTQRAKLQ 1276
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKAESELK----ELEKKHQQLCEEKNALQ-------EQLQAETELCAEAEEMRARLAARKQELE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1277 TENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKnalaHALQSAQHDCDLLREQYEEEMEAKTELQRAL 1356
Cdd:pfam01576 75 EILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAAR----QKLQLEKVTTEAKIKKLEEDILLLEDQNSKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1357 SKAnsevaqwrtkyetdaiqrteeleeaKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAA 1436
Cdd:pfam01576 151 SKE-------------------------RKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1437 LDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQK 1516
Cdd:pfam01576 206 LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1517 SIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLEFNQVKADYERKLAEKDEEIEQSKRNHLRVVDSLQTSL 1596
Cdd:pfam01576 286 ARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1597 DAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKEniaiverRNNLL 1676
Cdd:pfam01576 366 EQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAE-------KLSKL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1677 QSELEELRAMVEQSE-RARKLA------EQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEK 1749
Cdd:pfam01576 439 QSELESVSSLLNEAEgKNIKLSkdvsslESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQ 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1750 AKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKggkkqLQKLEVRVRELENELEAEQKRNA 1829
Cdd:pfam01576 519 LSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDK-----LEKTKNRLQQELDDLLVDLDHQR 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1830 ESIKGLRKSERRVKELsyqTEEDRKNMVRLQDLVDKlqlkvkaykrqaeeAEEQANSNLAKFRKVQHELDEAEERADMAE 1909
Cdd:pfam01576 594 QLVSNLEKKQKKFDQM---LAEEKAISARYAEERDR--------------AEAEAREKETRALSLARALEEALEAKEELE 656
|
730
....*....|....*..
gi 2163567613 1910 SQVNKLRARSRDIGAKK 1926
Cdd:pfam01576 657 RTNKQLRAEMEDLVSSK 673
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1255-1927 |
2.33e-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: 92.44 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1255 RSKLEEAQRTVTDLSTQRAKLQTENS------ELSRQLEEKEAFInqLTRGKLTYTQQLEDLKRQLEEeakaknalahaL 1328
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREkaeryqALLKEKREYEGYE--LLKEKEALERQKEAIERQLAS-----------L 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1329 QSAQHDCDLLREQYEEEMEAKTELQRALSKansevaQWRTKYETDAIQRTEELEEAKKKLAQrlqeAEEAVEAVNAKCSS 1408
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNK------KIKDLGEEEQLRVKEKIGELEAEIAS----LERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1409 LEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLE 1488
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1489 HLETFKRENKNLQEEILDLTEQLGasqksihELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLEFNQVKADYE 1568
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELA-------DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1569 RKLAEKD---EEIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKMEG------DLNEMEIQLSHANRTAAEAQKQ-- 1637
Cdd:TIGR02169 473 DLKEEYDrveKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGvhgtvaQLGSVGERYATAIEVAAGNRLNnv 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1638 --------VKALQgYLKD------TQLQLDDVVRANEDLK---------------------ENIAIVERRNNLLQSELEE 1682
Cdd:TIGR02169 553 vveddavaKEAIE-LLKRrkagraTFLPLNKMRDERRDLSilsedgvigfavdlvefdpkyEPAFKYVFGDTLVVEDIEA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1683 LR--------------------AMVEQSERARKLA------EQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEV 1736
Cdd:TIGR02169 632 ARrlmgkyrmvtlegelfeksgAMTGGSRAPRGGIlfsrsePAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1737 EEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEqLALKGGKKQLQKLEVR--- 1813
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE-EDLHKLEEALNDLEARlsh 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1814 --VRELENELEAEQKRNAESIKGLRKSERRVKELSYQTEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQANSNLAKF 1891
Cdd:TIGR02169 791 srIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870
|
730 740 750
....*....|....*....|....*....|....*.
gi 2163567613 1892 RKVQHELDEAEERADMAESQVNKLRARSRDIGAKKG 1927
Cdd:TIGR02169 871 EELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
940-1439 |
3.28e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 91.64 E-value: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 940 DECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEkkilqeshqQALDDLQAEedkvnTLAKAK 1019
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE---------AGLDDADAE-----AVEARR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1020 VKLEQQVDDLESSLEQEkkiRMDLERAKRKLEGdlklAQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQAISAQL 1099
Cdd:PRK02224 317 EELEDRDEELRDRLEEC---RVAAQAHNEEAES----LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1100 QKKLKELQARIEELEeeleaerTGRAKVEKLRSELLQELEETSERLEEAggatsvqlelnkkqEAEFQKLRRDLEEA-TL 1178
Cdd:PRK02224 390 EEEIEELRERFGDAP-------VDLGNAEDFLEELREERDELREREAEL--------------EATLRTARERVEEAeAL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1179 QHEATAATLRKK-----HADSVAELSEQldnlqrvKQKLEKEKSELKLELDDVNSNTEQLIKAK------TNLEKMCRTT 1247
Cdd:PRK02224 449 LEAGKCPECGQPvegspHVETIEEDRER-------VEELEAELEDLEEEVEEVEERLERAEDLVeaedriERLEERREDL 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1248 EDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAhA 1327
Cdd:PRK02224 522 EELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA-A 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1328 LQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAIqrtEELEEAKKKLAQRLQEAEEAVEAVNAKCS 1407
Cdd:PRK02224 601 IADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARI---EEAREDKERAEEYLEQVEEKLDELREERD 677
|
490 500 510
....*....|....*....|....*....|..
gi 2163567613 1408 SLEKTKHRLQNEIEDLMADVERSNAAAAALDK 1439
Cdd:PRK02224 678 DLQAEIGAVENELEELEELRERREALENRVEA 709
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
825-1509 |
3.29e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.13 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 825 MKLYFKIKPLLKSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDlQLQVQAEQdnladAEERCDQLi 904
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEE-----AKKKADAA- 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 905 KNKIQLEAKVKEMTERLEEEEEMNAELAAKKRKL-EDECSELKKDIDDLElslAKVEKEKHATENKVKnlTEEMAGLDEN 983
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaEKKKEEAKKKADAAK---KKAEEKKKADEAKKK--AEEDKKKADE 1409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 984 ITKLTKEKKILQESHQQALDDLQAEEdkvntlAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGD-LKLAQESIM 1062
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKADE------AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAEEAK 1483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1063 DLENDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELqarieeleeeleaertgRAKVEKLRSELLQELEETS 1142
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEA-----------------KKAEEAKKADEAKKAEEKK 1546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1143 ErleeaggatsvQLELNKKQEAEFQKLRRDLEEATLQHEATAATLRKkhadsvAELSEQLDNlQRVKQKLEKEKSELKLE 1222
Cdd:PTZ00121 1547 K-----------ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK------AEEAKKAEE-ARIEEVMKLYEEEKKMK 1608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1223 LDDVNSNTEQLIKAktnlekmcrttedqmnEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLT 1302
Cdd:PTZ00121 1609 AEEAKKAEEAKIKA----------------EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1303 YTQQLEDLKRQLEEEAKAKNALAHALQSAQhDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAiQRTEEL- 1381
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEAk 1750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1382 --EEAKKKLAQRLQEAEEAVEAVNAKCSS-----LEKTKHRLQNEIEDLMADVeRSNAAAAALDKKQRNFdkILSEWKQK 1454
Cdd:PTZ00121 1751 kdEEEKKKIAHLKKEEEKKAEEIRKEKEAvieeeLDEEDEKRRMEVDKKIKDI-FDNFANIIEGGKEGNL--VINDSKEM 1827
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 2163567613 1455 FEESQTELEASQ----KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTE 1509
Cdd:PTZ00121 1828 EDSAIKEVADSKnmqlEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEE 1886
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
887-1543 |
3.85e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 91.28 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 887 QAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEEEEEMNAELAAKKRKLEDEcselkKDIDDLelsLAKVEKEKHAT 966
Cdd:PRK03918 134 QGEIDAILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRT-----ENIEEL---IKEKEKELEEV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 967 ENKVKNLTEEMAGLDENITKLTKEKKILqESHQQALDDLQAEEDKVNtlaKAKVKLEQQVDDLESSLEQEKKIRMDLERA 1046
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESLE---GSKRKLEEKIRELEERIEELKKEIEELEEK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1047 KRKLEgDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQarieeleeeleaertgraK 1126
Cdd:PRK03918 282 VKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE------------------E 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1127 VEKLRSELLQELEETSERLEEaggatsvqLELNKKQEAEFQKLRRDLEEATLQheataatlrkkhadsvaELSEQLDNLQ 1206
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHEL--------YEEAKAKKEELERLKKRLTGLTPE-----------------KLEKELEELE 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1207 RVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEK---MCRTTEDQMNEHRSK--LEEAQRTVTDLSTQRAKLQTENSE 1281
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgKCPVCGRELTEEHRKelLEEYTAELKRIEKELKEIEEKERK 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1282 LSRQLEEKEAFINQLTRgkLTYTQQLEDLKRQLEEEAKAKNAlahalqsaqhdcdllreqyeEEMEAKTELQRALSKANS 1361
Cdd:PRK03918 478 LRKELRELEKVLKKESE--LIKLKELAEQLKELEEKLKKYNL--------------------EELEKKAEEYEKLKEKLI 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1362 EVAQwRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLE-KTKHRLQNEIEDLMADVERSNAAAAALDKK 1440
Cdd:PRK03918 536 KLKG-EIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKEL 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1441 QRNFDKILSEwKQKFEESQTELEASQKEARSLSTELFKLKNAYEEslEHLETFKRENKNLQEEILDLTEQLGASQKSIHE 1520
Cdd:PRK03918 615 EREEKELKKL-EEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREE 691
|
650 660
....*....|....*....|...
gi 2163567613 1521 LEKVRKQLDAEKLELQAALEEAE 1543
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELE 714
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
849-1482 |
9.68e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.59 E-value: 9.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 849 EEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEEEEEMN 928
Cdd:PTZ00121 1191 EELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 929 AELAAKKRKLED-ECSELKKDIDDLElslaKVEKEKHATENKVKnlTEEMAGLDENITKLTKEKKILQESHQQALDDLQA 1007
Cdd:PTZ00121 1271 AIKAEEARKADElKKAEEKKKADEAK----KAEEKKKADEAKKK--AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1008 EEdkvntlaKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNA 1087
Cdd:PTZ00121 1345 AE-------AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1088 RIEDEQAISAQLQKKLKELQARIEELEeeleaertgRAKVEKLRSELLQELEETSERLEEAGGATSVQLELNKKQEAEfq 1167
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEEAK---------KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD-- 1486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1168 KLRRDLEEAtlqheataatlrKKHADSVAELSEQLDNLQRVKQKLEKEKSElKLELDDVNSNTEQLIKA--KTNLEKMCR 1245
Cdd:PTZ00121 1487 EAKKKAEEA------------KKKADEAKKAAEAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAKKAeeKKKADELKK 1553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1246 TTEDQMNEHRSKLEEAQRtvtdlSTQRAKLQTENSELSRQLEEKEaFINQLTRGKLTYTQQLEDLKRqlEEEAKAKNALA 1325
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKK-----AEEDKNMALRKAEEAKKAEEAR-IEEVMKLYEEEKKMKAEEAKK--AEEAKIKAEEL 1625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1326 HALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAiQRTEEL----EEAKKKLAQRLQEAEEA--V 1399
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkkaeEDEKKAAEALKKEAEEAkkA 1704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1400 EAVNAKCSSLEKTKHRLQNEIEDLMADVERSnaaaaaldKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKL 1479
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
...
gi 2163567613 1480 KNA 1482
Cdd:PTZ00121 1777 KEA 1779
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
836-1721 |
1.08e-17 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 90.23 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 836 KSAETEKEMQTMKEEFGHLKEALEKS----EARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLE 911
Cdd:pfam01576 353 KHTQALEELTEQLEQAKRNKANLEKAkqalESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 912 AKVKEMTERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENitkltkek 991
Cdd:pfam01576 433 EKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQ-------- 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 992 kilqeshqqalddLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEgdlklaqesiMDLENDKQQL 1071
Cdd:pfam01576 505 -------------LEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQ----------RELEALTQQL 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1072 EERLKKKDfelntlnariedeqaisaqlqkklkelqarieeleeeleaertgraKVEKLRSELLQELEETSERLEEAGGA 1151
Cdd:pfam01576 562 EEKAAAYD----------------------------------------------KLEKTKNRLQQELDDLLVDLDHQRQL 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1152 TSvqlELNKKQE------AEFQKLRRDLEEATLQHEATAatlRKKHADSVAeLSEQLDNLQRVKQKLEKEKSELKLELDD 1225
Cdd:pfam01576 596 VS---NLEKKQKkfdqmlAEEKAISARYAEERDRAEAEA---REKETRALS-LARALEEALEAKEELERTNKQLRAEMED 668
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1226 VNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEaqrtvtdlstqraklqtenselsrqLEEKeafinqltrgkltyTQ 1305
Cdd:pfam01576 669 LVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEE-------------------------LEDE--------------LQ 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1306 QLEDLKRQLEEEAKAknalahalqsaqhdcdlLREQYEEEMEAKTEL----QRALSKansEVAQWRTKYETDAIQRTEEL 1381
Cdd:pfam01576 710 ATEDAKLRLEVNMQA-----------------LKAQFERDLQARDEQgeekRRQLVK---QVRELEAELEDERKQRAQAV 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1382 eEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAaaldkkqrnfDKILSEWKQkfeesqte 1461
Cdd:pfam01576 770 -AAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASR----------DEILAQSKE-------- 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1462 leaSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDlteqlGASQKSIHELEKvrKQLDAEKLELQAALEE 1541
Cdd:pfam01576 831 ---SEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIAS-----GASGKSALQDEK--RRLEARIAQLEEELEE 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1542 AEASLEHEEGKILRAQLEFNQVKADY--ERKLAEKDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEAlrLKKKMEGDLNE 1619
Cdd:pfam01576 901 EQSNTELLNDRLRKSTLQVEQLTTELaaERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKS--SIAALEAKIAQ 978
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1620 MEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQ 1699
Cdd:pfam01576 979 LEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQR 1058
|
890 900
....*....|....*....|..
gi 2163567613 1700 ELIEASERVQLLHSQNTSLINQ 1721
Cdd:pfam01576 1059 ELDDATESNESMNREVSTLKSK 1080
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
838-1450 |
1.17e-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: 90.13 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 838 AETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEM 917
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 918 TERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKV---KNLTEEMAGLDENITKLTKEKKIL 994
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVrggRAVEEVLKASIQGVHGTVAQLGSV 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 995 QESHQQAL--------------DDLQAEED--------------------KVNTLAKAKVKLEQQVDDLESSLEQEKKIR 1040
Cdd:TIGR02169 534 GERYATAIevaagnrlnnvvveDDAVAKEAiellkrrkagratflplnkmRDERRDLSILSEDGVIGFAVDLVEFDPKYE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1041 -------------MDLERAKR--------KLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQAISAQL 1099
Cdd:TIGR02169 614 pafkyvfgdtlvvEDIEAARRlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSL 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1100 QKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEEAggaTSVQLELNKKQEAEFQKLRrDLEEATLQ 1179
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL---EEDLSSLEQEIENVKSELK-ELEARIEE 769
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1180 HEATAATLRKKHADSVAELS-EQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKL 1258
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1259 EEAQRTVTDLSTQRAKLQTEnselsrqLEEKEAFINQLtrgkltyTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLL 1338
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEE-------LEELEAALRDL-------ESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1339 REQYEEEMEAKTELQRALSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQE-------AEEAVEAVNAKCSSLEK 1411
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGE--DEEIPEEELSLEDVQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKE 993
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 2163567613 1412 TKHRLQNEIEDL-----MADVERSNAAAAALDKKQRNFDKILSE 1450
Cdd:TIGR02169 994 KRAKLEEERKAIlerieEYEKKKREVFMEAFEAINENFNEIFAE 1037
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
935-1580 |
3.38e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 88.43 E-value: 3.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 935 KRKLEDECSELKKDIDDLELSLAKVEKekhaTENKVKNLtEEMAGLDENITKLTKEKKILQES--------HQQALDDLQ 1006
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALED----AREQIELL-EPIRELAERYAAARERLAELEYLraalrlwfAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1007 AEEDKvntLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGD-LKLAQESIMDLENDKQQLEERLKKKDFELNTL 1085
Cdd:COG4913 295 AELEE---LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAAL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1086 NARIEDEQAISAQLQKKLKELQARIEELEEELEAERTgRAKVEklRSELLQELEETSERLEEaggatsvqLELNKKQ-EA 1164
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEALEEELEALEEALA-EAEAA--LRDLRRELRELEAEIAS--------LERRKSNiPA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1165 EFQKLRRDLEEATLQHEA---------------------------TAAT---LRKKHADSVAELSEQLDNLQRVK-QKLE 1213
Cdd:COG4913 441 RLLALRDALAEALGLDEAelpfvgelievrpeeerwrgaiervlgGFALtllVPPEHYAAALRWVNRLHLRGRLVyERVR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1214 KEKSELKLELDDVNSNTEQLIKAKTNLEK------------MCRTTEDQMNEHRskleeaqRTVTD-----LSTQRAKLQ 1276
Cdd:COG4913 521 TGLPDPERPRLDPDSLAGKLDFKPHPFRAwleaelgrrfdyVCVDSPEELRRHP-------RAITRagqvkGNGTRHEKD 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1277 TENSELSR---------QLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLlrEQYEEEME 1347
Cdd:COG4913 594 DRRRIRSRyvlgfdnraKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV--ASAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1348 AKTELQRALSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADV 1427
Cdd:COG4913 672 ELEAELERLDASSDDL---------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1428 ER-----SNAAAAALDKK--QRNFDKILSEWKQKFEESQTELEAsqkearslstelfKLKNAYEESLEHLETFKRENKnl 1500
Cdd:COG4913 737 EAaedlaRLELRALLEERfaAALGDAVERELRENLEERIDALRA-------------RLNRAEEELERAMRAFNREWP-- 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1501 qeeilDLTEQLGASQKSIHELEKVRKQLDAEKLElqaaleeaeaslEHEEgKILRAQLEFNQV-KADYERKLAEKDEEIE 1579
Cdd:COG4913 802 -----AETADLDADLESLPEYLALLDRLEEDGLP------------EYEE-RFKELLNENSIEfVADLLSKLRRAIREIK 863
|
.
gi 2163567613 1580 Q 1580
Cdd:COG4913 864 E 864
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1021-1664 |
5.72e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 87.66 E-value: 5.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1021 KLEQQVDDLESSLEQEKKIRMDLERAKRKLE--GDLKLAQESIMDLENDKQQLEE-----RLKKKDFELNTLNARIEDEQ 1093
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1094 AISAQLQKKLKELQARIEELeeeleaertgRAKVEKLRSEL-------LQELEETSERLEEaggatsvQLELNKKQEAEF 1166
Cdd:COG4913 302 AELARLEAELERLEARLDAL----------REELDELEAQIrgnggdrLEQLEREIERLER-------ELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1167 QKLRRDLEEATLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRT 1246
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1247 TEDQMNEHRSKLEEAQRTVTDLstqrakLQTENSELS--------------------RQLEEKEAFINQL-TRGKLTYtQ 1305
Cdd:COG4913 445 LRDALAEALGLDEAELPFVGEL------IEVRPEEERwrgaiervlggfaltllvppEHYAAALRWVNRLhLRGRLVY-E 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1306 QLEDLKRQLEEEAKAKNALAHALQSAQHDC-DLLREQYEEEM-----EAKTELQRA--------LSKANSEVAQ------ 1365
Cdd:COG4913 518 RVRTGLPDPERPRLDPDSLAGKLDFKPHPFrAWLEAELGRRFdyvcvDSPEELRRHpraitragQVKGNGTRHEkddrrr 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1366 WRTKYET--DAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQ-- 1441
Cdd:COG4913 598 IRSRYVLgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAel 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1442 ---RNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSI 1518
Cdd:COG4913 678 erlDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1519 HELEKVRKQLDAeklELQAALEEAEASLEHEEGKILRAQLEFNQvkaDYERKLAEKDEEIEqSKRNHLRVVDSLQTslda 1598
Cdd:COG4913 758 ALGDAVERELRE---NLEERIDALRARLNRAEEELERAMRAFNR---EWPAETADLDADLE-SLPEYLALLDRLEE---- 826
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163567613 1599 etrsrNEALRLKKKMEGDLNEMEIQ-----LSHANRTAAEAQKQVK----ALQG--YLKDTQLQLDDVVRANEDLKE 1664
Cdd:COG4913 827 -----DGLPEYEERFKELLNENSIEfvadlLSKLRRAIREIKERIDplndSLKRipFGPGRYLRLEARPRPDPEVRE 898
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1072-1914 |
7.04e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 87.33 E-value: 7.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1072 EERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTgrAKVEKLRSELLQELEEtsERLEEAGGA 1151
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKL--KEQAKKALEYYQLKEK--LELEEEYLL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1152 TSVQLELNKKQEAEFQKLRRDLEEAT--LQHEATAATLRKKHADSVAELSEQLDNLQRVKQK-LEKEKSELKLELDDVNS 1228
Cdd:pfam02463 228 YLDYLKLNEERIDLLQELLRDEQEEIesSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKlLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1229 NTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLE 1308
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1309 DLKRQLEEEakaknaLAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKL 1388
Cdd:pfam02463 388 SAAKLKEEE------LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1389 AQRLQEAEEAVEAVNAKCsSLEKTKHRLQNEIEDLMADVERSNAA---AAALDKKQRNFDKILSEWKQKFEESQTELEAS 1465
Cdd:pfam02463 462 KDELELKKSEDLLKETQL-VKLQEQLELLLSRQKLEERSQKESKArsgLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1466 QKEARSLST-ELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEkvrkqLDAEKLELQAALEEAEA 1544
Cdd:pfam02463 541 YKVAISTAViVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE-----IDPILNLAQLDKATLEA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1545 SLEHEEGKILRAQLEFNQVKADYERKLAEKDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQL 1624
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEIL 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1625 SHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEE---LRAMVEQSERARKLAEQEL 1701
Cdd:pfam02463 696 RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEksrLKKEEKEEEKSELSLKEKE 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1702 IEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNM 1781
Cdd:pfam02463 776 LAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEE 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1782 EQTVKDLQLRLDEAEQLALKGGKKQLQKLEVRVRELENELEAEQKRNAESIKGLRKSERRVKELSYQTEEDRKNMVRLQD 1861
Cdd:pfam02463 856 LERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEE 935
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 2163567613 1862 LVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKVQHELDEAEERADMAESQVNK 1914
Cdd:pfam02463 936 EPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEE 988
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
854-1582 |
9.61e-17 |
|
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: 86.61 E-value: 9.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 854 LKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLiKNKIQ-LEAKVKEMTERLEEEEEMNAELA 932
Cdd:TIGR04523 24 YKNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNS-NNKIKiLEQQIKDLNDKLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 933 AKKRKLEDECSELKKDIDDLELSLAKVEKEKHATE-------NKVKNLTEEMAGLDENITKLTKEKKILqeshqqalddl 1005
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNNKYNDLKKQKEEL----------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1006 qaeEDKVNTLAKAKVKLEQQVDDLESSLeqekkirmdlerakrklegdlklaqesimdleNDKQQLEERLKKKDFELNTL 1085
Cdd:TIGR04523 172 ---ENELNLLEKEKLNIQKNIDKIKNKL--------------------------------LKLELLLSNLKKKIQKNKSL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1086 NARIEDEQAISAQLQKKLKELQARIeeleeeleaertgrakveklrSELLQELEETSERLEEaggaTSVQLELNKKQeae 1165
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEI---------------------NEKTTEISNTQTQLNQ----LKDEQNKIKKQ--- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1166 fqklrrdLEEATLQHEATAATLRkkhadsvaELSEQLDNLQRVKQKLEKEKSElkleldDVNSNTEQLIKaktNLEKMCR 1245
Cdd:TIGR04523 269 -------LSEKQKELEQNNKKIK--------ELEKQLNQLKSEISDLNNQKEQ------DWNKELKSELK---NQEKKLE 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1246 TTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLE-------DLKRQLEEEA 1318
Cdd:TIGR04523 325 EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKnlesqinDLESKIQNQE 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1319 KAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYE------TDAIQRTEELEEAKKKLAQRL 1392
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKnldntrESLETQLKVLSRSINKIKQNL 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1393 QEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEASQ--KEAR 1470
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEID 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1471 SLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEE 1550
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
730 740 750
....*....|....*....|....*....|..
gi 2163567613 1551 GKILRAQLEFNQVKAdyerKLAEKDEEIEQSK 1582
Cdd:TIGR04523 645 QEVKQIKETIKEIRN----KWPEIIKKIKESK 672
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1306-1798 |
1.33e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 86.25 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1306 QLEDLKRQLEE-EAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTElqrALSKANSEVAQWRTKYEtdaiqRTEELEEA 1384
Cdd:PRK02224 188 SLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARE---TRDEADEVLEEHEERRE-----ELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1385 KKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEA 1464
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1465 SQKEARSLS--------------TELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDA 1530
Cdd:PRK02224 340 HNEEAESLRedaddleeraeelrEEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1531 EKLELQAALEEAEASLEHEEGKILRAQLEFNQVK-----------------ADYERKLAEKDEEIEQSKRNHLRVVDSLQ 1593
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1594 TSLDA-ETRSRNEALRLKKKMEGDL-NEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVER 1671
Cdd:PRK02224 500 RAEDLvEAEDRIERLEERREDLEELiAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1672 RNNLLQSELEELRAMVEQSErARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEA-IQECRNAEEKA 1750
Cdd:PRK02224 580 KLAELKERIESLERIRTLLA-AIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEArIEEAREDKERA 658
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2163567613 1751 KKAITDAAMMAEELKKEQDT--------SAHLERMK------KNMEQTVKDLQLRLDEAEQL 1798
Cdd:PRK02224 659 EEYLEQVEEKLDELREERDDlqaeigavENELEELEelrerrEALENRVEALEALYDEAEEL 720
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
922-1828 |
2.66e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 85.41 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 922 EeeeemnaelAAKKRKLEDECSELKKDIDDLELSLA-KVEKEKHATENKVKNLTEEMAGLDENITKLTKEKkiLQESHQQ 1000
Cdd:pfam02463 172 K---------EALKKLIEETENLAELIIDLEELKLQeLKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK--LNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1001 ALDDLQAEEdkvntlaKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDF 1080
Cdd:pfam02463 241 LLQELLRDE-------QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1081 ElntlnaRIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEEaggatsVQLELNK 1160
Cdd:pfam02463 314 E------KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE------LLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1161 KQEAEFQKLRRDLEEATLQHEAtaatlrKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNL 1240
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEE------EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1241 EKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKeafINQLTRGKLTYTQQLEDLKRQLEEEAKA 1320
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESK---ARSGLKVLLALIKDGVGGRIISAHGRLG 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1321 KNALAHALQSAQH--DCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEA 1398
Cdd:pfam02463 533 DLGVAVENYKVAIstAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKAT 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1399 VEAVNAKCSSLEKTKHRlqnEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEarslstelfk 1478
Cdd:pfam02463 613 LEADEDDKRAKVVEGIL---KDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ---------- 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1479 LKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQL 1558
Cdd:pfam02463 680 ELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKK 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1559 EFNQVKADyERKLAEKDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEALR-LKKKMEGDLNEMEIQLSHANRTAAEAQKQ 1637
Cdd:pfam02463 760 EEKEEEKS-ELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEeLKEEAELLEEEQLLIEQEEKIKEEELEEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1638 VKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQnts 1717
Cdd:pfam02463 839 ALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK--- 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1718 lINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKKeQDTSAHLERMKKNMEQtvkDLQLRLDEAEQ 1797
Cdd:pfam02463 916 -ENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNK-RLLLAKEELGKVNLMA---IEEFEEKEERY 990
|
890 900 910
....*....|....*....|....*....|.
gi 2163567613 1798 LALKGGKKQLQKLEVRVRELENELEAEQKRN 1828
Cdd:pfam02463 991 NKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1008-1921 |
2.73e-16 |
|
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: 85.48 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1008 EEDKVNTLAKAKvKLEQQVDDLES------SLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFE 1081
Cdd:TIGR00606 158 QEDSNWPLSEGK-ALKQKFDEIFSatryikALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1082 lNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEE----TSERLEEAGGATSVQLE 1157
Cdd:TIGR00606 237 -REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvfqgTDEQLNDLYHNHQRTVR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1158 LNKKQEAEFQK-LRRDLEEATLQHEATAATLRKKhadSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKA 1236
Cdd:TIGR00606 316 EKERELVDCQReLEKLNKERRLLNQEKTELLVEQ---GRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQI 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1237 KT-------NLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKL----QTENSELSRQLEEKEAFINQLTRGkltyTQ 1305
Cdd:TIGR00606 393 KNfhtlvieRQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLgrtiELKKEILEKKQEELKFVIKELQQL----EG 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1306 QLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAktELQRALSKANSEVAQwrTKYETDAIQRTEELEEAK 1385
Cdd:TIGR00606 469 SSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKA--DLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDK 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1386 KKLAQRL-----QEAEEAVEAVN--AKCSSLEKTKHRLQNEI---EDLMADVERSNAAAAALDKKQRNFDKILSEWKQKF 1455
Cdd:TIGR00606 545 MDKDEQIrkiksRHSDELTSLLGyfPNKKQLEDWLHSKSKEInqtRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1456 EES----------QTELEASQKEARSLSTELFKLKNAYEESLEHLETFKREN--------------KNLQEEILDLTEQL 1511
Cdd:TIGR00606 625 EDKlfdvcgsqdeESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcqrvfqteAELQEFISDLQSKL 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1512 GASQKSIHELEKVRKQLDAEKLEL--QAALEEAEASLEHEEGKILRAQLEFNQVKADYERKLAEKDEEIEQSKRNHLRVV 1589
Cdd:TIGR00606 705 RLAPDKLKSTESELKKKEKRRDEMlgLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESA 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1590 DSLQTSLDAETRSRNEALRLKKKMEGDLNEMeiQLSHANRTAAEAQKQVKalqgylkDTQLQLDDVVRANEDLKENIAIV 1669
Cdd:TIGR00606 785 KVCLTDVTIMERFQMELKDVERKIAQQAAKL--QGSDLDRTVQQVNQEKQ-------EKQHELDTVVSKIELNRKLIQDQ 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1670 ERRNNLLQSELEELRA----MVEQSERARKLAEQeLIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQecrN 1745
Cdd:TIGR00606 856 QEQIQHLKSKTNELKSeklqIGTNLQRRQQFEEQ-LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS---S 931
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1746 AEEKAKKAITDAAMMAEELKK--------EQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlalkgGKKQLQKlEVRVREL 1817
Cdd:TIGR00606 932 KETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDDYLKQKETELNTVNAQLEECEK-----HQEKINE-DMRLMRQ 1005
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1818 ENELEAEQKRNAESIKGLRKSERRVKELsyqtEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKVQHE 1897
Cdd:TIGR00606 1006 DIDTQKIQERWLQDNLTLRKRENELKEV----EEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYE 1081
|
970 980
....*....|....*....|....
gi 2163567613 1898 LDEAEERADMAESQVNKLRARSRD 1921
Cdd:TIGR00606 1082 KEIKHFKKELREPQFRDAEEKYRE 1105
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
842-1754 |
4.64e-16 |
|
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: 84.71 E-value: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 842 KEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKnDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERL 921
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 922 EEEEEMNAELAAKKRKLEDECSELKKDIDdlelslakvekekHATENKVKNLTEEMAGLDENITKLTKEKKILQESH--- 998
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKtel 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 999 --QQALDDLQAEEDKVNTLAKAKVKLEQQ----VDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLE 1072
Cdd:TIGR00606 346 lvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1073 ERLKKKDFELNTLNARIEDEQAIsaqLQKKLKELQARIEELEEELeaerTGRAKVEKLRSELLQELEETSeRLEEAGGAT 1152
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEI---LEKKQEELKFVIKELQQLE----GSSDRILELDQELRKAERELS-KAEKNSLTE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1153 SVQLELNKKQEAEFQKLRRDLEEATLQHEATAATLRKKHADSVAElsEQLDNLQRVKQKLEKEKSELKLELDDVnSNTEQ 1232
Cdd:TIGR00606 498 TLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTK--DKMDKDEQIRKIKSRHSDELTSLLGYF-PNKKQ 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1233 LIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEkeafinqlTRGKLTYTQQLEDLKR 1312
Cdd:TIGR00606 575 LEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD--------VCGSQDEESDLERLKE 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1313 QLEEEAKAKNALAHALQsaqhdcdlLREQYEEEMEAKtelqralSKANSEVAQwrtkyetDAIQRTEELEEAKKKLAQRL 1392
Cdd:TIGR00606 647 EIEKSSKQRAMLAGATA--------VYSQFITQLTDE-------NQSCCPVCQ-------RVFQTEAELQEFISDLQSKL 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1393 QEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELE---ASQKEA 1469
Cdd:TIGR00606 705 RLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGtimPEEESA 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1470 RSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQL--GASQKSIHELEKVRKQLDaeklELQAALEEAEASLE 1547
Cdd:TIGR00606 785 KVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQvnQEKQEKQHELDTVVSKIE----LNRKLIQDQQEQIQ 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1548 HEEGKILRAQLEFNQVKADYERKLAEKDEEIEQSKRnhlrvvdsLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHA 1627
Cdd:TIGR00606 861 HLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE--------VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSK 932
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1628 NRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRN-NLLQSELEELRAMVEQSERARKLAEQELIEASE 1706
Cdd:TIGR00606 933 ETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETElNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKI 1012
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 2163567613 1707 RVQLLHSQNTSLI--NQKKKMEADISQLQTEV-EEAIQECRNAEEKAKKAI 1754
Cdd:TIGR00606 1013 QERWLQDNLTLRKreNELKEVEEELKQHLKEMgQMQVLQMKQEHQKLEENI 1063
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
835-1510 |
5.49e-16 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 84.46 E-value: 5.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 835 LKSAETEKEmqtmkeefghlkealeksearRKELEEKMvsmlqekNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKV 914
Cdd:pfam01576 419 ARLSESERQ---------------------RAELAEKL-------SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 915 KEMTERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKIL 994
Cdd:pfam01576 471 QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 995 QESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLegDLKLAQESIMDLEN--DKQQLE 1072
Cdd:pfam01576 551 QRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKF--DQMLAEEKAISARYaeERDRAE 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1073 ERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLE----EA 1148
Cdd:pfam01576 629 AEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEeledEL 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1149 GGATSVQLELNKKQEAEFQKLRRDLEEATLQHEATAATLRKKHADSVAELSE---QLDNLQRVKQKLEKEKSELKLELDD 1225
Cdd:pfam01576 709 QATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDerkQRAQAVAAKKKLELDLKELEAQIDA 788
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1226 VNSNTEQLIKaktnlekmcrttedQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLT-------R 1298
Cdd:pfam01576 789 ANKGREEAVK--------------QLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQedlaaseR 854
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1299 GKLTYTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKY--ETDAIQ 1376
Cdd:pfam01576 855 ARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELaaERSTSQ 934
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1377 RTE----ELEEAKKKLAQRLQEAEEAVEavnakcSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWK 1452
Cdd:pfam01576 935 KSEsarqQLERQNKELKAKLQEMEGTVK------SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVL 1008
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 2163567613 1453 QKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQ 1510
Cdd:pfam01576 1009 LQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATES 1066
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
907-1777 |
6.35e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 84.25 E-value: 6.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 907 KIQLEAKVKEMTERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITK 986
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 987 LTKEKKILQESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDD-LESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLE 1065
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKlLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1066 NDKQQLEERLKKKDFELNTLNA-RIEDEQAISAQLQKKLKELQARIEELEEELEAER------TGRAKVEKLRSELLQEL 1138
Cdd:pfam02463 328 KELKKEKEEIEELEKELKELEIkREAEEEEEEELEKLQEKLEQLEEELLAKKKLESErlssaaKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1139 EETSERLEEAGGATSVQLELNKKQEAEFQKLRRDLEEATLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSE 1218
Cdd:pfam02463 408 QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1219 LKLELDDVNSNTEQLIKA----KTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQR-AKLQTENSELSRQLEEKEAFI 1293
Cdd:pfam02463 488 LLLSRQKLEERSQKESKArsglKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIsTAVIVEVSATADEVEERQKLV 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1294 NQLTRGKLTYTqqledlKRQLEEEAKAKNALAHALQSAqhdcdLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETD 1373
Cdd:pfam02463 568 RALTELPLGAR------KLRLLIPKLKLPLKSIAVLEI-----DPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1374 AIQRTEELEEAKKKlAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQ 1453
Cdd:pfam02463 637 LKESAKAKESGLRK-GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKL 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1454 KFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKL 1533
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1534 ELQAALEEAEASLEHEEGKILRAQLEFNQVKADYERKLAEKDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKM 1613
Cdd:pfam02463 796 LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLK 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1614 EGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDtQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERA 1693
Cdd:pfam02463 876 EEELEEQKLKDELESKEEKEKEEKKELEEESQKL-NLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN 954
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1694 RKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQEcrNAEEKAKKAITDAAMMAEELKKEQDTSAH 1773
Cdd:pfam02463 955 KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE--KKKLIRAIIEETCQRLKEFLELFVSINKG 1032
|
....
gi 2163567613 1774 LERM 1777
Cdd:pfam02463 1033 WNKV 1036
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1603-1928 |
7.79e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.83 E-value: 7.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1603 RNEALRLKKKMEGDLN-------EMEIQLSHANRTAAEAQKqVKALQGYLKDTQLQLddVVRANEDLKENIAIVERRNNL 1675
Cdd:COG1196 174 KEEAERKLEATEENLErledilgELERQLEPLERQAEKAER-YRELKEELKELEAEL--LLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1676 LQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADIS--------------QLQTEVEEAIQ 1741
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArleerrreleerleELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1742 ECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKgGKKQLQKLEVRVRELENEL 1821
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE-ALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1822 EAEQKRNAESIKGLRKSERRVKELSYQTEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKVQHELDEA 1901
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330 340
....*....|....*....|....*..
gi 2163567613 1902 EERADMAESQVNKLRARSRDIGAKKGL 1928
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKAALLL 516
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1199-1866 |
1.07e-15 |
|
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: 83.48 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1199 SEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTdLSTQRAKLQTE 1278
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE-AQEEQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1279 NSELSRQLEEKEAFINQLTRgkltyTQQLEDLKRQLEEEAKAKNALAHALQSAQhdcdllrEQYEEEMEAKTELQRALSK 1358
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVLEE-----TQERINRARKAAPLAAHIKAVTQIEQQAQ-------RIHTELQSKMRSRAKLLMK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1359 ANSEVAQwrtkyETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEiEDLMADVERSNAAAAALD 1438
Cdd:TIGR00618 330 RAAHVKQ-----QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQ-QQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1439 KKQRNFDKILSEwKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGaSQKSI 1518
Cdd:TIGR00618 404 ILQREQATIDTR-TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ-TKEQI 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1519 HELEKVRKQLDAEKLELQAALE-EAEASLEH-----------------------------EEGKILRAQL--EFNQVKAD 1566
Cdd:TIGR00618 482 HLQETRKKAVVLARLLELQEEPcPLCGSCIHpnparqdidnpgpltrrmqrgeqtyaqleTSEEDVYHQLtsERKQRASL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1567 YER---------KLAEKDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEAL----RLKKKMEGDLNEMEIQLsHANRTAAE 1633
Cdd:TIGR00618 562 KEQmqeiqqsfsILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAceqhALLRKLQPEQDLQDVRL-HLQQCSQE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1634 AQKQVKALQGYLkdTQLQLDDV----VRANEDLKENIAIVERRNNLLQSELEEL---RAMVEQSERARKLAEQELIEAS- 1705
Cdd:TIGR00618 641 LALKLTALHALQ--LTLTQERVrehaLSIRVLPKELLASRQLALQKMQSEKEQLtywKEMLAQCQTLLRELETHIEEYDr 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1706 ---ERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELkkeQDTSAHLERMKKNME 1782
Cdd:TIGR00618 719 efnEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAEL---SHLAAEIQFFNRLRE 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1783 QTVKDLQLRLDEAEQLALKGGKKQLQKLEVRVRELENeLEAEQKRNAESIKGLRKSERRVKELSYQTEEDRKNMVRLQDL 1862
Cdd:TIGR00618 796 EDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQ-FLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
....
gi 2163567613 1863 VDKL 1866
Cdd:TIGR00618 875 SDKL 878
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
832-1369 |
1.39e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.80 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 832 KPLLKSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLqlqvQAEQDNLADAEERCDQLIKNKIQLE 911
Cdd:PRK03918 183 KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL----EELKEEIEELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 912 AKVKEMTERLEEEEEMNAELAAKKRKLE------DECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENIT 985
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 986 KLTKEKKILQEshqqALDDLQAEEDKVNTLAKAKVKLEQ--QVDDLESSLEQEKKIRM--DLERAKRKLEGDLKLAQESI 1061
Cdd:PRK03918 339 RLEELKKKLKE----LEKRLEELEERHELYEEAKAKKEEleRLKKRLTGLTPEKLEKEleELEKAKEEIEEEISKITARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1062 MDLENDKQQLE---ERLKKKDFELNTLNARI--EDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRS---- 1132
Cdd:PRK03918 415 GELKKEIKELKkaiEELKKAKGKCPVCGRELteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkese 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1133 -----ELLQELEETSERLEEaggatsVQLELNKKQEAEFQKLRRDLEEATLQHEATAATLRKKHA--DSVAELSEQLDNL 1205
Cdd:PRK03918 495 liklkELAEQLKELEEKLKK------YNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkKKLAELEKKLDEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1206 QRVKQKLEKEKSELKLE-LDDVNSNTEQLIKAKTNLEKMcRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSR 1284
Cdd:PRK03918 569 EEELAELLKELEELGFEsVEELEERLKELEPFYNEYLEL-KDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1285 QLEEKEAFINQLTRGKLtyTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRaLSKANSEVA 1364
Cdd:PRK03918 648 ELEELEKKYSEEEYEEL--REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVE 724
|
....*
gi 2163567613 1365 QWRTK 1369
Cdd:PRK03918 725 ELREK 729
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1409-1918 |
1.92e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 82.86 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1409 LEKTKHRLQNEIEDLMADVERSNAaaaaLDKKQRNF-DKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESL 1487
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNE----LHEKQKFYlRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1488 EHLETfkreNKNLQEEILDlteqlgASQKSIHELEKVRKQLDAEKLELQAAL---EEAEASLEHEEGKIlrAQLEFNQVK 1564
Cdd:pfam15921 152 HELEA----AKCLKEDMLE------DSNTQIEQLRKMMLSHEGVLQEIRSILvdfEEASGKKIYEHDSM--STMHFRSLG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1565 ADYERKLAEKDEEIEQSKRNHLRVVDSLQTsLDAETRSRNEAL--RLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQ 1642
Cdd:pfam15921 220 SAISKILRELDTEISYLKGRIFPVEDQLEA-LKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1643 GYLKDTQLQLDDvvrANEDLKENIAIVERRNNLLQSELEELRAM----VEQSERARKLAEQELIEAservqllhsqntsl 1718
Cdd:pfam15921 299 SQLEIIQEQARN---QNSMYMRQLSDLESTVSQLRSELREAKRMyedkIEELEKQLVLANSELTEA-------------- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1719 inqkkkmeadisqlQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQl 1798
Cdd:pfam15921 362 --------------RTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1799 alkggkkQLQKLEVRVRELENELEAEQKRNAESIKGLRKSERRVKELSYQTEEDRKnmvRLQDLVDKLqlkvkAYKRQAE 1878
Cdd:pfam15921 427 -------EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE---MLRKVVEEL-----TAKKMTL 491
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2163567613 1879 EAEEQANSNLAKfrkvqhELDEAEERADMAESQVNKLRAR 1918
Cdd:pfam15921 492 ESSERTVSDLTA------SLQEKERAIEATNAEITKLRSR 525
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1164-1866 |
2.41e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 82.27 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1164 AEFQKLRRdLEEATLQHEATAATLR--KKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELddvnsnteqLIKAKTNLE 1241
Cdd:COG4913 232 EHFDDLER-AHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALRLWFAQRRLEL---------LEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1242 KMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTEN-SELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKA 1320
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1321 KNALAHALQSAQHDCDLLREQYEEemeAKTELQRALSKANSEVAQWRTkyETDAIQRT-----EELEEAKKKLAQRLQEA 1395
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEA--EIASLERRksnipARLLALRDALAEALGLD 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1396 EEAVEAVnakCSSLE-KTKHRL-QNEIE--------DLMADVERSNAAAAALDK---KQR-NFDKIlsewkqkfEESQTE 1461
Cdd:COG4913 457 EAELPFV---GELIEvRPEEERwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1462 LEASQKEARSLSTELFKLKNAYEESLEHL-------------ETFKRENKNL---------------------------- 1500
Cdd:COG4913 526 PERPRLDPDSLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRAItragqvkgngtrhekddrrrirsryvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1501 ---QEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLEfnqvkadyeRKLAEKDEE 1577
Cdd:COG4913 606 fdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE---------REIAELEAE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1578 IEQskrnhlrvvdslqtsLDAETrsrnealrlkkkmeGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVR 1657
Cdd:COG4913 677 LER---------------LDASS--------------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1658 ANEDLKENI-AIVERRNNLLQSELEELRAMVEQSERARKLAEQelieaservqllhsqntsLINQKKKMEADISQLQTEV 1736
Cdd:COG4913 728 ELDELQDRLeAAEDLARLELRALLEERFAAALGDAVERELREN------------------LEERIDALRARLNRAEEEL 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1737 EEAIQE-CRNAEEKAKKAITDAAMMAEELK-----KEQDTSAHLERMK----KNMEQTVKDLQLRLDEAEQLAlkggKKQ 1806
Cdd:COG4913 790 ERAMRAfNREWPAETADLDADLESLPEYLAlldrlEEDGLPEYEERFKellnENSIEFVADLLSKLRRAIREI----KER 865
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163567613 1807 LQKLEvrvRELEN---------ELEAEQKRNAEsIKGLRKSERRVKELSYQTEED--RKNMVRLQDLVDKL 1866
Cdd:COG4913 866 IDPLN---DSLKRipfgpgrylRLEARPRPDPE-VREFRQELRAVTSGASLFDEElsEARFAALKRLIERL 932
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
839-1797 |
3.25e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.11 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 839 ETEKEMQTMKEEFGHLKEAlEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQdnladAEErcdqliKNKIQLEAKVKEMT 918
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEA-KKTETGKAEEARKAEEAKKKAEDARKAEEARK-----AED------ARKAEEARKAEDAK 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 919 ERLEEEEEMNAELAAKKRKLEDEcselkkdiddlelslAKVEKEKHATENKVKnlteemagldENITKLTKEKKIlqESH 998
Cdd:PTZ00121 1153 RVEIARKAEDARKAEEARKAEDA---------------KKAEAARKAEEVRKA----------EELRKAEDARKA--EAA 1205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 999 QQALDDLQAEEDKvntlakakvkleqqvddlesSLEQEKKIRmdlerakrklegDLKLAQESIMDLENDKQQLEERLKK- 1077
Cdd:PTZ00121 1206 RKAEEERKAEEAR--------------------KAEDAKKAE------------AVKKAEEAKKDAEEAKKAEEERNNEe 1253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1078 -KDFELNTLNARIEDEQAISAQLQKKLKELQarieeleeeleAERTGRAKVEKLRSELLQELEETSERLEEAGGATsvql 1156
Cdd:PTZ00121 1254 iRKFEEARMAHFARRQAAIKAEEARKADELK-----------KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD---- 1318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1157 ELNKKQEAEFQK---LRRDLEEATLQHEATAATLRKKhadsvaelSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQL 1233
Cdd:PTZ00121 1319 EAKKKAEEAKKKadaAKKKAEEAKKAAEAAKAEAEAA--------ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1234 IKAKtnlEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKeafinqltrgkltytQQLEDLKRQ 1313
Cdd:PTZ00121 1391 KKAD---EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA---------------KKADEAKKK 1452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1314 LEEEAKAKNALAHALQSAQhdCDLLREQYEEEMEAKtELQRALSKANSEVAQWRTKYEtdAIQRTEELEEA-KKKLAQRL 1392
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKK--ADEAKKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAE--AKKKADEAKKAeEAKKADEA 1527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1393 QEAEEAVEAVNAKcSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTEleasqkEARSL 1472
Cdd:PTZ00121 1528 KKAEEAKKADEAK-KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE------EVMKL 1600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1473 STELFKLKnAYEESLEHLETFKRENKNLQEEILDLTEQLGASQ-KSIHELEKVRKQldAEKLELQAALEEAEASLEHEEG 1551
Cdd:PTZ00121 1601 YEEEKKMK-AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEaEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKA 1677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1552 KILRAQLEFNQVKADYERKLAEKDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKMEGDlnemeiqlshaNRTA 1631
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED-----------KKKA 1746
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1632 AEAQKQVKALQgylKDTQLQLDDVVRANEDLKENIAIVErrnnllqselEELRAMVEQSERARKLAEQELIEASERVQLL 1711
Cdd:PTZ00121 1747 EEAKKDEEEKK---KIAHLKKEEEKKAEEIRKEKEAVIE----------EELDEEDEKRRMEVDKKIKDIFDNFANIIEG 1813
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1712 HSQNTSLINQKKKMEadISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAH---LERMKKNMEQTVKDL 1788
Cdd:PTZ00121 1814 GKEGNLVINDSKEME--DSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEkdlKEDDEEEIEEADEIE 1891
|
....*....
gi 2163567613 1789 QLRLDEAEQ 1797
Cdd:PTZ00121 1892 KIDKDDIER 1900
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
835-1522 |
9.48e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 80.55 E-value: 9.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 835 LKSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNladAEERCDQLIKNKIQLEAKV 914
Cdd:pfam15921 250 LKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTV 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 915 KEmterleeeeeMNAELAAKKRKLEDECSELKKDI--DDLELSLAKVEKEKHATENKvkNLTEEMAGLDENITKLTKEKK 992
Cdd:pfam15921 327 SQ----------LRSELREAKRMYEDKIEELEKQLvlANSELTEARTERDQFSQESG--NLDDQLQKLLADLHKREKELS 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 993 ILQESHQQ-----------------ALDDLQAEEDKVNTLAKA-----KVKLEQQVDDLE---SSLEQEKKIRMDLERAK 1047
Cdd:pfam15921 395 LEKEQNKRlwdrdtgnsitidhlrrELDDRNMEVQRLEALLKAmksecQGQMERQMAAIQgknESLEKVSSLTAQLESTK 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1048 RKLEGDLKLAQESIMDLENDKQ---QLEERLKKKDFELNTLNARIedeQAISAQLQKKLKELQarieELEEELEAERTGR 1124
Cdd:pfam15921 475 EMLRKVVEELTAKKMTLESSERtvsDLTASLQEKERAIEATNAEI---TKLRSRVDLKLQELQ----HLKNEGDHLRNVQ 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1125 AKVEKLR---------SELLQELEETSERLEEAGGATSVQLELNKKQ-EAEFQKLRRDLEEATLQHEATAATLRKKHAdS 1194
Cdd:pfam15921 548 TECEALKlqmaekdkvIEILRQQIENMTQLVGQHGRTAGAMQVEKAQlEKEINDRRLELQEFKILKDKKDAKIRELEA-R 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1195 VAEL-----------SEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNL----EKMCRTTED---QMNEHRS 1256
Cdd:pfam15921 627 VSDLelekvklvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFrnksEEMETTTNKlkmQLKSAQS 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1257 KLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLtRGKLTYTQQ-----------LEDLKRQLEEE----AKAK 1321
Cdd:pfam15921 707 ELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDAL-QSKIQFLEEamtnankekhfLKEEKNKLSQElstvATEK 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1322 NALAHALQsaqhdcdLLREQYEEEMEAKTELQRALSKANSEVAQWRtkyetDAIQRTEElEEAKKKLAQRLQEAE----- 1396
Cdd:pfam15921 786 NKMAGELE-------VLRSQERRLKEKVANMEVALDKASLQFAECQ-----DIIQRQEQ-ESVRLKLQHTLDVKElqgpg 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1397 ----EAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTeLEASQKEARSL 1472
Cdd:pfam15921 853 ytsnSSMKPRLLQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPT-VQLSKAEDKGR 931
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 2163567613 1473 STELFKLKNAYEESLEHLE----TFKRENKNLQEEILDLTEQLGASQKSIHELE 1522
Cdd:pfam15921 932 APSLGALDDRVRDCIIESSlrsdICHSSSNSLQTEGSKSSETCSREPVLLHAGE 985
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
841-1550 |
1.59e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.34 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 841 EKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEkndlqlqvqaeqdnLADAEERCDQLIKNKIQLEAKVkemter 920
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKE--------------LEEVLREINEISSELPELREEL------ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 921 leeeeemnAELAAKKRKLEdecsELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQESHQQ 1000
Cdd:PRK03918 224 --------EKLEKEVKELE----ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1001 ALDDLQAEEDKVNTLaKAKVKLEQQVDDLES---SLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKK 1077
Cdd:PRK03918 292 AEEYIKLSEFYEEYL-DELREIEKRLSRLEEeinGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAK 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1078 KDfELNTLNARIEDEQAisAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEEtserLEEAGGATSVqle 1157
Cdd:PRK03918 371 KE-ELERLKKRLTGLTP--EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE----LKKAKGKCPV--- 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1158 lnkkqeaefqkLRRDLEEatlqhEATAATLRKKHadsvAELSEQLDNLQRVKQKLEKEKSELKlELDDVNSNTEQLIKAK 1237
Cdd:PRK03918 441 -----------CGRELTE-----EHRKELLEEYT----AELKRIEKELKEIEEKERKLRKELR-ELEKVLKKESELIKLK 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1238 TNLEKMcRTTEDQMNEHR-SKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTrgkltytqQLEDLKRQLEE 1316
Cdd:PRK03918 500 ELAEQL-KELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA--------ELEKKLDELEE 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1317 EAKaknalahalqsaqhdcDLLREQYEEEMEAKTELQRalskansevaqwrtkyetdaiqRTEELEEAKKKLaqrlqeae 1396
Cdd:PRK03918 571 ELA----------------ELLKELEELGFESVEELEE----------------------RLKELEPFYNEY-------- 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1397 eaVEAVNAkcsslEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFeeSQTELEASQKEARSLSTEL 1476
Cdd:PRK03918 605 --LELKDA-----EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEELREEYLELSREL 675
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163567613 1477 FKLKNAYEESLEHLETFKRENKNLQEEIldltEQLGASQKSIHELEKVRKQLDA--EKLELQAALEEAEASLEHEE 1550
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEEL----EEREKAKKELEKLEKALERVEElrEKVKKYKALLKERALSKVGE 747
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1303-1900 |
2.03e-14 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 79.39 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1303 YTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVaqwrtkyeTDAIQRT-EEL 1381
Cdd:pfam15921 83 YSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL--------RNQLQNTvHEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1382 EEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHrlqnEIEDLMADVERSNAaaaaldKKQRNFDKILSewkQKFEESQTe 1461
Cdd:pfam15921 155 EAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ----EIRSILVDFEEASG------KKIYEHDSMST---MHFRSLGS- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1462 leASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEIL----DLTEQLgasqKSIHELE---------KVRKQL 1528
Cdd:pfam15921 221 --AISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLqqhqDRIEQL----ISEHEVEitgltekasSARSQA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1529 DAEKLELQAALEEAE-------ASLEHEEGKILRAQLEFNQVKADYERKLAEKDEEI--------------EQSKRNHLR 1587
Cdd:pfam15921 295 NSIQSQLEIIQEQARnqnsmymRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanseltearterDQFSQESGN 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1588 VVDSLQTSLdAETRSRNEALRLKKKMEGDLNEME----IQLSHANRTAAEAQKQVKALQGYLK----DTQLQLDDVVRAN 1659
Cdd:pfam15921 375 LDDQLQKLL-ADLHKREKELSLEKEQNKRLWDRDtgnsITIDHLRRELDDRNMEVQRLEALLKamksECQGQMERQMAAI 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1660 EDLKENIAIVERRNNLLQSELEELRAMVEQSErarklAEQELIEASERVqlLHSQNTSLINQKKKMEA---DISQLQTEV 1736
Cdd:pfam15921 454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELT-----AKKMTLESSERT--VSDLTASLQEKERAIEAtnaEITKLRSRV 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1737 EEAIQEC---RNAEEKAKKAITDAA----MMAEELKKEQDTSAHLERM-----------------KKNMEQTVKDLQLRL 1792
Cdd:pfam15921 527 DLKLQELqhlKNEGDHLRNVQTECEalklQMAEKDKVIEILRQQIENMtqlvgqhgrtagamqveKAQLEKEINDRRLEL 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1793 DEAEQLALKGGKKqLQKLEVRVRELENELEAEQKRNAESIKGLRKSERRVKELSYQTEEDRKNmvrLQDLVDKLQLKVKA 1872
Cdd:pfam15921 607 QEFKILKDKKDAK-IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNE---LNSLSEDYEVLKRN 682
|
650 660
....*....|....*....|....*...
gi 2163567613 1873 YKRQAEEAEEQANSNLAKFRKVQHELDE 1900
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1340-1917 |
3.39e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.54 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1340 EQYEEEMEAK--TELQRALSKANSEVAqwrtkyETDAIqrTEELEEAKKKLAQRLQEAEEAVEAVNAKcsslektkhrlQ 1417
Cdd:PRK02224 190 DQLKAQIEEKeeKDLHERLNGLESELA------ELDEE--IERYEEQREQARETRDEADEVLEEHEER-----------R 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1418 NEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEArslstelfKLKNAYEESLE-HLETFKRE 1496
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA--------GLDDADAEAVEaRREELEDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1497 NKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKIlraqlefnqvkADYERKLAEKDE 1576
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV-----------EDRREEIEELEE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1577 EIEQskrNHLRVVDSLQTSLDAETRsRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVV 1656
Cdd:PRK02224 392 EIEE---LRERFGDAPVDLGNAEDF-LEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHV 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1657 RANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQ--ELIEASERVQLLHSQNTSLINQKkkmEADISQLQT 1734
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRieRLEERREDLEELIAERRETIEEK---RERAEELRE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1735 EVEEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEqTVKDLQLRLDEAEQlalkggkkqlqklevRV 1814
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAED---------------EI 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1815 RELENELEAEQKRNAESIKGLRKSERRVKELSYQTEEDRknmvrlqdlVDKLQLKvkayKRQAEEAEEQANSNLAKFRKv 1894
Cdd:PRK02224 609 ERLREKREALAELNDERRERLAEKRERKRELEAEFDEAR---------IEEARED----KERAEEYLEQVEEKLDELRE- 674
|
570 580
....*....|....*....|...
gi 2163567613 1895 qhELDEAEERADMAESQVNKLRA 1917
Cdd:PRK02224 675 --ERDDLQAEIGAVENELEELEE 695
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1193-1742 |
4.65e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.03 E-value: 4.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1193 DSVAELSEQLDNLQRVKQKLEKEKSELKLeLDDVNSNTEQLIKAKTNLEKmCRTTEDQMN--EHRSKLEEAQRTVTDLST 1270
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERYAAARERLAE-LEYLRAALRlwFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1271 QRAKLQTENSELSRQLEEKEAFINQLTRGKLTY-TQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAK 1349
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1350 TELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQE-----------AEEAVEAVNAKCSSLEKTKHRL-- 1416
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiaslerrksniPARLLALRDALAEALGLDEAELpf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1417 --------------QNEIE--------DLMADVERSNAAAAALDK---KQR-NFDKIlsewkqkfEESQTELEASQKEAR 1470
Cdd:COG4913 463 vgelievrpeeerwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1471 SLSTELFKLKNAYEESLEHL-------------ETFKRENKNL-------------------------------QEEILD 1506
Cdd:COG4913 535 SLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRAItragqvkgngtrhekddrrrirsryvlgfdnRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1507 LTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLefnqvkadyERKLAEKDEEIEQSKRNHL 1586
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA---------EREIAELEAELERLDASSD 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1587 RV------VDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQ--LDDVVRA 1658
Cdd:COG4913 686 DLaaleeqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAaaLGDAVER 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1659 N--EDLKENIAIVERRNNLLQSELEELR-------------------AMVEQSERARKLAEQELIEASER-VQLLHSQnt 1716
Cdd:COG4913 766 ElrENLEERIDALRARLNRAEEELERAMrafnrewpaetadldadleSLPEYLALLDRLEEDGLPEYEERfKELLNEN-- 843
|
650 660
....*....|....*....|....*.
gi 2163567613 1717 slinqkkkMEADISQLQTEVEEAIQE 1742
Cdd:COG4913 844 --------SIEFVADLLSKLRRAIRE 861
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
899-1615 |
8.82e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 77.32 E-value: 8.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 899 RCDQLIKNKIQLEAKVKEMTERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHAT----ENKVKNLT 974
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERkqvlEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 975 EEMAGLDENITKLTKEKKILQE--SHQQALDDLQAEEDKVNT----LAKAKVKLEQQVDDLESSLEQEK--KIRMDLERA 1046
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEqlKKQQLLKQLRARIEELRAqeavLEETQERINRARKAAPLAAHIKAvtQIEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1047 KRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQA------ISAQLQKKLKELQ---ARIEELEEEL 1117
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAhevatsIREISCQQHTLTQhihTLQQQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1118 EAERTGRAKVEKLRSELLQELEETSERLEEAGgatsvQLELNKKQEaEFQKLRRDLEEATLQHEATAATLRKKHADSVA- 1196
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATIDTRTSAFRDLQG-----QLAHAKKQQ-ELQQRYAELCAAAITCTAQCEKLEKIHLQESAq 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1197 ---ELSEQLDNLQRVKQKlEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRA 1273
Cdd:TIGR00618 467 slkEREQQLQTKEQIHLQ-ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1274 KLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHALQsaqhdcdllrEQYEEEMEAKTELQ 1353
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE----------KLSEAEDMLACEQH 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1354 RALSKANSEVAQWRTKYETDAIQRTEELEE-AKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHR------LQNEIEDLMAD 1426
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRLHLQQCSQELALKLtALHALQLTLTQERVREHALSIRVLPKELLASRqlalqkMQSEKEQLTYW 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1427 VE---RSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEAsqkEARSLSTELFKLKNAYEESLEHLeTFKRENKNLQEE 1503
Cdd:TIGR00618 696 KEmlaQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA---REDALNQSLKELMHQARTVLKAR-TEAHFNNNEEVT 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1504 ILDLTEQlgASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLEFNQVKADYERKLAEKDEEIEQSKR 1583
Cdd:TIGR00618 772 AALQTGA--ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITH 849
|
730 740 750
....*....|....*....|....*....|..
gi 2163567613 1584 NHLRVVDSLQtSLDAETRSRNEALRLKKKMEG 1615
Cdd:TIGR00618 850 QLLKYEECSK-QLAQLTQEQAKIIQLSDKLNG 880
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1511-1867 |
1.91e-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: 76.25 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1511 LGASQKSIHELEKVRKQLDAEKLELQAALEEAeasleheeGKILRaqleFNQVKADYERKLAEKDEEIEQSKRNhLRVVD 1590
Cdd:TIGR02168 133 LGKRSYSIIEQGKISEIIEAKPEERRAIFEEA--------AGISK----YKERRKETERKLERTRENLDRLEDI-LNELE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1591 SLQTSLDAETRSRNEALRLKKKME--------GDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDL 1662
Cdd:TIGR02168 200 RQLKSLERQAEKAERYKELKAELRelelallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1663 KENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVE---EA 1739
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELEsleAE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1740 IQECRNAEEKAKKAITD--------AAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQLQKLE 1811
Cdd:TIGR02168 360 LEELEAELEELESRLEEleeqletlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2163567613 1812 VRVRELENELEAEQKRNAESIKGLRKSERRVKELSYQTEEDRKNMVRLQDLVDKLQ 1867
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1367-1904 |
2.08e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.87 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1367 RTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAA---AAALDKKQRN 1443
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELekeLESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1444 FDKILSEWKQKFEESQTELEASQKEARSLsTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEK 1523
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1524 VR---KQLDAEKLELQAALEEAEASLE-HEEGKILRAQLE-FNQVKADYE-RKLAEKDEEIEQSK---RNHLRVVDSLQT 1594
Cdd:PRK03918 336 KEerlEELKKKLKELEKRLEELEERHElYEEAKAKKEELErLKKRLTGLTpEKLEKELEELEKAKeeiEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1595 SLDAETRSRNEALRLKKKMEGD--LNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVvRANEDLKENIAIVERR 1672
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKL-RKELRELEKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1673 NNLLQSELEELRamvEQSERARKLAEQELIEASERVQLLHSQNTslinqkkKMEADISQLQTEVEEaIQECRNAEEKAKK 1752
Cdd:PRK03918 495 LIKLKELAEQLK---ELEEKLKKYNLEELEKKAEEYEKLKEKLI-------KLKGEIKSLKKELEK-LEELKKKLAELEK 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1753 AITDAAMMAEELKKEqdtsahlerMKKNMEQTVKDLQLRLDEAEQ-----LALKGGKKQLQKLEVRVRELENELEAEQKR 1827
Cdd:PRK03918 564 KLDELEEELAELLKE---------LEELGFESVEELEERLKELEPfyneyLELKDAEKELEREEKELKKLEEELDKAFEE 634
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2163567613 1828 NAESIKGLRKSERRVKELSYQ-TEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKVQHELDEAEER 1904
Cdd:PRK03918 635 LAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1565-1924 |
2.67e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.87 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1565 ADYERKLAEKDEEIEQSKRNHLR---VVDSLQTSLDAETRSRNEALR----LKKKMEGDLNEMEIQLSHANRTAAEAQKQ 1637
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1638 VKALQGYLKDTQLQLDD----VVRANEDLKENIAIVER----RNNLLQSELEELRAMVEQSERARKLAEQELIEASERVQ 1709
Cdd:TIGR02169 246 LASLEEELEKLTEEISElekrLEEIEQLLEELNKKIKDlgeeEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1710 LLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQ 1789
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1790 LRLDEAEQLalkggkkqLQKLEVRVRELENELEAEQKRNAESikglrksERRVKELSYQTEEDRKNMVRLQDLVDKLQLK 1869
Cdd:TIGR02169 406 RELDRLQEE--------LQRLSEELADLNAAIAGIEAKINEL-------EEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2163567613 1870 VKAYKRQAEEAEEqansnlaKFRKVQHELDEAEERADMAESQVNKLRARSRDIGA 1924
Cdd:TIGR02169 471 LYDLKEEYDRVEK-------ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
830-1322 |
4.24e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 74.67 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 830 KIKPLLKSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQ 909
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 910 LEAKVKEMTERLEEEEEMNA---ELAAKKRKLEDECSELKKDIDDLELSLAKVE---------------------KEKHA 965
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSLESqisELKKQNNQLKDNIEKKQQEINEKTTEISNTQtqlnqlkdeqnkikkqlsekqKELEQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 966 TENKVKNLTEEMAGLDENITKLTKEKKilQESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLER 1045
Cdd:TIGR04523 279 NNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1046 AKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRA 1125
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1126 KVEKLRSELLQELEETSERLEEAGGATSVQLELNKKQEAEFQKLRRDLEEATLQHEATAATL------RKKHADSVAELS 1199
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkklneeKKELEEKVKDLT 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1200 EQLDNLQRVKQKLEKEKSELKLELDDVNSNteqLIKAKTNLEKMCRTTE-DQMNEHRSKLEEAQRtvtdlstqraKLQTE 1278
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDE---LNKDDFELKKENLEKEiDEKNKEIEELKQTQK----------SLKKK 583
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2163567613 1279 NSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLeEEAKAKN 1322
Cdd:TIGR04523 584 QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL-EKAKKEN 626
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
825-1582 |
6.83e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 74.24 E-value: 6.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 825 MKLYFKIKPLLKSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLI 904
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 905 KNKIQLEAKvkemterleeeeemnaelaAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENI 984
Cdd:pfam02463 312 DEEKLKESE-------------------KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 985 TKLTKEKKILQESHQQALDDLQAEEDKVNTLAKAKVKLeqqvDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDL 1064
Cdd:pfam02463 373 EELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLL----LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1065 ENDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSER 1144
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAH 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1145 LEEAGGATSVQLELNKKQEAEFqklrrdleeatlqhEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELD 1224
Cdd:pfam02463 529 GRLGDLGVAVENYKVAISTAVI--------------VEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSI 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1225 DVNSNTEQLIKAKTNLEKMCRTTEDQMN----EHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGK 1300
Cdd:pfam02463 595 AVLEIDPILNLAQLDKATLEADEDDKRAkvveGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1301 LTYTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQ---- 1376
Cdd:pfam02463 675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEeeek 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1377 -RTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTK-HRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQK 1454
Cdd:pfam02463 755 sRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKeEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1455 FEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLE 1534
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 2163567613 1535 LQAALEEAEASLEHEEGKILRAQLEFNQVKADYERKLAEKDEEIEQSK 1582
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERN 962
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1033-1755 |
7.20e-13 |
|
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: 74.23 E-value: 7.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1033 LEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEE 1112
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1113 LEEELEAERTGRAKVEKLRSElLQELEETSERLEEAGGATSVQLELNKKQEAEFQklrRDLEEATLQHEATAATLRKKHA 1192
Cdd:TIGR00618 255 QLKKQQLLKQLRARIEELRAQ-EAVLEETQERINRARKAAPLAAHIKAVTQIEQQ---AQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1193 DSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCR------TTEDQMNEHRSKLEEAQRTVT 1266
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTlqqqktTLTQKLQSLCKELDILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1267 DLSTQRAKLQTENSELSR-----QLEEKEAFINQLTRGKLTYTQQLEdlKRQLEEEAKAKNALAHALQSAQHDCDLLREQ 1341
Cdd:TIGR00618 411 TIDTRTSAFRDLQGQLAHakkqqELQQRYAELCAAAITCTAQCEKLE--KIHLQESAQSLKEREQQLQTKEQIHLQETRK 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1342 YEEEMEAKTELQ---RALSKANSEVAQWRTkyetdAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQN 1418
Cdd:TIGR00618 489 KAVVLARLLELQeepCPLCGSCIHPNPARQ-----DIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1419 EIE----DLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEEslehletfK 1494
Cdd:TIGR00618 564 QMQeiqqSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHL--------Q 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1495 RENKNLQEEILDLT-EQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLEFNQVKADYERKLAE 1573
Cdd:TIGR00618 636 QCSQELALKLTALHaLQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1574 KDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKmegdlnemeiQLSHanRTAAEAQKQVKALQGYLKDTQLQld 1653
Cdd:TIGR00618 716 YDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART----------VLKA--RTEAHFNNNEEVTAALQTGAELS-- 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1654 dvvraneDLKENIaivERRNNLLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQ 1733
Cdd:TIGR00618 782 -------HLAAEI---QFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
730 740
....*....|....*....|..
gi 2163567613 1734 TEVEEAIQECRNAEEKAKKAIT 1755
Cdd:TIGR00618 852 LKYEECSKQLAQLTQEQAKIIQ 873
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
838-1579 |
2.51e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 72.70 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 838 AETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEM 917
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 918 TERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTE--EMAGLDENITKLTKEKKILQ 995
Cdd:pfam02463 355 EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLElaRQLEDLLKEEKKEELEILEE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 996 ESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERL 1075
Cdd:pfam02463 435 EEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1076 KKKDFELNTLNAriEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEEAGGATSVQ 1155
Cdd:pfam02463 515 LIKDGVGGRIIS--AHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLK 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1156 LELNKKQEAEFQKLRRDLEEATLQHEATAATLRKKHADSVAELSEQlDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIK 1235
Cdd:pfam02463 593 SIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLK-ESAKAKESGLRKGVSLEEGLAEKSEVKASLSEL 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1236 AKTNLEKMCRTTEDQMNEHRSKLEEAQRTvTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLE 1315
Cdd:pfam02463 672 TKELLEIQELQEKAESELAKEEILRRQLE-IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEE 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1316 EEAKAKNALAHALQSAQHdcdllreqyEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEA 1395
Cdd:pfam02463 751 EEEKSRLKKEEKEEEKSE---------LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQ 821
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1396 EEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSN----AAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEARS 1471
Cdd:pfam02463 822 LLIEQEEKIKEEELEELALELKEEQKLEKLAEEELErleeEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKE 901
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1472 LSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEG 1551
Cdd:pfam02463 902 LEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
|
730 740
....*....|....*....|....*...
gi 2163567613 1552 KILRAQLEFNQVKADYERKLAEKDEEIE 1579
Cdd:pfam02463 982 EFEEKEERYNKDELEKERLEEEKKKLIR 1009
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1286-1893 |
3.25e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.26 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1286 LEEKEAF--INQLtrgkLTYTQQLEDLKRQLEEEAKAKNALAHALQSAQhdcdllreQYEEEMEAKTELQRALSKANSEV 1363
Cdd:COG4913 218 LEEPDTFeaADAL----VEHFDDLERAHEALEDAREQIELLEPIRELAE--------RYAAARERLAELEYLRAALRLWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1364 AQwrTKYETdAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTkhRLQN---EIEDLMADVERSNAAAAALDKK 1440
Cdd:COG4913 286 AQ--RRLEL-LEAELEELRAELARLEAELERLEARLDALREELDELEAQ--IRGNggdRLEQLEREIERLERELEERERR 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1441 QRNFDKILSEWKQKFEESQTELEASQKEAR----SLSTELFKLKNAYEESLEHLETFKRENKNLQEEIldltEQLGASQK 1516
Cdd:COG4913 361 RARLEALLAALGLPLPASAEEFAALRAEAAalleALEEELEALEEALAEAEAALRDLRRELRELEAEI----ASLERRKS 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1517 SI-HELEKVRKQLdAEKL-----ELQAALEEAEASLEHEE-----GKILRAQ----LefnqVKADYERKLAEKdeeIEqs 1581
Cdd:COG4913 437 NIpARLLALRDAL-AEALgldeaELPFVGELIEVRPEEERwrgaiERVLGGFaltlL----VPPEHYAAALRW---VN-- 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1582 kRNHLR---VVDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSH--ANR-------TAAEAQKQVKAL----QGYL 1645
Cdd:COG4913 507 -RLHLRgrlVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAelGRRfdyvcvdSPEELRRHPRAItragQVKG 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1646 KDTQLQLDDVVRANEDL------KENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQELiEASERVQLLHSQntsli 1719
Cdd:COG4913 586 NGTRHEKDDRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWD----- 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1720 nqkkkmEADISQLQTEVEEAIQEcRNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTVKDLQLRLDEAEQla 1799
Cdd:COG4913 660 ------EIDVASAEREIAELEAE-LERLDASSDDLAALEEQLEELEAELEE---LEEELDELKGEIGRLEKELEQAEE-- 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1800 lkggkkQLQKLEVRVRELENELEAEQKRNAEsikglrksERRVKELSYQTEedrknmvrlQDLVDKLQLKVKAYKRQAEE 1879
Cdd:COG4913 728 ------ELDELQDRLEAAEDLARLELRALLE--------ERFAAALGDAVE---------RELRENLEERIDALRARLNR 784
|
650
....*....|....
gi 2163567613 1880 AEEQANSNLAKFRK 1893
Cdd:COG4913 785 AEEELERAMRAFNR 798
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1126-1833 |
5.44e-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: 71.29 E-value: 5.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1126 KVEKLRSELLQELEETSERLEEAGGATSVQLELNKKQEAEFQKLRRDLEEAtLQHEATAATLRKKHADSVAELSEQLDNL 1205
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEE-IQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1206 QRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQMN---------------EHRSKLEEAQRTVTDLST 1270
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfklkedhekiqhleeEYKKEINDKEKQVSLLLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1271 QRAKLQTENSELSRQLEEKEAFINQL--------------TRGKLTYTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCD 1336
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLeektklqdenlkelIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTIC 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1337 LLREQYEEEMEaktELQRALSKANSEVAQWRTKyetdaiqrTEELEEAKKKLAQRLQEAEEAVEAV----NAKCSSLEKT 1412
Cdd:pfam05483 328 QLTEEKEAQME---ELNKAKAAHSFVVTEFEAT--------TCSLEELLRTEQQRLEKNEDQLKIItmelQKKSSELEEM 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1413 KhRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLET 1492
Cdd:pfam05483 397 T-KFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVED 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1493 FKREnknlqeeildlteqlgasqksihelekvrkqLDAEKLElqaaleeaEASLEHEEGKILRAQLEFNQVKADYERKLA 1572
Cdd:pfam05483 476 LKTE-------------------------------LEKEKLK--------NIELTAHCDKLLLENKELTQEASDMTLELK 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1573 EKDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQL 1652
Cdd:pfam05483 517 KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1653 DDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKK----KMEAD 1728
Cdd:pfam05483 597 NNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKiseeKLLEE 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1729 ISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHlER-----MKKNMEQTVKDLQLRLdEAEQLALKGG 1803
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIE-ERdselgLYKNKEQEQSSAKAAL-EIELSNIKAE 754
|
730 740 750
....*....|....*....|....*....|
gi 2163567613 1804 KKQLQKLEVRVRELENELEAEQKRNAESIK 1833
Cdd:pfam05483 755 LLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
825-1765 |
5.58e-12 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 71.62 E-value: 5.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 825 MKLYFKIKPLLKsaeTEKEMQTMKEEFGHLKE-ALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQ- 902
Cdd:TIGR00606 265 MKLDNEIKALKS---RKKQMEKDNSELELKMEkVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQe 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 903 -----LIKNKIQLEAKVKEMTERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEM 977
Cdd:TIGR00606 342 ktellVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 978 AGLDENITKLTKEKKILQESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLA 1057
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKK 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1058 QEsiMDLENDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQaRIEELEEELEAERTGRA-------KVEKL 1130
Cdd:TIGR00606 502 EV--KSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDE-QIRKIKSRHSDELTSLLgyfpnkkQLEDW 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1131 RSELLQELEETSERLEEaggatsVQLELNKKQEAEFQkLRRDLEEATLQHEATAATLRKkhADSVAELSEQLDNLQRVKQ 1210
Cdd:TIGR00606 579 LHSKSKEINQTRDRLAK------LNKELASLEQNKNH-INNELESKEEQLSSYEDKLFD--VCGSQDEESDLERLKEEIE 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1211 KLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCR---TTEDQMNEHRSKLEEAQRTVTDlstqraKLQTENSELSRQLE 1287
Cdd:TIGR00606 650 KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQrvfQTEAELQEFISDLQSKLRLAPD------KLKSTESELKKKEK 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1288 EKEAFInqltrGKLTYTQQLEDLKRQLEEEAKAKNalahalQSAQHDCDLLREQYEEEmeaktELQRALSKANSEVAQWR 1367
Cdd:TIGR00606 724 RRDEML-----GLAPGRQSIIDLKEKEIPELRNKL------QKVNRDIQRLKNDIEEQ-----ETLLGTIMPEEESAKVC 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1368 TKYETDAIQRTEELEEAKKKLAQRLQEAEEaveavnakcSSLEKTKHRLQNEIEDlmadversnaaaaaldkKQRNFDKI 1447
Cdd:TIGR00606 788 LTDVTIMERFQMELKDVERKIAQQAAKLQG---------SDLDRTVQQVNQEKQE-----------------KQHELDTV 841
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1448 LsewkQKFEESQTELEASQKEARSLSTELFKLKN---AYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKV 1524
Cdd:TIGR00606 842 V----SKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETF 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1525 RKQLDAEKLELqaaleeaeASLEHEEGKIlrAQLEFNQVKADYERKLAEKDeeieqskrnhlrvvdslqtslDAETRSRN 1604
Cdd:TIGR00606 918 LEKDQQEKEEL--------ISSKETSNKK--AQDKVNDIKEKVKNIHGYMK---------------------DIENKIQD 966
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1605 EALRLKKKMEGDLNEMEIQLShanrtaaEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELR 1684
Cdd:TIGR00606 967 GKDDYLKQKETELNTVNAQLE-------ECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQ 1039
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1685 AMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEaiQECRNAEEKAKKAITDAAMMAEEL 1764
Cdd:TIGR00606 1040 HLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE--PQFRDAEEKYREMMIVMRTTELVN 1117
|
.
gi 2163567613 1765 K 1765
Cdd:TIGR00606 1118 K 1118
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1054-1695 |
6.15e-12 |
|
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: 71.41 E-value: 6.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1054 LKLAQESimdleNDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTG---------- 1123
Cdd:pfam12128 244 TKLQQEF-----NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGelsaadaava 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1124 --RAKVEKLRSELLQ---------------------ELEETSERLE-EAGGATSVQLELNKKQEAEFQKLRRDL------ 1173
Cdd:pfam12128 319 kdRSELEALEDQHGAfldadietaaadqeqlpswqsELENLEERLKaLTGKHQDVTAKYNRRRSKIKEQNNRDIagikdk 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1174 -----EEATLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNlekmcrttE 1248
Cdd:pfam12128 399 lakirEARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENF--------D 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1249 DQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLtrgkltyTQQLEDLKRQL------------EE 1316
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEER-------QSALDELELQLfpqagtllhflrKE 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1317 EAKAKNALAHALQSAQ-HDCDLLREQYEEEMEAKTELqralskansevaqWRTKYETDAIQRTEELeEAKKKLAQRLQEA 1395
Cdd:pfam12128 544 APDWEQSIGKVISPELlHRTDLDPEVWDGSVGGELNL-------------YGVKLDLKRIDVPEWA-ASEEELRERLDKA 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1396 EEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAA-AAALDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLST 1474
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGELEKASREETFARTAlKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1475 ELFKLKNAYEESLEHLETFKRENKnlqeeildlTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKIL 1554
Cdd:pfam12128 690 QLKQLDKKHQAWLEEQKEQKREAR---------TEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDL 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1555 RAQLEFNQVKADYERKLAEKDEEIEQSKRNH---LRVVDSLQTSLDAETRSRNEALRlkkKMEGDLNEMEIQLShanRTA 1631
Cdd:pfam12128 761 ASLGVDPDVIAKLKREIRTLERKIERIAVRRqevLRYFDWYQETWLQRRPRLATQLS---NIERAISELQQQLA---RLI 834
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163567613 1632 AEAQKQVKALQ---GYLKDTQLQLDDVVRANEDLKENIAIV--ERRNNLLQSELEELRAMVEQSERARK 1695
Cdd:pfam12128 835 ADTKLRRAKLEmerKASEKQQVRLSENLRGLRCEMSKLATLkeDANSEQAQGSIGERLAQLEDLKLKRD 903
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1088-1766 |
6.36e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.86 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1088 RIEDEQAISAQLQKKLKELQARIEELEEELEAErtgrAKVEKLRSELLQELEETSERLeeaggatsvqlelnKKQEAEFQ 1167
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRT----ENIEELIKEKEKELEEVLREI--------------NEISSELP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1168 KLRRDLEEAtlqheataatlrKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELddvnsnteqlikaktnlekmcRTT 1247
Cdd:PRK03918 218 ELREELEKL------------EKEVKELEELKEEIEELEKELESLEGSKRKLEEKI---------------------REL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1248 EDQMNEHRSKLEEAQRTVTDLSTQRaKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHA 1327
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1328 LQsaqhdcdlLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCS 1407
Cdd:PRK03918 344 KK--------KLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1408 SLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRnfDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEEsl 1487
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK-- 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1488 ehletfkrenknlQEEILDLTEQLgasqKSIHELEKVRKQLDAEKLElqAALEEAEASLEheegkilraqlEFNQVKADY 1567
Cdd:PRK03918 492 -------------ESELIKLKELA----EQLKELEEKLKKYNLEELE--KKAEEYEKLKE-----------KLIKLKGEI 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1568 ER--KLAEKDEEIEQSKRNHLRVVDSLQTSL-DAETRSRNEALRLKKKMEGDLNEMEIQLSHANRtAAEAQKQVKALQGY 1644
Cdd:PRK03918 542 KSlkKELEKLEELKKKLAELEKKLDELEEELaELLKELEELGFESVEELEERLKELEPFYNEYLE-LKDAEKELEREEKE 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1645 LKDTQLQLDDVvranedlKENIAIVERRNNLLQSELEELRAMVEQSERARKlaEQELIEASERVQLLHSQNTSLINQKKK 1724
Cdd:PRK03918 621 LKKLEEELDKA-------FEELAETEKRLEELRKELEELEKKYSEEEYEEL--REEYLELSRELAGLRAELEELEKRREE 691
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 2163567613 1725 MEADISQLQTEVEEaIQECRNAEEKAKKAITDAAMMAEELKK 1766
Cdd:PRK03918 692 IKKTLEKLKEELEE-REKAKKELEKLEKALERVEELREKVKK 732
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1206-1855 |
8.86e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.43 E-value: 8.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1206 QRVKQKLEKEKSELKlelddvnsNTEQLIKaktNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQ 1285
Cdd:TIGR04523 36 KQLEKKLKTIKNELK--------NKEKELK---NLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1286 LEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQ 1365
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1366 WRTKYETDAIQRT--EELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRN 1443
Cdd:TIGR04523 185 IQKNIDKIKNKLLklELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1444 FDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLehLETFKRENKNLQEEILDLTEQLGASQKSIHELEK 1523
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNQISQNNKIISQLNE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1524 VRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLEfNQVKADYERKLAEKDEEIEQSKRNHLRVVDSLQTSLDaetrsr 1603
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE-NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK------ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1604 nealrlKKKMEGDLNEMEIQLSHANRTaaEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEEL 1683
Cdd:TIGR04523 416 ------KLQQEKELLEKEIERLKETII--KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1684 RAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAitdaaMMAEE 1763
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKE-----NLEKE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1764 LKKEQDTSAHLERMKKNMEQTVKDLQLRLD--EAEQLALKggkKQLQKLEVRVRELENEL---EAEQKRNAESIKGLRKS 1838
Cdd:TIGR04523 563 IDEKNKEIEELKQTQKSLKKKQEEKQELIDqkEKEKKDLI---KEIEEKEKKISSLEKELekaKKENEKLSSIIKNIKSK 639
|
650
....*....|....*..
gi 2163567613 1839 ERRVKELSYQTEEDRKN 1855
Cdd:TIGR04523 640 KNKLKQEVKQIKETIKE 656
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1249-1700 |
9.40e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 9.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1249 DQMNEHRSKLEEAQRTVTDLSTQRAKLQtensELSRQLEEKEAFINQLtRGKLTYTQQLEDLKRQLEEEAKAKNALAHAL 1328
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEEL-REELEKLEKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1329 QSAqhdcdllrEQYEEEMEAKTELQRALSKANSEVAQWRTkyetdaiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSS 1408
Cdd:COG4717 146 ERL--------EELEERLEELRELEEELEELEAELAELQE-------ELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1409 LEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDK------------ILSEWKQKFEESQTELEASQKEARSLS--- 1473
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLAllf 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1474 TELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQK-SIHELEKVRKQLdAEKLELQAALEEAEASLEHEEGK 1552
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDlSPEELLELLDRI-EELQELLREAEELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1553 ILRAQLeFNQVKADYERKLAEKDEEIEQsKRNHLRVVDSLQTSLDAETRSRNEALRlkkkmEGDLNEMEIQLSHANRTAA 1632
Cdd:COG4717 370 QEIAAL-LAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLE-----ALDEEELEEELEELEEELE 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1633 EAQKQVKALQGYLKDTQLQLDDVVRANE--DLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQE 1700
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1380-1823 |
1.37e-11 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 69.33 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1380 ELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSE--------- 1450
Cdd:pfam05622 4 EAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEEnfrletard 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1451 -WKQKFEE----------SQTELEASQKEARSLSTELFKLKNA-------------YEESLEHLETFKRENKNLQEEILD 1506
Cdd:pfam05622 84 dYRIKCEElekevlelqhRNEELTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1507 LTEQLGASQKSIHELEKVRKQLDAEKLELQaaleEAEASLEHEEGKILRAQLEFNQVKADYERKLAEKD----------E 1576
Cdd:pfam05622 164 YMQRTLQLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKErliierdtlrE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1577 EIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQvkALQGYLKDTQLQLDDVV 1656
Cdd:pfam05622 240 TNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEG--SYRERLTELQQLLEDAN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1657 RANEDLKEniaiverRNNLLQSELEELRAMVEQSERArkLAEQElieaservqllhSQNTSLINQKKKMEADISQLqTEV 1736
Cdd:pfam05622 318 RRKNELET-------QNRLANQRILELQQQVEELQKA--LQEQG------------SKAEDSSLLKQKLEEHLEKL-HEA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1737 EEAIQECRNA-EEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQ---TVKDLQLRLDEAEQLALKGGKKQL 1807
Cdd:pfam05622 376 QSELQKKKEQiEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksVIKTLDPKQNPASPPEIQALKNQL 455
|
490
....*....|....*.
gi 2163567613 1808 QKLEVRVRELENELEA 1823
Cdd:pfam05622 456 LEKDKKIEHLERDFEK 471
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1190-1911 |
2.04e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.48 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1190 KHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEaqrtvtDLS 1269
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNG------ELS 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1270 TQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQyeeemeAK 1349
Cdd:pfam12128 312 AADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSK------IK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1350 TELQRALSKANSEVAQwrtKYETDAIQRTEElEEAKKKLAQRLQEAEEAVEAvnakcsSLEKTKHRLQNEIEDLMAdveR 1429
Cdd:pfam12128 386 EQNNRDIAGIKDKLAK---IREARDRQLAVA-EDDLQALESELREQLEAGKL------EFNEEEYRLKSRLGELKL---R 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1430 SNAAAAALDKK--QRNFDKILsewkqkfEESQTELEASQKEARSLSTELFKLKNAYEESLEHLetfKRENKNLQEeildl 1507
Cdd:pfam12128 453 LNQATATPELLlqLENFDERI-------ERAREEQEAANAEVERLQSELRQARKRRDQASEAL---RQASRRLEE----- 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1508 teqlgasQKSihELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLefnqvkadyerkLAEKDEEIEQSKRNHLR 1587
Cdd:pfam12128 518 -------RQS--ALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPEL------------LHRTDLDPEVWDGSVGG 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1588 VVDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIa 1667
Cdd:pfam12128 577 ELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDL- 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1668 ivERRNNLLQSeleELRAMVEQSERARKLAEqelieasERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAE 1747
Cdd:pfam12128 656 --RRLFDEKQS---EKDKKNKALAERKDSAN-------ERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVV 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1748 EKAKKAiTDAAMMAEELKKEQDTSAHLERMKKNMEQTVKdlQLRLDEAEQLALKGGKKQLQKLEVRVRELENELeAEQKR 1827
Cdd:pfam12128 724 EGALDA-QLALLKAAIAARRSGAKAELKALETWYKRDLA--SLGVDPDVIAKLKREIRTLERKIERIAVRRQEV-LRYFD 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1828 NAESIKGLRKSER--RVKELSYQTEEDRKNMVRLQDLVdKLQLKVKAYKRQA-EEAEEQANSNLAKFRKVQHELDEAEER 1904
Cdd:pfam12128 800 WYQETWLQRRPRLatQLSNIERAISELQQQLARLIADT-KLRRAKLEMERKAsEKQQVRLSENLRGLRCEMSKLATLKED 878
|
....*..
gi 2163567613 1905 ADMAESQ 1911
Cdd:pfam12128 879 ANSEQAQ 885
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
927-1621 |
2.81e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.10 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 927 MNAELAAKKRKLEDECSE----LKKDIDDLELSLAKVEKEKHATENKVKNL----TEEMAGLDENITKLTKEKKILQESH 998
Cdd:pfam12128 284 TSAELNQLLRTLDDQWKEkrdeLNGELSAADAAVAKDRSELEALEDQHGAFldadIETAAADQEQLPSWQSELENLEERL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 999 QQALDDLQAEEDKVNTLaKAKVKlEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKlAQESIMDLENDKQQLEERLKKK 1078
Cdd:pfam12128 364 KALTGKHQDVTAKYNRR-RSKIK-EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQ-ALESELREQLEAGKLEFNEEEY 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1079 DFELNTLNARIEDEQA-ISAQLQKKLKELQARIEELEEELEAErtgRAKVEKLRSELLQeleetserleeAGGATSVQLE 1157
Cdd:pfam12128 441 RLKSRLGELKLRLNQAtATPELLLQLENFDERIERAREEQEAA---NAEVERLQSELRQ-----------ARKRRDQASE 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1158 LNKKQEAEFQKLRRDLEEATLQHEATAATLrkkHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTE-QLIKA 1236
Cdd:pfam12128 507 ALRQASRRLEERQSALDELELQLFPQAGTL---LHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGElNLYGV 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1237 KTNLEKM----CRTTEDQMNEHRSKLEEAqrtvtdLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKR 1312
Cdd:pfam12128 584 KLDLKRIdvpeWAASEEELRERLDKAEEA------LQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRR 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1313 QLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEA-KTELQRALSKANSEVAQWRTKYEtdaiQRTEELEEAKK-KLAQ 1390
Cdd:pfam12128 658 LFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQlDKKHQAWLEEQKEQKREARTEKQ----AYWQVVEGALDaQLAL 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1391 RLQEAEEAVEAVNAKCSSLEKTKHR--------------LQNEIEDLMADVERsnaaAAALDKKQRNFDKILSE-WKQKF 1455
Cdd:pfam12128 734 LKAAIAARRSGAKAELKALETWYKRdlaslgvdpdviakLKREIRTLERKIER----IAVRRQEVLRYFDWYQEtWLQRR 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1456 EESQTELEASQKEARSLSTELFKLKnayeeslehlETFKRENKNLQEEildlteqLGASQKSIHELEKVRKQLDAE---- 1531
Cdd:pfam12128 810 PRLATQLSNIERAISELQQQLARLI----------ADTKLRRAKLEME-------RKASEKQQVRLSENLRGLRCEmskl 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1532 -KLELQAALEEAEASLEHEegkilRAQLEfnqvkaDYERKLAEKDEEIEQSKRNHLRVVDSLQTSLDAET--RSRNEALR 1608
Cdd:pfam12128 873 aTLKEDANSEQAQGSIGER-----LAQLE------DLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETweSLREEDHY 941
|
730
....*....|...
gi 2163567613 1609 LKKKMEGDLNEME 1621
Cdd:pfam12128 942 QNDKGIRLLDYRK 954
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1016-1218 |
3.90e-11 |
|
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: 67.10 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1016 AKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQAI 1095
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1096 SAQLQKKLKEL---------QARIEELEEELEAERTGRA-----KVEKLRSELLQELEETSERLEEAGGATSVQLELNKK 1161
Cdd:COG4942 99 LEAQKEELAELlralyrlgrQPPLALLLSPEDFLDAVRRlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1162 QEAEFQKLRRDLEEATLQHEATAATLRKK---HADSVAELSEQLDNLQRVKQKLEKEKSE 1218
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKElaeLAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1200-1897 |
4.48e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 68.21 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1200 EQLDNLQRVKQKLEKEKSELKlelddvnsnteqliKAKTNLEKMCRTTEDQMNEHRsKLEEAQRTVTDlstqraKLQTEN 1279
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIK--------------KWKVSIEAELKQKENKLQENR-KIIEAQRKAIQ------ELQFEN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1280 SELSRQLEEKeafinqltrgkltyTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKA 1359
Cdd:pfam05483 130 EKVSLKLEEE--------------IQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKM 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1360 NSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDK 1439
Cdd:pfam05483 196 ILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1440 KQRNFDKILSEWKQKFEESQTELEASQKE-ARSLSTE-------------LFKLKNAYEESLEHLETFKRENK----NLQ 1501
Cdd:pfam05483 276 KTKLQDENLKELIEKKDHLTKELEDIKMSlQRSMSTQkaleedlqiatktICQLTEEKEAQMEELNKAKAAHSfvvtEFE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1502 EEILDLTEQLGASQKsihELEKVRKQLDAEKLELQAALEEAEASLEHEEGKilraqlefnQVKADYERKLAEKDEEIEQS 1581
Cdd:pfam05483 356 ATTCSLEELLRTEQQ---RLEKNEDQLKIITMELQKKSSELEEMTKFKNNK---------EVELEELKKILAEDEKLLDE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1582 KRNHLRVVDSLQTSldaetrsRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQ-LDDVVRANE 1660
Cdd:pfam05483 424 KKQFEKIAEELKGK-------EQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKnIELTAHCDK 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1661 DLKENIAIVERRNNL---LQSELEELRAMVEQSERARKlaeqelieaseRVQLLHSQNTSLINQKKKMEADISQLQTEVE 1737
Cdd:pfam05483 497 LLLENKELTQEASDMtleLKKHQEDIINCKKQEERMLK-----------QIENLEEKEMNLRDELESVREEFIQKGDEVK 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1738 EAIQEcrnAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQlrlDEAEQLALKGG--KKQLQKLEVRVR 1815
Cdd:pfam05483 566 CKLDK---SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH---QENKALKKKGSaeNKQLNAYEIKVN 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1816 ELENELEAEQKRNAESIKGLRK-------SERRVKELSYQTEEDRKNMVRLQDLVDK-LQLKV-------KAYKRQAEEA 1880
Cdd:pfam05483 640 KLELELASAKQKFEEIIDNYQKeiedkkiSEEKLLEEVEKAKAIADEAVKLQKEIDKrCQHKIaemvalmEKHKHQYDKI 719
|
730
....*....|....*..
gi 2163567613 1881 EEQANSNLAKFRKVQHE 1897
Cdd:pfam05483 720 IEERDSELGLYKNKEQE 736
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1057-1285 |
5.61e-11 |
|
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: 66.71 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1057 AQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQ 1136
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1137 ELEETSERLEE-------AGGATSVQLELNKKQEAEFQKLRRDLEEATLQHEATAATLRkkhadsvaelsEQLDNLQRVK 1209
Cdd:COG4942 98 ELEAQKEELAEllralyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR-----------ADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163567613 1210 QKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQ 1285
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1184-1923 |
6.55e-11 |
|
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: 68.06 E-value: 6.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1184 AATLRKKHADSVAELSEQLDNLQRVKQKL-EKEKSELKLElDDVNSNTEQLIKAKTNL---EKMCRTTEDqMNEHRSKLE 1259
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELeELSARESDLE-QDYQAASDHLNLVQTALrqqEKIERYQED-LEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1260 EAQRTVTDLSTQRAKLQTenselsrQLEEKEAFINQLTrgkltytQQLEDLKRQLEEE---AKAKNALAHALQSAQHDCD 1336
Cdd:COG3096 365 EQEEVVEEAAEQLAEAEA-------RLEAAEEEVDSLK-------SQLADYQQALDVQqtrAIQYQQAVQALEKARALCG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1337 LlreqyeeemeaktelqRALSKANseVAQWRTKYETDAIQRTEELEEakkkLAQRLQEAEEAVEAVNAKCSSLEKtkhrl 1416
Cdd:COG3096 431 L----------------PDLTPEN--AEDYLAAFRAKEQQATEEVLE----LEQKLSVADAARRQFEKAYELVCK----- 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1417 qneiedLMADVERSNA--AAAALDKKQRNFdKILSEWKQKFEESQTELE---ASQKEARSLSTELFKLKNAYEESLEHLE 1491
Cdd:COG3096 484 ------IAGEVERSQAwqTARELLRRYRSQ-QALAQRLQQLRAQLAELEqrlRQQQNAERLLEEFCQRIGQQLDAAEELE 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1492 TFKREnknLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQA------ALEEAEASLEHEEGKIL---RAQLEFNQ 1562
Cdd:COG3096 557 ELLAE---LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArapawlAAQDALERLREQSGEALadsQEVTAAMQ 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1563 VKADYERKLAEKDEEIEQSKRNHLRVVDSL-QTSLDAETRsrneALRLKKKMEGDL-NEM--EIQLSHA---------NR 1629
Cdd:COG3096 634 QLLEREREATVERDELAARKQALESQIERLsQPGGAEDPR----LLALAERLGGVLlSEIydDVTLEDApyfsalygpAR 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1630 TA------AEAQKQVKALQGYLKDTQL------QLDDVVRANEDLKENIAIVERRNNLLQS---------------ELEE 1682
Cdd:COG3096 710 HAivvpdlSAVKEQLAGLEDCPEDLYLiegdpdSFDDSVFDAEELEDAVVVKLSDRQWRYSrfpevplfgraarekRLEE 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1683 LRAmvEQSERARKLAEQELieASERVQLLHSQNTSLINQKKKM------EADISQLQ---TEVEEAIQECRNAEEKAKKA 1753
Cdd:COG3096 790 LRA--ERDELAEQYAKASF--DVQKLQRLHQAFSQFVGGHLAVafapdpEAELAALRqrrSELERELAQHRAQEQQLRQQ 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1754 ITDAAMMAEELKKEQDTSAHLErmKKNMEQTVKDLQLRLDEAEQ----LALKGgkKQLQKLEVRVRELEN---------- 1819
Cdd:COG3096 866 LDQLKEQLQLLNKLLPQANLLA--DETLADRLEELREELDAAQEaqafIQQHG--KALAQLEPLVAVLQSdpeqfeqlqa 941
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1820 ---ELEAEQKRNAESIKGLRKSERRVKELSYQTEEDRKNmvRLQDLVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKVQH 1896
Cdd:COG3096 942 dylQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLG--ENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQ 1019
|
810 820
....*....|....*....|....*..
gi 2163567613 1897 ELDEAEERADMAESQVNKLRARSRDIG 1923
Cdd:COG3096 1020 VLASLKSSRDAKQQTLQELEQELEELG 1046
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1468-1920 |
7.35e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1468 EARSLSTELFKLKNAYEESLEhletfKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEasLE 1547
Cdd:COG4913 226 AADALVEHFDDLERAHEALED-----AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1548 HEEGKILRAQLEFNQVKADYERkLAEKDEEIEQSKRNH-LRVVDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSH 1626
Cdd:COG4913 299 ELRAELARLEAELERLEARLDA-LREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1627 A----NRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKEN-------IAIVERRNNLLQSELEELRAMVEqseRARK 1695
Cdd:COG4913 378 SaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRElreleaeIASLERRKSNIPARLLALRDALA---EALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1696 LAEQ------ELIE----------ASERVqlLHSQNTSL-------------INQKK----------------------- 1723
Cdd:COG4913 455 LDEAelpfvgELIEvrpeeerwrgAIERV--LGGFALTLlvppehyaaalrwVNRLHlrgrlvyervrtglpdperprld 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1724 ------KMEADISQLQTEVEEAIQE------CRNAEE--KAKKAITDAAMMAeelkkeQDTSAHlermKKNMEQTVK-DL 1788
Cdd:COG4913 533 pdslagKLDFKPHPFRAWLEAELGRrfdyvcVDSPEElrRHPRAITRAGQVK------GNGTRH----EKDDRRRIRsRY 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1789 QLRLDEAEQLALKggKKQLQKLEVRVRELENELEA---------EQKRNAESIKGLRKSERRVKELSYQ---TEEDRKNM 1856
Cdd:COG4913 603 VLGFDNRAKLAAL--EAELAELEEELAEAEERLEAleaeldalqERREALQRLAEYSWDEIDVASAEREiaeLEAELERL 680
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163567613 1857 VRLQDLVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKVQHELDEAEERADMAESQVNKLRARSR 1920
Cdd:COG4913 681 DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
839-1463 |
7.66e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 7.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 839 ETEKEMQTMKEEFGHLKEA---LEKSEARRKELE------EKMVSMLQEKNDLQ-----LQVQAEQDNLADAEERCDQLI 904
Cdd:COG4913 222 DTFEAADALVEHFDDLERAheaLEDAREQIELLEpirelaERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 905 KNKIQLEAKVkemterleeeeemnAELAAKKRKLEDECSELK--------KDIDDLELSLAKVEKEKHATENKVKNLTEE 976
Cdd:COG4913 302 AELARLEAEL--------------ERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 977 MAGLDENITKLTKEKKILQESHQQALDDLQAEEDKVNT----LAKAKVKLEQQVDDLES---SLEQEKK-IRMDLERAKR 1048
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEalaeAEAALRDLRRELRELEAeiaSLERRKSnIPARLLALRD 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1049 KLEGDLKLAQESI------MDLENDKQQLE---ERLkkkdfeLNTLNARIEDEQAISAQLQKKLKELQARieeleeelEA 1119
Cdd:COG4913 448 ALAEALGLDEAELpfvgelIEVRPEEERWRgaiERV------LGGFALTLLVPPEHYAAALRWVNRLHLR--------GR 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1120 ERTGRAKvEKLRSELLQELEETS--ERLE-EAGGATS-VQLELNKkqeaefqklRRDLE----EATLQHEATAATL---- 1187
Cdd:COG4913 514 LVYERVR-TGLPDPERPRLDPDSlaGKLDfKPHPFRAwLEAELGR---------RFDYVcvdsPEELRRHPRAITRagqv 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1188 -----RKKHADSVAELSEQL---DNLQRVKQkLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTTE--DQMNEHRSK 1257
Cdd:COG4913 584 kgngtRHEKDDRRRIRSRYVlgfDNRAKLAA-LEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEID 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1258 LEEAQRTVTDLSTQRAKLQTENSELS---RQLEEKEAfinqltrgkltytqQLEDLKRQLEEEAKAKNALAHALQSAQHD 1334
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDLAaleEQLEELEA--------------ELEELEEELDELKGEIGRLEKELEQAEEE 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1335 CDLLREQYEEEMEAKTELQRAlskansEVAQWRTKYETDAIQRT--EELEEAKKKLAQRLQEAEEAVEAVnakcssLEKT 1412
Cdd:COG4913 729 LDELQDRLEAAEDLARLELRA------LLEERFAAALGDAVERElrENLEERIDALRARLNRAEEELERA------MRAF 796
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2163567613 1413 KHRLQNEIEDLMADVERSNAAAAALDKKQRNfdkILSEWKQKFEESQTELE 1463
Cdd:COG4913 797 NREWPAETADLDADLESLPEYLALLDRLEED---GLPEYEERFKELLNENS 844
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1192-1408 |
1.34e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.56 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1192 ADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQ 1271
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1272 RAKLQTENSELSRQL-----EEKEAFI------NQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLRE 1340
Cdd:COG4942 99 LEAQKEELAELLRALyrlgrQPPLALLlspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2163567613 1341 QYEEEMEAKTELQRALSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSS 1408
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1438-1922 |
1.91e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1438 DKKQRNFDKILSEWKQKFEESQTELE--ASQKE-ARSLSTELFKLKNAYEESLEHLETfkrenknLQEEILDLTEqlgas 1514
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIEryEEQREqARETRDEADEVLEEHEERREELET-------LEAEIEDLRE----- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1515 qkSIHELEKVRKQLDAEKLELQAALEEAEASLEHeegkiLRAQLEFNQvkADYERKLAEKDEEieQSKRNHLRvvDSLQT 1594
Cdd:PRK02224 266 --TIAETEREREELAEEVRDLRERLEELEEERDD-----LLAEAGLDD--ADAEAVEARREEL--EDRDEELR--DRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1595 SLDAETRSRNEALRLKKKMEgDLNEmeiqlshanrTAAEAQKQVKALQGYLKDTQLQLDDvvrANEDLKEniaiverrnn 1674
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDAD-DLEE----------RAEELREEAAELESELEEAREAVED---RREEIEE---------- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1675 lLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLinqkkkmEADISQLQTEVEEAIQ--------ECRNA 1746
Cdd:PRK02224 389 -LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL-------EATLRTARERVEEAEAlleagkcpECGQP 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1747 EEKAKkaitdaamMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLAlkggkkqlqKLEVRVRELENELEAeqk 1826
Cdd:PRK02224 461 VEGSP--------HVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV---------EAEDRIERLEERRED--- 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1827 rnaesikglrkSERRVKELSYQTEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKVQHELDEAEERAD 1906
Cdd:PRK02224 521 -----------LEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
490
....*....|....*.
gi 2163567613 1907 maesQVNKLRARSRDI 1922
Cdd:PRK02224 590 ----SLERIRTLLAAI 601
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
929-1134 |
2.62e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.40 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 929 AELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQESHQQALDDLQAE 1008
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1009 E-----------DKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKK 1077
Cdd:COG4942 117 GrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2163567613 1078 KDFELNTLNARIEDEQAISAQLQKKLKELQARIE--ELEEELEAERTGRAKVEKLRSEL 1134
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEELEALIArlEAEAAAAAERTPAAGFAALKGKL 255
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1536-1931 |
7.58e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 7.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1536 QAALEEAEASLEHEEGKILRAQLefnqvkADYERKLAEKDEEI---EQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKK 1612
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKDLHERL------NGLESELAELDEEIeryEEQREQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1613 MEgDLNEmeiqlshanrTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKE-------NIAIVERRNNLLQSELEELRA 1685
Cdd:PRK02224 260 IE-DLRE----------TIAETEREREELAEEVRDLRERLEELEEERDDLLAeaglddaDAEAVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1686 MVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVE---EAIQECRNAEEKAKKAITDAAM--- 1759
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEdrrEEIEELEEEIEELRERFGDAPVdlg 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1760 -MAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLaLKGGK---------------------KQLQKLEVRVREL 1817
Cdd:PRK02224 409 nAEDFLEELREERDELREREAELEATLRTARERVEEAEAL-LEAGKcpecgqpvegsphvetieedrERVEELEAELEDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1818 ENELEAEQKRnAESIKGLRKSERRVKELsyqtEEDRKNMVRLqdlvdklqlkVKAYKRQAEEAEEQANSNLAKFRKVQHE 1897
Cdd:PRK02224 488 EEEVEEVEER-LERAEDLVEAEDRIERL----EERREDLEEL----------IAERRETIEEKRERAEELRERAAELEAE 552
|
410 420 430
....*....|....*....|....*....|....
gi 2163567613 1898 LDEAEERADMAESQVNKLRARSRDIGAKKGLNEE 1931
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEVAELNSKLAELKE 586
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
937-1592 |
1.28e-09 |
|
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: 63.92 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 937 KLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTkEKKILQESH---QQALDDLQAEEDKVN 1013
Cdd:TIGR01612 1108 KYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVA-DKAISNDDPeeiEKKIENIVTKIDKKK 1186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1014 TLAKAKVKLEQQVDDLE---SSLEQEKKIRMD------------LERAKRKLEGDLKLAQESIMDLENDKQQ-------- 1070
Cdd:TIGR01612 1187 NIYDEIKKLLNEIAEIEkdkTSLEEVKGINLSygknlgklflekIDEEKKKSEHMIKAMEAYIEDLDEIKEKspeienem 1266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1071 -LEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQAR---IEELEEELEAERTGRAKVEKLRSELLQELEETSERLE 1146
Cdd:TIGR01612 1267 gIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKslkIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLN 1346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1147 EAGGATSVqLELNKkqeaeFQKLRRDLEEATLQHEATaatlrKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDV 1226
Cdd:TIGR01612 1347 EIANIYNI-LKLNK-----IKKIIDEVKEYTKEIEEN-----NKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDDK 1415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1227 NSNteQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTdlstqrakLQTENSELSrqlEEKEAFI--NQLTRGKLTYT 1304
Cdd:TIGR01612 1416 DID--ECIKKIKELKNHILSEESNIDTYFKNADENNENVL--------LLFKNIEMA---DNKSQHIlkIKKDNATNDHD 1482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1305 QQLEDLKRQLEEEAKAKNAlAHALQSAQHDCDLLREQYEEEMeakTELQRALSKAnsEVAQWRTKYETDAIQRTEELEEA 1384
Cdd:TIGR01612 1483 FNINELKEHIDKSKGCKDE-ADKNAKAIEKNKELFEQYKKDV---TELLNKYSAL--AIKNKFAKTKKDSEIIIKEIKDA 1556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1385 KKKLAQRLQEAEEaveavnaKCSSLEKTKHRlqneIEDLMADVERSNAAAAALDKKQRNFDKIL---SEWKQKFEESQTE 1461
Cdd:TIGR01612 1557 HKKFILEAEKSEQ-------KIKEIKKEKFR----IEDDAAKNDKSNKAAIDIQLSLENFENKFlkiSDIKKKINDCLKE 1625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1462 LEASQKEARSLS-----TELFKLKNAYEESLEHLETFKRENKNLqeeildlteqlgasqksihelekvrkqldaeklelq 1536
Cdd:TIGR01612 1626 TESIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQKKNI------------------------------------ 1669
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 2163567613 1537 aalEEAEASLEHEEGKILRAQLEFNQVKADYERKLAEKDEEIEQSKRNHLRVVDSL 1592
Cdd:TIGR01612 1670 ---EDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIESIKEL 1722
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
841-1423 |
1.61e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 63.06 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 841 EKEMQTMKEEFGHLKEALEKSEARRKELEEKMvSMLQEKNDLQLQVQ---AEQDNLADAEERCDQLIKnKIQLEAKVKEM 917
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHAYLTQKREAQEEQL-KKQQLLKQLRARIEelrAQEAVLEETQERINRARK-AAPLAAHIKAV 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 918 TERLEEEEEMNAELAAKKRKLEDE---CSELKKDIDDLElSLAKVEKEKHATENKVKNLTEEMAGLDEnitKLTKEKKIL 994
Cdd:TIGR00618 303 TQIEQQAQRIHTELQSKMRSRAKLlmkRAAHVKQQSSIE-EQRRLLQTLHSQEIHIRDAHEVATSIRE---ISCQQHTLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 995 QESHQQAlDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQ----- 1069
Cdd:TIGR00618 379 QHIHTLQ-QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQcekle 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1070 -----QLEERLKKKDFELNTLNA---RIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSeLLQELEET 1141
Cdd:TIGR00618 458 kihlqESAQSLKEREQQLQTKEQihlQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTR-RMQRGEQT 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1142 SERLEEAGGATSVQLELNKKQEAEFQKlrrdlEEATLQHEATAATLRKKhadsvaELSEQLDNLQRVKQKLEKE-KSELK 1220
Cdd:TIGR00618 537 YAQLETSEEDVYHQLTSERKQRASLKE-----QMQEIQQSFSILTQCDN------RSKEDIPNLQNITVRLQDLtEKLSE 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1221 LELDDVNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDL---------STQRAKLQTENSELSRQLEEKEA 1291
Cdd:TIGR00618 606 AEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLtltqervreHALSIRVLPKELLASRQLALQKM 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1292 --FINQLTRGKLTYTQQLEDLKRQLEEEAKAK---------------------NALAHALQSAQHDCDLLREQYEEEMEA 1348
Cdd:TIGR00618 686 qsEKEQLTYWKEMLAQCQTLLRELETHIEEYDrefneienassslgsdlaareDALNQSLKELMHQARTVLKARTEAHFN 765
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2163567613 1349 KTELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDL 1423
Cdd:TIGR00618 766 NNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEK 840
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
844-1697 |
1.80e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.05 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 844 MQTMKEEFGHLKEAL----EKSEARRK--ELEEKMVSMLQEkndLQLQVQAEQDNLADAEERCDQLiknkiqleAKVKEM 917
Cdd:PRK04863 275 MRHANERRVHLEEALelrrELYTSRRQlaAEQYRLVEMARE---LAELNEAESDLEQDYQAASDHL--------NLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 918 TERLEEEEEMNAELAAKKRKLEdECSELKKDIDDLelsLAKVEKEKHATENKVKNLTEEMA----GLDENITK---LTKE 990
Cdd:PRK04863 344 LRQQEKIERYQADLEELEERLE-EQNEVVEEADEQ---QEENEARAEAAEEEVDELKSQLAdyqqALDVQQTRaiqYQQA 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 991 KKILQESHQQ-ALDDLQAE--EDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAK---RKLEGDL------KLAQ 1058
Cdd:PRK04863 420 VQALERAKQLcGLPDLTADnaEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYqlvRKIAGEVsrseawDVAR 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1059 ESIMDLENDKQQLEeRLKKKDFELNTLNARIEDEQaisaQLQKKLKELQARIEELEEELeaertgrAKVEKLRSELLQEL 1138
Cdd:PRK04863 500 ELLRRLREQRHLAE-QLQQLRMRLSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDE-------DELEQLQEELEARL 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1139 EETSERLEEAG-GATSVQLELnKKQEAEFQKLRRdLEEATLQHEATAATLRKKHADSVAElSEQLDNLqrVKQKLEKEKs 1217
Cdd:PRK04863 568 ESLSESVSEAReRRMALRQQL-EQLQARIQRLAA-RAPAWLAAQDALARLREQSGEEFED-SQDVTEY--MQQLLERER- 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1218 ELKLELDDVNSNTEQLIKAKTNL--------EKMCRTTEDQMNEHRSK------LEEAQRT------------VTDLSTQ 1271
Cdd:PRK04863 642 ELTVERDELAARKQALDEEIERLsqpggsedPRLNALAERFGGVLLSEiyddvsLEDAPYFsalygparhaivVPDLSDA 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1272 RAKLQTE------------------NSELSRQLEEKEAFINQLTR-------------GKLTYTQQLEDLKRQLEEEAK- 1319
Cdd:PRK04863 722 AEQLAGLedcpedlyliegdpdsfdDSVFSVEELEKAVVVKIADRqwrysrfpevplfGRAAREKRIEQLRAEREELAEr 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1320 -AKNA--------LAHALQS--AQHDCDLLREQYEEEMEaktELQRALSKANSEVAQwrtkyetdaiqrteeLEEAKKKL 1388
Cdd:PRK04863 802 yATLSfdvqklqrLHQAFSRfiGSHLAVAFEADPEAELR---QLNRRRVELERALAD---------------HESQEQQQ 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1389 AQRLQEAEEAVEAVN--AKCSSLEKTKHrLQNEIEDLMADVERSNAAAAALDKKQRNFDKI-------------LSEWKQ 1453
Cdd:PRK04863 864 RSQLEQAKEGLSALNrlLPRLNLLADET-LADRVEEIREQLDEAEEAKRFVQQHGNALAQLepivsvlqsdpeqFEQLKQ 942
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1454 KFEESQTELEASQKEARSLsTELFKLKN--AYEESLEHL-------ETFKRENKNLQEEILDLTEQLGASQKSIHELEKV 1524
Cdd:PRK04863 943 DYQQAQQTQRDAKQQAFAL-TEVVQRRAhfSYEDAAEMLaknsdlnEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQV 1021
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1525 RKQLDAEKLELQAALEEAEASLEheegkilraQLEFnQVKADYERKLAEKDEEIEQSKRNHLRVVDSLQTSLDAETRSRN 1604
Cdd:PRK04863 1022 LASLKSSYDAKRQMLQELKQELQ---------DLGV-PADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMD 1091
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1605 EALRLKKKMEGDLnemeiqlsHANRTAAEAQKQVKalqgylkdtqlqlDDVVRAnedLKENiaIVERRnnLLQSEL---- 1680
Cdd:PRK04863 1092 NLTKKLRKLERDY--------HEMREQVVNAKAGW-------------CAVLRL---VKDN--GVERR--LHRRELayls 1143
|
970
....*....|....*...
gi 2163567613 1681 -EELRAMVEQSERARKLA 1697
Cdd:PRK04863 1144 aDELRSMSDKALGALRLA 1161
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
829-1221 |
1.98e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 829 FKIKPLLKSAETEKEMQTMKEEFGHLKEALEKSEARR---KELEEKMVSMLQEKNDLQLQVQAEQDNLADAEE----RCD 901
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 902 QLIKNKIQLEAKVKEMTERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLE--------------------------LS 955
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrelteehrkelleeytAE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 956 LAKVEKEKHATENKVKNLTEEMAGLDeniTKLTKEKKILQEshQQALDDLQAEEDKVNTLAKAkvKLEQQVDDLESSLEQ 1035
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELE---KVLKKESELIKL--KELAEQLKELEEKLKKYNLE--ELEKKAEEYEKLKEK 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1036 EKKIRMDLERAKRKLegdlklaqESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQAIS-AQLQKKLKELQA---RIE 1111
Cdd:PRK03918 534 LIKLKGEIKSLKKEL--------EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPfynEYL 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1112 ELEEELEAERTGRAKVEKLRSEL---LQELEETSERLEEAGGATSvqlELNKK-QEAEFQKLRRDLEEATLQHEATAATL 1187
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELdkaFEELAETEKRLEELRKELE---ELEKKySEEEYEELREEYLELSRELAGLRAEL 682
|
410 420 430
....*....|....*....|....*....|....
gi 2163567613 1188 rKKHADSVAELSEQLDNLQRVKQKLEKEKSELKL 1221
Cdd:PRK03918 683 -EELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
862-1204 |
2.25e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 862 EARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEmterleeeeemnAELAAKKRKLEDE 941
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV------------ASAEREIAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 942 CSELKKDIDDLElslaKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQESHQQALDDLQAEEDKVNTLAKAkvK 1021
Cdd:COG4913 677 LERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--L 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1022 LEQQVDDLESSlEQEKKIRMDLERAKRKLEGDLKLAQESIMDLendkqqLEERLKKKDFELNTLNARIEDEQAISAQLQK 1101
Cdd:COG4913 751 LEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERA------MRAFNREWPAETADLDADLESLPEYLALLDR 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1102 ----KLKELQARIeeleeELEAERTGRAKVEKLRSELLQELEETSERLEEA---------GGATSVQLELNKKQEAEFQK 1168
Cdd:COG4913 824 leedGLPEYEERF-----KELLNENSIEFVADLLSKLRRAIREIKERIDPLndslkripfGPGRYLRLEARPRPDPEVRE 898
|
330 340 350
....*....|....*....|....*....|....*.
gi 2163567613 1169 LRRDLEEATLQHEATAATLRKKHADSVAELSEQLDN 1204
Cdd:COG4913 899 FRQELRAVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
836-1413 |
2.36e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 62.43 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 836 KSAETEKEMQTMKEEFGHLKEALEKSEARRKELE--------EKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNK 907
Cdd:pfam05483 170 KTKKYEYEREETRQVYMDLNNNIEKMILAFEELRvqaenarlEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQI 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 908 IQLEAKVKEMTERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKL 987
Cdd:pfam05483 250 TEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 988 TKEKkilqESHQQALDDLQAEEDKVNTLAKAKV-------KLEQQvdDLESSLEQEKKIRMDLERAKRKLEGDLKLAQES 1060
Cdd:pfam05483 330 TEEK----EAQMEELNKAKAAHSFVVTEFEATTcsleellRTEQQ--RLEKNEDQLKIITMELQKKSSELEEMTKFKNNK 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1061 IMDLENDKQQLEERLK----KKDFElNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSEL-- 1134
Cdd:pfam05483 404 EVELEELKKILAEDEKlldeKKQFE-KIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELek 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1135 --LQELEETS-------ERLEEAGGATSVQLELNKKQEaefqklrrDLEEATLQHEATAatlrkKHADSVAELSEQL-DN 1204
Cdd:pfam05483 483 ekLKNIELTAhcdklllENKELTQEASDMTLELKKHQE--------DIINCKKQEERML-----KQIENLEEKEMNLrDE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1205 LQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSR 1284
Cdd:pfam05483 550 LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENK 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1285 QLEEKEAFINQL------TRGKL-----TYTQQLEDLK----RQLEEEAKAKNALAHALQsAQHDCDLLREQYEEEMEA- 1348
Cdd:pfam05483 630 QLNAYEIKVNKLelelasAKQKFeeiidNYQKEIEDKKiseeKLLEEVEKAKAIADEAVK-LQKEIDKRCQHKIAEMVAl 708
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163567613 1349 ----KTELQRALSKANSEVAQWRTK----------YETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTK 1413
Cdd:pfam05483 709 mekhKHQYDKIIEERDSELGLYKNKeqeqssakaaLEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
961-1419 |
2.68e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 961 KEKHATENKVKNLTEEMAGLDENITKLTKEKKILQEsHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIR 1040
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELRE-ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1041 mDLERAKRKLEGDLKLAQESI-MDLENDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEeleeelea 1119
Cdd:COG4717 160 -ELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE-------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1120 ertgRAKVEKLRSELLQELEETSERLEEAGGATSVQLelnkkqeaefqklrrdleeATLQHEATAATLRKKHADSVAELS 1199
Cdd:COG4717 231 ----QLENELEAAALEERLKEARLLLLIAAALLALLG-------------------LGGSLLSLILTIAGVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1200 EQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTEN 1279
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1280 SELSRQ-------LEEKEAFINQLTRGK--LTYTQQLEDLKRQLEEEAKAKNALAhalqsAQHDCDLLREQYEEEMEAKT 1350
Cdd:COG4717 368 LEQEIAallaeagVEDEEELRAALEQAEeyQELKEELEELEEQLEELLGELEELL-----EALDEEELEEELEELEEELE 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2163567613 1351 ELQRALSKANSEVAqwRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKC---SSLEKTKHRLQNE 1419
Cdd:COG4717 443 ELEEELEELREELA--ELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKlalELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1097-1331 |
3.68e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1097 AQLQKKLKELQARIEELEEEleaertgRAKVEKLRSELLQELEETSERLEEAGgatsvqlELNKKQEAEFQKLRRDLEEA 1176
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKE-------LAALKKEEKALLKQLAALERRIAALA-------RRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1177 TLQHEAtaatLRKKHADSVAELSEQLDNLQRVKQKlekekSELKLELDdvNSNTEQLIKAKTNLEKMCRTTEDQMNEHRS 1256
Cdd:COG4942 89 EKEIAE----LRAELEAQKEELAELLRALYRLGRQ-----PPLALLLS--PEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1257 KLEEAQRTVTDLSTQRAKL-------QTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHALQ 1329
Cdd:COG4942 158 DLAELAALRAELEAERAELeallaelEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
..
gi 2163567613 1330 SA 1331
Cdd:COG4942 238 AA 239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
836-1233 |
3.76e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 836 KSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVK 915
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 916 EMterleeeeemnAELAAKKRKLEDE--CSELKKDIDDLELSLAKVEKEKhatenKVKNLTEEMAGLDENITKLtkEKKI 993
Cdd:PRK02224 437 TA-----------RERVEEAEALLEAgkCPECGQPVEGSPHVETIEEDRE-----RVEELEAELEDLEEEVEEV--EERL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 994 lqeshqQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEE 1073
Cdd:PRK02224 499 ------ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1074 RLKKKDFELNTLNARIEDEQAISAQLqkklkELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEEaggats 1153
Cdd:PRK02224 573 EVAELNSKLAELKERIESLERIRTLL-----AAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEA------ 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1154 vqlelnKKQEAEFQKLRRDLEEATlqheataaTLRKKHADSVAELSEQLDNLQR----VKQKLEkEKSELKLELDDVNSN 1229
Cdd:PRK02224 642 ------EFDEARIEEAREDKERAE--------EYLEQVEEKLDELREERDDLQAeigaVENELE-ELEELRERREALENR 706
|
....
gi 2163567613 1230 TEQL 1233
Cdd:PRK02224 707 VEAL 710
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1078-1851 |
4.73e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.90 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1078 KDFELNTLNARIEDEQAISAQlqkklKELQARIEELEEELEAERTGRAKVEKL---RSELLQELEETSERLEEAGGATSV 1154
Cdd:PRK04863 272 ADYMRHANERRVHLEEALELR-----RELYTSRRQLAAEQYRLVEMARELAELneaESDLEQDYQAASDHLNLVQTALRQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1155 QlELNKKQEAEFQKLRRDLEEAT----LQHEATAATLRKKHA--DSVAELSEQLDNLQR--------------VKQKLEK 1214
Cdd:PRK04863 347 Q-EKIERYQADLEELEERLEEQNevveEADEQQEENEARAEAaeEEVDELKSQLADYQQaldvqqtraiqyqqAVQALER 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1215 EKSELK---LELDDVNSNTEQLIKAKTNLEKMCRTTEDQMN---EHRSKLEEAQRTVTDL--STQRAKLQTENSELSRQL 1286
Cdd:PRK04863 426 AKQLCGlpdLTADNAEDWLEEFQAKEQEATEELLSLEQKLSvaqAAHSQFEQAYQLVRKIagEVSRSEAWDVARELLRRL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1287 EEKEAFINQLTRGKltytQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLlREQYEEEMEAKTELQRALSKANSEVAQW 1366
Cdd:PRK04863 506 REQRHLAEQLQQLR----MRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-EDELEQLQEELEARLESLSESVSEARER 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1367 RTKYEtdaiQRTEELEEAKKKLAQRLQEAEEAVEAVNakcsslektkhRLQNEIEDLMADVERSNAAAAALDKKQRnfdk 1446
Cdd:PRK04863 581 RMALR----QQLEQLQARIQRLAARAPAWLAAQDALA-----------RLREQSGEEFEDSQDVTEYMQQLLERER---- 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1447 ilsEWKQKFEESQTELEASQKEARSLStelfklkNAYEESLEHLETFK-RENKNLQEEILD---------LTEQLGASQK 1516
Cdd:PRK04863 642 ---ELTVERDELAARKQALDEEIERLS-------QPGGSEDPRLNALAeRFGGVLLSEIYDdvsledapyFSALYGPARH 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1517 SI--HELEKVRKQL-------------------------DAEKLELQAALEEAEASL-------------EHEEGKILRA 1556
Cdd:PRK04863 712 AIvvPDLSDAAEQLagledcpedlyliegdpdsfddsvfSVEELEKAVVVKIADRQWrysrfpevplfgrAAREKRIEQL 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1557 QLEFNQVkadyERKLAEKDEEIEQSKRNH----LRVVDSLQTSLDAETRSRNEALRLKK-KMEGDLNEMEIQLSHANRTA 1631
Cdd:PRK04863 792 RAEREEL----AERYATLSFDVQKLQRLHqafsRFIGSHLAVAFEADPEAELRQLNRRRvELERALADHESQEQQQRSQL 867
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1632 AEAQKQVKALQGYLKDTQLQLDD-----VVRANEDLKE-------------NIAIVERRNNLLQS---ELEELRAMVEQS 1690
Cdd:PRK04863 868 EQAKEGLSALNRLLPRLNLLADEtladrVEEIREQLDEaeeakrfvqqhgnALAQLEPIVSVLQSdpeQFEQLKQDYQQA 947
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1691 ERARKLAEQELIEASERVQLLH----SQNTSLINQkkkmEADIS-QLQTEVEEAIQECRNAEEKAKKA---ITDAAMMAE 1762
Cdd:PRK04863 948 QQTQRDAKQQAFALTEVVQRRAhfsyEDAAEMLAK----NSDLNeKLRQRLEQAEQERTRAREQLRQAqaqLAQYNQVLA 1023
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1763 ELKKEQDTsahLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQLQKLEVRVRELENELEAEQKRNAESIKGLRKSERRV 1842
Cdd:PRK04863 1024 SLKSSYDA---KRQMLQELKQELQDLGVPADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKL 1100
|
....*....
gi 2163567613 1843 KELSYQTEE 1851
Cdd:PRK04863 1101 ERDYHEMRE 1109
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1577-1892 |
4.90e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.57 E-value: 4.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1577 EIEQSKRNHLRVVDSLQ--TSLDAETRSRNEAL-----RLKKKMEGDLNEMEIQLSHANrtAAEAQKQVKAL-QGYLKdt 1648
Cdd:COG3206 88 EILKSRPVLERVVDKLNldEDPLGEEASREAAIerlrkNLTVEPVKGSNVIEISYTSPD--PELAAAVANALaEAYLE-- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1649 qlqlddvvranEDLKENIAIVERRNNLLQSELEELRAMVEQSERARK--LAEQELIEASERVQLLHSQNTSLINQKKKME 1726
Cdd:COG3206 164 -----------QNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEAR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1727 ADISQLQTEVEeAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ---TVKDLQLRLDEAEQLALKGG 1803
Cdd:COG3206 233 AELAEAEARLA-ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRAQLQQEA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1804 KKQLQKLEVRVRELENELEAEQKRnaesikgLRKSERRVKELSyqteedrKNMVRLQDLVDKLQLKVKAYK---RQAEEA 1880
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQ-------LAQLEARLAELP-------ELEAELRRLEREVEVARELYEsllQRLEEA 377
|
330
....*....|..
gi 2163567613 1881 EEQANSNLAKFR 1892
Cdd:COG3206 378 RLAEALTVGNVR 389
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
839-1240 |
5.00e-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: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 839 ETEKEMQTMKEEFGHLKEALEKSEarrKELEEKMVSMLQEKNDLQ--------LQVQAEQDNLADAEERCDQLIKNKIQL 910
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIKKQLSEKQ---KELEQNNKKIKELEKQLNqlkseisdLNNQKEQDWNKELKSELKNQEKKLEEI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 911 EAKVKEMTERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKE 990
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 991 KKILQESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQ 1070
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1071 LEERLKKKDFELNTLNARI----------EDEQAISAQLQKKL------KELQARIEELEEELEAERTGRAKVEKLRSEL 1134
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKkeleekvkdlTKKISSLKEKIEKLesekkeKESKISDLEDELNKDDFELKKENLEKEIDEK 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1135 LQELEETSERLEEAGGATSVQLELNKKQEAEFQKLRRDLEEatlqHEATAATLRKKHADSVAE---LSEQLDNLQRVKQK 1211
Cdd:TIGR04523 567 NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE----KEKKISSLEKELEKAKKEnekLSSIIKNIKSKKNK 642
|
410 420
....*....|....*....|....*....
gi 2163567613 1212 LEKEKSELKLELDDVNSNTEQLIKAKTNL 1240
Cdd:TIGR04523 643 LKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1090-1485 |
5.83e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1090 EDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRS--ELLQELEETSERLEEAGGatsvQLELNKKQEAEFQ 1167
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPE----RLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1168 KLRRDLEEATLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTT 1247
Cdd:COG4717 160 ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1248 EDQ-----------------------------------------------MNEHRSKLEEAQRTVTDLSTQRAKLQTENS 1280
Cdd:COG4717 240 ALEerlkearlllliaaallallglggsllsliltiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1281 ELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAhaLQSAQHDCDLLREQY----EEEMEAKTELQRAL 1356
Cdd:COG4717 320 ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAgvedEEELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1357 SKANSEVAQWRTKYETDAIQRTEELEEAKKK-LAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVErsnaaaa 1435
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE------- 470
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1436 aldkkqrnfdkiLSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEE 1485
Cdd:COG4717 471 ------------LAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
842-1315 |
5.98e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 842 KEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQD--NLADAEERCDQLIKNKIQLEAKVKEMte 919
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLEEL-- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 920 rleeeeemnAELAAKKRKLEDECSELKKDIDDLElslakvEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQESHQ 999
Cdd:COG4717 159 ---------RELEEELEELEAELAELQEELEELL------EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1000 QALDDLQAEEDKVNTLAKA-KVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQE--SIMDLENDKQQLEERLK 1076
Cdd:COG4717 224 ELEEELEQLENELEAAALEeRLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGllALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1077 KKDFELNTLNARIEDE--QAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSEL-LQELEETSERLEEAGGATS 1153
Cdd:COG4717 304 AEELQALPALEELEEEelEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqLEELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1154 V-QLELNKKQEAEFQKLRRDLEEATLQ-HEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTE 1231
Cdd:COG4717 384 EeELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELE 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1232 QLiKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLST-QRAKLQTENSELSRQLEEKEAFINQLTRGKltYTQQLEDL 1310
Cdd:COG4717 464 QL-EEDGELAELLQELEELKAELRELAEEWAALKLALELlEEAREEYREERLPPVLERASEYFSRLTDGR--YRLIRIDE 540
|
....*
gi 2163567613 1311 KRQLE 1315
Cdd:COG4717 541 DLSLK 545
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
931-1592 |
6.18e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 61.07 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 931 LAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDE---NITKLTKEKKILQESHQQALDDLQA 1007
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSalnELSSLEDMKNRYESEIKTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1008 EEDKVNtlakakvkleqqvdDLESSLEQEKKIRMDLERAKRklegdlklaqESIMDLENDKQQLE---ERLKKKDFELNT 1084
Cdd:PRK01156 268 ELEKNN--------------YYKELEERHMKIINDPVYKNR----------NYINDYFKYKNDIEnkkQILSNIDAEINK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1085 LNARIedeqaisaqlqKKLKELQArieeleeeleaERTGRAKVEKLRSELLQELEETSERLEEAGGATSVQLELNKKQEA 1164
Cdd:PRK01156 324 YHAII-----------KKLSVLQK-----------DYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1165 EFQKLRR---DLEEATLQHEATAATLRKKHAD---SVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKT 1238
Cdd:PRK01156 382 YSKNIERmsaFISEILKIQEIDPDAIKKELNEinvKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTT 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1239 NLEKMCRTTEDQMNEHRSKLEE----AQRTVTDLSTQRaklqtenselsRQLEEKEAFIN-QLTRGKLTYTQQLEDLKRQ 1313
Cdd:PRK01156 462 LGEEKSNHIINHYNEKKSRLEEkireIEIEVKDIDEKI-----------VDLKKRKEYLEsEEINKSINEYNKIESARAD 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1314 LEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAK-TELQRALSKansevaqwRTKYETDAIQ-RTEELEEAKKKLAQR 1391
Cdd:PRK01156 531 LEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKrTSWLNALAV--------ISLIDIETNRsRSNEIKKQLNDLESR 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1392 LQEAEEAVEAVNakcSSLEKTKHRLQNEIEDL---MADVERSNAAAAALDKKQRNFDKILSEwKQKFEESQTELEA---- 1464
Cdd:PRK01156 603 LQEIEIGFPDDK---SYIDKSIREIENEANNLnnkYNEIQENKILIEKLRGKIDNYKKQIAE-IDSIIPDLKEITSrind 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1465 SQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQK---SIHELEKVRKQLDAEKLELQAALEE 1541
Cdd:PRK01156 679 IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKikkAIGDLKRLREAFDKSGVPAMIRKSA 758
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 2163567613 1542 AEASLEHEEGKILRAQLEFNQVKADyerklaeKDEEIEQSKRNHLRVVDSL 1592
Cdd:PRK01156 759 SQAMTSLTRKYLFEFNLDFDDIDVD-------QDFNITVSRGGMVEGIDSL 802
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1443-1903 |
6.56e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.19 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1443 NFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELE 1522
Cdd:TIGR04523 128 KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1523 KVRKQLDaeklELQAALEEAEASLEHEEGKILRAQLEFNQVKAdyerKLAEKDEEIEQSKRNHLRVVDSLQtsldAETRS 1602
Cdd:TIGR04523 208 KKIQKNK----SLESQISELKKQNNQLKDNIEKKQQEINEKTT----EISNTQTQLNQLKDEQNKIKKQLS----EKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1603 RNEALRLKKKMEGDLNEMEIQLSHANRTAA-----EAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQ 1677
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1678 SELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAITDA 1757
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1758 AMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLD-------------EAEQLALKGGKKQLQKLEVRVRELENELEAE 1824
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqnlEQKQKELKSKEKELKKLNEEKKELEEKVKDL 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1825 QKRNAESIKGLRKSERRVKELSYQTEEDRKNMVRLQDLVDKLQLK--VKAYKRQAEEAEEQANSNLAKFRKVQHELDEAE 1902
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEkeIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
|
.
gi 2163567613 1903 E 1903
Cdd:TIGR04523 596 K 596
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1159-1923 |
6.74e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.51 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1159 NKKQEAEFQKLrrdLEEAT-------LQHEA-------TAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELD 1224
Cdd:PRK04863 252 TQSDRDLFKHL---ITESTnyvaadyMRHANerrvhleEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQ 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1225 DVNSNTEQLIKAKTNL---EKMCRTTEDqMNEHRSKLEEAQRTVTDLSTQRAklqtensELSRQLEEKEAFINQLtRGKL 1301
Cdd:PRK04863 329 DYQAASDHLNLVQTALrqqEKIERYQAD-LEELEERLEEQNEVVEEADEQQE-------ENEARAEAAEEEVDEL-KSQL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1302 TYTQQLEDLkrqLEEEAKAKNALAHALQSAQHDCDLlreqyeeemeaktelqRALSKANseVAQWRTKYETDAIQRTEEL 1381
Cdd:PRK04863 400 ADYQQALDV---QQTRAIQYQQAVQALERAKQLCGL----------------PDLTADN--AEDWLEEFQAKEQEATEEL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1382 EEakkkLAQRLQEAEEAVEAVNAKCSSLEKtkhrlqneiedLMADVERSNAAAAALDK-----KQRNFDKILSEWKQKFE 1456
Cdd:PRK04863 459 LS----LEQKLSVAQAAHSQFEQAYQLVRK-----------IAGEVSRSEAWDVARELlrrlrEQRHLAEQLQQLRMRLS 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1457 ESQTELEaSQKEARSLSTELFKLKNAYEESLEHLETFKREnknLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQ 1536
Cdd:PRK04863 524 ELEQRLR-QQQRAERLLAEFCKRLGKNLDDEDELEQLQEE---LEARLESLSESVSEARERRMALRQQLEQLQARIQRLA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1537 A---ALEEAEASLEHeegkiLRAQ-----------LEFNQVKADYERKLAEKDEEIEQSKRNHLRVVDSLQTsldAETRS 1602
Cdd:PRK04863 600 ArapAWLAAQDALAR-----LREQsgeefedsqdvTEYMQQLLERERELTVERDELAARKQALDEEIERLSQ---PGGSE 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1603 RNEALRLKKKMEGDL-NEM--EIQLSHANRTAA---------------EAQKQVKALQGYLKDTQL------QLDDVVRA 1658
Cdd:PRK04863 672 DPRLNALAERFGGVLlSEIydDVSLEDAPYFSAlygparhaivvpdlsDAAEQLAGLEDCPEDLYLiegdpdSFDDSVFS 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1659 NEDLKENIAIVERRNNLLQSELEEL----RA----MVEQSERARKLAEQELIEASERVQL---LHSQNTSLINQKKKM-- 1725
Cdd:PRK04863 752 VEELEKAVVVKIADRQWRYSRFPEVplfgRAarekRIEQLRAEREELAERYATLSFDVQKlqrLHQAFSRFIGSHLAVaf 831
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1726 ----EADISQLQT---EVEEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERmkKNMEQTVKDLQLRLDEAEQL 1798
Cdd:PRK04863 832 eadpEAELRQLNRrrvELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD--ETLADRVEEIREQLDEAEEA 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1799 A--LKGGKKQLQKLEVRV---RELENELEAEQKRNAESIKGLRKSERRVKELSYQTE-------EDRKNMV-RLQDLVDK 1865
Cdd:PRK04863 910 KrfVQQHGNALAQLEPIVsvlQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfsyEDAAEMLaKNSDLNEK 989
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 2163567613 1866 LQLKVKAYKRQAEEAEEQANSNLAKFRKVQHELDEAEERADMAESQVNKLRARSRDIG 1923
Cdd:PRK04863 990 LRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLG 1047
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1645-1892 |
9.04e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 9.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1645 LKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQELIEASERVQllhsqntSLINQKKK 1724
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1725 MEADISQLQTEVEEAIqecRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQL--ALKG 1802
Cdd:COG4942 95 LRAELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALraELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1803 GKKQLQKLEVRVRELENELEAEQKRNAESIKGLRKSErrvKELSYQTEEDRKNMVRLQDLVDKLQlkvkayKRQAEEAEE 1882
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLE------AEAAAAAER 242
|
250
....*....|
gi 2163567613 1883 QANSNLAKFR 1892
Cdd:COG4942 243 TPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1464-1708 |
1.14e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1464 ASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAE 1543
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1544 ASLEHEEGKILRaqlefnQVKADYerklaekdeeiEQSKRNHLRVVDSLQTSLDAETRSRNEAlRLKKKMEGDLNEMEIQ 1623
Cdd:COG4942 97 AELEAQKEELAE------LLRALY-----------RLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1624 LSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQELIE 1703
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
....*
gi 2163567613 1704 ASERV 1708
Cdd:COG4942 239 AAERT 243
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1310-1703 |
1.26e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 59.52 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1310 LKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVaqwrtkyETDAIQRTEELEEAKKKLA 1389
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAEL-------KEELRQSREKHEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1390 QRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEE---SQTELEASQ 1466
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAErkqLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1467 KEARSLSTELFKLKNAYEESLEHLETfkrenknLQEEILDLTEQLGASQKSIHELEKVRKqldaeklELQAALEEAEASL 1546
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLTTAHRKEAENEALLE-------ELRSLQERLNASE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1547 EHEEGkilraqlefnqVKADYERKLAEKDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSH 1626
Cdd:pfam07888 251 RKVEG-----------LGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1627 ANRTAAEAQKQVKALQGylKDTQLQLDDVVRANEDLKENIAIVERRNnllqsELEELRA--MVEQSERARKLAE-QELIE 1703
Cdd:pfam07888 320 IEKLSAELQRLEERLQE--ERMEREKLEVELGREKDCNRVQLSESRR-----ELQELKAslRVAQKEKEQLQAEkQELLE 392
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1235-1465 |
1.59e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1235 KAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQL 1314
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1315 EEEakaKNALAHALQSAQHdcdLLREQYEEEMEAKTELQRALSKAN--SEVAQWRTKYETDAIQRTEELEEAKKKLAQRL 1392
Cdd:COG4942 100 EAQ---KEELAELLRALYR---LGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2163567613 1393 QEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEAS 1465
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1284-1922 |
1.76e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.65 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1284 RQLEEKeafINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEV 1363
Cdd:TIGR04523 36 KQLEKK---LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1364 A---QWRTKYETDAIQRTEELEEAKKKLAQRLQE---AEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAAL 1437
Cdd:TIGR04523 113 KndkEQKNKLEVELNKLEKQKKENKKNIDKFLTEikkKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1438 DKKQRNFDKILS---EWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGAS 1514
Cdd:TIGR04523 193 KNKLLKLELLLSnlkKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1515 QKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLEfnqvkaDYERKLAEKDEEIEQSKRNHLRVVDSLQT 1594
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELK------NQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1595 SLDAETRSRNEALRLKKKmegdLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNN 1674
Cdd:TIGR04523 347 LKKELTNSESENSEKQRE----LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1675 LLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAI 1754
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1755 TDAAMMAEELKK-EQDTSAHLERMKK-NMEQTVKDLQLRLDEAEQLALKGGKKQlQKLEVRVRELENELEaEQKRNAESI 1832
Cdd:TIGR04523 503 EEKKELEEKVKDlTKKISSLKEKIEKlESEKKEKESKISDLEDELNKDDFELKK-ENLEKEIDEKNKEIE-ELKQTQKSL 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1833 KglrKSERRVKELSYQTEEDRKNMVRLQDLVDKLQLKVkayKRQAEEAEEQANSNLAKFRKVQHELDEAEERADMAESQV 1912
Cdd:TIGR04523 581 K---KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL---EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
650
....*....|
gi 2163567613 1913 NKLRARSRDI 1922
Cdd:TIGR04523 655 KEIRNKWPEI 664
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1485-1926 |
1.80e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1485 ESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLEFNQVK 1564
Cdd:PTZ00121 1061 EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR 1140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1565 ADYERKLAEKDEEIEQSKRnhlrvvdsLQTSLDAETRSRNEAlrlKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGy 1644
Cdd:PTZ00121 1141 KAEEARKAEDAKRVEIARK--------AEDARKAEEARKAED---AKKAEAARKAEEVRKAEELRKAEDARKAEAARKA- 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1645 lkDTQLQLDDVVRANEDLKenIAIVERrnnllqseLEELRAMVEQSERARKLAEQELIEASERVQLLH-SQNTSLINQKK 1723
Cdd:PTZ00121 1209 --EEERKAEEARKAEDAKK--AEAVKK--------AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHfARRQAAIKAEE 1276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1724 KMEADISQLQTEVEEA-----IQECRNAEEKAKKA-----ITDAAMMAEELKKEQDTSAH-LERMKKNMEQTVKDLQLRL 1792
Cdd:PTZ00121 1277 ARKADELKKAEEKKKAdeakkAEEKKKADEAKKKAeeakkADEAKKKAEEAKKKADAAKKkAEEAKKAAEAAKAEAEAAA 1356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1793 DEAEQLALKGGKKQLQKLEVRVRELENELEAEQKRNAESIKGLRKSERRVKELSYQTEEDRKNMVRLQDLVDKLQlKVKA 1872
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADE 1435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2163567613 1873 YKRQAEEAE--EQANSNLAKFRKVQHELDEAEERADMAESQVNKLRARSRDIGAKK 1926
Cdd:PTZ00121 1436 AKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1627-1909 |
2.05e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1627 ANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKlaeqELIEASE 1706
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1707 RVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKaitdaammAEELKKEQDTSAHLERMKKNMEQTVK 1786
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE--------LKELKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1787 DLQLRLDEAEQLaLKGGKKQLQKLE---VRVRELENELEAEQKRNAESIKGLRKSER-RVKELSYQTEEDRKNMVRLQDL 1862
Cdd:PRK03918 311 EIEKRLSRLEEE-INGIEERIKELEekeERLEELKKKLKELEKRLEELEERHELYEEaKAKKEELERLKKRLTGLTPEKL 389
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2163567613 1863 VDKLQLKVKAyKRQAEEAEEQANSNLAKFRKVQHELDEAEERADMAE 1909
Cdd:PRK03918 390 EKELEELEKA-KEEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
935-1289 |
2.78e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 58.75 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 935 KRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEkkilQESHQQALDDLqaeEDKVNT 1014
Cdd:pfam07888 68 REQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQ----RAAHEARIREL---EEDIKT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1015 LAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQA 1094
Cdd:pfam07888 141 LTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1095 ISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELlqeleetserleeaggatSVQLELNKKQEAEFQKLRRDLE 1174
Cdd:pfam07888 221 KLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL------------------SSMAAQRDRTQAELHQARLQAA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1175 EATLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQMNEH 1254
Cdd:pfam07888 283 QLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSES 362
|
330 340 350
....*....|....*....|....*....|....*...
gi 2163567613 1255 RSKLEEAQRTVTDLSTQRAKLQTENSEL---SRQLEEK 1289
Cdd:pfam07888 363 RRELQELKASLRVAQKEKEQLQAEKQELleyIRQLEQR 400
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1305-1770 |
2.87e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1305 QQLEDLKRQLEEEAKAKnalaHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWrtkyetDAIQRTEELEEA 1384
Cdd:COG4717 71 KELKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL------PLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1385 KKKLAQRLQEAEEAVEAVnakcsslektkHRLQNEIEDLMADVERSNAAAAALdkkqrnFDKILSEWKQKFEESQTELEA 1464
Cdd:COG4717 141 LAELPERLEELEERLEEL-----------RELEEELEELEAELAELQEELEEL------LEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1465 SQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQ-EEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAE 1543
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAAlEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1544 ASLEHEEGKILRAQLEFNQVKADYERKLAEKDEEIEQSKR--NHLRVVDSLQTSLDAETRSRNEALR-LKKKMEGDLNEM 1620
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEEllAALGLPPDLSPEELLELLDRIEELQeLLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1621 EIQLSHANRTAAEAQKQVKALQGYlkdtqLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLA--E 1698
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEEL-----RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEelE 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163567613 1699 QELIEASERVQLLHSQNTSLINQKKKMEAD--ISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKKEQDT 1770
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1028-1903 |
2.94e-08 |
|
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: 59.29 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1028 DLESSLEQEKKIRMDLERAKrklegDLKLAQESIMDLENDK--------QQLEERLKKKDFElntlnaRIEDEQAISAQL 1099
Cdd:TIGR01612 484 DIDENSKQDNTVKLILMRMK-----DFKDIIDFMELYKPDEvpskniigFDIDQNIKAKLYK------EIEAGLKESYEL 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1100 QKKLKELQARIEELEEELEAertgraKVEKLRSELLQELEETSERLEEAGGATSVQLELNKK-----QEAEFQKLRRDLE 1174
Cdd:TIGR01612 553 AKNWKKLIHEIKKELEEENE------DSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKiknisDKNEYIKKAIDLK 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1175 EATLQHEATAATLRKKhadSVAELSEQLDNLQRVKQKLEKEKSEL-KLELDDVNSNTEQLIKaktnlEKMCRTTEDQ--M 1251
Cdd:TIGR01612 627 KIIENNNAYIDELAKI---SPYQVPEHLKNKDKIYSTIKSELSKIyEDDIDALYNELSSIVK-----ENAIDNTEDKakL 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1252 NEHRSKLEEAQRTVTDLSTQRAKL-----QTENSELSRQLEEKEAFINQLTRGKLTYTqqLEDLKRQLEEEAKAKNALAh 1326
Cdd:TIGR01612 699 DDLKSKIDKEYDKIQNMETATVELhlsniENKKNELLDIIVEIKKHIHGEINKDLNKI--LEDFKNKEKELSNKINDYA- 775
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1327 alqsaqhdcdllreQYEEEmeaktelqraLSKANSEVAQWRTKY-ETDAIQRTEElEEAKkklaQRLQEAEEAVEAVNAK 1405
Cdd:TIGR01612 776 --------------KEKDE----------LNKYKSKISEIKNHYnDQINIDNIKD-EDAK----QNYDKSKEYIKTISIK 826
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1406 CSSLEKTKHRLQNEIEDLMADVER----SNAAAAALDKKQRNFDKILSEWKQKFEESQ-TELEASQKEARSLSTELfklK 1480
Cdd:TIGR01612 827 EDEIFKIINEMKFMKDDFLNKVDKfinfENNCKEKIDSEHEQFAELTNKIKAEISDDKlNDYEKKFNDSKSLINEI---N 903
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1481 NAYEESLEHLETFKREN------KNLQEEILD-------LTEQLGASQKSIHELEKVRK----QLDAEKLELQAALEEA- 1542
Cdd:TIGR01612 904 KSIEEEYQNINTLKKVDeyikicENTKESIEKfhnkqniLKEILNKNIDTIKESNLIEKsykdKFDNTLIDKINELDKAf 983
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1543 -EASLEHEEGKILRAQLEFNQVKADY----ERKLAEKDEEIEQSKRNHLR----------------------VVDSLQTS 1595
Cdd:TIGR01612 984 kDASLNDYEAKNNELIKYFNDLKANLgknkENMLYHQFDEKEKATNDIEQkiedanknipnieiaihtsiynIIDEIEKE 1063
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1596 LDAETRSRN-EALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKalqgYLKDTQLQLDDVVRANEDLKENIAIVERRNN 1674
Cdd:TIGR01612 1064 IGKNIELLNkEILEEAEINITNFNEIKEKLKHYNFDDFGKEENIK----YADEINKIKDDIKNLDQKIDHHIKALEEIKK 1139
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1675 LLQSELEELRAMVEQSER-ARKLAEQELIEASERVQllhsQN-TSLINQKKKMEADISQLQTEVEEaIQECRNAEEKAKK 1752
Cdd:TIGR01612 1140 KSENYIDEIKAQINDLEDvADKAISNDDPEEIEKKI----ENiVTKIDKKKNIYDEIKKLLNEIAE-IEKDKTSLEEVKG 1214
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1753 -----AITDAAMMAEELKKEQDTSAHlerMKKNMEQTVKDLQLRLDEAEQLALKGGKKQLQKLEVRVRELENELEAE--- 1824
Cdd:TIGR01612 1215 inlsyGKNLGKLFLEKIDEEKKKSEH---MIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDhhi 1291
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1825 -QKRNAESIKGLRKSERRVKELSYQTEEdrknmvrLQDLVDKLQLKVKAYKRQAEEAEEQANS-----NLAKFRKVQHEL 1898
Cdd:TIGR01612 1292 iSKKHDENISDIREKSLKIIEDFSEESD-------INDIKKELQKNLLDAQKHNSDINLYLNEianiyNILKLNKIKKII 1364
|
....*
gi 2163567613 1899 DEAEE 1903
Cdd:TIGR01612 1365 DEVKE 1369
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1432-1672 |
3.29e-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: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1432 AAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESlehletfKRENKNLQEEILDLTEQL 1511
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL-------ARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1512 GASQKSIHELekvRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLEFNQV--KADYERKLAEKDEEIeqskrnhlrvV 1589
Cdd:COG4942 86 AELEKEIAEL---RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrRLQYLKYLAPARREQ----------A 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1590 DSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIV 1669
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
...
gi 2163567613 1670 ERR 1672
Cdd:COG4942 233 EAE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1610-1843 |
3.62e-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: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1610 KKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVE- 1688
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1689 -QSERARKLAEQELIEASERVQ-LLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKK 1766
Cdd:COG4942 102 qKEELAELLRALYRLGRQPPLAlLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2163567613 1767 EQDTS-AHLERMKKNMEQTVKDLQLRLDEAEQLAlkggkKQLQKLEVRVRELENELEAEQKRNAESIKGLRKSERRVK 1843
Cdd:COG4942 182 ELEEErAALEALKAERQKLLARLEKELAELAAEL-----AELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
964-1197 |
3.85e-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: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 964 HATENKVKNLTEEMAGLDENITKLTKEKKILQESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSL----EQEKKI 1039
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1040 RMDLERAKRKLEGDLKLAQESimdleNDKQQLEERLKKKDFelNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEA 1119
Cdd:COG4942 96 RAELEAQKEELAELLRALYRL-----GRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2163567613 1120 ERTGRAKVEklrsELLQELEETSERLEEAGGATSVQLELNKKQEAEFQKLRRDLEEATLQHEATAATLRKKHADSVAE 1197
Cdd:COG4942 169 LEAERAELE----ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1446-1690 |
4.05e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1446 KILSEWKQKFEESQTEL--EASQKEARSLSTELFKLKNAYEESLEHLETFKRENKnlqeeILDLTEQLGASQKSIHELEK 1523
Cdd:COG3206 152 AVANALAEAYLEQNLELrrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1524 VRKQLDAEKLELQAALEEAEASLEHEEGKI--LRAQLEFNQVKADYERKLAEKDEEIEQSKRNHLRVVdSLQTSLDA-ET 1600
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDALpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVI-ALRAQIAAlRA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1601 RSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQgylkDTQLQLddvvranEDLKENIAIVERRNNLLQSEL 1680
Cdd:COG3206 306 QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELP----ELEAEL-------RRLEREVEVARELYESLLQRL 374
|
250
....*....|
gi 2163567613 1681 EELRAMVEQS 1690
Cdd:COG3206 375 EEARLAEALT 384
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1501-1724 |
7.51e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1501 QEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLEFNQVkadyERKLAEKDEEIEQ 1580
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL----EAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1581 SKRNHLRVVDSLQTSLDA-ETRSRNEALRLKKKMEgDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRAN 1659
Cdd:COG4942 95 LRAELEAQKEELAELLRAlYRLGRQPPLALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2163567613 1660 EDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKK 1724
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1041-1570 |
7.93e-08 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 57.35 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1041 MDLERAKRKLEgDLKLaqesimDLEndKQQLEERLKKKDFELNTLNARiEDEQAI----SAQLQKKLKELQARIEELEEE 1116
Cdd:pfam05701 70 EELESTKRLIE-ELKL------NLE--RAQTEEAQAKQDSELAKLRVE-EMEQGIadeaSVAAKAQLEVAKARHAAAVAE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1117 LEAERTGRAKVEKLRSELLQELEETSERLEEAGGATsvqlelnkkQEAEfqklrRDLEEATLQHEATAATLRKKHADSV- 1195
Cdd:pfam05701 140 LKSVKEELESLRKEYASLVSERDIAIKRAEEAVSAS---------KEIE-----KTVEELTIELIATKESLESAHAAHLe 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1196 AELSEQLDNLQRVKQKLEKEKsELKLELDDVNSNTEQLIKAKtnlekmcrttedqmnEHRSKLEEAQRTVTDLSTQRAKL 1275
Cdd:pfam05701 206 AEEHRIGAALAREQDKLNWEK-ELKQAEEELQRLNQQLLSAK---------------DLKSKLETASALLLDLKAELAAY 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1276 QTENSELSRQLEEKEAFINQLTRGKLTYTQ-QLEDLKRQLE---EEAKAKNALAHALQS----AQHDCDLLREQYEEEME 1347
Cdd:pfam05701 270 MESKLKEEADGEGNEKKTSTSIQAALASAKkELEEVKANIEkakDEVNCLRVAAASLRSelekEKAELASLRQREGMASI 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1348 AKTELQRALSKANSEVAQWRTKyETDAiqrTEELEEAKKKLAQRLQEAEEA-----------------VEAVNAKCSSLE 1410
Cdd:pfam05701 350 AVSSLEAELNRTKSEIALVQAK-EKEA---REKMVELPKQLQQAAQEAEEAkslaqaareelrkakeeAEQAKAAASTVE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1411 KTKHRLQNEIEDLMADVERSNAAAAALdkkqrnfdkilsewkqkfEESQTELEASQKEARSLSTELfKLKNAYEESLEHL 1490
Cdd:pfam05701 426 SRLEAVLKEIEAAKASEKLALAAIKAL------------------QESESSAESTNQEDSPRGVTL-SLEEYYELSKRAH 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1491 ETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEaslEHEEGKiLRAQLEFNQVKADYERK 1570
Cdd:pfam05701 487 EAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEERKEALKIALEKAE---KAKEGK-LAAEQELRKWRAEHEQR 562
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1231-1879 |
8.20e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 57.50 E-value: 8.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1231 EQLIKAKTNLEKMcrttEDQMNEHRSKLEEAQRTVTDlSTQrAKLQTENSELSRQLEEKEAFiNQLTRGKLTYTQQLEDL 1310
Cdd:PRK10246 191 EQHKSARTELEKL----QAQASGVALLTPEQVQSLTA-SLQ-VLTDEEKQLLTAQQQQQQSL-NWLTRLDELQQEASRRQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1311 KRQL---EEEAKAKNALAhALQSAQhDCDLLREQYEEEMEAKTELQRALSKANS------EVAQWRTKYETDAIQRTEEL 1381
Cdd:PRK10246 264 QALQqalAAEEKAQPQLA-ALSLAQ-PARQLRPHWERIQEQSAALAHTRQQIEEvntrlqSTMALRARIRHHAAKQSAEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1382 EEAKKKLAQRLQEAE------EAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNA------------AAAALDK--KQ 1441
Cdd:PRK10246 342 QAQQQSLNTWLAEHDrfrqwnNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNAlpaitltltadeVAAALAQhaEQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1442 RNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKnayeeslEHLETFKRENKNLQEEILDLtEQLGASQKSIHEL 1521
Cdd:PRK10246 422 RPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRN-------AALNEMRQRYKEKTQQLADV-KTICEQEARIKDL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1522 EKVRKQLDAEK------------------LEL------QAALEEAEASLEhEEGKILRAQLE--FNQVKADYE--RKLAE 1573
Cdd:PRK10246 494 EAQRAQLQAGQpcplcgstshpaveayqaLEPgvnqsrLDALEKEVKKLG-EEGAALRGQLDalTKQLQRDESeaQSLRQ 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1574 KDEEIEQSKRN-------HLRVVDSLQTSLDAETRSRNEALRLKKKMEgdlneMEIQLSHANRTAAEAQKQVKALQGYLK 1646
Cdd:PRK10246 573 EEQALTQQWQAvcaslniTLQPQDDIQPWLDAQEEHERQLRLLSQRHE-----LQGQIAAHNQQIIQYQQQIEQRQQQLL 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1647 DTQLQLDDVVRANEDlkENIAIVER------------RNNLLQSELEELRAMVE-------QSERARKLAEQELIEASER 1707
Cdd:PRK10246 648 TALAGYALTLPQEDE--EASWLATRqqeaqswqqrqnELTALQNRIQQLTPLLEtlpqsddLPHSEETVALDNWRQVHEQ 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1708 VQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKaitdAAMMAEElkkeqdTSAHLERMKKNMEQtvkd 1787
Cdd:PRK10246 726 CLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFL----AALLDEE------TLTQLEQLKQNLEN---- 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1788 lqlRLDEAEQLALKGGKKQLQKLEVRVRELENELEAE--QKRNAESIKGLRKSERRVKELSYQTEEDRKNMVRLQDLVdk 1865
Cdd:PRK10246 792 ---QRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEqiQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALM-- 866
|
730
....*....|....
gi 2163567613 1866 lqLKVKAYKRQAEE 1879
Cdd:PRK10246 867 --QQIAQATQQVED 878
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1338-1623 |
9.02e-08 |
|
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: 57.44 E-value: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1338 LREQYEE---EMEAKTELQRALSKANSEVAQWRTKY---ETDAIQRTEELE----EAKKKLAQRLQEAEEAVEAvnAKCS 1407
Cdd:pfam17380 301 LRQEKEEkarEVERRRKLEEAEKARQAEMDRQAAIYaeqERMAMERERELErirqEERKRELERIRQEEIAMEI--SRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1408 SLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQtelEASQKEARSLStelfklknayEESL 1487
Cdd:pfam17380 379 ELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLE----------EERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1488 EHLETFKRENKNLQEEILDLTEQLGASQKSIHELEK-VRKQLDAEKLE---LQAALEEAEASLEHEEGK--ILRAQLEFN 1561
Cdd:pfam17380 446 REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKeKRDRKRAEEQRrkiLEKELEERKQAMIEEERKrkLLEKEMEER 525
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163567613 1562 Q--VKADYERKLAEKDEEIEQSKRNHLRVVDSLQTSldAETRSRNEALRLKKKMEGDLNEMEIQ 1623
Cdd:pfam17380 526 QkaIYEEERRREAEEERRKQQEMEERRRIQEQMRKA--TEERSRLEAMEREREMMRQIVESEKA 587
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1123-1423 |
9.13e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 57.65 E-value: 9.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1123 GRAKVEKLRSELLQELEETSERLEEAggATSVQlelnkkqeaEFQKLRRDLEEATLQH---------EATAATLRKKHAD 1193
Cdd:COG3096 779 GRAAREKRLEELRAERDELAEQYAKA--SFDVQ---------KLQRLHQAFSQFVGGHlavafapdpEAELAALRQRRSE 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1194 SVAELSEQLDNLQRVKQKLEKEKSELKL--------ELDDVNSNTEQLIKAKTNLEKmCRTTEDQMNEHRSKLEEAQRTV 1265
Cdd:COG3096 848 LERELAQHRAQEQQLRQQLDQLKEQLQLlnkllpqaNLLADETLADRLEELREELDA-AQEAQAFIQQHGKALAQLEPLV 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1266 TDLST---QRAKLQTENSELSRQLEEKEAFINQLT-----RGKLTYtqqlEDLKRQLEEEAKAKNALAHALQSAQHDCDL 1337
Cdd:COG3096 927 AVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALSevvqrRPHFSY----EDAVGLLGENSDLNEKLRARLEQAEEARRE 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1338 LREQYEEEMEAKTELQRALSKANSevaQWRTKYET--DAIQRTEELE-----EAKKKLAQRLQEAEEAVEAVNAKCSSLE 1410
Cdd:COG3096 1003 AREQLRQAQAQYSQYNQVLASLKS---SRDAKQQTlqELEQELEELGvqadaEAEERARIRRDELHEELSQNRSRRSQLE 1079
|
330
....*....|...
gi 2163567613 1411 KTKHRLQNEIEDL 1423
Cdd:COG3096 1080 KQLTRCEAEMDSL 1092
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
29-69 |
1.22e-07 |
|
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: 49.74 E-value: 1.22e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2163567613 29 LCFVPHPQLEFIRARVTARAGNGVTVTTEMGETLTVPEADV 69
Cdd:pfam02736 5 LVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
940-1147 |
1.35e-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: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 940 DECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEkkilqeshqqalddLQAEEDKVNTLAKAK 1019
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR--------------IRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1020 VKLEQQVDDLESSLEQEKKIRMDLERAKRKLEG----DLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQAI 1095
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2163567613 1096 SAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEE 1147
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
828-1249 |
1.48e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 56.38 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 828 YFKIKPLLKSAE-----TEKEMQTMKEEFGHLKEALEKSEARRKELEEKMvsmlqekNDLQLQVQAEQDNLADAEErcdq 902
Cdd:PRK04778 100 FRKAKHEINEIEslldlIEEDIEQILEELQELLESEEKNREEVEQLKDLY-------RELRKSLLANRFSFGPALD---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 903 liknkiQLEAKVKEMTERLEEEEEMNAE---LAAKK--RKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKN----L 973
Cdd:PRK04778 169 ------ELEKQLENLEEEFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 974 TEEMAGLDENitKLTKEKKILQESHQQALDDLqaEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGD 1053
Cdd:PRK04778 243 VEEGYHLDHL--DIEKEIQDLKEQIDENLALL--EELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1054 LKLAQEsimdlENDKQQLE-ERLKKKdFELNtlnariEDEQAISAQLQKKLKELQARIEELEEELeaertgrAKVEKLRS 1132
Cdd:PRK04778 319 LEHAKE-----QNKELKEEiDRVKQS-YTLN------ESELESVRQLEKQLESLEKQYDEITERI-------AEQEIAYS 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1133 ELLQELEETSERLEEAggatsvqlelnKKQEAEFQKLRRDLEEATLQHEATAATLRKKHADSV------------AELSE 1200
Cdd:PRK04778 380 ELQEELEEILKQLEEI-----------EKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKryleksnlpglpEDYLE 448
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2163567613 1201 QLDNLQRVKQKLEKEKSELKLELDDVNSnteQLIKAKTNLEKMCRTTED 1249
Cdd:PRK04778 449 MFFEVSDEIEALAEELEEKPINMEAVNR---LLEEATEDVETLEEETEE 494
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1255-1470 |
1.49e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1255 RSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEE--KEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHALQSAQ 1332
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1333 HDCDLLREQYEEEMEAKT--ELQRALSKANSEVAQWRTKYETD--AIQRT-EELEEAKKKLAQRLQEAEEAVEAVNAkcs 1407
Cdd:COG3206 247 AQLGSGPDALPELLQSPViqQLRAQLAELEAELAELSARYTPNhpDVIALrAQIAALRAQLQQEAQRILASLEAELE--- 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163567613 1408 SLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFD---KILSEWKQKFEESQTELEASQKEAR 1470
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEvarELYESLLQRLEEARLAEALTVGNVR 389
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1391-1559 |
1.56e-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: 54.55 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1391 RLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEA--SQKE 1468
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1469 ARSLSTELfklknayeeslehlETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEh 1548
Cdd:COG1579 91 YEALQKEI--------------ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE- 155
|
170
....*....|.
gi 2163567613 1549 EEGKILRAQLE 1559
Cdd:COG1579 156 AELEELEAERE 166
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1347-1583 |
1.70e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1347 EAKTELQRALSKANSEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMAD 1426
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAE--------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1427 VERSNAAaaaLDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILD 1506
Cdd:COG4942 92 IAELRAE---LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163567613 1507 LTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQlefnQVKADYERKLAEKDEEIEQSKR 1583
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEAEAAAAAE 241
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
835-1330 |
2.13e-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: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 835 LKSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEkndlqlqvqaeqdnladaeercdqliKNKIQLEAKV 914
Cdd:TIGR00618 442 LCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQE--------------------------TRKKAVVLAR 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 915 KEmterleeeeemnaELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKhATENKVKNLTEEMAGLDENITKLTKEKKIL 994
Cdd:TIGR00618 496 LL-------------ELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ-RGEQTYAQLETSEEDVYHQLTSERKQRASL 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 995 QESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDL----ESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQ 1070
Cdd:TIGR00618 562 KEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLqdltEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQEL 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1071 LEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTG-----RAKVEKLRSELLQELEETSERL 1145
Cdd:TIGR00618 642 ALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYwkemlAQCQTLLRELETHIEEYDREFN 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1146 EEAGGATSVQLELNKKQEAEFQKLRRDLEEATLQHEATAATLRKKHADSVAEL--SEQLDNLQRVKQKLEKEKSELKLEL 1223
Cdd:TIGR00618 722 EIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALqtGAELSHLAAEIQFFNRLREEDTHLL 801
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1224 DDVNSNTEQLIKAKTN-LEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQtENSELSRQLEEKEAFINQLTrGKLT 1302
Cdd:TIGR00618 802 KTLEAEIGQEIPSDEDiLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYE-ECSKQLAQLTQEQAKIIQLS-DKLN 879
|
490 500 510
....*....|....*....|....*....|...
gi 2163567613 1303 YTQQL-----EDLKRQLEEEAKAKNALAHALQS 1330
Cdd:TIGR00618 880 GINQIkiqfdGDALIKFLHEITLYANVRLANQS 912
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1462-1918 |
2.36e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1462 LEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEE 1541
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1542 AEASLEHEEGkilraqlefnqvkadyERKLAEKDEEIEQskrnhlrvvdslqtsLDAETRSRNEALRLKKKMEGDLNEME 1621
Cdd:COG4717 128 LPLYQELEAL----------------EAELAELPERLEE---------------LEERLEELRELEEELEELEAELAELQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1622 IQLSHANRTAAEAQKQvkalqgYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQEL 1701
Cdd:COG4717 177 EELEELLEQLSLATEE------ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1702 IEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKK 1779
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1780 NMEQTVKDLQLRLDEAEQLALKGGKKQLQKLEVRVRELENELEAE-QKRNAESIKGLRKS----------ERRVKELSYQ 1848
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlAEAGVEDEEELRAAleqaeeyqelKEELEELEEQ 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163567613 1849 TEEDRKNMVRLQDLVDKLQLKVKA--YKRQAEEAEEQANSNLAKFRKVQHELDEAEE--RADMAESQVNKLRAR 1918
Cdd:COG4717 411 LEELLGELEELLEALDEEELEEELeeLEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELEELKAE 484
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1379-1910 |
2.77e-07 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 55.42 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1379 EELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKhrlqNEIEDLMADVERsnaaaAALDKKQRNFDKILSewKQKFEEs 1458
Cdd:pfam05701 42 LELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTK----RLIEELKLNLER-----AQTEEAQAKQDSELA--KLRVEE- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1459 qTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDL-TEQLGASQK------SIHELEKVRKQLDAE 1531
Cdd:pfam05701 110 -MEQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLvSERDIAIKRaeeavsASKEIEKTVEELTIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1532 KLELQAALEEAEAS-LEHEEGKIlRAQLEFNQVKADYERKLAEKDEEIEQSkRNHLRVVDSLQTSLDAetrsrNEALRLK 1610
Cdd:pfam05701 189 LIATKESLESAHAAhLEAEEHRI-GAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKLET-----ASALLLD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1611 KK------MEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLkdtqlqlddvvranEDLKENIAIVERRNNLLQSELEELR 1684
Cdd:pfam05701 262 LKaelaayMESKLKEEADGEGNEKKTSTSIQAALASAKKEL--------------EEVKANIEKAKDEVNCLRVAAASLR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1685 AMVEQserarklaeqeliEASERVQLLHSQNTSLINqkkkmeadISQLQTEVEEAIQECRNAEEKAKKAitdAAMMAEEL 1764
Cdd:pfam05701 328 SELEK-------------EKAELASLRQREGMASIA--------VSSLEAELNRTKSEIALVQAKEKEA---REKMVELP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1765 KKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlalkgGKKQLQKLEVRVRELENELEA---EQKRNAESIKGLRKSErr 1841
Cdd:pfam05701 384 KQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQ-----AKAAASTVESRLEAVLKEIEAakaSEKLALAAIKALQESE-- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1842 vKELSYQTEEDRKNMV------------RLQDLVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKVQHELDE-------AE 1902
Cdd:pfam05701 457 -SSAESTNQEDSPRGVtlsleeyyelskRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEErkealkiAL 535
|
....*...
gi 2163567613 1903 ERADMAES 1910
Cdd:pfam05701 536 EKAEKAKE 543
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1248-1404 |
3.14e-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: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1248 EDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTrgkltytQQLEDLKRQLEEEAKAK--NALA 1325
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE-------ARIKKYEEQLGNVRNNKeyEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163567613 1326 HALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNA 1404
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1491-1918 |
4.00e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1491 ETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDaeklELQAALEEAEASLEHEEgkILRAQLEFNQVKADYERK 1570
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE----ELEAELEELREELEKLE--KLLQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1571 LAEKDEEIEQskrnhlrvvdslqtsLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQvkalqgYLKDTQL 1650
Cdd:COG4717 141 LAELPERLEE---------------LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE------ELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1651 QLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADIS 1730
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1731 QLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQLQ 1808
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1809 KLEVRVRELENELEAE-QKRNAESIKGLRKS----------ERRVKELSYQTEEDRKNMVRLQDLVDKLQLKVKA--YKR 1875
Cdd:COG4717 360 EEELQLEELEQEIAALlAEAGVEDEEELRAAleqaeeyqelKEELEELEEQLEELLGELEELLEALDEEELEEELeeLEE 439
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2163567613 1876 QAEEAEEQANSNLAKFRKVQHE---------LDEAEERADMAESQVNKLRAR 1918
Cdd:COG4717 440 ELEELEEELEELREELAELEAEleqleedgeLAELLQELEELKAELRELAEE 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1650-1927 |
4.21e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1650 LQLDDVVRANEDLKENIAIVERRnnllQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADI 1729
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRR----IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1730 SQLQtEVEEAIQECRNAEEKAKKaitDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDL-QLRLDEAEQLALKGGKKQLQ 1808
Cdd:PRK03918 231 KELE-ELKEEIEELEKELESLEG---SKRKLEEKIRELEERIEELKKEIEELEEKVKELkELKEKAEEYIKLSEFYEEYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1809 KLEVRVRELENELEAEQKRNAESIKGLRKSERRVKELSYQTEEDRKNMVRLQDLVDKLQlKVKAYKRQAEEAEEQANSNl 1888
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGL- 384
|
250 260 270
....*....|....*....|....*....|....*....
gi 2163567613 1889 aKFRKVQHELDEAEERADMAESQVNKLRARSRDIGAKKG 1927
Cdd:PRK03918 385 -TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1025-1653 |
4.76e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.91 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1025 QVDDLESSLEQEKKIRMD-------LERAKRKLEGDLKLAQESIMDLENdkqqLEERLKKKDFELNTLNARIEDEQAISA 1097
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDeileinsLERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1098 QLQKKLKELQARIEELEEeleaertgraKVEKLRSEL--LQELEETSERLEEAGGATSVQLELNKKQEAEFqklrRDLEE 1175
Cdd:PRK01156 215 ITLKEIERLSIEYNNAMD----------DYNNLKSALneLSSLEDMKNRYESEIKTAESDLSMELEKNNYY----KELEE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1176 ATLQHEATAATLRKKHADSVAELSEQLDNLqrvKQKLEKEKSELKlELDDVNSNTEQLIKAKTNLEKMCRTTEDqMNEHR 1255
Cdd:PRK01156 281 RHMKIINDPVYKNRNYINDYFKYKNDIENK---KQILSNIDAEIN-KYHAIIKKLSVLQKDYNDYIKKKSRYDD-LNNQI 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1256 SKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTytqQLEDLKRQLEEEAKAKNALAHALQSAQHDC 1335
Cdd:PRK01156 356 LELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEI---DPDAIKKELNEINVKLQDISSKVSSLNQRI 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1336 DLLREQYEEemeakTELQRALSKANSEVAQWRTKYETDAIQR-TEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKH 1414
Cdd:PRK01156 433 RALRENLDE-----LSRNMEMLNGQSVCPVCGTTLGEEKSNHiINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKE 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1415 RLQNEiedlmaDVERSNAAAAALDKKQRNFDKILSEwKQKFEESQTELEASQKEARSLSTELFKLKN-AYEESLEHLETF 1493
Cdd:PRK01156 508 YLESE------EINKSINEYNKIESARADLEDIKIK-INELKDKHDKYEEIKNRYKSLKLEDLDSKRtSWLNALAVISLI 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1494 KRENKNLQEEilDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKI--LRAQLEFNQVKAD-YERK 1570
Cdd:PRK01156 581 DIETNRSRSN--EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIqeNKILIEKLRGKIDnYKKQ 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1571 LAEKDEEIEQSKRNHLRVVDS------LQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTaAEAQKQVKALQGY 1644
Cdd:PRK01156 659 IAEIDSIIPDLKEITSRINDIednlkkSRKALDDAKANRARLESTIEILRTRINELSDRINDINET-LESMKKIKKAIGD 737
|
....*....
gi 2163567613 1645 LKDTQLQLD 1653
Cdd:PRK01156 738 LKRLREAFD 746
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
832-1423 |
6.31e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 832 KPLLKSAETEKEMQTMKEEFGHLKEALEKSEARRK--ELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLI----- 904
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRleLLEAELEELRAELARLEAELERLEARLDALREELDELEaqirg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 905 ---KNKIQLEAKVkemterleeeeemnAELAAKKRKLEDECSELKKDIDDLELSLAKVEKE----KHATENKVKNLTEEM 977
Cdd:COG4913 335 nggDRLEQLEREI--------------ERLERELEERERRRARLEALLAALGLPLPASAEEfaalRAEAAALLEALEEEL 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 978 AGLDENITKLTKEKKILQEshqqALDDLQAEedkVNTLAKAKVKLEQQVDDLESSLEQEKKI------------------ 1039
Cdd:COG4913 401 EALEEALAEAEAALRDLRR----ELRELEAE---IASLERRKSNIPARLLALRDALAEALGLdeaelpfvgelievrpee 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1040 ---RMDLERAKRKL-------EGDLKLAQESImdlenDKQQLEERL---KKKDFELNTLNARIeDEQAISAQLQKKLKEL 1106
Cdd:COG4913 474 erwRGAIERVLGGFaltllvpPEHYAAALRWV-----NRLHLRGRLvyeRVRTGLPDPERPRL-DPDSLAGKLDFKPHPF 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1107 QARIEELEeeleaerTGRAKVEKLRSEllQELEETSERLEEAG----GATSVQLELNKKQEAEF----------QKLRRD 1172
Cdd:COG4913 548 RAWLEAEL-------GRRFDYVCVDSP--EELRRHPRAITRAGqvkgNGTRHEKDDRRRIRSRYvlgfdnraklAALEAE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1173 LEEATLQHeATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEK--SELKLELDDVNSNTEQLIKAKTNLEKMcrttEDQ 1250
Cdd:COG4913 619 LAELEEEL-AEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDLAAL----EEQ 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1251 MNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLT-RGKLTYTQQLEDLKRQLEEEAKAKnALAHALQ 1329
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdLARLELRALLEERFAAALGDAVER-ELRENLE 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1330 SAQHDCDLLREQYEEEMEAKteLQRALSKANSEVAQWRTKYET----DAI---QRTEELEEAKKKLAQRLQEAEEavEAV 1402
Cdd:COG4913 773 ERIDALRARLNRAEEELERA--MRAFNREWPAETADLDADLESlpeyLALldrLEEDGLPEYEERFKELLNENSI--EFV 848
|
650 660
....*....|....*....|.
gi 2163567613 1403 NAKCSSLEKTKHRLQNEIEDL 1423
Cdd:COG4913 849 ADLLSKLRRAIREIKERIDPL 869
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1320-1472 |
6.34e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.40 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1320 AKNALAHALQSAQHDCDLLREqyEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRlqeaeeaV 1399
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK-------E 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163567613 1400 EAVNAKCSSLEKTKHRLQNEIEDlmadversnaaaaaLDKKQRNFDKILSEWKQKFEESQTELEA----SQKEARSL 1472
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKE--------------LEQKQQELEKKEEELEELIEEQLQELERisglTAEEAKEI 158
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
857-1510 |
7.77e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 54.44 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 857 ALEKSEARRKE-LEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEEEEEMNAELAAKK 935
Cdd:pfam10174 46 ALRKEEAARISvLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 936 RKLEDECSELKKDIDDLELslaKVEKEKHATENKvknlteemaglDENItkltkeKKILQESHQQALDDLQAEEDkvNTL 1015
Cdd:pfam10174 126 ERQAKELFLLRKTLEEMEL---RIETQKQTLGAR-----------DESI------KKLLEMLQSKGLPKKSGEED--WER 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1016 AKAKVKLEQQVDDLESSLEQEKK----IRMDLERAKRKLEGDLKL-AQESIMDLENDK-QQLEERLKKKDFELNTLNARI 1089
Cdd:pfam10174 184 TRRIAEAEMQLGHLEVLLDQKEKenihLREELHRRNQLQPDPAKTkALQTVIEMKDTKiSSLERNIRDLEDEVQMLKTNG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1090 EdeqAISAQLQKKLKELQArieeleeELEAERTGRAKVEKLRSELLQ---ELEETSERLEEAGGATSvqlelNKKQEAEF 1166
Cdd:pfam10174 264 L---LHTEDREEEIKQMEV-------YKSHSKFMKNKIDQLKQELSKkesELLALQTKLETLTNQNS-----DCKQHIEV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1167 QK---LRRDLEEATLQHEATAATLRKKHADSV-AELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEK 1242
Cdd:pfam10174 329 LKeslTAKEQRAAILQTEVDALRLRLEEKESFlNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1243 MCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKL----TYTQQLEDLKRQL---- 1314
Cdd:pfam10174 409 QLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLeeleSLKKENKDLKEKVsalq 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1315 ----EEEAKAKNALAHA--LQSAQHDCDLLREQYEEEMEAKTE----LQRALSKANSEVAQWRTKYE-TDAIQRTEE--- 1380
Cdd:pfam10174 489 peltEKESSLIDLKEHAssLASSGLKKDSKLKSLEIAVEQKKEecskLENQLKKAHNAEEAVRTNPEiNDRIRLLEQeva 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1381 --LEEAKK------KLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIE------DLMADVERSNAAAAALDKKQRNFDK 1446
Cdd:pfam10174 569 ryKEESGKaqaeveRLLGILREVENEKNDKDKKIAELESLTLRQMKEQNkkvaniKHGQQEMKKKGAQLLEEARRREDNL 648
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163567613 1447 ILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQ 1510
Cdd:pfam10174 649 ADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQE 712
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
932-1749 |
7.82e-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: 54.57 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 932 AAKKRKLEDECSELKKDiddlelsLAKVEKEKHATENKVKNLTEEMAgldenitKLTKEKKILQESHQQALDDLQaeedK 1011
Cdd:COG3096 277 ANERRELSERALELRRE-------LFGARRQLAEEQYRLVEMARELE-------ELSARESDLEQDYQAASDHLN----L 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1012 VNTLAKAKVKLEQQVDDLESsleqekkirmdlerakrkLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIED 1091
Cdd:COG3096 339 VQTALRQQEKIERYQEDLEE------------------LTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAD 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1092 -EQAISAQLQKKLKELQARieeleeeleaERTGRAKV----EKLRSELLQELEETSERLEEAggATSVQLELNkkqeaef 1166
Cdd:COG3096 401 yQQALDVQQTRAIQYQQAV----------QALEKARAlcglPDLTPENAEDYLAAFRAKEQQ--ATEEVLELE------- 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1167 QKLRrDLEEATLQHEATAATLRK-------KHADSVA-ELSEQLDNLQRVKQKLEkeksELKLELDDVNSNTEQLIKAKT 1238
Cdd:COG3096 462 QKLS-VADAARRQFEKAYELVCKiageverSQAWQTArELLRRYRSQQALAQRLQ----QLRAQLAELEQRLRQQQNAER 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1239 NLEKMCR------TTEDQMNEHrskLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGK---LTYTQQLED 1309
Cdd:COG3096 537 LLEEFCQrigqqlDAAEELEEL---LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawLAAQDALER 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1310 LKRQLEEEAKAKNALAHALQS-------AQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTK---------YETD 1373
Cdd:COG3096 614 LREQSGEALADSQEVTAAMQQllerereATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERlggvllseiYDDV 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1374 AIQR----------------TEELEEAKKKLAQR-----------------------LQEAEEAVEAVNAK--------- 1405
Cdd:COG3096 694 TLEDapyfsalygparhaivVPDLSAVKEQLAGLedcpedlyliegdpdsfddsvfdAEELEDAVVVKLSDrqwrysrfp 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1406 ------CSSLEKTKHRLQNEIEDLmadVERSNAAAAALDKKQR---NFDKILSEWK------------QKFEESQTELEA 1464
Cdd:COG3096 774 evplfgRAAREKRLEELRAERDEL---AEQYAKASFDVQKLQRlhqAFSQFVGGHLavafapdpeaelAALRQRRSELER 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1465 SQKEARSLSTElfkLKNAYEESLEHLETFKR--------ENKNLQEEILDLTEQLGASQKSIHELEKVRKQLdaEKLELQ 1536
Cdd:COG3096 851 ELAQHRAQEQQ---LRQQLDQLKEQLQLLNKllpqanllADETLADRLEELREELDAAQEAQAFIQQHGKAL--AQLEPL 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1537 AAleeaeasleheegkILRAQ-LEFNQVKADYERKLAEKDEEIEQ--------SKRNHLRVVDSLQtsLDAETRSRNEAL 1607
Cdd:COG3096 926 VA--------------VLQSDpEQFEQLQADYLQAKEQQRRLKQQifalsevvQRRPHFSYEDAVG--LLGENSDLNEKL 989
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1608 RLkkkmegdlnemeiQLSHANRTAAEAQKQVKALQGYLKD-TQLQLDDVVR---ANEDLKEniaiverrnnlLQSELEEL 1683
Cdd:COG3096 990 RA-------------RLEQAEEARREAREQLRQAQAQYSQyNQVLASLKSSrdaKQQTLQE-----------LEQELEEL 1045
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2163567613 1684 --RAMVEQSERARklaeqelieasERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEK 1749
Cdd:COG3096 1046 gvQADAEAEERAR-----------IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERD 1102
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
836-1106 |
7.85e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 54.52 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 836 KSAETEKEMQTMKEEFGHLKEALEKS-----EARRKELEEkMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKI-- 908
Cdd:PLN02939 118 NSKDGEQLSDFQLEDLVGMIQNAEKNilllnQARLQALED-LEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIhv 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 909 -----QLEAKVKEMTERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKekhaTENKVKNLTEEMAGLDEN 983
Cdd:PLN02939 197 eileeQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAE----TEERVFKLEKERSLLDAS 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 984 ITKLtKEKKILQESHQQALDDLQAEE--DKVNTLAKAKVKLEQQVDDLESSLEQEKkirmDLERAKRKLEGDLKLAQES- 1060
Cdd:PLN02939 273 LREL-ESKFIVAQEDVSKLSPLQYDCwwEKVENLQDLLDRATNQVEKAALVLDQNQ----DLRDKVDKLEASLKEANVSk 347
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2163567613 1061 ----IMDLENDK-QQLEERLKKKDFELNTlnaRIEDEQAISAQLQKKLKEL 1106
Cdd:PLN02939 348 fssyKVELLQQKlKLLEERLQASDHEIHS---YIQLYQESIKEFQDTLSKL 395
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1476-1915 |
8.22e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 54.09 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1476 LFKLKNAYEEsLEHLETFKRE--NKNLQEEI-----LDLTeqlGASQKSIHELEKVRKQLDAEKL-ELQAALEEAEASLE 1547
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELskvkkLNLT---GETQEKFEEWRKKWDDIVTKSLpDIEELLFEAEELND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1548 heEGKILRAQLEFNQVkadyERKLAEKDEEIEQskrnhlrVVDSLQTSLDAETRSRNEALRLKKK--------------- 1612
Cdd:pfam06160 78 --KYRFKKAKKALDEI----EELLDDIEEDIKQ-------ILEELDELLESEEKNREEVEELKDKyrelrktllanrfsy 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1613 ------MEGDLNEMEIQLSHANrTAAEAQKQVKAlQGYLKDTQLQLDDVvraNEDLKENIAIVERRNNLLQSELEELRAM 1686
Cdd:pfam06160 145 gpaideLEKQLAEIEEEFSQFE-ELTESGDYLEA-REVLEKLEEETDAL---EELMEDIPPLYEELKTELPDQLEELKEG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1687 VEQSERAR-KLAEQELIEASERVQLLHSQNTSLINQK--KKMEADISQLQTEVEEaIQECRNAEEKAKKaitdaammaeE 1763
Cdd:pfam06160 220 YREMEEEGyALEHLNVDKEIQQLEEQLEENLALLENLelDEAEEALEEIEERIDQ-LYDLLEKEVDAKK----------Y 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1764 LKKEQDT-SAHLERMKKNMEQTVKDLQL-----RLDEAEQLALKGGKKQLQKLEVRVRELEN------------------ 1819
Cdd:pfam06160 289 VEKNLPEiEDYLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVErleekevayselqeelee 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1820 ------ELEAEQKRNAESIKGLRKSERRVKELSYQTEEDRKNMVRlqdLVDKLQLKV--KAYKRQAEEAEEQANSNLAKF 1891
Cdd:pfam06160 369 ileqleEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKR---LVEKSNLPGlpESYLDYFFDVSDEIEDLADEL 445
|
490 500
....*....|....*....|....
gi 2163567613 1892 RKVQHELDEAEERADMAESQVNKL 1915
Cdd:pfam06160 446 NEVPLNMDEVNRLLDEAQDDVDTL 469
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
858-1398 |
8.24e-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: 54.20 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 858 LEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEEEEemnaeLAAKKRK 937
Cdd:TIGR00618 316 LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHT-----LQQQKTT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 938 LEDECSELKKDIDDLELSLAKVEKEkHATENkvkNLTEEMAGLDENITKLTKEKKILQESHQQALDDLQAEEDKVNTLAK 1017
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQATIDTR-TSAFR---DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1018 AKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEE------RLKKKDFELNTLNARIED 1091
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNpgpltrRMQRGEQTYAQLETSEED 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1092 EQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEEAGGATSVQLELNKKQE-------- 1163
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLrklqpeqd 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1164 -----AEFQKLRRDLEEATLQHEATAATLRKK----HADSVAELSEQ-LDNLQRVKQKLEKEKSELKLELDDVNSNTEQL 1233
Cdd:TIGR00618 627 lqdvrLHLQQCSQELALKLTALHALQLTLTQErvreHALSIRVLPKElLASRQLALQKMQSEKEQLTYWKEMLAQCQTLL 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1234 IKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQ 1313
Cdd:TIGR00618 707 RELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAE 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1314 LEEEAKAKNALAHAL--------QSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAiQRTEELEEAK 1385
Cdd:TIGR00618 787 IQFFNRLREEDTHLLktleaeigQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYE-ECSKQLAQLT 865
|
570
....*....|...
gi 2163567613 1386 KKLAQRLQEAEEA 1398
Cdd:TIGR00618 866 QEQAKIIQLSDKL 878
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1022-1663 |
9.18e-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: 54.19 E-value: 9.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1022 LEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLklaqESIMDLENDKQQLEERLKkkdfelnTLNARIEDEQAISAQLQK 1101
Cdd:COG3096 517 LRAQLAELEQRLRQQQNAERLLEEFCQRIGQQL----DAAEELEELLAELEAQLE-------ELEEQAAEAVEQRSELRQ 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1102 KLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEeaggATSVQLElnkkQEAEFQKLRRDLEEatlQHE 1181
Cdd:COG3096 586 QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTA----AMQQLLE----REREATVERDELAA---RKQ 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1182 ATAATLRKKHADSVAELSEqldnLQRVKQKLekeKSELKLEL-DDVnsnteqlikaktnlekmcrTTEDQmnEHRSKLEE 1260
Cdd:COG3096 655 ALESQIERLSQPGGAEDPR----LLALAERL---GGVLLSEIyDDV-------------------TLEDA--PYFSALYG 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1261 AQR---TVTDLSTQRAKLQT--------------ENS--ELSRQLEEKE-AFINQLTRGKLTYT--------------QQ 1306
Cdd:COG3096 707 PARhaiVVPDLSAVKEQLAGledcpedlyliegdPDSfdDSVFDAEELEdAVVVKLSDRQWRYSrfpevplfgraareKR 786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1307 LEDLKRQLEEEAK--AKNA--------LAHALQS--AQHDCDLLREQYEEEMEA----KTELQRALSKANSEVAQWRTKY 1370
Cdd:COG3096 787 LEELRAERDELAEqyAKASfdvqklqrLHQAFSQfvGGHLAVAFAPDPEAELAAlrqrRSELERELAQHRAQEQQLRQQL 866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1371 ---------------------ETDAIQRTEELE-------EAKKKLAQR-------------LQEAEEAVEAVNAKCSSL 1409
Cdd:COG3096 867 dqlkeqlqllnkllpqanllaDETLADRLEELReeldaaqEAQAFIQQHgkalaqleplvavLQSDPEQFEQLQADYLQA 946
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1410 EKTKHRLQNEIEDLMADVERSNA-----AAAALDKKQRNFDKI---LSEWKQKFEESQTELEASQKEARSLSTELFKLKN 1481
Cdd:COG3096 947 KEQQRRLKQQIFALSEVVQRRPHfsyedAVGLLGENSDLNEKLrarLEQAEEARREAREQLRQAQAQYSQYNQVLASLKS 1026
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1482 AYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSihELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAqlefn 1561
Cdd:COG3096 1027 SRDAKQQTLQELEQELEELGVQADAEAEERARIRRD--ELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKA----- 1099
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1562 qvkadyERKLAEKDEEIEQSKRNHLRVvdslqtsldaetrsrneaLRLKKK--MEGDLNEMEIQLSHANRTAAEAQKQVK 1639
Cdd:COG3096 1100 ------ERDYKQEREQVVQAKAGWCAV------------------LRLARDndVERRLHRRELAYLSADELRSMSDKALG 1155
|
730 740
....*....|....*....|....
gi 2163567613 1640 ALQGYLKDTQlQLDDVVRANEDLK 1663
Cdd:COG3096 1156 ALRLAVADNE-HLRDALRLSEDPR 1178
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1015-1563 |
9.68e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 53.98 E-value: 9.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1015 LAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDfelNTLNARIEDEQA 1094
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAE---EALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1095 ISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELL---QELEETSERLEEaggaTSVQLELNKKQEAEFQKLRR 1171
Cdd:pfam05557 81 KKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQraeLELQSTNSELEE----LQERLDLLKAKASEAEQLRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1172 DLEEAtlQHEATAATLRKKhadsvaELSEQLDNLQRVKQKLEKEKSELkLELDDVNSNTEQLIKAKTNLEKMCRTT---E 1248
Cdd:pfam05557 157 NLEKQ--QSSLAEAEQRIK------ELEFEIQSQEQDSEIVKNSKSEL-ARIPELEKELERLREHNKHLNENIENKlllK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1249 DQMNEHRSKLEEAQRTVTDLstqrAKLQTENSELSRQLEEKE-----------------AFINQLTRGKLTYTQQLEDLK 1311
Cdd:pfam05557 228 EEVEDLKRKLEREEKYREEA----ATLELEKEKLEQELQSWVklaqdtglnlrspedlsRRIEQLQQREIVLKEENSSLT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1312 RQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQRTEelEEAKKKLAQR 1391
Cdd:pfam05557 304 SSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTM--SNYSPQLLER 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1392 LQEAEEAVEAVNAKCSSLEktkHRLQNEIEDLMADVERSNAAAAALDKKQRNFD--------KILSEWKQKFEESQTELE 1463
Cdd:pfam05557 382 IEEAEDMTQKMQAHNEEME---AQLSVAEEELGGYKQQAQTLERELQALRQQESladpsyskEEVDSLRRKLETLELERQ 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1464 ASQKEARSLSTELFK--LKNAYEES------------LEHLETFKRENKNLQEEILDLTEQL----GASQKSIHELEKVR 1525
Cdd:pfam05557 459 RLREQKNELEMELERrcLQGDYDPKktkvlhlsmnpaAEAYQQRKNQLEKLQAEIERLKRLLkkleDDLEQVLRLPETTS 538
|
570 580 590
....*....|....*....|....*....|....*...
gi 2163567613 1526 KQLDAEKLELQAALEEAEASLEHEEGKILRAQLEFNQV 1563
Cdd:pfam05557 539 TMNFKEVLDLRKELESAELKNQRLKEVFQAKIQEFRDV 576
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
929-1110 |
1.03e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 929 AELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQESHQQALDDLQ-- 1006
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1007 -AEEDKVNTLAKAK---------VKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLK 1076
Cdd:COG3883 99 gGSVSYLDVLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190
....*....|....*....|....*....|....
gi 2163567613 1077 KKDFELNTLNARIEDEQAISAQLQKKLKELQARI 1110
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
856-1126 |
1.16e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 856 EALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVkemterleeeeemnAELAAKK 935
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL--------------AALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 936 RKLEDECSELKKDIDDLELSLAKVEKE--KHATENKVKNLteemagldenitkltkekkILQESHQQALDDLQAeedkVN 1013
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRAlyRLGRQPPLALL-------------------LSPEDFLDAVRRLQY----LK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1014 TLAKAkvkLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQ 1093
Cdd:COG4942 143 YLAPA---RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
250 260 270
....*....|....*....|....*....|...
gi 2163567613 1094 AISAQLQKKLKELQARIEELEEELEAERTGRAK 1126
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1051-1323 |
1.22e-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: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1051 EGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEdeqaisaQLQKKLKELQARIEELeeeleaertgRAKVEKL 1130
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-------ELQAELEALQAEIDKL----------QAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1131 RSELLQELEETSERL----EEAGGATSVQLELNKKQEAEFqkLRRdleeatlqheataATLRKKHADSVAELseqLDNLQ 1206
Cdd:COG3883 78 EAEIEERREELGERAralyRSGGSVSYLDVLLGSESFSDF--LDR-------------LSALSKIADADADL---LEELK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1207 RVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEkmcrttedqmnehrSKLEEAQRTVTDLSTQRAKLQTENSELSRQL 1286
Cdd:COG3883 140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELE--------------AQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
250 260 270
....*....|....*....|....*....|....*..
gi 2163567613 1287 EEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNA 1323
Cdd:COG3883 206 AAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
836-1096 |
1.25e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 836 KSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEkmvsmlqEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVk 915
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNE-------EAANLRERLESLERRIAATERRLEDLEEQIEELSEDI- 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 916 emterleeeeemnAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQ 995
Cdd:TIGR02168 855 -------------ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 996 ESHQQALDDLQAEEDKVNTLAKAkvKLEQQVDDLESSLEQEKKIRMDLERAKRKLEgDLKLAQESI----MDLENDKQQL 1071
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQER--LSEEYSLTLEEAEALENKIEDDEEEARRRLK-RLENKIKELgpvnLAAIEEYEEL 998
|
250 260
....*....|....*....|....*.
gi 2163567613 1072 EERLKKKDFELNTLNARIED-EQAIS 1096
Cdd:TIGR02168 999 KERYDFLTAQKEDLTEAKETlEEAIE 1024
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1005-1142 |
1.27e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.24 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1005 LQAEEDKVNTLAKAKVKLEQQVDDLEssLEQEKKIrmdlERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNT 1084
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEAL--LEAKEEI----HKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEK 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2163567613 1085 LNARIEDEQAISAQLQKKLKELQarieeleeeleaertgrAKVEKLRSELLQELEETS 1142
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKE-----------------EELEELIEEQLQELERIS 148
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1293-1903 |
1.31e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1293 INQLTRGKLtytqQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYE- 1371
Cdd:PRK01156 161 INSLERNYD----KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNn 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1372 -TDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLqNEIEDLMADVERSNAAAAALDKKQ-RNFDKILS 1449
Cdd:PRK01156 237 lKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERH-MKIINDPVYKNRNYINDYFKYKNDiENKKQILS 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1450 EWK---QKFEESQTELEasqkearslstELFKLKNAYEESlehletfKRENKNLQEEILDLTEQLGASQKSIHELEKVRK 1526
Cdd:PRK01156 316 NIDaeiNKYHAIIKKLS-----------VLQKDYNDYIKK-------KSRYDDLNNQILELEGYEMDYNSYLKSIESLKK 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1527 QLDAEKLELQAALEEAEASLEHEE--GKILRAQL-EFNQVKADYERKLA----------EKDEEIEQSKR--NHLRVVDS 1591
Cdd:PRK01156 378 KIEEYSKNIERMSAFISEILKIQEidPDAIKKELnEINVKLQDISSKVSslnqriralrENLDELSRNMEmlNGQSVCPV 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1592 LQTSL--DAETRSRNEALRLKKKMEGDLNEMEIQLSHANrtaaEAQKQVKALQGYLkdtqlqlddvvrANEDLKENIAiv 1669
Cdd:PRK01156 458 CGTTLgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDID----EKIVDLKKRKEYL------------ESEEINKSIN-- 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1670 erRNNLLQSELEELRAmVEQSERARKLAEQELIEASERVQLLH-----SQNTSLINqkkkMEADISQLQteveeaIQECR 1744
Cdd:PRK01156 520 --EYNKIESARADLED-IKIKINELKDKHDKYEEIKNRYKSLKledldSKRTSWLN----ALAVISLID------IETNR 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1745 NAEEKAKKAITDAAMMAEELKKE-QDTSAHLERMKKNMEQTVKDLQLRLDEAEqlALKGGKKQLQKLEVRVRELENELEA 1823
Cdd:PRK01156 587 SRSNEIKKQLNDLESRLQEIEIGfPDDKSYIDKSIREIENEANNLNNKYNEIQ--ENKILIEKLRGKIDNYKKQIAEIDS 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1824 EQKRNAESIKGLRKSERRVKELSYQTEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQANSnLAKFRKVQHELDEAEE 1903
Cdd:PRK01156 665 IIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLES-MKKIKKAIGDLKRLRE 743
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1424-1830 |
1.59e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1424 MADVERSNAAAAALDKKQRNFDKILSEwKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEhLETFKRENKNLQEE 1503
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPLYQE-LEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1504 ILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLEFNQVKADYERKLAEKDEEIEQSKR 1583
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1584 NHLRVVDSLQTSLDAETRSRNEALRLkkkMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLK 1663
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLLL---IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1664 ENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQkkkmeADISQLQTEVEEAIQEC 1743
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE-----LQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1744 RNAEEkakKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlalkggKKQLQKLEVRVRELENELEA 1823
Cdd:COG4717 380 GVEDE---EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL------EEELEELEEELEELEEELEE 450
|
....*..
gi 2163567613 1824 EQKRNAE 1830
Cdd:COG4717 451 LREELAE 457
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1275-1573 |
1.86e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 53.09 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1275 LQTENSELSRQLEEKE-----AFINQLTRGKLTYTQQLEDLKRQLEEE--AKAKNALAHALQSAQHDcdlLREQYEEEME 1347
Cdd:NF033838 67 LEKILSEIQKSLDKRKhtqnvALNKKLSDIKTEYLYELNVLKEKSEAEltSKTKKELDAAFEQFKKD---TLEPGKKVAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1348 AKTELQRALSKANSEVAQWRTKYETDAIqRTEELEEAKKKLaqRLQEAEEAVEAVNAKCSSLEKTkhrlqneIEDLMADV 1427
Cdd:NF033838 144 ATKKVEEAEKKAKDQKEEDRRNYPTNTY-KTLELEIAESDV--EVKKAELELVKEEAKEPRDEEK-------IKQAKAKV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1428 ERSNAAAAALDKkqrnfdkILSEWKQKFEESQTELEASQKEA---RSLSTELFKLKN-AYEESLEHLET-FKRENK---- 1498
Cdd:NF033838 214 ESKKAEATRLEK-------IKTDREKAEEEAKRRADAKLKEAvekNVATSEQDKPKRrAKRGVLGEPATpDKKENDakss 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1499 --NLQEEILDLT-----EQLGASQKSIHELEKVRKQLDAE-----------KLELQAA-----LEEAEASLEHEEGKILR 1555
Cdd:NF033838 287 dsSVGEETLPSPslkpeKKVAEAEKKVEEAKKKAKDQKEEdrrnyptntykTLELEIAesdvkVKEAELELVKEEAKEPR 366
|
330
....*....|....*...
gi 2163567613 1556 AQLEFNQVKADYERKLAE 1573
Cdd:NF033838 367 NEEKIKQAKAKVESKKAE 384
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1444-1905 |
1.98e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.05 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1444 FDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEhletfkrenkNLQEEILDLTEQLGASQKSIHELEK 1523
Cdd:TIGR00618 178 YTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQ----------VLEKELKHLREALQQTQQSHAYLTQ 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1524 VRKQLDaEKLELQAALEEAEASLEHEEGKIlrAQLEFNQVKADYERK---LAEKDEEIEQSKRNHLRVVDSLQTSLDAET 1600
Cdd:TIGR00618 248 KREAQE-EQLKKQQLLKQLRARIEELRAQE--AVLEETQERINRARKaapLAAHIKAVTQIEQQAQRIHTELQSKMRSRA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1601 RSR-NEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRAnedLKENIAIVERRNNLLQSE 1679
Cdd:TIGR00618 325 KLLmKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHT---LQQQKTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1680 LEELRAMV------------EQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQT-EVEEAIQECRNA 1746
Cdd:TIGR00618 402 LDILQREQatidtrtsafrdLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLkEREQQLQTKEQI 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1747 EEKAKKAITDAAMMAEELKKEQdtsahLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQLQKLEVRVRELENELEAEQK 1826
Cdd:TIGR00618 482 HLQETRKKAVVLARLLELQEEP-----CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1827 RNA---ESIKGLRKSERRVKELSYQTEED----RKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKVQHELD 1899
Cdd:TIGR00618 557 QRAslkEQMQEIQQSFSILTQCDNRSKEDipnlQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ 636
|
....*.
gi 2163567613 1900 EAEERA 1905
Cdd:TIGR00618 637 CSQELA 642
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1652-1925 |
2.02e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1652 LDDVVRANEDLKENIAIVERRN-----NLLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLinqkKKME 1726
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDlherlNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL----ETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1727 ADISQLQteveEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHlermkknmeqtvkdlQLRLDEAEQLALKGGKKQ 1806
Cdd:PRK02224 258 AEIEDLR----ETIAETEREREELAEEVRDLRERLEELEEERDDLLA---------------EAGLDDADAEAVEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1807 LQKLEVRVRELENELEAEQKRNAESIKGLRKserRVKELSYQTEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQANS 1886
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLRE---DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260 270
....*....|....*....|....*....|....*....
gi 2163567613 1887 NLAKFRKVQHELDEAEERADMAESQVNKLRARSRDIGAK 1925
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1006-1222 |
2.30e-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: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1006 QAEEDKVNTLAKAKVKLEQQVDDLESSLEQ-EKKirmdLERAKRK-----LEGDLKLAQESIMDLENDKQQLEERLKKKD 1079
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEaEAA----LEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1080 FELNTLNARIEDEQAISA---------QLQKKLKELQARIEELEEELEAE----RTGRAKVEKLRSELLQELEETSERLE 1146
Cdd:COG3206 240 ARLAALRAQLGSGPDALPellqspviqQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163567613 1147 eaggatsVQLELNKKQEAEFQKLRRDLEEATLQHEATAATLRkkhadsvaELSEQLDNLQRVKQKLEKEKSELKLE 1222
Cdd:COG3206 320 -------AELEALQAREASLQAQLAQLEARLAELPELEAELR--------RLEREVEVARELYESLLQRLEEARLA 380
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1272-1827 |
2.94e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.65 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1272 RAKLQTENSELSRQLEEKEAFI--NQLTRGKLTYTQQLEDLKRQLEEEAKAKNA---LAHALQSaqhdcdllREQYEEEM 1346
Cdd:COG3096 217 RDYLLPENSGVRKAFQDMEAALreNRMTLEAIRVTQSDRDLFKHLITEATNYVAadyMRHANER--------RELSERAL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1347 EAKTELQRALSKANSEvaQWRTKYETDAIqrtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRlQNEIEDLMAD 1426
Cdd:COG3096 289 ELRRELFGARRQLAEE--QYRLVEMAREL---EELSARESDLEQDYQAASDHLNLVQTALRQQEKIERY-QEDLEELTER 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1427 VERSNAAAAALDKKQrnfdkilsewkqkfEESQTELEASQKEARSLSTELFKlknaYEESLEHLETfkrenknlqeeild 1506
Cdd:COG3096 363 LEEQEEVVEEAAEQL--------------AEAEARLEAAEEEVDSLKSQLAD----YQQALDVQQT-------------- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1507 lteQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEgkilraqlEFNQVKADYERKLAEKDEEIEQskrnhl 1586
Cdd:COG3096 411 ---RAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQ--------QATEEVLELEQKLSVADAARRQ------ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1587 rvvdslqtsldaetrsRNEALRLKKKMEGdlnemEIQLSHANRTAAEAQKQVKALQgylkdtqlqlddvvranedlkeni 1666
Cdd:COG3096 474 ----------------FEKAYELVCKIAG-----EVERSQAWQTARELLRRYRSQQ------------------------ 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1667 AIVERRNNLlQSELEELRAMVEQSERARKLAEqeliEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQ---EC 1743
Cdd:COG3096 509 ALAQRLQQL-RAQLAELEQRLRQQQNAERLLE----EFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEqrsEL 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1744 RNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTVKDLQlRLDEAEQLALKgGKKQLQKLEVRVRELENELEA 1823
Cdd:COG3096 584 RQQLEQLRARIKELAARAPAWLAAQDA---LERLREQSGEALADSQ-EVTAAMQQLLE-REREATVERDELAARKQALES 658
|
....
gi 2163567613 1824 EQKR 1827
Cdd:COG3096 659 QIER 662
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
936-1331 |
3.47e-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: 51.61 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 936 RKLEDECSELKKDIDDLELSLAKVEKEKHATENKvknLTEEMAGLDEnitkltkekkiLQESHQQALDDLQAEEDKVNTL 1015
Cdd:pfam19220 23 RSLKADFSQLIEPIEAILRELPQAKSRLLELEAL---LAQERAAYGK-----------LRRELAGLTRRLSAAEGELEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1016 AKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQAI 1095
Cdd:pfam19220 89 VARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARER 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1096 SAQLQKKLKELQARIEELEEELeaertgrAKVEKLRSELLQELEETSERLEEAGGATSVQLELNKKQEAEFqklrrDLEE 1175
Cdd:pfam19220 169 LALLEQENRRLQALSEEQAAEL-------AELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQL-----EEAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1176 ATLQHEATAATLRKKHADSVAELSEQLdnLQRVKQKLeKEKSElklELDDVNSNTEQLIKAKTNLEKMCRTTEDQMNEHR 1255
Cdd:pfam19220 237 EAHRAERASLRMKLEALTARAAATEQL--LAEARNQL-RDRDE---AIRAAERRLKEASIERDTLERRLAGLEADLERRT 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163567613 1256 SKLEEAQRtvtdlstQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHALQSA 1331
Cdd:pfam19220 311 QQFQEMQR-------ARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRLKEE 379
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
996-1180 |
3.95e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 996 ESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERL 1075
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1076 K--KKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEEELeaertgrAKVEKLRSELLQELEETSERLEEAGGATS 1153
Cdd:COG1579 83 GnvRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEEL-------AELEAELAELEAELEEKKAELDEELAELE 155
|
170 180
....*....|....*....|....*..
gi 2163567613 1154 VQLElnkKQEAEFQKLRRDLEEATLQH 1180
Cdd:COG1579 156 AELE---ELEAEREELAAKIPPELLAL 179
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1456-1931 |
4.00e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.13 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1456 EESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQL---GASQKSIHELEKVRKQLdaek 1532
Cdd:pfam10174 112 ELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLqskGLPKKSGEEDWERTRRI---- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1533 LELQAALEEAEASLEHEEGKILRAQLEF---NQVKADYERKLA------EKDEEIEQSKRNHLRV---VDSLQTSLDAET 1600
Cdd:pfam10174 188 AEAEMQLGHLEVLLDQKEKENIHLREELhrrNQLQPDPAKTKAlqtvieMKDTKISSLERNIRDLedeVQMLKTNGLLHT 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1601 RSRNEalrlkkkmegDLNEMEIQLSHAN--RTAAEAQKQ--------VKALQGYLKDTQLQLDDVVRANEDLKENIAIVE 1670
Cdd:pfam10174 268 EDREE----------EIKQMEVYKSHSKfmKNKIDQLKQelskkeseLLALQTKLETLTNQNSDCKQHIEVLKESLTAKE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1671 RRNNLLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAE--- 1747
Cdd:pfam10174 338 QRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDkql 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1748 ----EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNM-EQTVKDLQLRLDEAEQL--ALKGGKKQLQKLEVRVRELENE 1820
Cdd:pfam10174 418 aglkERVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESLkkENKDLKEKVSALQPELTEKESS 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1821 LEAEQKRNAESIKGLRKSERRVKELSYQTEEDRKNMVRLQDLVDKLQlkvkaykrQAEEAEEQANSNLAKFRKVQHELDE 1900
Cdd:pfam10174 498 LIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVAR 569
|
490 500 510
....*....|....*....|....*....|.
gi 2163567613 1901 AEERADMAESQVNKLRARSRDIGAKKGLNEE 1931
Cdd:pfam10174 570 YKEESGKAQAEVERLLGILREVENEKNDKDK 600
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
826-1140 |
4.25e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 826 KLYFKIKPLLKSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIK 905
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 906 NKIQLEAKVKEMTERLeeeeemnAELAAKKRKLEDEC-SELKKDIDDLE------LSLAKVEKEKHATENKVKNLTEEma 978
Cdd:PRK03918 557 KLAELEKKLDELEEEL-------AELLKELEELGFESvEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEE-- 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 979 gLDENITKLTKEKKILQESHQQaLDDLQAEEDKvntlakakvkleqqvDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQ 1058
Cdd:PRK03918 628 -LDKAFEELAETEKRLEELRKE-LEELEKKYSE---------------EEYEELREEYLELSRELAGLRAELEELEKRRE 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1059 ESIMDLENDKQQLEERLKKKDfELNTLNARIEDEQAisaqLQKKLKELQARIeeleeeleaERTGRAKVEKLRSELLQEL 1138
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKK-ELEKLEKALERVEE----LREKVKKYKALL---------KERALSKVGEIASEIFEEL 756
|
..
gi 2163567613 1139 EE 1140
Cdd:PRK03918 757 TE 758
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1559-1907 |
4.70e-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: 51.22 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1559 EFNQVKADYERKLAEKDEEIEQSKRNHLRVVDsLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQV 1638
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLE-LEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1639 KALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSL 1718
Cdd:pfam19220 100 REAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1719 INQKKKMEADISQLQTEVEEAiqECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKnMEQTVKDLQLRLDEAEQL 1798
Cdd:pfam19220 180 QALSEEQAAELAELTRRLAEL--ETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEA-HRAERASLRMKLEALTAR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1799 ALkGGKKQLQKLEVRVRELENELEAEQKRNAESIKGLRKSERRVKELsyqteedrknmvrlqdlvdklqlkvkayKRQAE 1878
Cdd:pfam19220 257 AA-ATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGL----------------------------EADLE 307
|
330 340
....*....|....*....|....*....
gi 2163567613 1879 EAEEQansnlakFRKVQHELDEAEERADM 1907
Cdd:pfam19220 308 RRTQQ-------FQEMQRARAELEERAEM 329
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1420-1924 |
4.97e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1420 IEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKL------KNAYEESLEHLETF 1493
Cdd:PRK01156 185 IDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELssledmKNRYESEIKTAESD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1494 KRENKNLQEEILDLTEQLG--------ASQKSIHELEKVRKQLDaeklELQAALEEAEASLEHEEGKILRAQlEFNQVKA 1565
Cdd:PRK01156 265 LSMELEKNNYYKELEERHMkiindpvyKNRNYINDYFKYKNDIE----NKKQILSNIDAEINKYHAIIKKLS-VLQKDYN 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1566 DYERKLAEKDE------EIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVK 1639
Cdd:PRK01156 340 DYIKKKSRYDDlnnqilELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQ 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1640 ALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNN--LLQSELEElramvEQSERARKLAEQELIEASERVQLLHSQNTS 1717
Cdd:PRK01156 420 DISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpVCGTTLGE-----EKSNHIINHYNEKKSRLEEKIREIEIEVKD 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1718 LINQKKKMEADISQLQT-EVEEAIQECRNAEEKAKK---------AITDAAMMAEELKkEQDTSAHLERMKKNMEQTVKD 1787
Cdd:PRK01156 495 IDEKIVDLKKRKEYLESeEINKSINEYNKIESARADledikikinELKDKHDKYEEIK-NRYKSLKLEDLDSKRTSWLNA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1788 LQLRLD---EAEQLALKGGKKQLQKLEVRVRELENELEAEQKRNAESIkglRKSERRVKELSYQTEEDRKNMVrlqdLVD 1864
Cdd:PRK01156 574 LAVISLidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSI---REIENEANNLNNKYNEIQENKI----LIE 646
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1865 KLQLKVKAYKRQaeeaeeqansnLAKFRKVQHELDEAEERADMAESQVNKLRARSRDIGA 1924
Cdd:PRK01156 647 KLRGKIDNYKKQ-----------IAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKA 695
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
965-1917 |
4.99e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 51.75 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 965 ATENKVKNLTEEMAGLdenITKLTKEKKILQESHQQALDDLQAEEDKVNTLAKAKVKLEQQvddlESSLEQekkirmdLE 1044
Cdd:NF041483 302 ANEQRTRTAKEEIARL---VGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAA----EDTAAQ-------LA 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1045 RAKRKLEGDLKLAQESIMDLENDKQQLEERLKKkdfELNTLNARIEDEQAISAQLQK-----KLKELQARieeLEEELEA 1119
Cdd:NF041483 368 KAARTAEEVLTKASEDAKATTRAAAEEAERIRR---EAEAEADRLRGEAADQAEQLKgaakdDTKEYRAK---TVELQEE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1120 ERTGRAKVEKLRSELLQELE--------ETSERLEEAGGATSVQL--------ELNKKQEAEFQKLRRD-LEEATLQHEA 1182
Cdd:NF041483 442 ARRLRGEAEQLRAEAVAEGErirgearrEAVQQIEEAARTAEELLtkakadadELRSTATAESERVRTEaIERATTLRRQ 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1183 TAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLElddvnsnTEQLIKAKTnlEKMCRTTEDQMNEHRSKLEEAQ 1262
Cdd:NF041483 522 AEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELREE-------TERAIAARQ--AEAAEELTRLHTEAEERLTAAE 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1263 RTVTDLSTQRAKLQTENSELSRQLEEKEAfinQLTRgklTYTQQLEDLKRQLEEEAKAKNALAHAlqSAQHDCDLLREQY 1342
Cdd:NF041483 593 EALADARAEAERIRREAAEETERLRTEAA---ERIR---TLQAQAEQEAERLRTEAAADASAARA--EGENVAVRLRSEA 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1343 EEEMEA-KTELQRALSKANSEVAQWRTKYETDAiqrTEELEEAKKKLAQRLQEAEEAVEAVNAKcsslektkhrlqneie 1421
Cdd:NF041483 665 AAEAERlKSEAQESADRVRAEAAAAAERVGTEA---AEALAAAQEEAARRRREAEETLGSARAE---------------- 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1422 dlmADVERSNAAAAAldkkqrnfDKILSEWKQKFEESQTELEASQKEARSLSTELfkLKNAYEESLEHLETFKRENKNLQ 1501
Cdd:NF041483 726 ---ADQERERAREQS--------EELLASARKRVEEAQAEAQRLVEEADRRATEL--VSAAEQTAQQVRDSVAGLQEQAE 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1502 EEIldlteqLGASQKSIHELEKVRKQLDAEKLELQA-ALEEAEASLEHEEGKILRAQLEFNQVKADYERKLAEKDEE--- 1577
Cdd:NF041483 793 EEI------AGLRSAAEHAAERTRTEAQEEADRVRSdAYAERERASEDANRLRREAQEETEAAKALAERTVSEAIAEaer 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1578 -----IEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKMEGDlnemeiQLSHANRTAAEAQKQVKALQGYLKDTQLQL 1652
Cdd:NF041483 867 lrsdaSEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSD------AAAQADRLIGEATSEAERLTAEARAEAERL 940
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1653 DDVVRANEDLK--ENIAIVERRNNLLQSELEELRAMV--------EQSERARKLAEQELIEASERVQLLHSQntslinqk 1722
Cdd:NF041483 941 RDEARAEAERVraDAAAQAEQLIAEATGEAERLRAEAaetvgsaqQHAERIRTEAERVKAEAAAEAERLRTE-------- 1012
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1723 KKMEADiSQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAhLERMKKNMEQTVKDLQLRLDEAEQLALKG 1802
Cdd:NF041483 1013 AREEAD-RTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEA-LRTTTEAEAQADTMVGAARKEAERIVAEA 1090
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1803 GKKQLQKLEvRVRELENELEAEQKRNAESIKGlRKSERRVKELSYQTE-------EDRKNMVRLQDLVDKLqlkVKAYKR 1875
Cdd:NF041483 1091 TVEGNSLVE-KARTDADELLVGARRDATAIRE-RAEELRDRITGEIEElherarrESAEQMKSAGERCDAL---VKAAEE 1165
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....
gi 2163567613 1876 QAEEAEEQ-------ANSNLAKFR-----KVQHELDEAEERADMAESQVNKLRA 1917
Cdd:NF041483 1166 QLAEAEAKakelvsdANSEASKVRiaavkKAEGLLKEAEQKKAELVREAEKIKA 1219
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
835-1092 |
6.01e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 835 LKSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMlqeknDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKV 914
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 915 KEMTERLEEEEEMNAELAAkkrklEDECSELKKDIDDLELSLAkvEKEKHATEN--KVKNLTEEMAGLDENItkltkekk 992
Cdd:COG3206 243 AALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAALRAQL-------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 993 ilQESHQQALDDLQAEedkVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRklegDLKLAQESIMDLENDKQQLE 1072
Cdd:COG3206 308 --QQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLER----EVEVARELYESLLQRLEEAR 378
|
250 260
....*....|....*....|
gi 2163567613 1073 ERLkkkdfELNTLNARIEDE 1092
Cdd:COG3206 379 LAE-----ALTVGNVRVIDP 393
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1124-1332 |
7.82e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1124 RAKVEKLRSELLQELEETSERLEEAggatsvqlelnkkqEAEFQKLRR-----DLEEATLQHEATAATLRKKHADSVAEL 1198
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEA--------------EAALEEFRQknglvDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1199 SEQLDNLQRVKQKLEKEKSELKLELDD--VNSNTEQLIKAKTNLEKMCRT----------TEDQMNEHRSKL-EEAQRTV 1265
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARytpnhpdviaLRAQIAALRAQLqQEAQRIL 315
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163567613 1266 TDLSTQRAKLQTENSELSRQLEEKEAFINQLTRgkltYTQQLEDLKRQLEEEAKAKNALAHALQSAQ 1332
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1086-1570 |
8.12e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.89 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1086 NARIEDEQAISAQLQKKLKELQ-----ARIEELEEELEAERTGRAKVEKLRsELLQELEETSERLEEAGGATSVQLELNK 1160
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMElehkrARIELEKKASALKRQLDRESDRNQ-ELQKRIRLLEKREAEAEEALREQAELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1161 KQEAEFQKLRRDLEEATLQhEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNL 1240
Cdd:pfam05557 80 LKKKYLEALNKKLNEKESQ-LADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1241 EKMCRTtedqMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSR---------QLEEKEAFINQLTRGKLTYTQQLEDLK 1311
Cdd:pfam05557 159 EKQQSS----LAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARipelekeleRLREHNKHLNENIENKLLLKEEVEDLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1312 RQLeeeakaknalahalqsaqhdcdllrEQYEEEMEAKTELQRALSKANSEVAQWRTKYETDA--IQRTEELEEAKKKLA 1389
Cdd:pfam05557 235 RKL-------------------------EREEKYREEAATLELEKEKLEQELQSWVKLAQDTGlnLRSPEDLSRRIEQLQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1390 QRLQEAEEAVEAVNAKCSSLEKTKHRLQNE-------IEDLMADVERSNAAAAALDK------KQRNFDKILSEwkqKFE 1456
Cdd:pfam05557 290 QREIVLKEENSSLTSSARQLEKARRELEQElaqylkkIEDLNKKLKRHKALVRRLQRrvllltKERDGYRAILE---SYD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1457 ESQTELEASQKEA---RSLSTELFKLKNAYEESLEHLETFKRE--NKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAE 1531
Cdd:pfam05557 367 KELTMSNYSPQLLeriEEAEDMTQKMQAHNEEMEAQLSVAEEElgGYKQQAQTLERELQALRQQESLADPSYSKEEVDSL 446
|
490 500 510
....*....|....*....|....*....|....*....
gi 2163567613 1532 KLELQAAleEAEASLEHEEGKILRAQLEFNQVKADYERK 1570
Cdd:pfam05557 447 RRKLETL--ELERQRLREQKNELEMELERRCLQGDYDPK 483
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
838-1222 |
1.01e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.28 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 838 AETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQdnladaeercdQLIKnkiQLEAKVKEm 917
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHE-----------ARIR---ELEEDIKT- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 918 terleeeeemnaeLAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMagldeniTKLTKEKKILQES 997
Cdd:pfam07888 141 -------------LTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL-------RSLSKEFQELRNS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 998 HQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGdlklaqesimdlenDKQQLEERLKK 1077
Cdd:pfam07888 201 LAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG--------------LGEELSSMAAQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1078 KDFELNTLN-ARIEdeqaiSAQLQKKLKELQARIeeleeeleaeRTGRAKVEKLRSELLQELEETSERLEeaggatsvql 1156
Cdd:pfam07888 267 RDRTQAELHqARLQ-----AAQLTLQLADASLAL----------REGRARWAQERETLQQSAEADKDRIE---------- 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163567613 1157 elnkKQEAEFQKLRRDLEEATLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKL---EKEKSELKLE 1222
Cdd:pfam07888 322 ----KLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLrvaQKEKEQLQAE 386
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1338-1618 |
1.13e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.85 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1338 LREQYEEE--MEAKTELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLaQRLQEAEEAVEAVNAKCSSLEKTKHR 1415
Cdd:COG5022 832 LRETEEVEfsLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQL-QELKIDVKSISSLKLVNLELESEIIE 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1416 LQNEIE-DLMADVERSNAAAAALDKKQRNFDKILSEWKQKfeESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFK 1494
Cdd:COG5022 911 LKKSLSsDLIENLEFKTELIARLKKLLNNIDLEEGPSIEY--VKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGN 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1495 REN---KNLQEEILDLTEQLGASQKSIHELEKVRKQLDaeklELQAALeeaeaSLEHEEGKILRAQLEFNQVKADYERKL 1571
Cdd:COG5022 989 KANselKNFKKELAELSKQYGALQESTKQLKELPVEVA----ELQSAS-----KIISSESTELSILKPLQKLKGLLLLEN 1059
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2163567613 1572 AEKDEEIEQSK-RNHLRVVDSLQTSLDAETRSRNEALRLKKKMEGDLN 1618
Cdd:COG5022 1060 NQLQARYKALKlRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRN 1107
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
993-1698 |
1.24e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 50.57 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 993 ILQESHQQALDD-LQAEEDKVNTLAKAKVKLEQQVDDL--ESSLEQEKKIRMDLERAkrklegdlklAQESIMDLENDKQ 1069
Cdd:PRK10246 212 LLTPEQVQSLTAsLQVLTDEEKQLLTAQQQQQQSLNWLtrLDELQQEASRRQQALQQ----------ALAAEEKAQPQLA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1070 QLEerLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVeklRSELLQELEETSERLEEAG 1149
Cdd:PRK10246 282 ALS--LAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQ---SAELQAQQQSLNTWLAEHD 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1150 GATSVQLELnKKQEAEFQKLRRDLEEATLQHEATAATLRKKHADSVAELSeqldnlqrvkqklekekselkLELDDVNSN 1229
Cdd:PRK10246 357 RFRQWNNEL-AGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLT---------------------LTADEVAAA 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1230 TEQLikaktnlekmcrtteDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLED 1309
Cdd:PRK10246 415 LAQH---------------AEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLAD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1310 LKRQLEEEAKAKNALAH--ALQSAQhDCDLLREQYEEEMEAKTEL-----QRALSKANSEVAQWRT-----KYETDAIQR 1377
Cdd:PRK10246 480 VKTICEQEARIKDLEAQraQLQAGQ-PCPLCGSTSHPAVEAYQALepgvnQSRLDALEKEVKKLGEegaalRGQLDALTK 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1378 TEELEEAKkklAQRLQEAEEAV-EAVNAKCSSLEKTKHrLQNEIEDLMADVERsnaaaaaldkkqrnFDKILSEWKQKfE 1456
Cdd:PRK10246 559 QLQRDESE---AQSLRQEEQALtQQWQAVCASLNITLQ-PQDDIQPWLDAQEE--------------HERQLRLLSQR-H 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1457 ESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEK--LE 1534
Cdd:PRK10246 620 ELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTplLE 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1535 LQAALEEAEASLE----------HEEGKILRAQLEFNQVKADYERKLAEKDEEIEQSKRNHLRVVDS---LQTSLDAETR 1601
Cdd:PRK10246 700 TLPQSDDLPHSEEtvaldnwrqvHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQqafLAALLDEETL 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1602 SRNEAlrLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIV-ERRNNLLQSE- 1679
Cdd:PRK10246 780 TQLEQ--LKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQgEIRQQLKQDAd 857
|
730 740
....*....|....*....|
gi 2163567613 1680 -LEELRAMVEQSERARKLAE 1698
Cdd:PRK10246 858 nRQQQQALMQQIAQATQQVE 877
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
858-1109 |
1.56e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.01 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 858 LEKSEARRKELEEKMVSMlqEKNDLQLQVQAEQDNLADAEERCDQLIKNKiqlEAKVKEMTERLEeeeemnaELAAKKRK 937
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDM--KIDHIQQQIKTYNKNIEEQRKKNGENIARK---QNKYDELVEEAK-------TIKAEIEE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 938 LEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENIT------KLTKEKKILQESHQQaLDDLQAEEDK 1011
Cdd:PHA02562 239 LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGGVcptctqQISEGPDRITKIKDK-LKELQHSLEK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1012 VNTlakAKVKLEQQVDDLessLEQEKKIRmDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNariED 1091
Cdd:PHA02562 318 LDT---AIDELEEIMDEF---NEQSKKLL-ELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQ---DE 387
|
250
....*....|....*...
gi 2163567613 1092 EQAISAQLQKKLKELQAR 1109
Cdd:PHA02562 388 LDKIVKTKSELVKEKYHR 405
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
976-1147 |
1.65e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 976 EMAGLDENITKLTKEKKILQESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKirmDLERAKRKLEG--- 1052
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYEEQLGNvrn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1053 --DLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIeeleeeleaeRTGRAKVEKL 1130
Cdd:COG1579 88 nkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL----------DEELAELEAE 157
|
170
....*....|....*..
gi 2163567613 1131 RSELLQELEETSERLEE 1147
Cdd:COG1579 158 LEELEAEREELAAKIPP 174
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
646-670 |
1.65e-05 |
|
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: 47.34 E-value: 1.65e-05
10 20
....*....|....*....|....*
gi 2163567613 646 HRENLNKLMANLKTTHPHFVRCLIP 670
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1435-1612 |
1.98e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1435 AALDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLEtfkrENKNLQEEILDlTEQLGAS 1514
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK----KYEEQLGNVRN-NKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1515 QKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLEFNQVKADYERKLAEKDEEIEQskrnHLRVVDSLQT 1594
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE----LEAEREELAA 170
|
170
....*....|....*...
gi 2163567613 1595 SLDAETRSRNEALRLKKK 1612
Cdd:COG1579 171 KIPPELLALYERIRKRKN 188
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1248-1475 |
1.98e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1248 EDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTrgkltytQQLEDLKRQLEE----EAKAKNA 1323
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-------AEIDKLQAEIAEaeaeIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1324 LAHALQSAQHDCDLLreQYEEEMEAKTELQRALSKAnsEVAQWRTKYETDAIQRT----EELEEAKKKLAQRLQEAEEAV 1399
Cdd:COG3883 88 LGERARALYRSGGSV--SYLDVLLGSESFSDFLDRL--SALSKIADADADLLEELkadkAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163567613 1400 EAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTE 1475
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1247-1474 |
1.98e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1247 TEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKA------ 1320
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAlyrsgg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1321 KNALAHALQSAQHDCDLLR--EQYEEEMEAKTELQRALSKANSEVAQwrtkYETDAIQRTEELEEAKKKLAQRLQEAEEA 1398
Cdd:COG3883 101 SVSYLDVLLGSESFSDFLDrlSALSKIADADADLLEELKADKAELEA----KKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163567613 1399 VEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLST 1474
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1335-1547 |
2.02e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.54 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1335 CDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKH 1414
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1415 RLQNEIEDLM------ADV------ERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELE------ASQKEARSLSTEL 1476
Cdd:PRK05771 118 ELEQEIERLEpwgnfdLDLslllgfKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvVLKELSDEVEEEL 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163567613 1477 fkLKNAYEE-SLEHLETFKRENKNLQEEILDLTEQLgasQKSIHELEKVRKQLDAEKL----ELQAALEEAEASLE 1547
Cdd:PRK05771 198 --KKLGFERlELEEEGTPSELIREIKEELEEIEKER---ESLLEELKELAKKYLEELLalyeYLEIELERAEALSK 268
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1373-1759 |
2.12e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.91 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1373 DAIQRTEELEEAKKKLAQrlqeaeeAVEAVNAKCSSLEKTKHRLQNeiedLMADVERSNAAAAALDKKQRNFDKILSEWK 1452
Cdd:pfam19220 14 EMADRLEDLRSLKADFSQ-------LIEPIEAILRELPQAKSRLLE----LEALLAQERAAYGKLRRELAGLTRRLSAAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1453 QKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKR-------ENKNLQEEILDLTEQLGASQKSIHELEKVR 1525
Cdd:pfam19220 83 GELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERqlaaeteQNRALEEENKALREEAQAAEKALQRAEGEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1526 KQ-------LDAEKLELQAALEEAEASLEheegkilraqlefnqvkadyerKLAEKDEEIEQSKRNHLRVVDSLQTSLDA 1598
Cdd:pfam19220 163 ATarerlalLEQENRRLQALSEEQAAELA----------------------ELTRRLAELETQLDATRARLRALEGQLAA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1599 ETRSRNEALRL----KKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNN 1674
Cdd:pfam19220 221 EQAERERAEAQleeaVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1675 LLQSELEELRAMVEQSERARKLAEQE--------------LIEASERVQLLHSQNTSLinqKKKMEADISQLQTEVEEAI 1740
Cdd:pfam19220 301 GLEADLERRTQQFQEMQRARAELEERaemltkalaakdaaLERAEERIASLSDRIAEL---TKRFEVERAALEQANRRLK 377
|
410
....*....|....*....
gi 2163567613 1741 QECRNaeEKAKKAITDAAM 1759
Cdd:pfam19220 378 EELQR--ERAERALAQGAL 394
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1043-1197 |
2.29e-05 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 49.37 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1043 LERAKRKLEGDLKLAQESIMDLENDKQQLEERLKkkdfELNTLNARIEDEQaisAQLQKKLKELQARieeleeELEAERT 1122
Cdd:COG1193 502 IERARELLGEESIDVEKLIEELERERRELEEERE----EAERLREELEKLR---EELEEKLEELEEE------KEEILEK 568
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2163567613 1123 GRAKVEKLRSELLQELEETSERLEEAggatsvqlelnKKQEAEFQKLRRDLEEATLQHEATAATLRKKHADSVAE 1197
Cdd:COG1193 569 AREEAEEILREARKEAEELIRELREA-----------QAEEEELKEARKKLEELKQELEEKLEKPKKKAKPAKPP 632
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1688-1927 |
2.69e-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: 48.61 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1688 EQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKKE 1767
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1768 QDTSAHLER-MKKNMEQTVKDLQLRLDEAEQLALKGgkKQLQKLEVRVRELENELEAEQKRNAESIKGLRKSERRVKELS 1846
Cdd:COG4942 103 KEELAELLRaLYRLGRQPPLALLLSPEDFLDAVRRL--QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1847 YQTEEDRKnmvRLQDLVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKVQHELDEAEERADMAESqvnklRARSRDIGAKK 1926
Cdd:COG4942 181 AELEEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE-----RTPAAGFAALK 252
|
.
gi 2163567613 1927 G 1927
Cdd:COG4942 253 G 253
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1193-1470 |
2.75e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1193 DSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQR 1272
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1273 AKLQTENSELSRQLEEKEAFINQLTRGKLTytqqLEDLKRQLEEeakaknaLAHALQSAQHDCDLLREQYEE--EMEAKT 1350
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGS----IDKLRKEIER-------LEWRQQTEVLSPEEEKELVEKikELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1351 ELQRALSKANSEVAQWRTKYETDAIQRtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERS 1430
Cdd:COG1340 150 EKAKKALEKNEKLKELRAELKELRKEA-EEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADEL 228
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2163567613 1431 NAAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEAR 1470
Cdd:COG1340 229 HEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1134-1419 |
2.81e-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: 49.35 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1134 LLQELEETSERLEEAGGATSVQLELNKKQEAEFQKL--RRDLEEATLQHEAT---AATLRKKHADSVAELSEQLDNLQRV 1208
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARQAEmdrQAAIYAEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1209 KQKLEKEK---SELKLELDDVNSnTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENS----- 1280
Cdd:pfam17380 357 ERKRELERirqEEIAMEISRMRE-LERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEearqr 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1281 ELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTE--------- 1351
Cdd:pfam17380 436 EVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQamieeerkr 515
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1352 --LQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNE 1419
Cdd:pfam17380 516 klLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESE 585
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1066-1235 |
2.90e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1066 NDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERL 1145
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1146 EEAGgaTSVQLELNKKQEAEFQKLRRDLEEATLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDD 1225
Cdd:COG1579 83 GNVR--NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
170
....*....|
gi 2163567613 1226 VNSNTEQLIK 1235
Cdd:COG1579 161 LEAEREELAA 170
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1363-1502 |
3.01e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.05 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1363 VAQWRTKYETDA------IQRTEELEeakKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERsnAAAAA 1436
Cdd:PRK00409 504 IEEAKKLIGEDKeklnelIASLEELE---RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK--EAQQA 578
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163567613 1437 LDKKQRNFDKILSEWKQKFEESQTELEASQ-KEARSlstelfKLKNAYEESLEHLETFKRENKNLQE 1502
Cdd:PRK00409 579 IKEAKKEADEIIKELRQLQKGGYASVKAHElIEARK------RLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
969-1871 |
3.11e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 49.28 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 969 KVKNLTEEMAGLDENITKLTKEKKILQESHQQalddLQAEEDKVntlakakVKLEQQVDDLessLEQEKKIrMDLERAKR 1048
Cdd:TIGR01612 535 KAKLYKEIEAGLKESYELAKNWKKLIHEIKKE----LEEENEDS-------IHLEKEIKDL---FDKYLEI-DDEIIYIN 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1049 KLEGDLKlaqESIMDLENDKQQLEERLK-KKDFELNtlNARIEDEQAISA-QLQKKLKELQARIEELEEELEAERTGraK 1126
Cdd:TIGR01612 600 KLKLELK---EKIKNISDKNEYIKKAIDlKKIIENN--NAYIDELAKISPyQVPEHLKNKDKIYSTIKSELSKIYED--D 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1127 VEKLRSELLQELEETSerLEEAGGATSVQlELNKKQEAEFQKLRrDLEEATLQ-HEATAATLRKKHADSVAEL-----SE 1200
Cdd:TIGR01612 673 IDALYNELSSIVKENA--IDNTEDKAKLD-DLKSKIDKEYDKIQ-NMETATVElHLSNIENKKNELLDIIVEIkkhihGE 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1201 QLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENS 1280
Cdd:TIGR01612 749 INKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKED 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1281 ELSRQLEE----KEAFINQLTRgkltYTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLlrEQYEEEMEAKTELQRAL 1356
Cdd:TIGR01612 829 EIFKIINEmkfmKDDFLNKVDK----FINFENNCKEKIDSEHEQFAELTNKIKAEISDDKL--NDYEKKFNDSKSLINEI 902
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1357 SKansevaqwrtkyetdAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEdlmaDVERSNaaaaA 1436
Cdd:TIGR01612 903 NK---------------SIEEEYQNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILNKNID----TIKESN----L 959
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1437 LDKKQRN-FDKILSEWKQKFEESQTELEASQKEARslSTELFKLKNAYEESL---------EHLETFKRENKNLQEEILD 1506
Cdd:TIGR01612 960 IEKSYKDkFDNTLIDKINELDKAFKDASLNDYEAK--NNELIKYFNDLKANLgknkenmlyHQFDEKEKATNDIEQKIED 1037
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1507 LTEQLGASQKSIH--------ELEK-VRKQLDAEKLELqaaLEEAEASLEHeegkilraqleFNQVKAD---YERKLAEK 1574
Cdd:TIGR01612 1038 ANKNIPNIEIAIHtsiyniidEIEKeIGKNIELLNKEI---LEEAEINITN-----------FNEIKEKlkhYNFDDFGK 1103
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1575 DEEIEQSKRNHlRVVDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEA--QKQVKALQGYLKDTQLQL 1652
Cdd:TIGR01612 1104 EENIKYADEIN-KIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAisNDDPEEIEKKIENIVTKI 1182
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1653 DDVVRANEDLKE---NIAIVERRnnllQSELEELRAM-VEQSERARKLAEQELIEASERvqllhSQNTSlinqkKKMEAD 1728
Cdd:TIGR01612 1183 DKKKNIYDEIKKllnEIAEIEKD----KTSLEEVKGInLSYGKNLGKLFLEKIDEEKKK-----SEHMI-----KAMEAY 1248
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1729 ISQLQtEVEEAIQECRNaeEKAKKAITDAAMMAEELKKEQDTSAHLerMKKNMEQTVKD-----LQLRLDEAEQLALKGG 1803
Cdd:TIGR01612 1249 IEDLD-EIKEKSPEIEN--EMGIEMDIKAEMETFNISHDDDKDHHI--ISKKHDENISDireksLKIIEDFSEESDINDI 1323
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2163567613 1804 KKQLQK--LEVRVRELENELEAEQKRNAESIKGLRKSER---RVKELSYQTEEDRKNMVRLQDLVDKLQLKVK 1871
Cdd:TIGR01612 1324 KKELQKnlLDAQKHNSDINLYLNEIANIYNILKLNKIKKiidEVKEYTKEIEENNKNIKDELDKSEKLIKKIK 1396
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
987-1319 |
3.39e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.14 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 987 LTKEKKILQESHQQALDDLqaeeDKVNTLAKAKVKLEQQVDDLEsslEQEKKIRMDLERAKRKLEGDLK--LAQESIMDL 1064
Cdd:PRK11281 54 LEAEDKLVQQDLEQTLALL----DKIDRQKEETEQLKQQLAQAP---AKLRQAQAELEALKDDNDEETRetLSTLSLRQL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1065 EndkQQLEER---LKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRakvEKLRSELLQELE-- 1139
Cdd:PRK11281 127 E---SRLAQTldqLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGG---KALRPSQRVLLQae 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1140 ------ETSERLEEAGGATSVQLELNKKQE---AEFQKLRRDLeeATLQhEATAATLRKKHADSVAELSEQLDNLQRVKQ 1210
Cdd:PRK11281 201 qallnaQNDLQRKSLEGNTQLQDLLQKQRDyltARIQRLEHQL--QLLQ-EAINSKRLTLSEKTVQEAQSQDEAARIQAN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1211 KLEKEKSELKLEL--------DDVNSNTEQLIKAKTNLEKMC---RTTEDQ-------------MNEHRSKLEEAQrTVT 1266
Cdd:PRK11281 278 PLVAQELEINLQLsqrllkatEKLNTLTQQNLRVKNWLDRLTqseRNIKEQisvlkgslllsriLYQQQQALPSAD-LIE 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2163567613 1267 DLSTQRAKLQTENSELSRQ---LEEKEAFINQLTRG-KLTYTQQLED-LKRQLEEEAK 1319
Cdd:PRK11281 357 GLADRIADLRLEQFEINQQrdaLFQPDAYIDKLEAGhKSEVTDEVRDaLLQLLDERRE 414
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1275-1541 |
3.89e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.99 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1275 LQTENSELSRQLEEKEAFIN-QLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQ 1353
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1354 ---RALSKANSEVAQWRTKYETDAIQRTEEL-------EEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTkhrlqneiedl 1423
Cdd:pfam00038 103 ndlVGLRKDLDEATLARVDLEAKIESLKEELaflkknhEEEVRELQAQVSDTQVNVEMDAARKLDLTSA----------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1424 MADVERSNAAAAALDKKQrnfdkiLSEW-KQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQE 1502
Cdd:pfam00038 172 LAEIRAQYEEIAAKNREE------AEEWyQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLER 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2163567613 1503 EILDLTE----QLGASQKSIHELEkvrKQLDAEKLELQAALEE 1541
Cdd:pfam00038 246 QLAETEEryelQLADYQELISELE---AELQETRQEMARQLRE 285
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
838-1084 |
4.09e-05 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 48.62 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 838 AETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQdnladaeercdqlikNKIQLEAKVKEM 917
Cdd:pfam18971 603 AKSTGNYDEVKKAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANS---------------QKDEIFALINKE 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 918 TERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENItKLTKEKKILQES 997
Cdd:pfam18971 668 ANRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDL-GINPEWISKVEN 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 998 HQQALDDLQAEEDK-VNTLAKAKVKLEQQVDDLESSLEQEKKI-RMDLERAKRKLEGDLKLAQESIMDLEN-DKQQLEER 1074
Cdd:pfam18971 747 LNAALNEFKNGKNKdFSKVTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKNfSKEQLAQQ 826
|
250
....*....|
gi 2163567613 1075 LKKKDfELNT 1084
Cdd:pfam18971 827 AQKNE-DFNT 835
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1590-1802 |
4.31e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1590 DSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIV 1669
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1670 ER------RNNLLQ--------SELEELRAMVEQSERARKLAEQELIEASERvqlLHSQNTSLINQKKKMEADISQLQTE 1735
Cdd:COG4942 110 LRalyrlgRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAE---LAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1736 ---VEEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTVKDLQLRLDEAEQLALKG 1802
Cdd:COG4942 187 raaLEALKAERQKLLARLEKELAELAAELAELQQEAEE---LEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
969-1224 |
4.35e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 969 KVKNLTEEMAGLDENI----TKLTKEKKILQESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLEsslEQEKKIRMDLE 1044
Cdd:PHA02562 175 KIRELNQQIQTLDMKIdhiqQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELT---DELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1045 rakrKLEGDLKLAQESIMDLENDKQQL--EERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIeeleeeleaert 1122
Cdd:PHA02562 252 ----DPSAALNKLNTAAAKIKSKIEQFqkVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSL------------ 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1123 grakveklrSELLQELEETSERLEEAGGATSVQLELNKKQEAEFQKLRRDLEEAtLQHEATAATLRKKHADSVAELSEQL 1202
Cdd:PHA02562 316 ---------EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKA-KKVKAAIEELQAEFVDNAEELAKLQ 385
|
250 260
....*....|....*....|..
gi 2163567613 1203 DNLQrvkqKLEKEKSELKLELD 1224
Cdd:PHA02562 386 DELD----KIVKTKSELVKEKY 403
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
864-1787 |
4.70e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.89 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 864 RRKELEEKMVSMLQEKNDlqlQVQAEQDNLADAEERCDQLIKNKIqlEAKVKEMTERLEEEEEMNAELAAKKRKLEDECS 943
Cdd:TIGR01612 501 RMKDFKDIIDFMELYKPD---EVPSKNIIGFDIDQNIKAKLYKEI--EAGLKESYELAKNWKKLIHEIKKELEEENEDSI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 944 ELKKDIDDLELSLAKVEKE-------KHATENKVKNLTEEmaglDENITKLTKEKKILqESHQQALDDLqaeedkvntla 1016
Cdd:TIGR01612 576 HLEKEIKDLFDKYLEIDDEiiyinklKLELKEKIKNISDK----NEYIKKAIDLKKII-ENNNAYIDEL----------- 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1017 kAKVKLEQQVDDLESSLEQEKKIRMDLERAkrkLEGDL--------KLAQESIMDLENDKQQLEERLKKKDFELNTL-NA 1087
Cdd:TIGR01612 640 -AKISPYQVPEHLKNKDKIYSTIKSELSKI---YEDDIdalynelsSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIqNM 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1088 RIEDEQAISAQLQKKLKELQARIEELEeeleaertgrakvEKLRSELLQELEETSERLEEAGGATSVQLELNKKQEAEFQ 1167
Cdd:TIGR01612 716 ETATVELHLSNIENKKNELLDIIVEIK-------------KHIHGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELN 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1168 KLRRDLEEATLQH--EATAATLRKKHADSVAELSEQLDNLQRVKQ-KLEKEKSELKLELDDVNSNTEQLIkaktNLEKMC 1244
Cdd:TIGR01612 783 KYKSKISEIKNHYndQINIDNIKDEDAKQNYDKSKEYIKTISIKEdEIFKIINEMKFMKDDFLNKVDKFI----NFENNC 858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1245 RttEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTEN--------SELSRQLEEKEAFINQLTRGKlTYTQQLEDLKRQLEE 1316
Cdd:TIGR01612 859 K--EKIDSEHEQFAELTNKIKAEISDDKLNDYEKKfndsksliNEINKSIEEEYQNINTLKKVD-EYIKICENTKESIEK 935
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1317 EAKAKNALAHALQS---AQHDCDLLREQYEEEME-----AKTELQRALSKA--------NSEVAQW--------RTKYET 1372
Cdd:TIGR01612 936 FHNKQNILKEILNKnidTIKESNLIEKSYKDKFDntlidKINELDKAFKDAslndyeakNNELIKYfndlkanlGKNKEN 1015
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1373 DAIQRTEELEEAKKKLAQRLQEAEEAVEAVN-AKCSSLEKTKHRLQNEI----EDLMADV-ERSNAAAAALDK-----KQ 1441
Cdd:TIGR01612 1016 MLYHQFDEKEKATNDIEQKIEDANKNIPNIEiAIHTSIYNIIDEIEKEIgkniELLNKEIlEEAEINITNFNEikeklKH 1095
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1442 RNFDKILSEWKQKFEEsqteleasqkEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEIldlteqlgasQKSIHEL 1521
Cdd:TIGR01612 1096 YNFDDFGKEENIKYAD----------EINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEI----------KAQINDL 1155
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1522 EKVrkqldAEKLELQAALEEAEASLEHEEGKILRAQLEFNQVKadyerKLAEKDEEIEQSKRNHLRVVD-SLQTSLDAET 1600
Cdd:TIGR01612 1156 EDV-----ADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIK-----KLLNEIAEIEKDKTSLEEVKGiNLSYGKNLGK 1225
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1601 RSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQkQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSEL 1680
Cdd:TIGR01612 1226 LFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSP-EIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIR 1304
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1681 EELRAMVEQSERARKLAEqelIEASERVQLLHSQ-NTSLINQKKKMEADISQLQT-----EVEEAIQECRNAEEKAKKAI 1754
Cdd:TIGR01612 1305 EKSLKIIEDFSEESDIND---IKKELQKNLLDAQkHNSDINLYLNEIANIYNILKlnkikKIIDEVKEYTKEIEENNKNI 1381
|
970 980 990
....*....|....*....|....*....|...
gi 2163567613 1755 TDAAMMAEELKKEQDTSAHLERMKKNMEQTVKD 1787
Cdd:TIGR01612 1382 KDELDKSEKLIKKIKDDINLEECKSKIESTLDD 1414
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1680-1913 |
5.18e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1680 LEELRAMVEQSERARKlAEQELIEASERVQLLhsqntslinqkkkmeADISQLQTEVEEAIQECRNAEE-----KAKKAI 1754
Cdd:COG4913 224 FEAADALVEHFDDLER-AHEALEDAREQIELL---------------EPIRELAERYAAARERLAELEYlraalRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1755 TDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQLQklevrvrELENELEAEQKRNAESIKG 1834
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE-------QLEREIERLERELEERERR 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1835 LRKSERRVKELSYQTEEDRKNMVRLQDLVDKLqlkVKAYKRQAEEAEEQANSNLAKFRKVQHELDEAE-ERADMAESQVN 1913
Cdd:COG4913 361 RARLEALLAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELEaEIASLERRKSN 437
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
929-1066 |
5.53e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 47.36 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 929 AELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENIT-KLTKEKKILQeshQQALDDLQA 1007
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKdLLTDEGGAIA---RKEIKDLQK 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163567613 1008 EEDKVNTLAKAKVK-----LEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLEN 1066
Cdd:cd22656 187 ELEKLNEEYAAKLKakideLKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEK 250
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1755-1922 |
6.01e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 48.10 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1755 TDAAMMAEELKKEQDTsahLERMKKNMEQTVKDLQLRLDEAEQlALKGGKKQLQKLEVRVRELENELEAEQKRNAESIKG 1834
Cdd:pfam05667 310 NEAPAATSSPPTKVET---EEELQQQREEELEELQEQLEDLES-SIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1835 LRKSERRVKELsyqtEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQAnsnLAKFRKVQHELDEAEERADMAESQVNK 1914
Cdd:pfam05667 386 YKVKKKTLDLL----PDAEENIAKLQALVDASAQRLVELAGQWEKHRVPL---IEEYRALKEAKSNKEDESQRKLEEIKE 458
|
....*...
gi 2163567613 1915 LRARSRDI 1922
Cdd:pfam05667 459 LREKIKEV 466
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
836-1059 |
7.19e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 836 KSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKvk 915
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 916 emterLEEEEEMNAELAAKKRKLEDEcSELK-----KDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKE 990
Cdd:COG4942 99 -----LEAQKEELAELLRALYRLGRQ-PPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163567613 991 KKILQESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQE 1059
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1626-1851 |
7.41e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1626 HANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQELIEAS 1705
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1706 ERVQ-----------LLHSQNTS-LINQKKKMEAdISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKKEqdtsah 1773
Cdd:COG3883 93 RALYrsggsvsyldvLLGSESFSdFLDRLSALSK-IADADADLLEELKADKAELEAKKAELEAKLAELEALKAE------ 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2163567613 1774 LERMKKNMEQTVKDLQLRLDEAEQlalkggkkQLQKLEVRVRELENELEAEQKRNAESIKGLRKSERRVKELSYQTEE 1851
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSA--------EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
927-1165 |
7.42e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.61 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 927 MNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEkhatenkVKNLTEEMAGLDENITKLTKEKKILqeSHQQALD-DL 1005
Cdd:PRK05771 66 LPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERL--EPWGNFDlDL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1006 QAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKkirmdLERAKRKLEGDLKLaqesIMDLENDKQQLEERLKKKDFElntl 1085
Cdd:PRK05771 137 SLLLGFKYVSVFVGTVPEDKLEELKLESDVEN-----VEYISTDKGYVYVV----VVVLKELSDEVEEELKKLGFE---- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1086 NARIEDEQAISAQLQKKLKELqarieeleeeleaertgrAKVEKLRSELLQELEETSERLEEAGGATSVQLElNKKQEAE 1165
Cdd:PRK05771 204 RLELEEEGTPSELIREIKEEL------------------EEIEKERESLLEELKELAKKYLEELLALYEYLE-IELERAE 264
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1079-1325 |
8.44e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1079 DFELNTLNARIEDEQAISAQLQKKLKELQARIeeleeeleaertgrakveklrSELLQELEETSERLEEAggatsvqlel 1158
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAEL---------------------EELNEEYNELQAELEAL---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1159 nkkqEAEFQKLRRDLEEAtlqhEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEkselklELDDVNSNTEQLIKAKT 1238
Cdd:COG3883 64 ----QAEIDKLQAEIAEA----EAEIEERREELGERARALYRSGGSVSYLDVLLGSE------SFSDFLDRLSALSKIAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1239 NLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEA 1318
Cdd:COG3883 130 ADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
....*..
gi 2163567613 1319 KAKNALA 1325
Cdd:COG3883 210 AAAAAAA 216
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1432-1855 |
8.54e-05 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 47.75 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1432 AAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKL-KNAYEESLEHLetFKRENKNLQEEILDLTEQ 1510
Cdd:pfam13166 82 KPIFTLGEESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLeADFLDECWKKI--KRKKNSALSEALNGFKYE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1511 LGASQKSIHELEKvrKQLDAEKLELQAALEEAEASLEhEEGKILRAQLEFNQVKADYerklAEKDEEIEQSKRNHLRVVD 1590
Cdd:pfam13166 160 ANFKSRLLREIEK--DNFNAGVLLSDEDRKAALATVF-SDNKPEIAPLTFNVIDFDA----LEKAEILIQKVIGKSSAIE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1591 SLQTSLDAETRSRnEALRLKKKMEGD--LNEMEIQLS-------HANRTAAEAQKQVK-ALQGYLKDTQ---LQLDDVV- 1656
Cdd:pfam13166 233 ELIKNPDLADWVE-QGLELHKAHLDTcpFCGQPLPAErkaaleaHFDDEFTEFQNRLQkLIEKVESAISsllAQLPAVSd 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1657 --RANEDLKENIAIVERRNNLLQSELEELRamveqserarKLAEQELIEASERVQLlhsqnTSLINQKKKMEADISQLQT 1734
Cdd:pfam13166 312 laSLLSAFELDVEDIESEAEVLNSQLDGLR----------RALEAKRKDPFKSIEL-----DSVDAKIESINDLVASINE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1735 EVEEAIQECRNAEEKAKKAITD-AAMMAEELKKEQDTsahLERMKKNMEQTVKDLQLRLDEAEqlalkggkKQLQKLEVR 1813
Cdd:pfam13166 377 LIAKHNEITDNFEEEKNKAKKKlRLHLVEEFKSEIDE---YKDKYAGLEKAINSLEKEIKNLE--------AEIKKLREE 445
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2163567613 1814 VRELENELEAEqKRNAESI-KGLRKSERRVKELSYqtEEDRKN 1855
Cdd:pfam13166 446 IKELEAQLRDH-KPGADEInKLLKAFGFGELELSF--NEEGKG 485
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
855-1177 |
1.15e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.20 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 855 KEALEKSEARRKELE---EKMVSMLQ--EKNDLQLQvQAEqdnlADAEERCDQLIKNKIQLEAKVKEMTerleeeeeMNA 929
Cdd:PLN02939 113 NEQQTNSKDGEQLSDfqlEDLVGMIQnaEKNILLLN-QAR----LQALEDLEKILTEKEALQGKINILE--------MRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 930 ELAAKKRKLedeCSELKKDIDDLELSLAKVEKEkhatenkvknLTEEMAGLDENITKLTKEKKILQESHQQALDDLQAEE 1009
Cdd:PLN02939 180 SETDARIKL---AAQEKIHVEILEEQLEKLRNE----------LLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1010 DKVNTLAKAK---VKLEQQVDDLESSLeqekkirmdlerakRKLEGDLKLAQESIMDLENDKQQ-LEERLKKKDFELNTL 1085
Cdd:PLN02939 247 AELIEVAETEervFKLEKERSLLDASL--------------RELESKFIVAQEDVSKLSPLQYDcWWEKVENLQDLLDRA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1086 NARIEDEQAISAQ---LQKKLKELQARIeeleeeleaertGRAKVEKLRSELL----QELEETSERLEEAGGATSVQLEL 1158
Cdd:PLN02939 313 TNQVEKAALVLDQnqdLRDKVDKLEASL------------KEANVSKFSSYKVellqQKLKLLEERLQASDHEIHSYIQL 380
|
330
....*....|....*....
gi 2163567613 1159 NKKQEAEFQKLRRDLEEAT 1177
Cdd:PLN02939 381 YQESIKEFQDTLSKLKEES 399
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
856-1413 |
1.17e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 856 EALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTER----LEEEEEMNAEL 931
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEynnaMDDYNNLKSAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 932 aAKKRKLEDECSELKKDIDDLELSLAKVEKEKhateNKVKNLTEEMAGLDEN--------ITKLTKEKKILqESHQQALD 1003
Cdd:PRK01156 242 -NELSSLEDMKNRYESEIKTAESDLSMELEKN----NYYKELEERHMKIINDpvyknrnyINDYFKYKNDI-ENKKQILS 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1004 DLQAEEDKVNTLAKAKVKLEQQVDDLEssleqEKKIRM-DLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFEL 1082
Cdd:PRK01156 316 NIDAEINKYHAIIKKLSVLQKDYNDYI-----KKKSRYdDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMS 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1083 NTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAErtgRAKVEKLRSElLQELEETSERLEEAG-----GATSVQLE 1157
Cdd:PRK01156 391 AFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSL---NQRIRALREN-LDELSRNMEMLNGQSvcpvcGTTLGEEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1158 LNKKQEAEFQKLRRDLEEAT-LQHEATAATLRKKHADSVAEL--SEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLI 1234
Cdd:PRK01156 467 SNHIINHYNEKKSRLEEKIReIEIEVKDIDEKIVDLKKRKEYleSEEINKSINEYNKIESARADLEDIKIKINELKDKHD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1235 K---AKTNLEKMCRTTEDQMNEHRSKLeEAQRTVTDLSTqrakLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLK 1311
Cdd:PRK01156 547 KyeeIKNRYKSLKLEDLDSKRTSWLNA-LAVISLIDIET----NRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSI 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1312 RQLEEEAKAKNALAHALQSAQHDCDLLREQ---YEEEMEAKTELQRALSKANSEVAQWRT--KYETDAIQRTE----ELE 1382
Cdd:PRK01156 622 REIENEANNLNNKYNEIQENKILIEKLRGKidnYKKQIAEIDSIIPDLKEITSRINDIEDnlKKSRKALDDAKanraRLE 701
|
570 580 590
....*....|....*....|....*....|.
gi 2163567613 1383 EAKKKLAQRLQEAEEAVEAVNAKCSSLEKTK 1413
Cdd:PRK01156 702 STIEILRTRINELSDRINDINETLESMKKIK 732
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
854-1394 |
1.38e-04 |
|
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: 47.05 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 854 LKEALEKSEARRKELEEKMVSMLQEKNDLQLQ-----VQAEQDNLADAEERCDQLIKNKIQLEAK----VKEMTERLEEE 924
Cdd:pfam07111 120 LRAALAGAEMVRKNLEEGSQRELEEIQRLHQEqlsslTQAHEEALSSLTSKAEGLEKSLNSLETKrageAKQLAEAQKEA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 925 EEMNAELAAKKRKLEDECS---ELKKDIDDLELSlakvEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQESHQQA 1001
Cdd:pfam07111 200 ELLRKQLSKTQEELEAQVTlveSLRKYVGEQVPP----EVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1002 LDDLQAEEDKVNTLAKAKVKLEQQVDDLESSL------------EQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQ 1069
Cdd:pfam07111 276 THMLALQEEELTRKIQPSDSLEPEFPKKCRSLlnrwrekvfalmVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQA 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1070 QLEERLKKKdfelntlNARIEDEQAISAQLQKKLKELQ-ARIEELEEELEAERTGRAKVEKLRSELLQeLEETSERLEEA 1148
Cdd:pfam07111 356 ILQRALQDK-------AAEVEVERMSAKGLQMELSRAQeARRRQQQQTASAEEQLKFVVNAMSSTQIW-LETTMTRVEQA 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1149 GGATSvqlELNKKQEAEFQKLR-------RDLEEATLQHEATAATLRKKHADsvAELSEQLDNLQRVKQKLEKE------ 1215
Cdd:pfam07111 428 VARIP---SLSNRLSYAVRKVHtikglmaRKVALAQLRQESCPPPPPAPPVD--ADLSLELEQLREERNRLDAElqlsah 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1216 --KSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQ---TENSELSRQ-LEEK 1289
Cdd:pfam07111 503 liQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRqelTQQQEIYGQaLQEK 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1290 EAFINQLTRgkltytQQLEDLKRQLEEEAKAKNALAHALQSAQHdcdllreQYEEEMEAKTELQRALSKANSEVAQWRTK 1369
Cdd:pfam07111 583 VAEVETRLR------EQLSDTKRRLNEARREQAKAVVSLRQIQH-------RATQEKERNQELRRLQDEARKEEGQRLAR 649
|
570 580
....*....|....*....|....*
gi 2163567613 1370 yetdaiqRTEELEEAKKKLAQRLQE 1394
Cdd:pfam07111 650 -------RVQELERDKNLMLATLQQ 667
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1484-1623 |
1.58e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1484 EESLEHLeTFKRENKNLQEEILDLTEQ---LGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQLEf 1560
Cdd:COG2433 379 EEALEEL-IEKELPEEEPEAEREKEHEereLTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE- 456
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2163567613 1561 nqvkadyERKLAEKDEEIeqSKRNhlRVVDSLQTSLDaETRSRNEALRLKKKMEGDLNEMEIQ 1623
Cdd:COG2433 457 -------ERREIRKDREI--SRLD--REIERLERELE-EERERIEELKRKLERLKELWKLEHS 507
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1163-1429 |
1.58e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.07 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1163 EAEFQKLRRDLEEATLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLek 1242
Cdd:pfam00038 24 EQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSA-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1243 mcrttEDQMNEHRSKLEEAQRTVTDLstqRAKLQTENSELSRQLEEKEAFINQLTRgkltytqQLEDLKRQLEEEAKAKN 1322
Cdd:pfam00038 102 -----ENDLVGLRKDLDEATLARVDL---EAKIESLKEELAFLKKNHEEEVRELQA-------QVSDTQVNVEMDAARKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1323 ALAHALQSaqhdcdlLREQYEEemeaktelQRALSKANSEvAQWRTKYE---TDAIQRTEELEEAKKKLAQ---RLQEAE 1396
Cdd:pfam00038 167 DLTSALAE-------IRAQYEE--------IAAKNREEAE-EWYQSKLEelqQAAARNGDALRSAKEEITElrrTIQSLE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2163567613 1397 EAVEAVNAKCSSLEK----TKHRLQNEIED---LMADVER 1429
Cdd:pfam00038 231 IELQSLKKQKASLERqlaeTEERYELQLADyqeLISELEA 270
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
847-1288 |
1.74e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.74 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 847 MKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLiknkiqlEAKVKEMTERLEEEEE 926
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL-------QTEVDALRLRLEEKES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 927 MNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQE------SHQQ 1000
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTdssntdTALT 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1001 ALDDLQAEEDKV-NTLAKAKVKLEQQVDDLESSLEQEKKirmDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKD 1079
Cdd:pfam10174 440 TLEEALSEKERIiERLKEQREREDRERLEELESLKKENK---DLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKD 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1080 FELNTLNARIEDEQAISAQLQKKLKELQarieeleEELEAERTGRAKVEKLRselLQELEETSERLEEAGGATSVQLELN 1159
Cdd:pfam10174 517 SKLKSLEIAVEQKKEECSKLENQLKKAH-------NAEEAVRTNPEINDRIR---LLEQEVARYKEESGKAQAEVERLLG 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1160 KKQEAEFQKLRRDLEEATLQheataaTLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTN 1239
Cdd:pfam10174 587 ILREVENEKNDKDKKIAELE------SLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEEL 660
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2163567613 1240 LEKMCRTTEdQMNEHRSKLEEAQRTVTDLSTQRAKLQTENselSRQLEE 1288
Cdd:pfam10174 661 MGALEKTRQ-ELDATKARLSSTQQSLAEKDGHLTNLRAER---RKQLEE 705
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1668-1786 |
1.77e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1668 IVERRNNLLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEA----DISQLQTEVEEAIQEC 1743
Cdd:PRK00409 503 IIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeedkLLEEAEKEAQQAIKEA 582
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2163567613 1744 RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVK 1786
Cdd:PRK00409 583 KKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEK 625
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1211-1426 |
1.80e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1211 KLEKEK-SELKLELDDVN---SNTEQLIKAKTNLEKMCRTTEDQMN-EHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQ 1285
Cdd:PHA02562 170 KLNKDKiRELNQQIQTLDmkiDHIQQQIKTYNKNIEEQRKKNGENIaRKQNKYDELVEEAKTIKAEIEELTDELLNLVMD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1286 LEEKEAFINQLTRGKLTYTQQLEDLKR----------------QLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAK 1349
Cdd:PHA02562 250 IEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIM 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1350 TELQRALSKANsevaQWRTKYETD--AIQRTEELEEAKKKLAQRLQEA----EEAVEAVNA-------KCSSLEKTKHRL 1416
Cdd:PHA02562 330 DEFNEQSKKLL----ELKNKISTNkqSLITLVDKAKKVKAAIEELQAEfvdnAEELAKLQDeldkivkTKSELVKEKYHR 405
|
250
....*....|
gi 2163567613 1417 QNeIEDLMAD 1426
Cdd:PHA02562 406 GI-VTDLLKD 414
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1561-1904 |
1.95e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.48 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1561 NQVKADYERKLAEKDEEIEQS---KRNHLRVVDSLQTSLDAETRSRNEaLRLKKKMEGDLnEMEIQLS--HANR--TAAE 1633
Cdd:COG3096 267 NYVAADYMRHANERRELSERAlelRRELFGARRQLAEEQYRLVEMARE-LEELSARESDL-EQDYQAAsdHLNLvqTALR 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1634 AQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEEL--------RAMVEQSERArkLAEQELIEAS 1705
Cdd:COG3096 345 QQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLksqladyqQALDVQQTRA--IQYQQAVQAL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1706 ERVQ-LLHSQNTSLINQKKKMEAdisqLQTEVEEAIQECRNAEEK-----AKKAITDAAM-----MAEELKKEQdtsAHl 1774
Cdd:COG3096 423 EKARaLCGLPDLTPENAEDYLAA----FRAKEQQATEEVLELEQKlsvadAARRQFEKAYelvckIAGEVERSQ---AW- 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1775 ermkknmeQTVKDLQLRLDEAEQLAlkggkKQLQKLEVRVRELENELEAEQKrnaesikglrkSERRVKELSYQTEEDRK 1854
Cdd:COG3096 495 --------QTARELLRRYRSQQALA-----QRLQQLRAQLAELEQRLRQQQN-----------AERLLEEFCQRIGQQLD 550
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1855 NmvrlQDLVDKLQLKVKAykrQAEEAEEQANSNLAKFRKVQHELDEAEER 1904
Cdd:COG3096 551 A----AEELEELLAELEA---QLEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
862-1421 |
1.98e-04 |
|
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: 46.28 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 862 EARRKELEEKMVSMLQEKNDLQLQVQA-EQDNLADAEERCdqliknkiQLEAKVKEMTERLEEEEEMNAElAAKKRKLED 940
Cdd:pfam07111 74 ELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAG--------QAEAEGLRAALAGAEMVRKNLE-EGSQRELEE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 941 ECSELKKDIDDL----ELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQESHQQALDDLQAEEDKVNTLA 1016
Cdd:pfam07111 145 IQRLHQEQLSSLtqahEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1017 K-AKVKLEQQVDDLESSLEQEKKIRM--DLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIED-- 1091
Cdd:pfam07111 225 KyVGEQVPPEVHSQTWELERQELLDTmqHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKkc 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1092 --------EQAISAQLQKKLKELQAR-----IEELEEELEAERTGRAKVEKLRSELLQEleETSERLEEAGGATSVQLEL 1158
Cdd:pfam07111 305 rsllnrwrEKVFALMVQLKAQDLEHRdsvkqLRGQVAELQEQVTSQSQEQAILQRALQD--KAAEVEVERMSAKGLQMEL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1159 NKKQEAefqklRRDLEEATLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSnTEQLIKAKT 1238
Cdd:pfam07111 383 SRAQEA-----RRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHT-IKGLMARKV 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1239 NLEkmcrttedQMNEHRSKLEEAQRTV-TDLSTQRAKLQTENSELSRQLEEKEAFINQ-LTRGKltytQQLEDLKRQLEE 1316
Cdd:pfam07111 457 ALA--------QLRQESCPPPPPAPPVdADLSLELEQLREERNRLDAELQLSAHLIQQeVGRAR----EQGEAERQQLSE 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1317 EAKaknALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYeTDAIQrtEELEEAKKKLAQRLQEAE 1396
Cdd:pfam07111 525 VAQ---QLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIY-GQALQ--EKVAEVETRLREQLSDTK 598
|
570 580
....*....|....*....|....*....
gi 2163567613 1397 ----EAVEAVNAKCSSLEKTKHRLQNEIE 1421
Cdd:pfam07111 599 rrlnEARREQAKAVVSLRQIQHRATQEKE 627
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1430-1637 |
2.01e-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: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1430 SNAAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTE 1509
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1510 QLG----ASQKS-------------------IHELEKVRKQLDAEK------LELQAALEEAEASLEHEEGKILRAQLEF 1560
Cdd:COG3883 87 ELGerarALYRSggsvsyldvllgsesfsdfLDRLSALSKIADADAdlleelKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163567613 1561 NQVKADYERKLAEKDEEIEQSKRNHLRVVDSLQtSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQ 1637
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA-ELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
939-1165 |
2.01e-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: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 939 EDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQESHQQALDDLQAEEDKVNTLAKA 1018
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1019 KVKLEQQVDDLESSLEQEK--------KIRMDLERAKRKLEGDLKLAQEsimDLENDKQQLEERLkkkdfelntlnariE 1090
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESfsdfldrlSALSKIADADADLLEELKADKA---ELEAKKAELEAKL--------------A 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2163567613 1091 DEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEEAGGATSVQLELNKKQEAE 1165
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1030-1341 |
2.44e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1030 ESSLEQEKKIRMDLER-AKRKL-EGDLKLAQesimdlendkQQLEERLKkkdfelntLNARIEDEQAISAQLQKKLKELQ 1107
Cdd:PRK11281 32 NGDLPTEADVQAQLDAlNKQKLlEAEDKLVQ----------QDLEQTLA--------LLDKIDRQKEETEQLKQQLAQAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1108 ARIeeleeeleaeRTGRAKVEKLRSELLQELEETSERLEEAggatsvQLE--LNKKQEaEFQKLRRDLEEATLQheatAA 1185
Cdd:PRK11281 94 AKL----------RQAQAELEALKDDNDEETRETLSTLSLR------QLEsrLAQTLD-QLQNAQNDLAEYNSQ----LV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1186 TLRKKHADSVAELSEQLDNLQRVKQKLEKEKSE-----------LKLELDDVNSNTEQ--------------------LI 1234
Cdd:PRK11281 153 SLQTQPERAQAALYANSQRLQQIRNLLKGGKVGgkalrpsqrvlLQAEQALLNAQNDLqrkslegntqlqdllqkqrdYL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1235 KAKTN-LEKMCRTTEDQMNEHRskLEEAQRTVTDLSTQRAKLQ-TENSELSRQLEekeafIN-QLTRGKLTYTQQLEDLK 1311
Cdd:PRK11281 233 TARIQrLEHQLQLLQEAINSKR--LTLSEKTVQEAQSQDEAARiQANPLVAQELE-----INlQLSQRLLKATEKLNTLT 305
|
330 340 350
....*....|....*....|....*....|
gi 2163567613 1312 RQleeEAKAKNALAHALQSAQHdcdlLREQ 1341
Cdd:PRK11281 306 QQ---NLRVKNWLDRLTQSERN----IKEQ 328
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1097-1547 |
2.48e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1097 AQLQKKLKElqarieeleeeleaertgrakveklRSELLQELEETSERLEEaggatsvQLELNKKQEAEFQKLRRDLEEA 1176
Cdd:pfam07888 34 NRLEECLQE-------------------------RAELLQAQEAANRQREK-------EKERYKRDREQWERQRRELESR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1177 TLQHEATAATLRKKHadsvAELSEQLDNLQRVKQKLEKEKSELKleldDVNSNTEQLIKaktNLEKMCRTTEDQMNEHRS 1256
Cdd:pfam07888 82 VAELKEELRQSREKH----EELEEKYKELSASSEELSEEKDALL----AQRAAHEARIR---ELEEDIKTLTQRVLERET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1257 KLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEafinqltrgkltytqqlEDLKRQLEEEAKAKNALahalqsAQHDCD 1336
Cdd:pfam07888 151 ELERMKERAKKAGAQRKEEEAERKQLQAKLQQTE-----------------EELRSLSKEFQELRNSL------AQRDTQ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1337 LLREQyeeemEAKTELQRALSKANSEVAQwrtkyetdaiqrTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRL 1416
Cdd:pfam07888 208 VLQLQ-----DTITTLTQKLTTAHRKEAE------------NEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRT 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1417 QneiedlmADVERSNAAAAALDKKQRNFDKILSE----WKQKFEESQTELEASQKEARSLSTELFKLKNAYEEslEHLET 1492
Cdd:pfam07888 271 Q-------AELHQARLQAAQLTLQLADASLALREgrarWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE--ERMER 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2163567613 1493 FKRENKNLQEEILDLTeQLGASQKSIHEL-------EKVRKQLDAEKLELQAALEEAEASLE 1547
Cdd:pfam07888 342 EKLEVELGREKDCNRV-QLSESRRELQELkaslrvaQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1739-1924 |
3.28e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1739 AIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlALKGGKKQLQKLEVRVRELE 1818
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-ELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1819 NELEAEQKRNAESIKGLRKS------------------ERRVKELSYQTEEDRKNMV-------RLQDLVDKLQLKVKAY 1873
Cdd:COG4942 97 AELEAQKEELAELLRALYRLgrqpplalllspedfldaVRRLQYLKYLAPARREQAEelradlaELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2163567613 1874 KRQAEEAEEQANSNLAKFRKVQHELDEAEERADMAESQVNKLRARSRDIGA 1924
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
836-1050 |
3.37e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 836 KSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLAdaeERCDQLIKNKIQLEAKVK 915
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA---ELLRALYRLGRQPPLALL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 916 EMTERLEEEEEMNAELAAKKRkledecsELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQ 995
Cdd:COG4942 126 LSPEDFLDAVRRLQYLKYLAP-------ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2163567613 996 ESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQ--EKKIRMDLERAKRKL 1050
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAaaERTPAAGFAALKGKL 255
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1670-1918 |
3.49e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.91 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1670 ERRNNLLQSELEELRAMVE-QSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEE 1748
Cdd:pfam00038 24 EQQNKLLETKISELRQKKGaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAEN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1749 --KAKKAITDAAMMA--------EELKKEqdtsahLERMKKNMEQTVKDLQLRL-DEAEQLALKGGKKQlqKLEVRVREL 1817
Cdd:pfam00038 104 dlVGLRKDLDEATLArvdleakiESLKEE------LAFLKKNHEEEVRELQAQVsDTQVNVEMDAARKL--DLTSALAEI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1818 ENELEAEQKRNAESIKGLRKSerrvkelsyQTEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKVQHE 1897
Cdd:pfam00038 176 RAQYEEIAAKNREEAEEWYQS---------KLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQ 246
|
250 260
....*....|....*....|.
gi 2163567613 1898 LDEAEERADMAESQVNKLRAR 1918
Cdd:pfam00038 247 LAETEERYELQLADYQELISE 267
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1495-1793 |
3.49e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.91 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1495 RENKNLQEEILDLTEQLGASQKSIH-----ELEKVRKQLDaeklelQAALEEAEASLEheegkILRAQLEFNQVKADYER 1569
Cdd:pfam00038 25 QQNKLLETKISELRQKKGAEPSRLYslyekEIEDLRRQLD------TLTVERARLQLE-----LDNLRLAAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1570 KLAEKdEEIEQSKRNHLRVVDSL---QTSLDAETRSRNEALR-LKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYL 1645
Cdd:pfam00038 94 ELNLR-TSAENDLVGLRKDLDEAtlaRVDLEAKIESLKEELAfLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1646 KDTQLQLDDVVRAN-EDLKENiaiverrnnlLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKK 1724
Cdd:pfam00038 173 AEIRAQYEEIAAKNrEEAEEW----------YQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKAS 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2163567613 1725 MEADISQLQteveeaiqecrnaeekakkaitdaAMMAEELKKEQDTSAHLER----MKKNMEQTVKDLQLRLD 1793
Cdd:pfam00038 243 LERQLAETE------------------------ERYELQLADYQELISELEAelqeTRQEMARQLREYQELLN 291
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1306-1496 |
3.50e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1306 QLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYEtdaiQRTEELeeak 1385
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE----ERREEL---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1386 KKLAQRLQEAEEAVEAVNA------------KCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNfdkiLSEWKQ 1453
Cdd:COG3883 89 GERARALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE----LEALKA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2163567613 1454 KFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRE 1496
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1123-1329 |
4.03e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1123 GRAKVEKLRSELLQELEETSER-LEEAggatsvQLEL-NKKQEA------EFQKLRRDLEeatlqheataatlrKKHADS 1194
Cdd:PRK12704 21 GYFVRKKIAEAKIKEAEEEAKRiLEEA------KKEAeAIKKEAlleakeEIHKLRNEFE--------------KELRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1195 VAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEaqrtVTDLSTQRAK 1274
Cdd:PRK12704 81 RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER----ISGLTAEEAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163567613 1275 lqtenSELSRQLEEKeafinqltrgkltYTQQLEDLKRQLEEEAK------AKNALAHALQ 1329
Cdd:PRK12704 157 -----EILLEKVEEE-------------ARHEAAVLIKEIEEEAKeeadkkAKEILAQAIQ 199
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1441-1844 |
4.29e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1441 QRNFDKI---LSEWKQKFEEsqteleasqkeaRSLSTELFKLKNAY--EESLEHLETFKRENKNLQeeildlTEQLGASQ 1515
Cdd:PRK04778 24 RKRNYKRideLEERKQELEN------------LPVNDELEKVKKLNltGQSEEKFEEWRQKWDEIV------TNSLPDIE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1516 KSIHELEKvrkqlDAEKLELQAA---LEEAEASLEHEEGKILRAQLEFNQVKADYErklaEKDEEIEQSKRNHlrvvDSL 1592
Cdd:PRK04778 86 EQLFEAEE-----LNDKFRFRKAkheINEIESLLDLIEEDIEQILEELQELLESEE----KNREEVEQLKDLY----REL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1593 QTSLDAETRSRNEALrlkKKMEGDLNEMEIQLSH------------ANRTAAEAQKQVKALQGYLKD-----TQL----- 1650
Cdd:PRK04778 153 RKSLLANRFSFGPAL---DELEKQLENLEEEFSQfveltesgdyveAREILDQLEEELAALEQIMEEipellKELqtelp 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1651 -QLDDVVRANEDLKENIAIVERRNnlLQSELEELRAMVEQSERArkLAEQELIEASERVQLLHSQNTSLInqkkkmeadi 1729
Cdd:PRK04778 230 dQLQELKAGYRELVEEGYHLDHLD--IEKEIQDLKEQIDENLAL--LEELDLDEAEEKNEEIQERIDQLY---------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1730 SQLQTEVEeaiqeCRNAEEKAKKAITDAAMMAEELKKEqdTSAHLERMKKNME------QTVKDLQLRLDEAE------Q 1797
Cdd:PRK04778 296 DILEREVK-----ARKYVEKNSDTLPDFLEHAKEQNKE--LKEEIDRVKQSYTlneselESVRQLEKQLESLEkqydeiT 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1798 LALKGGKKQLQKLEVRVRELENEL---EAEQKRNAESIKGLRKSERRVKE 1844
Cdd:PRK04778 369 ERIAEQEIAYSELQEELEEILKQLeeiEKEQEKLSEMLQGLRKDELEARE 418
|
|
| F-BAR_PSTPIP2 |
cd07672 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ... |
1231-1419 |
4.33e-04 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 2; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 2 (PSTPIP2), also known as Macrophage Actin-associated tYrosine Phosphorylated protein (MAYP), is mostly expressed in hematopoietic cells but is also expressed in the brain. It is involved in regulating cell adhesion and motility. Mutations in the gene encoding murine PSTPIP2 can cause autoinflammatory disorders such as chronic multifocal osteomyelitis and macrophage autoinflammatory disease. PSTPIP2 contains an N-terminal F-BAR domain and lacks the PEST motifs and SH3 domain that are found in PSTPIP1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153356 [Multi-domain] Cd Length: 240 Bit Score: 44.17 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1231 EQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDL 1310
Cdd:cd07672 8 DCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKKKPCGQTEINTLKRSLDVFKQQIDNVGQSHIQLAQTLRDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1311 KRQLE---EEAKAKNALAHALQSAQHDCDLLreQYEEEMEAK-TELQRALSKANSEVAQWRTKYETDAIQRteelEEAKK 1386
Cdd:cd07672 88 AKKMEdfrERQKLARKKIELIMDAIHKQRAM--QFKKTMESKkNYEQKCRDKDEAEQAVNRNANLVNVKQQ----EKLFA 161
|
170 180 190
....*....|....*....|....*....|...
gi 2163567613 1387 KLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNE 1419
Cdd:cd07672 162 KLAQSKQNAEDADRLYMQNISVLDKIREDWQKE 194
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1306-1546 |
4.56e-04 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 43.94 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1306 QLEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVaqwrtkyeTDAIQRTEELEEAK 1385
Cdd:pfam06008 20 NLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAES--------ERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1386 KKLAQRLQEAEEAVEAVNAKCSSL-EKTKHRLQNEIEDLMADVERSNaaaaaLDKKQRNFDKILSEWKQKFEESQTELEA 1464
Cdd:pfam06008 92 KNLIDNIKEINEKVATLGENDFALpSSDLSRMLAEAQRMLGEIRSRD-----FGTQLQNAEAELKAAQDLLSRIQTWFQS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1465 SQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLteqLGASQKSIHELEKVRKQLDAEKLELQAALEEAEA 1544
Cdd:pfam06008 167 PQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRL---NLANQANLREFQRKKEEVSEQKNQLEETLKTARD 243
|
..
gi 2163567613 1545 SL 1546
Cdd:pfam06008 244 SL 245
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
832-1186 |
4.78e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 832 KPLLKSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMlQEKNDLQLQVQAEQDNLADAEERcdQLikNKIQLE 911
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKAR-QAEMDRQAAIYAEQERMAMERER--EL--ERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 912 AKVKEMTERLEEEEEMNAElaaKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDenitKLTKEK 991
Cdd:pfam17380 357 ERKRELERIRQEEIAMEIS---RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEME----QIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 992 KILQESHQQALDDLQAEEdkVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKlegdlklaqesimdlenDKQQL 1071
Cdd:pfam17380 430 EEARQREVRRLEEERARE--MERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD-----------------RKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1072 EERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEEEleaertgRAKVEKLRSEllQELEETSERLEEAGGA 1151
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERR-------REAEEERRKQ--QEMEERRRIQEQMRKA 561
|
330 340 350
....*....|....*....|....*....|....*
gi 2163567613 1152 TSVQLELnKKQEAEFQKLRRDLEEATLQHEATAAT 1186
Cdd:pfam17380 562 TEERSRL-EAMEREREMMRQIVESEKARAEYEATT 595
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1617-1758 |
5.05e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1617 LNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSEL------EELRAM---V 1687
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnKEYEALqkeI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163567613 1688 EQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAITDAA 1758
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1205-1329 |
5.83e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 42.61 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1205 LQRVKQkLEKEKSELKLELDDVNSNTEQLIKAKTNL-EKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELS 1283
Cdd:pfam08614 13 LDRTAL-LEAENAKLQSEPESVLPSTSSSKLSKASPqSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELE 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2163567613 1284 RQLEEKEAFINQLTRGKltytQQLEDLKRQLEEEAKAKNALAHALQ 1329
Cdd:pfam08614 92 KKLREDERRLAALEAER----AQLEEKLKDREEELREKRKLNQDLQ 133
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1565-1783 |
6.30e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 45.21 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1565 ADYERklAEKDEEI-EQSKRNHLRVVDSLQTSLDAETRSR--NEALRLKKKMEGDLNEMEIQLSHANRT----AAEAQKQ 1637
Cdd:NF012221 1562 ADKER--AEADRQRlEQEKQQQLAAISGSQSQLESTDQNAleTNGQAQRDAILEESRAVTKELTTLAQGldalDSQATYA 1639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1638 VKALQ--------GYLKDTQLQLDDVVR-ANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQelieaserv 1708
Cdd:NF012221 1640 GESGDqwrnpfagGLLDRVQEQLDDAKKiSGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQ--------- 1710
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2163567613 1709 qllhsqntslinqkkkmeaDISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ 1783
Cdd:NF012221 1711 -------------------DIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQ 1766
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1623-1828 |
6.76e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.48 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1623 QLSHANRTAAEAQKQVKALQgylKDTQLQLDDVVRANEDLKENiaiverrnnllQSELEELRAMVEQSERARKLAEQELI 1702
Cdd:pfam00261 23 KLEEAEKRAEKAEAEVAALN---RRIQLLEEELERTEERLAEA-----------LEKLEEAEKAADESERGRKVLENRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1703 EASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLE------- 1775
Cdd:pfam00261 89 KDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEaseekas 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2163567613 1776 RMKKNMEQTVKDLQLRLDEAEQLALKgGKKQLQKLEVRVRELENELEAEQKRN 1828
Cdd:pfam00261 169 EREDKYEEQIRFLTEKLKEAETRAEF-AERSVQKLEKEVDRLEDELEAEKEKY 220
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1745-1931 |
7.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1745 NAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLaLKGGKKQLQKLEVRVRELE---NEL 1821
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE-LPELREELEKLEKEVKELEelkEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1822 EAEQKRNAESIKGLRKSERRVKELSYQTEEDRKNMVRLQDLVDKLQlKVKAYKRQAEEAEEQANSNLAKFRKVQHELDEA 1901
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190
....*....|....*....|....*....|
gi 2163567613 1902 EERADMAESQVNKLRARSRDIGAKKGLNEE 1931
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKE 349
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
933-1239 |
7.78e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 44.65 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 933 AKKRKLEDECSELK----KDIDDLELSLAKVEKEKHATENKVKNLTEEMAG----------LDENITKLTKEK-KILQES 997
Cdd:PTZ00108 1031 AKKKDLVKELKKLGyvrfKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEElgaavsydylLSMPIWSLTKEKvEKLNAE 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 998 HQQALDDLQA-EEDKVNTLAKAKvkLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESI--MDLENDKQQLEER 1074
Cdd:PTZ00108 1111 LEKKEKELEKlKNTTPKDMWLED--LDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKlkKKEKKKKKSSADK 1188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1075 LKKKDFELNTLNARIEDEQAISAQLQKKLKELQAriEELEEELEAERTGRAKVEKLRSELLQELEETSERLEEAGGATSV 1154
Cdd:PTZ00108 1189 SKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSG--SDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLS 1266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1155 QLELNKKQEAEFQKLRRDLEEATlqheaTAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSEL-KLELDDVNSNTEQL 1233
Cdd:PTZ00108 1267 KEGKPKNAPKRVSAVQYSPPPPS-----KRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKsEKKTARKKKSKTRV 1341
|
....*.
gi 2163567613 1234 IKAKTN 1239
Cdd:PTZ00108 1342 KQASAS 1347
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1099-1856 |
7.87e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.43 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1099 LQKKLKELQarieeleeeleaertgrAKVEKLRSELLQELEETSERLEEAGGATSVQLelnKKQEAefqklrrdleeatl 1178
Cdd:pfam10174 1 LQAQLRDLQ-----------------RENELLRRELDIKESKLGSSMNSIKTFWSPEL---KKERA-------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1179 qheataatLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELD---DVNSnteqlikaktNLEKMCRTTEDQMNEHR 1255
Cdd:pfam10174 47 --------LRKEEAARISVLKEQYRVTQEENQHLQLTIQALQDELRaqrDLNQ----------LLQQDFTTSPVDGEDKF 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1256 SKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFIN--QLTRG-------KLTYTQQLEDL-KRQLEEEAKAKNALA 1325
Cdd:pfam10174 109 STPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIEtqKQTLGardesikKLLEMLQSKGLpKKSGEEDWERTRRIA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1326 HALQSAQHDCDLLREQYEEEMEAKTELQRALSKANsevaqwrtkyetdaiqrteelEEAKKKLAQRLQEAEEaveavnAK 1405
Cdd:pfam10174 189 EAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQP---------------------DPAKTKALQTVIEMKD------TK 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1406 CSSLEKTKHRLQNEIEDLmadveRSNAAAAALDK----KQRNFDKILSEW-KQKFEESQTELEASQKEARSLSTELFKLK 1480
Cdd:pfam10174 242 ISSLERNIRDLEDEVQML-----KTNGLLHTEDReeeiKQMEVYKSHSKFmKNKIDQLKQELSKKESELLALQTKLETLT 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1481 NAYEESLEHLETFK-------RENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLEHEEGKI 1553
Cdd:pfam10174 317 NQNSDCKQHIEVLKesltakeQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKI 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1554 LRAQLEFNQVkadyERKLAEKDEEIEQSKRNhlrvVDSLQT---SLDAETRSRNEAL--------RLKKKMEGDLNEMEI 1622
Cdd:pfam10174 397 NVLQKKIENL----QEQLRDKDKQLAGLKER----VKSLQTdssNTDTALTTLEEALsekeriieRLKEQREREDRERLE 468
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1623 QLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSEL----EELRAMVEQSERARKLAE 1698
Cdd:pfam10174 469 ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVeqkkEECSKLENQLKKAHNAEE 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1699 QELI--EASERVQLLHSQNTSLINQKKKMEADISQLQteveEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1776
Cdd:pfam10174 549 AVRTnpEINDRIRLLEQEVARYKEESGKAQAEVERLL----GILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIK 624
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1777 MKKNMEQ--TVKDLQLRLDEAEQLALKGGKKQLQKLEVRVRELENELEAEQKRNAESIKGLRKSERRVKELSyqtEEDRK 1854
Cdd:pfam10174 625 HGQQEMKkkGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLR---AERRK 701
|
..
gi 2163567613 1855 NM 1856
Cdd:pfam10174 702 QL 703
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1162-1687 |
8.72e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.13 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1162 QEAEFQKLRRDLEEATL-------QHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLElddvnsnteqli 1234
Cdd:pfam15964 156 QELKSQTQEETLREQTLldssgnmQNSWCTPEDSRVHQTSKRPASHNLAERLKSATTGEDEKWRLELE------------ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1235 KAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQ--------RAKLQTENSELSRQLEEKEAFINQLTRGklTYTQQ 1306
Cdd:pfam15964 224 KLKLLYEAKTEVLESQVKSLRKDLAESQKTCEDLKERlkhkeslvAASTSSRVGGLCLKCAQHEAVLAQTHTN--VHMQT 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1307 LEDLKRQLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKK 1386
Cdd:pfam15964 302 IERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKELASQQE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1387 KLAQRLQEAEEAV----EAVNAKCSSLEKTKHRLQNEIEDLMAD----VERSNAAAAALDKKQRNFDKILSEWKQKFEES 1458
Cdd:pfam15964 382 KRAQEKEALRKEMkkerEELGATMLALSQNVAQLEAQVEKVTREknslVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQT 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1459 QTELEASQKEARSLST-----------ELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIH--ELEKVR 1525
Cdd:pfam15964 462 KMKKDEAEKEHREYRTktgrqleikdqEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHltRLEKES 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1526 KQL----DAEKLELQAALEEAEAS------------LEHEEGKILRAQLEFNQVKADYERKLAEKDEEIEQSKRNHLrvv 1589
Cdd:pfam15964 542 IQQsfsnEAKAQALQAQQREQELTqkmqqmeaqhdkTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQKSRSEV--- 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1590 dslqTSLDAETRSRNEALrlkKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRanedlKENIAIV 1669
Cdd:pfam15964 619 ----EQLSQEKEYLQDRL---EKLQKRNEELEEQCVQHGRMHERMKQRLRQLDKHCQATAQQLVQLLS-----KQNQLFK 686
|
570
....*....|....*...
gi 2163567613 1670 ERRNnlLQSELEELRAMV 1687
Cdd:pfam15964 687 ERQN--LTEEVQSLRSQV 702
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1446-1769 |
8.73e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1446 KILSEWKQKFEESQTELEASQKEARSLSTELFKLKNayeesLEHLETFKRENKNLQEEILDLTEQLGASQKsiHELEKVR 1525
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRK-----LEEAEKARQAEMDRQAAIYAEQERMAMERE--RELERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1526 KQLDAEKLElqaALEEAEASLEHEEGKIL-RAQLEFNQ----VKADYERKLAEKDEEIEQSKRNHLRVVDSLQTSLDAET 1600
Cdd:pfam17380 355 QEERKRELE---RIRQEEIAMEISRMRELeRLQMERQQknerVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1601 RSRNEALRLKKkmegdlnEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKEniaIVERRNNLLQSEL 1680
Cdd:pfam17380 432 ARQREVRRLEE-------ERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKR---AEEQRRKILEKEL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1681 EELRAMVEQSERARKLAEQELIEaservqllhsQNTSLINQKKKMEADiSQLQTEVEeaIQECRNAEEKAKKAITDAAMM 1760
Cdd:pfam17380 502 EERKQAMIEEERKRKLLEKEMEE----------RQKAIYEEERRREAE-EERRKQQE--MEERRRIQEQMRKATEERSRL 568
|
....*....
gi 2163567613 1761 aEELKKEQD 1769
Cdd:pfam17380 569 -EAMERERE 576
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1042-1863 |
8.80e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1042 DLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQAiSAQLQKKLKELQARIEELEEELEAER 1121
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQT-ALRQQEKIERYQEDLEELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1122 TGRAKVEKLRSELLQELEETSERLEEAggatsvqlelnKKQEAEFQKLRRDLEEATLQ-HEATAATLRKKHADSVAELSe 1200
Cdd:COG3096 368 EVVEEAAEQLAEAEARLEAAEEEVDSL-----------KSQLADYQQALDVQQTRAIQyQQAVQALEKARALCGLPDLT- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1201 qLDNlqrvkqkLEKEKSELKLELDDVnsnTEQLIKAKTNLekmcrtteDQMNEHRSKLEEAQRTVTDLS--TQRAKLQTE 1278
Cdd:COG3096 436 -PEN-------AEDYLAAFRAKEQQA---TEEVLELEQKL--------SVADAARRQFEKAYELVCKIAgeVERSQAWQT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1279 NSELSRQLEEKEAFINQLTrgklTYTQQLEDLKRQLEEEAKAKNALAHALQSAQHDCDlLREQYEEEMEAKTELQRALSK 1358
Cdd:COG3096 497 ARELLRRYRSQQALAQRLQ----QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-AAEELEELLAELEAQLEELEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1359 ANSEVAQWRTKYEtdaiQRTEELEEAKKKLAQR---LQEAEEAVEAVNAKC-----SSLEKTKHR---LQNEIEdlmADV 1427
Cdd:COG3096 572 QAAEAVEQRSELR----QQLEQLRARIKELAARapaWLAAQDALERLREQSgealaDSQEVTAAMqqlLERERE---ATV 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1428 ERSNAAAA--ALDKKQRN-------FDKILSEWKQKFE-------------ESQTELEASQKEARS------LSTELFKL 1479
Cdd:COG3096 645 ERDELAARkqALESQIERlsqpggaEDPRLLALAERLGgvllseiyddvtlEDAPYFSALYGPARHaivvpdLSAVKEQL 724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1480 kNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEE--AEASLEHEEGKILRAQ 1557
Cdd:COG3096 725 -AGLEDCPEDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSDRQWRYSRFPEVPLFGRAAREKrlEELRAERDELAEQYAK 803
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1558 LEFNQvkadyeRKLAEKDEEIEQSKRNHLRVVdsLQTSLDAETRSRNEALRlkkKMEGDLNEMEIQLSHANRTAAEAQKQ 1637
Cdd:COG3096 804 ASFDV------QKLQRLHQAFSQFVGGHLAVA--FAPDPEAELAALRQRRS---ELERELAQHRAQEQQLRQQLDQLKEQ 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1638 VKALQGYLKDTQLQLDDVVRAN-EDLKE-----------------NIAIVERRNNLLQS---ELEELRAMVEQSERARKL 1696
Cdd:COG3096 873 LQLLNKLLPQANLLADETLADRlEELREeldaaqeaqafiqqhgkALAQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRR 952
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1697 AEQELIEASERVQLLHSQNTSLINQKKKMEADIS-QLQTEVEEAIQECRNAEEKAKKA---ITDAAMMAEELKKEQDTSA 1772
Cdd:COG3096 953 LKQQIFALSEVVQRRPHFSYEDAVGLLGENSDLNeKLRARLEQAEEARREAREQLRQAqaqYSQYNQVLASLKSSRDAKQ 1032
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1773 hleRMKKNMEQTVKDLQLRLD-EAEQLAlKGGKKQLQKLEVRVRELENELEAE---QKRNAESIKG-LRKSERRVKELSY 1847
Cdd:COG3096 1033 ---QTLQELEQELEELGVQADaEAEERA-RIRRDELHEELSQNRSRRSQLEKQltrCEAEMDSLQKrLRKAERDYKQERE 1108
|
890
....*....|....*.
gi 2163567613 1848 QTEEDRKNMVRLQDLV 1863
Cdd:COG3096 1109 QVVQAKAGWCAVLRLA 1124
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1124-1769 |
8.84e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.43 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1124 RAKVEKLRSELLQELE----ETSERLEEaggatsvqleLNKKQEAEFQKLRR----DLEEATLQHEATAATLRKKHADSV 1195
Cdd:NF041483 599 RAEAERIRREAAEETErlrtEAAERIRT----------LQAQAEQEAERLRTeaaaDASAARAEGENVAVRLRSEAAAEA 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1196 AEL-SEQLDNLQRVKQKLEKEKSELKLELddvnsnTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTD-----LS 1269
Cdd:NF041483 669 ERLkSEAQESADRVRAEAAAAAERVGTEA------AEALAAAQEEAARRRREAEETLGSARAEADQERERAREqseelLA 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1270 TQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLED----LKRQLEEE-AKAKNALAHALQ----SAQHDCDLLR- 1339
Cdd:NF041483 743 SARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDsvagLQEQAEEEiAGLRSAAEHAAErtrtEAQEEADRVRs 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1340 EQYEEEMEAKTELQRALSKANSEVAQWRTKYE---TDAIQRTEELEEAKKKLAQRLQ-EAEEAVEAVNAKCSSLEKTKHR 1415
Cdd:NF041483 823 DAYAERERASEDANRLRREAQEETEAAKALAErtvSEAIAEAERLRSDASEYAQRVRtEASDTLASAEQDAARTRADARE 902
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1416 LQNEIedlmadveRSNAAAAAldkkQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLehLETFKR 1495
Cdd:NF041483 903 DANRI--------RSDAAAQA----DRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQL--IAEATG 968
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1496 ENKNLQEEIldlTEQLGASQKSihelekvrkqldAEKLELQAALEEAEASLEHEEgkiLRAQlefnqVKADYERKLAEKD 1575
Cdd:NF041483 969 EAERLRAEA---AETVGSAQQH------------AERIRTEAERVKAEAAAEAER---LRTE-----AREEADRTLDEAR 1025
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1576 EEIEQSKRNHLRVVDSLQTSLDAE-----TRSRNEALRLKKKMEGDLNEM-EIQLSHANRTAAEAQKQVKALqgylkdtq 1649
Cdd:NF041483 1026 KDANKRRSEAAEQADTLITEAAAEadqltAKAQEEALRTTTEAEAQADTMvGAARKEAERIVAEATVEGNSL-------- 1097
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1650 lqlddVVRANEDLKENI--------AIVERRNNL---LQSELEEL--RAMVEQSERAR----------KLAEQELIEASE 1706
Cdd:NF041483 1098 -----VEKARTDADELLvgarrdatAIRERAEELrdrITGEIEELheRARRESAEQMKsagercdalvKAAEEQLAEAEA 1172
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2163567613 1707 RVQLLHSQNTS-----LINQKKKMEADISQLQTEVEEAIQEcrnAEEKAKKAITDAAMMAEELKKEQD 1769
Cdd:NF041483 1173 KAKELVSDANSeaskvRIAAVKKAEGLLKEAEQKKAELVRE---AEKIKAEAEAEAKRTVEEGKRELD 1237
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
929-1092 |
9.14e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 929 AELAAKKRKLEDEC---SELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQESHQQALDDL 1005
Cdd:PRK11637 54 QDIAAKEKSVRQQQqqrASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQLDAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1006 --------------------------------QAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGD 1053
Cdd:PRK11637 134 frqgehtglqlilsgeesqrgerilayfgylnQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQA 213
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2163567613 1054 LKLAQESIMDLEN----DKQQLEErLKKKDFELNTLNARIEDE 1092
Cdd:PRK11637 214 RNERKKTLTGLESslqkDQQQLSE-LRANESRLRDSIARAERE 255
|
|
| COG6 |
smart01087 |
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ... |
1367-1542 |
1.01e-03 |
|
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localisation.
Pssm-ID: 215018 Cd Length: 598 Bit Score: 43.85 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1367 RTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQrnfdK 1446
Cdd:smart01087 9 RSDLEKRLLKINGEFLSEFKPVAEQLQRLSEDVQKLNNSCDSMKDQLNTAKNQTQDLISEASELQEELALLELKK----K 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1447 ILSEWKQKFEESQTELEASQKEARSLSTELF----KLKNAYEESLEHLETfkrENKNLQEEILDLTEQL--GASQKSIHE 1520
Cdd:smart01087 85 LLDAFLSKFTLSQDELDVLTSREGPIDDEFFqvldKVQEIHEDCSVLLQN---EYQTAGLEIMEKMNQLleRAYERLYRW 161
|
170 180
....*....|....*....|..
gi 2163567613 1521 LEKVRKQLDAEKLELQAALEEA 1542
Cdd:smart01087 162 LQSELRNLTTDNPEILSLLRQA 183
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1249-1470 |
1.05e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.44 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1249 DQMNEHRSKleeaqrtvtDLSTQRAKLQTENSELSRQLEEKEAfinqltrgkltyTQQLEDL-KRQLEEEAKAKNALAha 1327
Cdd:NF012221 1545 DAVSKHAKQ---------DDAAQNALADKERAEADRQRLEQEK------------QQQLAAIsGSQSQLESTDQNALE-- 1601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1328 lQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVA-------QWRTKYET---DAIQrtEELEEAKKKLAQRLQEAEE 1397
Cdd:NF012221 1602 -TNGQAQRDAILEESRAVTKELTTLAQGLDALDSQATyagesgdQWRNPFAGgllDRVQ--EQLDDAKKISGKQLADAKQ 1678
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163567613 1398 AVEAVNAKC-SSLEKTKHRLQNEiEDLMADVERSNAAAAAlDKKQRNFDKILSEWKQKFEESQTELEASQKEAR 1470
Cdd:NF012221 1679 RHVDNQQKVkDAVAKSEAGVAQG-EQNQANAEQDIDDAKA-DAEKRKDDALAKQNEAQQAESDANAAANDAQSR 1750
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
996-1278 |
1.06e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.91 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 996 ESHQQALD---DLQAEEDKVNTLAKAKVKLEQQVDDLESSlEQEKKIRMD-LERAKRKLEgDLKLAQESIMDLENDKQQL 1071
Cdd:COG0497 141 DAQRELLDafaGLEELLEEYREAYRAWRALKKELEELRAD-EAERARELDlLRFQLEELE-AAALQPGEEEELEEERRRL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1072 E--ERLKKKdfeLNTLNARI-EDEQAISAQLQKKLKELQarieeleeeleaertGRAKVEKLRSELLQELEETSERLEEA 1148
Cdd:COG0497 219 SnaEKLREA---LQEALEALsGGEGGALDLLGQALRALE---------------RLAEYDPSLAELAERLESALIELEEA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1149 GGATSVQLElnkKQEAEFQKLRRdLEE--ATLQHeataatLRKKHADSVAELSEQLDNLQrvkQKLEkekselklELDDV 1226
Cdd:COG0497 281 ASELRRYLD---SLEFDPERLEE-VEErlALLRR------LARKYGVTVEELLAYAEELR---AELA--------ELENS 339
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2163567613 1227 NSNTEQLIKAKTNLEKMCRTTEDQMNEHRSK----LEEA-QRTVTDLSTQRAKLQTE 1278
Cdd:COG0497 340 DERLEELEAELAEAEAELLEAAEKLSAARKKaakkLEKAvTAELADLGMPNARFEVE 396
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1027-1224 |
1.08e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1027 DDLESSLEQ-EKKI--RMDLERAKRKLEGDLKLAqESIMDLENDKQQLEERlkkkdfelnTLNARIEDEQAISAQLQKKL 1103
Cdd:COG2433 346 DAYKNKFERvEKKVppDVDRDEVKARVIRGLSIE-EALEELIEKELPEEEP---------EAEREKEHEERELTEEEEEI 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1104 KELQARIEELeeeleaertgRAKVEKLRSELlQELEETSERLEEaggatsvqlELNKKQEAEFQKLRRDLEeatlqheat 1183
Cdd:COG2433 416 RRLEEQVERL----------EAEVEELEAEL-EEKDERIERLER---------ELSEARSEERREIRKDRE--------- 466
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2163567613 1184 aatlrkkhadsVAELSEQLDNLQRVKQKLEKEKSELKLELD 1224
Cdd:COG2433 467 -----------ISRLDREIERLERELEEERERIEELKRKLE 496
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1593-1772 |
1.09e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1593 QTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDvvrANEDLKENIAIVERR 1672
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE---AEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1673 NNLLQ------SELEEL-----------------------RAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKK 1723
Cdd:COG3883 92 ARALYrsggsvSYLDVLlgsesfsdfldrlsalskiadadADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2163567613 1724 KMEADISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSA 1772
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1203-1480 |
1.16e-03 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 43.69 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1203 DNLQRVKQKLEKEKSELKlelddVNSNTEQLIKAKTN-LEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSE 1281
Cdd:pfam09726 395 DALVRLEQDIKKLKAELQ-----ASRQTEQELRSQISsLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1282 LSRQL-EEKEAfinqltrgKLTYTQQL-EDLKRQLEEEAKAKNALAHALQSAQHDCDLLReqyeeemeaktelqralska 1359
Cdd:pfam09726 470 LEKRLkAEQEA--------RASAEKQLaEEKKRKKEEEATAARAVALAAASRGECTESLK-------------------- 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1360 nsevaqwrtkyetdaiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRlQNEIEDLMadversnAAAAALDK 1439
Cdd:pfam09726 522 ----------------QRKRELESEIKKLTHDIKLKEEQIRELEIKVQELRKYKES-EKDTEVLM-------SALSAMQD 577
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2163567613 1440 KQRNFDKILS-EWKQKFE------ESQTELEASQKEARSLSTELFKLK 1480
Cdd:pfam09726 578 KNQHLENSLSaETRIKLDlfsalgDAKRQLEIAQGQIYQKDQEIKDLK 625
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1527-1658 |
1.16e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.11 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1527 QLDAEKLELQAALEEAEASLEHeegkiLRAQLEFNQVKADYERKLAEKDEEIEQSKRNHLRvVDSL-------QTSLDAE 1599
Cdd:COG1566 80 DLQAALAQAEAQLAAAEAQLAR-----LEAELGAEAEIAAAEAQLAAAQAQLDLAQRELER-YQALykkgavsQQELDEA 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1600 TRSRNEALRLKKKMEGDLNEMEIQLShANRTAAEAQKQVKALQGYLKDTQLQLDD-VVRA 1658
Cdd:COG1566 154 RAALDAAQAQLEAAQAQLAQAQAGLR-EEEELAAAQAQVAQAEAALAQAELNLARtTIRA 212
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1307-1414 |
1.17e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1307 LEDLKRQLEEEAKAknalahaLQSAQHDCDLLREQYEEEMEA-----KTELQRALSKANSEVAQwrTKYETDAIQRTEEL 1381
Cdd:PRK00409 525 LEELERELEQKAEE-------AEALLKEAEKLKEELEEKKEKlqeeeDKLLEEAEKEAQQAIKE--AKKEADEIIKELRQ 595
|
90 100 110
....*....|....*....|....*....|...
gi 2163567613 1382 EEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKH 1414
Cdd:PRK00409 596 LQKGGYASVKAHELIEARKRLNKANEKKEKKKK 628
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1767-1931 |
1.22e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1767 EQDTSAHLERMKKNMEQtvkdlqlrLDEAEQLALKGgKKQLQKLEvRVRELENELEaEQKRNAESIKGLR------KSER 1840
Cdd:COG4913 220 EPDTFEAADALVEHFDD--------LERAHEALEDA-REQIELLE-PIRELAERYA-AARERLAELEYLRaalrlwFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1841 RVKELSYQTEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQ-ANSNLAKFRKVQHELDEAEERADMAESQVNKLRARS 1919
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALL 368
|
170
....*....|..
gi 2163567613 1920 RDIGAKKGLNEE 1931
Cdd:COG4913 369 AALGLPLPASAE 380
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
778-906 |
1.36e-03 |
|
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).
Pssm-ID: 409646 [Multi-domain] Cd Length: 149 Bit Score: 40.95 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 778 LIITR-IQAQaRGQLMRIEFK-KILERRDALLVIQWNIRAFMGVKnwpwmKLYFKIKPLLKSAETEKEMQTMKEEFGHLK 855
Cdd:cd21759 19 LIRSRwRKAQ-WCALSVIKLKnKILYRREALIKIQKTVRGYLARK-----KHRPRIKGLRKIRALEKQLKEMEEIASQLK 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2163567613 856 EALEKSEARRKELEEKMVSMLQE-KNDlqlqvqaEQDNLADAEERCDQLIKN 906
Cdd:cd21759 93 KDKDKWTKQVKELKKEIDALIKKiKTN-------DMITRKEIDKLYNALVKK 137
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1186-1316 |
1.51e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.70 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1186 TLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKmCRTTEdqMNEHRSKLEEAQRTV 1265
Cdd:smart00787 144 GLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELED-CDPTE--LDRAKEKLKKLLQEI 220
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2163567613 1266 TDLSTQRAklqtensELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEE 1316
Cdd:smart00787 221 MIKVKKLE-------ELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
943-1238 |
1.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 943 SELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQESHQQALDDLQAEEDKVNTLAKAKVKL 1022
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1023 EQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIE--DEQAISAQLQ 1100
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1101 KKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEEA----GGATSVQLELNKKQEAEFQKLRRDLEEA 1176
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAlsalLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2163567613 1177 TLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKT 1238
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1529-1772 |
1.65e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1529 DAEKLELQAALEEAEASLEHEEGKILRAQLEFNQVKADYERKLAEKDEEIEQskrnhlrvVDSLQTSLDaetrsrnealr 1608
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE--------IDKLQAEIA----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1609 lkkKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQ--------LDDVVRAN----EDLKENIAIVERRNNLL 1676
Cdd:COG3883 76 ---EAEAEIEERREELGERARALYRSGGSVSYLDVLLGSESFSdfldrlsaLSKIADADadllEELKADKAELEAKKAEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1677 QSELEELRAMVEQSERARKLAEQELIEASERVQllhsqntSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAITD 1756
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLA-------QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
250
....*....|....*.
gi 2163567613 1757 AAMMAEELKKEQDTSA 1772
Cdd:COG3883 226 AAAAAAAAAAAAAAAA 241
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1190-1413 |
1.73e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1190 KHADSVAELSEQLDNLQRVKQKLEKEKSELKLELddvnsnteqlIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLS 1269
Cdd:PRK05771 37 KEELSNERLRKLRSLLTKLSEALDKLRSYLPKLN----------PLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1270 TQRAKLQTENSELSRQLEEKEAFIN------QLTRGKLTY------------TQQLEDLKRQLEEEAKAKN-----ALAH 1326
Cdd:PRK05771 107 EEISELENEIKELEQEIERLEPWGNfdldlsLLLGFKYVSvfvgtvpedkleELKLESDVENVEYISTDKGyvyvvVVVL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1327 ALQSAQHDCDLLREQYEE-EMEAKTELQRALSKANSEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQEAEEAVEAVNAK 1405
Cdd:PRK05771 187 KELSDEVEEELKKLGFERlELEEEGTPSELIREIKEELEEIEKERE----SLLEELKELAKKYLEELLALYEYLEIELER 262
|
....*...
gi 2163567613 1406 CSSLEKTK 1413
Cdd:PRK05771 263 AEALSKFL 270
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1573-1910 |
1.76e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1573 EKDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEALR----LKKKMEGDLNEME-IQLSHANRTAAEAQKQVKALQGYLKD 1647
Cdd:PLN02939 46 QKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRtvmeLPQKSTSSDDDHNrASMQRDEAIAAIDNEQQTNSKDGEQL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1648 TQLQLDDVVRANEDLKENIAIVER--------------RNNLLQSELEELRAMVEQSERARKLAEQELIeaseRVQLLHS 1713
Cdd:PLN02939 126 SDFQLEDLVGMIQNAEKNILLLNQarlqaledlekiltEKEALQGKINILEMRLSETDARIKLAAQEKI----HVEILEE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1714 QntsLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTS---AHLERMKKNMEQTVKDLQL 1790
Cdd:PLN02939 202 Q---LEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEervFKLEKERSLLDASLRELES 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1791 RLDEAEQLALKGGKKQLQKLEVRVRELENELEAEQKRNAESIKGLRKS---ERRVKELSYQTEEdrKNMVRLQ-DLVDKL 1866
Cdd:PLN02939 279 KFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNqdlRDKVDKLEASLKE--ANVSKFSsYKVELL 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2163567613 1867 QLKVKAYKRQAEEAEEQANS-------NLAKFRKVQHELDEAEERADMAES 1910
Cdd:PLN02939 357 QQKLKLLEERLQASDHEIHSyiqlyqeSIKEFQDTLSKLKEESKKRSLEHP 407
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
839-1078 |
1.85e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 839 ETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIK--NKIQLE-AKVK 915
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNryKSLKLEdLDSK 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 916 EMTERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLdENITKLTKEKKILQ 995
Cdd:PRK01156 567 RTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNL-NNKYNEIQENKILI 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 996 ESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERL 1075
Cdd:PRK01156 646 EKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETL 725
|
...
gi 2163567613 1076 KKK 1078
Cdd:PRK01156 726 ESM 728
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1260-1707 |
1.90e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1260 EAQRTVTDLSTQRAKLQTENSELSrqLEEKEAFINQLTRGKLTYTQQLEDLKR----QLEEEAKAKNALAHALQSAQHDc 1335
Cdd:COG5185 129 EIVALKDELIKVEKLDEIADIEAS--YGEVETGIIKDIFGKLTQELNQNLKKLeifgLTLGLLKGISELKKAEPSGTVN- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1336 DLLREQYEEEMEAKTELQRALSKANSEVAQwrtkyetdaiQRTEELEEAKKKLAQRLQEAEEAVEAVNakcsSLEKTKHR 1415
Cdd:COG5185 206 SIKESETGNLGSESTLLEKAKEIINIEEAL----------KGFQDPESELEDLAQTSDKLEKLVEQNT----DLRLEKLG 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1416 LQNEIedlmadVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEAS-QKEARSLSTELFKLKNAYEESLehletfk 1494
Cdd:COG5185 272 ENAES------SKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEeQLAAAEAEQELEESKRETETGI------- 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1495 renKNLQEEILDLTEQLGASQKSIHElekvrkqlDAEKLELQAALEEAEASLEHEEGKILRAQLEFNQVKADYERKLAEK 1574
Cdd:COG5185 339 ---QNLTAEIEQGQESLTENLEAIKE--------EIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEI 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1575 DEEIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEiQLSHANRTAAEAQKQVKALQGYLKDTQLQLDD 1654
Cdd:COG5185 408 LATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVM-READEESQSRLEEAYDEINRSVRSKKEDLNEE 486
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2163567613 1655 VVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQELIEASER 1707
Cdd:COG5185 487 LTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIL 539
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
830-1028 |
2.02e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 830 KIKPLLKSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERcdqlIKNKIQ 909
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR----IKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 910 LEAKVKEmterleeeeemNAELAAkkrkledecseLKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTK 989
Cdd:COG1579 81 QLGNVRN-----------NKEYEA-----------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
|
170 180 190
....*....|....*....|....*....|....*....
gi 2163567613 990 EKKILQESHQQALDDLQAEEDKvntLAKAKVKLEQQVDD 1028
Cdd:COG1579 139 ELEEKKAELDEELAELEAELEE---LEAEREELAAKIPP 174
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1488-1928 |
2.02e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.97 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1488 EHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAAL--------EEAEASLEHEEGKILRAQLE 1559
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIalrragglEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1560 FNQVKADYERKLAEKDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVK 1639
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1640 ALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLI 1719
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1720 NQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLA 1799
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1800 LKGGKKQLQKLEVRVRELENELEAEQKRNAESIKGLRKSERRVKELSYQTEEDRKNMVRLQDLVDKLQLKVKAYKRQAEE 1879
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2163567613 1880 AEEQANSNLAKFRKVQHELDEAEERADMAESQVNKLRARSRDIGAKKGL 1928
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAA 524
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1530-1930 |
2.11e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1530 AEKLELQAALEEAEaSLEHEEGKILRAQLEFNQVKADYERKLAEKDEEIEQSKRNHLRVVDSLQ---------------- 1593
Cdd:pfam05557 48 DRNQELQKRIRLLE-KREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKnelselrrqiqraele 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1594 -TSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYL-------------KDTQLQLDDVVRAN 1659
Cdd:pfam05557 127 lQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIqsqeqdseivknsKSELARIPELEKEL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1660 EDLKENIAIVE---RRNNLLQSELEELRAMVEQSERARKLA----------EQELIE-----------------ASERVQ 1709
Cdd:pfam05557 207 ERLREHNKHLNeniENKLLLKEEVEDLKRKLEREEKYREEAatlelekeklEQELQSwvklaqdtglnlrspedLSRRIE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1710 LLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKakkaITDAAMMAEELK--------------KEQD-TSAHL 1774
Cdd:pfam05557 287 QLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKK----IEDLNKKLKRHKalvrrlqrrvllltKERDgYRAIL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1775 ERMKK--NMEQTVKDLQLRLDEAEQLALKgGKKQLQKLEVRVRELENELEAEQKRNA---ESIKGLRKSErRVKELSYQT 1849
Cdd:pfam05557 363 ESYDKelTMSNYSPQLLERIEEAEDMTQK-MQAHNEEMEAQLSVAEEELGGYKQQAQtleRELQALRQQE-SLADPSYSK 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1850 EEdrKNMVRLQdlVDKLQLKVKAYKRQAEEAEE-------QANSNLAKFRKVQHELDEAEERADMAESQVNKLRArsrDI 1922
Cdd:pfam05557 441 EE--VDSLRRK--LETLELERQRLREQKNELEMelerrclQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQA---EI 513
|
....*...
gi 2163567613 1923 GAKKGLNE 1930
Cdd:pfam05557 514 ERLKRLLK 521
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1172-1506 |
2.14e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1172 DLEEATLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQM 1251
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1252 NEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHALqsa 1331
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1332 qhdcdllreQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEK 1411
Cdd:COG4372 174 ---------QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1412 TKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLE 1491
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330
....*....|....*
gi 2163567613 1492 TFKRENKNLQEEILD 1506
Cdd:COG4372 325 AKKLELALAILLAEL 339
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1373-1689 |
2.60e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1373 DAIQRTEELEEAKKKLAQRLQEAeeaveavnakcsslektkhrlqneiEDLMADVERSNAAAAALDKKqrnfdkiLSEWK 1452
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQT-------------------------LALLDKIDRQKEETEQLKQQ-------LAQAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1453 QKFEESQTELEASQKEARSLSTELFKlknayEESLEHLETF--KREN--KNLQEEILDLTEQLGASQKSiheLEKVRKQL 1528
Cdd:PRK11281 94 AKLRQAQAELEALKDDNDEETRETLS-----TLSLRQLESRlaQTLDqlQNAQNDLAEYNSQLVSLQTQ---PERAQAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1529 DAEKLELQ------AALEEAEASLEHEEGKILRAQLEFNQVKADYERKLAEKDE---EIEQSKRNHLRVVdslQTSLDAE 1599
Cdd:PRK11281 166 YANSQRLQqirnllKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTqlqDLLQKQRDYLTAR---IQRLEHQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1600 TRSRNEALRLKKkmegdlnemeiqLSHANRTAAEAQKQVKALQG----YLK---DTQLQL-DDVVRANEDL----KENIA 1667
Cdd:PRK11281 243 LQLLQEAINSKR------------LTLSEKTVQEAQSQDEAARIqanpLVAqelEINLQLsQRLLKATEKLntltQQNLR 310
|
330 340
....*....|....*....|..
gi 2163567613 1668 IVERRNNLLQSEleelRAMVEQ 1689
Cdd:PRK11281 311 VKNWLDRLTQSE----RNIKEQ 328
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1258-1529 |
2.62e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1258 LEEAQRTVTdlstQRAKLQTENSELSRQLEEKEAFINQLTRgkltytqQLEDLKRQLEEEAKAKNAlahALQSAQhdcdl 1337
Cdd:PRK11281 65 LEQTLALLD----KIDRQKEETEQLKQQLAQAPAKLRQAQA-------ELEALKDDNDEETRETLS---TLSLRQ----- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1338 LREQYEEEMEAKTELQRALSKANSEVAQWRTKYE------TDAIQRTEELEEAKKKL----------AQRLQEAEEAveA 1401
Cdd:PRK11281 126 LESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPEraqaalYANSQRLQQIRNLLKGGkvggkalrpsQRVLLQAEQA--L 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1402 VNAKcSSLEKTKHRLQNEIEDLM-ADVERSNAAAAALDKKQRNFDKILSEWK-QKFEESQTELEASQKEARSLSTELFKl 1479
Cdd:PRK11281 204 LNAQ-NDLQRKSLEGNTQLQDLLqKQRDYLTARIQRLEHQLQLLQEAINSKRlTLSEKTVQEAQSQDEAARIQANPLVA- 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2163567613 1480 knayeESLEHletfkreNKNLQEEILDLTEQLGA-SQKSIheleKVRKQLD 1529
Cdd:PRK11281 282 -----QELEI-------NLQLSQRLLKATEKLNTlTQQNL----RVKNWLD 316
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1191-1405 |
2.65e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1191 HADSvaELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEkmcrTTEDQMNEHRSKLEEAQRTVTDLST 1270
Cdd:COG3883 13 FADP--QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE----ALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1271 Q---RAKLQTENSELSRQLE------EKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAhALQSAQHDCDLLREQ 1341
Cdd:COG3883 87 ElgeRARALYRSGGSVSYLDvllgseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA-ELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2163567613 1342 YEeemEAKTELQRALSKANSEVAQWRTKyETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAK 1405
Cdd:COG3883 166 LE---AAKAELEAQQAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1379-1576 |
2.73e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1379 EELEEAKKKLAQRLQEA-EEAVEAVNAKCSSLEKTKHRLQN---EIEDLMADVERSNAAAAALDKKQRNFDKILSEW--- 1451
Cdd:PHA02562 205 EEQRKKNGENIARKQNKyDELVEEAKTIKAEIEELTDELLNlvmDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYekg 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1452 ------KQKFEESQTELEASQKEARSLSTELFKLKNAYEEslehLETFKRENKNLQEEILDLTEQLGASQKSIhelekvr 1525
Cdd:PHA02562 285 gvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDE----LEEIMDEFNEQSKKLLELKNKISTNKQSL------- 353
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2163567613 1526 KQLDAEKLELQAALEEAEASLEHEEGKILRAQLEFNQVKADYERKLAEKDE 1576
Cdd:PHA02562 354 ITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYH 404
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
840-1110 |
2.94e-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: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 840 TEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDN--LADAEERCDQLIKNKIQLEAKVKEM 917
Cdd:pfam09731 159 VKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPplLDAAPETPPKLPEHLDNVEEKVEKA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 918 TERLEEEEEMNaELAAKKRklEDECSELKKDIDDLELSLAKVEKEKHATENKVknlteeMAGLDENITKLTKE----KKI 993
Cdd:pfam09731 239 QSLAKLVDQYK-ELVASER--IVFQQELVSIFPDIIPVLKEDNLLSNDDLNSL------IAHAHREIDQLSKKlaelKKR 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 994 LQESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEE 1073
Cdd:pfam09731 310 EEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQE 389
|
250 260 270
....*....|....*....|....*....|....*..
gi 2163567613 1074 RLKKKDFELNtLNARIEDEQAIsaqLQKKLKELQARI 1110
Cdd:pfam09731 390 IELQREFLQD-IKEKVEEERAG---RLLKLNELLANL 422
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
1649-1749 |
2.94e-03 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 40.72 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1649 QLQLDDVVRANEDLKENIAIVE-----------RRNNLL---------QSELEELRAMVEQSERARKLAEQELIEASERV 1708
Cdd:pfam05266 60 KLQVDDSRSVFESLMESFAELEkhgfdvkapqsRINKLLslkdrqtklLEELKKLEKKIAEEESEKRKLEEEIDELEKKI 139
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2163567613 1709 QLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEK 1749
Cdd:pfam05266 140 LELERQLALAKEKKEAADKEIARLKSEAEKLEQEIQDVELE 180
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
939-1401 |
2.96e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 939 EDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEM------AGLDENITKLTKEKKILQESHQQALDDLQAEEDKV 1012
Cdd:COG5185 78 KSESSVKARKFLKEKKLDTKILQEYVNSLIKLPNYEWSAdilislLYLYKSEIVALKDELIKVEKLDEIADIEASYGEVE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1013 NTLAKAKVKLEQQ----VDDLESSLEQEKKIRMDLERAKRKL-EGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNA 1087
Cdd:COG5185 158 TGIIKDIFGKLTQelnqNLKKLEIFGLTLGLLKGISELKKAEpSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1088 RIEDEQAIS--AQLQKKLKE-LQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEEAGGATSVQLELNKKQE- 1163
Cdd:COG5185 238 FQDPESELEdlAQTSDKLEKlVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEq 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1164 -------AEFQKLRRDLEEATLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKsELKLELDDVNSNTEQLIKA 1236
Cdd:COG5185 318 laaaeaeQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSE-ELDSFKDTIESTKESLDEI 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1237 KTNLEKMCR----TTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQleDLKR 1312
Cdd:COG5185 397 PQNQRGYAQeilaTLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYD--EINR 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1313 QLEEEAKAKNALAHALQSAqhdcdlLREQYEEEMEAKTELQRALSKANSEVaQWRTKYETDAIQRTEELEEAKKKLAQRL 1392
Cdd:COG5185 475 SVRSKKEDLNEELTQIESR------VSTLKATLEKLRAKLERQLEGVRSKL-DQVAESLKDFMRARGYAHILALENLIPA 547
|
....*....
gi 2163567613 1393 QEAEEAVEA 1401
Cdd:COG5185 548 SELIQASNA 556
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1657-1920 |
3.28e-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: 42.42 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1657 RANEDLKENIAIVERRNNL------LQSELEELRAMVEQSERARKLAEQELieasERVQLLHSQNTSLINQKKKMEADIS 1730
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLeeaekaRQAEMDRQAAIYAEQERMAMEREREL----ERIRQEERKRELERIRQEEIAMEIS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1731 QLQtEVEEAIQECRNAEEKAKKAItDAAMMAEELKKEqdtsahleRMKKNMEQTVKDLQLRLDEAEqlalkGGKKQLQKL 1810
Cdd:pfam17380 376 RMR-ELERLQMERQQKNERVRQEL-EAARKVKILEEE--------RQRKIQQQKVEMEQIRAEQEE-----ARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1811 -EVRVRELENELEAEQKRNaESIKGLRKSERRVKELSYQTEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQANSNLA 1889
Cdd:pfam17380 441 eEERAREMERVRLEEQERQ-QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE 519
|
250 260 270
....*....|....*....|....*....|..
gi 2163567613 1890 K-FRKVQHELDEAEERADMAESQVNKLRARSR 1920
Cdd:pfam17380 520 KeMEERQKAIYEEERRREAEEERRKQQEMEER 551
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1753-1931 |
3.32e-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: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1753 AITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQlALKGGKKQLQKLEVRVRELENELEAEQKRNAESI 1832
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA-ELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1833 KGLRKSERRVKEL-----SYQTEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKVQHELDEAEERADM 1907
Cdd:COG3883 93 RALYRSGGSVSYLdvllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180
....*....|....*....|....
gi 2163567613 1908 AESQVNKLRARSRDIGAKKGLNEE 1931
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEA 196
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1076-1222 |
3.35e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1076 KKKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEEeleaertgRAKVEKLRSELLQELEETSERLEEAGGATSVQ 1155
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKL--------RNEFEKELRERRNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1156 LELNKKQEAEFQKLRRDLEEATLQHEATAATLRKKHADSVAELsEQLDNLQR---VKQKLEKEKSELKLE 1222
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLTAeeaKEILLEKVEEEARHE 170
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1185-1523 |
3.48e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 41.48 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1185 ATLRKKHADSVAELSEqldnLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQ----MNEHRSKLEE 1260
Cdd:pfam09728 21 AALCKKYAELLEEMKR----LQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQnkklKEESKKLAKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1261 AQRTVTDLStqrAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEeeakaknalahalqsaqhdcdlLRE 1340
Cdd:pfam09728 97 EEEKRKELS---EKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYE----------------------LRE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1341 QYEEEMEAKTELQRALSKAnsevaqwrtkyetdaiqRTEELEEAKKKLAQRLQEAEeaVEAVNAKCSSLEKTKHRLQNEI 1420
Cdd:pfam09728 152 LHFEKLLKTKELEVQLAEA-----------------KLQQATEEEEKKAQEKEVAK--ARELKAQVQTLSETEKELREQL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1421 EDLMadversnaaaaaldKKQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNL 1500
Cdd:pfam09728 213 NLYV--------------EKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKL 278
|
330 340
....*....|....*....|...
gi 2163567613 1501 QEEILDLTEQLGASQKSIHELEK 1523
Cdd:pfam09728 279 KEELEKLQKKLEKLENLCRALQA 301
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
866-1227 |
3.72e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 866 KELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEEEEEMNAELAAKKRKLEDECSEL 945
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 946 KKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQESHQQALDDLQAEEDKVNTLAKAKVKLEQQ 1025
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1026 VDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKE 1105
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1106 LQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEEAGGATSVQLELNKKQEAEFQKLRRDLEEATLQHEATAA 1185
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2163567613 1186 TLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVN 1227
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1435-1786 |
3.76e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 42.01 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1435 AALDKKQRNFDKILSEWKQKfeESQTELEASQKEArslstelfKLKNAYeesLEHLETFKRENKNLQ---EEILDLTEQL 1511
Cdd:pfam03528 4 EDLQQRVAELEKENAEFYRL--KQQLEAEFNQKRA--------KFKELY---LAKEEDLKRQNAVLQeaqVELDALQNQL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1512 GASQKSIHEL---------------EKVRKQLDAEKLELQAALEEAEASLEHE-EGKILRAQLEFNQVKADYERKLAEKD 1575
Cdd:pfam03528 71 ALARAEMENIkavatvsentkqeaiDEVKSQWQEEVASLQAIMKETVREYEVQfHRRLEQERAQWNQYRESAEREIADLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1576 EEIEQSKRNHLRVVDSLQTSLDAEtrsrnealrlkkKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGY-LKDTQLQLDD 1654
Cdd:pfam03528 151 RRLSEGQEEENLEDEMKKAQEDAE------------KLRSVVMPMEKEIAALKAKLTEAEDKIKELEASkMKELNHYLEA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1655 VVRANEDLKENIAIVERRNNLLQSELEELRAmvEQSERARKLaEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQT 1734
Cdd:pfam03528 219 EKSCRTDLEMYVAVLNTQKSVLQEDAEKLRK--ELHEVCHLL-EQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMES 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2163567613 1735 EVEEaiQECRNAEEKAKKaitdaammAEELKKEQDTSAHLERMKKNMEQTVK 1786
Cdd:pfam03528 296 VLTS--EQLRQVEEIKKK--------DQEEHKRARTHKEKETLKSDREHTVS 337
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
932-1215 |
3.78e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.15 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 932 AAKKRKLEDECSELKKDIDDLELSLAK---------VEKEKHATENKVKNLTEEMaGLDENITKLTKE------------ 990
Cdd:PLN03229 428 KTPVRELEGEVEKLKEQILKAKESSSKpselalnemIEKLKKEIDLEYTEAVIAM-GLQERLENLREEfskansqdqlmh 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 991 -------KKILQE-----SHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIR--MDLERAKRKLEGDLKL 1056
Cdd:PLN03229 507 pvlmekiEKLKDEfnkrlSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKevMDRPEIKEKMEALKAE 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1057 AQESIMDLEN--DKQQLEERLK-KKDFELNTLNARIEDEQAISAQLQKKLKELQARIEELEeeleaertgRAKVEKLRSE 1133
Cdd:PLN03229 587 VASSGASSGDelDDDLKEKVEKmKKEIELELAGVLKSMGLEVIGVTKKNKDTAEQTPPPNL---------QEKIESLNEE 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1134 LLQELEE---TSE--------RLEEAGGATSVQLELNKKQEAEFQKLRRDLEEATlqheaTAATLRKKHADSVAELSEQL 1202
Cdd:PLN03229 658 INKKIERvirSSDlkskiellKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEAL-----NSSELKEKFEELEAELAAAR 732
|
330
....*....|...
gi 2163567613 1203 DNLQRVKQKLEKE 1215
Cdd:PLN03229 733 ETAAESNGSLKND 745
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1676-1770 |
3.79e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1676 LQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQEcrnaEEKAKKAIT 1755
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQE----RKQKRKEIT 222
|
90
....*....|....*
gi 2163567613 1756 DAAMMAEELkKEQDT 1770
Cdd:PRK11448 223 DQAAKRLEL-SEEET 236
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1635-1881 |
3.94e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1635 QKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHsQ 1714
Cdd:pfam02029 69 AKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWS-T 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1715 NTSLINQKKKMEADISQLQTEVE------EAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDL 1788
Cdd:pfam02029 148 EVRQAEEEGEEEEDKSEEAEEVPtenfakEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1789 ----QLRLDEAEQLALKGGKKQLQKLEVRVRELENElEAEQKRNA--------ESIKGLRKSERRVKELSYQTEEDRKNM 1856
Cdd:pfam02029 228 gglsQSQEREEEAEVFLEAEQKLEELRRRRQEKESE-EFEKLRQKqqeaelelEELKKKREERRKLLEEEEQRRKQEEAE 306
|
250 260
....*....|....*....|....*
gi 2163567613 1857 VRLQDLVDKLQLKVKAYKRQAEEAE 1881
Cdd:pfam02029 307 RKLREEEEKRRMKEEIERRRAEAAE 331
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
834-1108 |
4.04e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 834 LLKSAETEKEMQTMKEEFGHLKEALEKSEARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDQLIkNKIQleak 913
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLL-NEVK---- 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 914 vkemtERLEEEEEMNAELAAKKRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNlteeMAGLDENITKLT--KEK 991
Cdd:pfam15921 664 -----TSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS----MEGSDGHAMKVAmgMQK 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 992 KILQESHQqaLDDLQAeedKVNTLAKAKVKLEQQVDDLEsslEQEKKIRMDLERA---KRKLEGDLKLAQESIMDLENDK 1068
Cdd:pfam15921 735 QITAKRGQ--IDALQS---KIQFLEEAMTNANKEKHFLK---EEKNKLSQELSTVateKNKMAGELEVLRSQERRLKEKV 806
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2163567613 1069 QQLEERLKKKDFELNTLNARI--EDEQAISAQLQKKL--KELQA 1108
Cdd:pfam15921 807 ANMEVALDKASLQFAECQDIIqrQEQESVRLKLQHTLdvKELQG 850
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1460-1550 |
4.19e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1460 TELEASQKEARSLSTELFKLKNAYEE-SLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDA---EKLEL 1535
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEaSFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQrygKIPEL 490
|
90
....*....|....*
gi 2163567613 1536 QAALEEAEASLEHEE 1550
Cdd:COG0542 491 EKELAELEEELAELA 505
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1569-1917 |
4.20e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1569 RKLAEKDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQGYLKDT 1648
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1649 QLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEAD 1728
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1729 ISQLQTEVEEAIQEcrNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQLQ 1808
Cdd:COG4372 166 LAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1809 KLEVRVRELENELEAEQKRNAESIKGLRKSERR-VKELSYQTEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQANSN 1887
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEeLEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330 340 350
....*....|....*....|....*....|
gi 2163567613 1888 LAKFRKVQHELDEAEERADMAESQVNKLRA 1917
Cdd:COG4372 324 LAKKLELALAILLAELADLLQLLLVGLLDN 353
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
974-1107 |
4.26e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.97 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 974 TEEMAGLDENITKLTKEKKILQESHQQALDDLQAeedkvntlAKAK-VKLEQQVDDLESSLEqekkirmDLERAKRKLEG 1052
Cdd:pfam05911 680 TEENKRLKEEFEQLKSEKENLEVELASCTENLES--------TKSQlQESEQLIAELRSELA-------SLKESNSLAET 744
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2163567613 1053 DLKLAQESIMDLENDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQ 1107
Cdd:pfam05911 745 QLKCMAESYEDLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQ 799
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1145-1290 |
4.42e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.28 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1145 LEEAGGATSVQLELNKKQEAEFQKLRRDLEEATLQHEATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELD 1224
Cdd:pfam09787 49 LEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEE 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163567613 1225 DV----NSNTEQLIKAKTNLEKMCR--TTEDQMNEHRSKLEEAQRTVTDL----STQRAKLQTENSELSRQLEEKE 1290
Cdd:pfam09787 129 ELrrskATLQSRIKDREAEIEKLRNqlTSKSQSSSSQSELENRLHQLTETliqkQTMLEALSTEKNSLVLQLERME 204
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1494-1751 |
4.58e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.94 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1494 KRENKNLQEEILDLTEQLGASQKSIHELEKVrkqldaekleLQAALEEAEASLEHEEGKILRA--QLEFNQVKADYERKL 1571
Cdd:pfam05667 250 KRIAEQLRSAALAGTEATSGASRSAQDLAEL----------LSSFSGSSTTDTGLTKGSRFTHteKLQFTNEAPAATSSP 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1572 AEKDEEIEQSKRNHLRVVDSLQTSLDaETRSRnealrlKKKMEGDLNEMEIQLSHANRTAAEAQKQvkalqgylkdtqlq 1651
Cdd:pfam05667 320 PTKVETEEELQQQREEELEELQEQLE-DLESS------IQELEKEIKKLESSIKQVEEELEELKEQ-------------- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1652 lddvvraNEDLKENIAIVERRNNLL---QSELEELRAMVEQS-ERARKLAEQ------ELIEASERVQLLHSQNTSLINQ 1721
Cdd:pfam05667 379 -------NEELEKQYKVKKKTLDLLpdaEENIAKLQALVDASaQRLVELAGQwekhrvPLIEEYRALKEAKSNKEDESQR 451
|
250 260 270
....*....|....*....|....*....|
gi 2163567613 1722 KKkmeADISQLQTEVEEAIQECRNAEEKAK 1751
Cdd:pfam05667 452 KL---EEIKELREKIKEVAEEAKQKEELYK 478
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1013-1242 |
4.83e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1013 NTLAKAKVK-LEQQVDDLESSL---------------EQEKKIRMDLERAKRKLEGDLKLAQesimDLENDKQQLEERLK 1076
Cdd:PHA02562 169 DKLNKDKIReLNQQIQTLDMKIdhiqqqiktynknieEQRKKNGENIARKQNKYDELVEEAK----TIKAEIEELTDELL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1077 KKDFELNTLNARIEDEQAISAQLQKKLKELQarieeleeeleaertgraKVEKLRSE------LLQELEETSERLEE-AG 1149
Cdd:PHA02562 245 NLVMDIEDPSAALNKLNTAAAKIKSKIEQFQ------------------KVIKMYEKggvcptCTQQISEGPDRITKiKD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1150 GATSVQLELNKKQEA--EFQKLRRDLEEATLQHEATAATLRKKHADSVAELSEQLDnLQRVKQKLEKEKSELKLELDDVN 1227
Cdd:PHA02562 307 KLKELQHSLEKLDTAidELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKK-VKAAIEELQAEFVDNAEELAKLQ 385
|
250
....*....|....*
gi 2163567613 1228 SNTEQLIKAKTNLEK 1242
Cdd:PHA02562 386 DELDKIVKTKSELVK 400
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
979-1105 |
4.89e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 979 GLDENITKLTKEKKILQESHQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEkkirmdLERAKRKLEGDLKlaq 1058
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTE------LDRAKEKLKKLLQ--- 218
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2163567613 1059 eSIMDLENDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKE 1105
Cdd:smart00787 219 -EIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
938-1237 |
5.15e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.87 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 938 LEDECSELKKDIDDLELSLA--KVEKEKHATENKvKNLTEEMAGLDENITKLTKEKKILQesHQQALDDLQAEEDKVNTL 1015
Cdd:COG5185 251 TSDKLEKLVEQNTDLRLEKLgeNAESSKRLNENA-NNLIKQFENTKEKIAEYTKSIDIKK--ATESLEEQLAAAEAEQEL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1016 AKAKVKLEQQVDDLESSLEQEKKI---RMDLERAKRKLEGDLKLAQESIMDLENDKQQLEErlKKKDFELNTLNARiEDE 1092
Cdd:COG5185 328 EESKRETETGIQNLTAEIEQGQESlteNLEAIKEEIENIVGEVELSKSSEELDSFKDTIES--TKESLDEIPQNQR-GYA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1093 QAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEEagGATSVQLELNKKQEAEFQKLRRD 1172
Cdd:COG5185 405 QEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADE--ESQSRLEEAYDEINRSVRSKKED 482
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2163567613 1173 LEEATLQHEATAATLRKKHADSVAELSEQLDNL-QRVKQKLEKEKSELKLELDDVNSNTEQLIKAK 1237
Cdd:COG5185 483 LNEELTQIESRVSTLKATLEKLRAKLERQLEGVrSKLDQVAESLKDFMRARGYAHILALENLIPAS 548
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1160-1324 |
5.93e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.58 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1160 KKQEAEFQKLRRDLEEATLQheATAATLRKKHADS-VAELSEQLDNLqrvkqkleKEKSELKLElDDVNSNTEQLIKAKT 1238
Cdd:pfam05911 20 EKAEAEALALKQQLESVTLQ--KLTAEERAAHLDGaLKECMQQLRNV--------KEEQEQKIH-DVVLKKTKEWEKIKA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1239 NLEKmcrttedqmnehrsKLEEaqrtvtdLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEA 1318
Cdd:pfam05911 89 ELEA--------------KLVE-------TEQELLRAAAENDALSRSLQERENLLMKLSEEKSQAEAEIEALKSRLESCE 147
|
....*.
gi 2163567613 1319 KAKNAL 1324
Cdd:pfam05911 148 KEINSL 153
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1682-1917 |
5.99e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.43 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1682 ELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKkmeadisQLQTEVEEAIQECRNAEEKAKKAITDAAmma 1761
Cdd:pfam04012 12 NIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQK-------QLERRLEQQTEQAKKLEEKAQAALTKGN--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1762 EELKKEqdtsahLERMKKNMEQTVKDLQLRLDEAEQLALKGgKKQLQKLEVRVRELENELEAEQKRnAESIKGLRKSERR 1841
Cdd:pfam04012 82 EELARE------ALAEKKSLEKQAEALETQLAQQRSAVEQL-RKQLAALETKIQQLKAKKNLLKAR-LKAAKAQEAVQTS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163567613 1842 VKELSYQTEEDRKNMVRlqdlvdklqlkvkayKRQAE-EAEEQANSNLAKFRKVQHELDEAEERADMAESQVNKLRA 1917
Cdd:pfam04012 154 LGSLSTSSATDSFERIE---------------EKIEErEARADAAAELASAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1600-1845 |
6.00e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1600 TRSRNEALRLKKKMEGDLNEM------EIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERR- 1672
Cdd:pfam15905 52 TARKVKSLELKKKSQKNLKESkdqkelEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQl 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1673 ------NNLLQSELEE------LRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQ---TEVE 1737
Cdd:pfam15905 132 leltrvNELLKAKFSEdgtqkkMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEeklVSTE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1738 EAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLAlkggKKQLQKLEVRVREL 1817
Cdd:pfam15905 212 KEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQEL----SKQIKDLNEKCKLL 287
|
250 260
....*....|....*....|....*...
gi 2163567613 1818 ENELEAEQKRNAEsikglrKSERRVKEL 1845
Cdd:pfam15905 288 ESEKEELLREYEE------KEQTLNAEL 309
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
1160-1383 |
6.08e-03 |
|
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];
Pssm-ID: 227680 [Multi-domain] Cd Length: 524 Bit Score: 41.32 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1160 KKQEAEFQKLRRDLEE-------ATLQHEATAATLRKKHADSVAELSEQLDNLQrvkqkleKEKSELKLELDDVNSNTEQ 1232
Cdd:COG5391 311 IQLESEEESLTRLLESlnnllllVLNFSGVFAKRLEQNQNSILNEGVVQAETLR-------SSLKELLTQLQDEIKSRES 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1233 LIKAKTNLEKmcrtTEDQMNEHRSKLEEAQRtvtdlstqraKLQTENSELSRQLEEKEAFINQLTRGKLTYTQQleDLKR 1312
Cdd:COG5391 384 LILTDSNLEK----LTDQNLEDVEELSRSLR----------KNSSQRAVVSQQPEGLTSFSKLSYKLRDFVQEK--SRSK 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2163567613 1313 QLEEEAKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRA-LSKANSEVAQWRTKYETDAIQRTEELEE 1383
Cdd:COG5391 448 SIESLQQDKEKLEEQLAIAEKDAQEINEELKNELKFFFSVRNSdLEKILKSVADSHIEWAEENLEIWKSVKE 519
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1225-1921 |
6.09e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1225 DVNSNTEQLIK-AKTNLEKMCRTTEDQMNEHRSkleEAQRTVTDLSTQRAKLQTE--------NSELSRQLEEKEAFINQ 1295
Cdd:NF041483 69 DIGYQAEQLLRnAQIQADQLRADAERELRDARA---QTQRILQEHAEHQARLQAElhteavqrRQQLDQELAERRQTVES 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1296 LTRGKLTYTQQL----EDLKRQLEEE--AKAKNALAHALQSAQHDCDLLREQYEEEME------------AKTELQRALS 1357
Cdd:NF041483 146 HVNENVAWAEQLrartESQARRLLDEsrAEAEQALAAARAEAERLAEEARQRLGSEAEsaraeaeailrrARKDAERLLN 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1358 -------KANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCsslEKTKHRLQNEIEDLMADVERS 1430
Cdd:NF041483 226 aastqaqEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEA---EKVVAEAKEAAAKQLASAESA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1431 NAAAAALDKKQrnFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKN------AYEESLEHLETFKREnknlQEEI 1504
Cdd:NF041483 303 NEQRTRTAKEE--IARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAekartvAAEDTAAQLAKAART----AEEV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1505 LDLTEQ--LGASQKSIHELEKVRKQLDAEKLELQAALEEAEASLE-----------------HEEGKILRAQLEfnQVKA 1565
Cdd:NF041483 377 LTKASEdaKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKgaakddtkeyraktvelQEEARRLRGEAE--QLRA 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1566 DY----ERKLAEKDEE----IEQSKRNHLRVV-------DSLQTSLDAET-RSRNEALR----LKKKMEGDLnemEIQLS 1625
Cdd:NF041483 455 EAvaegERIRGEARREavqqIEEAARTAEELLtkakadaDELRSTATAESeRVRTEAIErattLRRQAEETL---ERTRA 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1626 HANRTAAEAQKQVKALQGYLKDTQLQL-DDVVRANEDLKENIAIVERRnnlLQSELEELRAMVEQ--------SERARKL 1696
Cdd:NF041483 532 EAERLRAEAEEQAEEVRAAAERAARELrEETERAIAARQAEAAEELTR---LHTEAEERLTAAEEaladaraeAERIRRE 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1697 AEQEL----IEASERVQLLHSQntslinqkkkMEADISQLQTE-VEEAIQECRNAEEKAKKAITDAAMMAEELKKE-QDT 1770
Cdd:NF041483 609 AAEETerlrTEAAERIRTLQAQ----------AEQEAERLRTEaAADASAARAEGENVAVRLRSEAAAEAERLKSEaQES 678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1771 S--------AHLERMKKNMEQTVKDLQ----LRLDEAEQLaLKGGKKQLQKLEVRVRELENELEAEQKR-----NAESIK 1833
Cdd:NF041483 679 AdrvraeaaAAAERVGTEAAEALAAAQeeaaRRRREAEET-LGSARAEADQERERAREQSEELLASARKrveeaQAEAQR 757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1834 GLRKSERRVKELSYQTEEDRKNmVR--LQDLVDKLQLKVKAYKRQAEEAEEQANsnlakfRKVQHELD----EAEERADM 1907
Cdd:NF041483 758 LVEEADRRATELVSAAEQTAQQ-VRdsVAGLQEQAEEEIAGLRSAAEHAAERTR------TEAQEEADrvrsDAYAERER 830
|
810
....*....|....
gi 2163567613 1908 AESQVNKLRARSRD 1921
Cdd:NF041483 831 ASEDANRLRREAQE 844
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1182-1408 |
6.23e-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: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1182 ATAATLRKKHADSVAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEE- 1260
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1261 ---AQRT---------------VTDLSTQRAKLQTENSELSRQLEEKEAFINQLTRGKltytQQLEDLKRQLEEEAKAKN 1322
Cdd:COG3883 92 araLYRSggsvsyldvllgsesFSDFLDRLSALSKIADADADLLEELKADKAELEAKK----AELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1323 ALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAV 1402
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
....*.
gi 2163567613 1403 NAKCSS 1408
Cdd:COG3883 248 GAGAAG 253
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
839-1734 |
6.73e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.74 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 839 ETEKEMQTMKEEF-GHLKEALEKSEARRKeleekmvsMLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEM 917
Cdd:PTZ00440 557 KDEKLKRSMKNDIkNKIKYIEENVDHIKD--------IISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYI 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 918 TERLEeeeemnaelaakKRKLEDECSELKKDIDDLElslaKVEKEKHATENkVKNLteemagLDENITKLTKEKKILQES 997
Cdd:PTZ00440 629 LNKFY------------KGDLQELLDELSHFLDDHK----YLYHEAKSKED-LQTL------LNTSKNEYEKLEFMKSDN 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 998 HQQALDDLQAEEDKVNTLAKAKVK--LEQQVDDLESSLEQEKKIRMDLERAkrklegdLKLAQESIMDLENDKQQLEERL 1075
Cdd:PTZ00440 686 IDNIIKNLKKELQNLLSLKENIIKkqLNNIEQDISNSLNQYTIKYNDLKSS-------IEEYKEEEEKLEVYKHQIINRK 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1076 KKKDFELNTLNARIEDEQAISAQLQKKLKELQARieeleeeleaertgrakvEKLRSELLQELEEtserleeaggatsvQ 1155
Cdd:PTZ00440 759 NEFILHLYENDKDLPDGKNTYEEFLQYKDTILNK------------------ENKISNDINILKE--------------N 806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1156 LELNKKQEAEFQKLRRDLEEATLQHEATAATLRKKhadsvaeLSEQLDNLQRvkQKLEKEKSELKLELDDVNSNTEQLIK 1235
Cdd:PTZ00440 807 KKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQK-------FPTEDENLNL--KELEKEFNENNQIVDNIIKDIENMNK 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1236 aKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAK-LQTENSELSRQLEEKEAFINQLTRGKLTYTQQLED----- 1309
Cdd:PTZ00440 878 -NINIIKTLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQhMKIINTDNIIQKNEKLNLLNNLNKEKEKIEKQLSDtkinn 956
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1310 LKRQLEeeaKAKNALAHALQSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLA 1389
Cdd:PTZ00440 957 LKMQIE---KTLEYYDKSKENINGNDGTHLEKLDKEKDEWEHFKSEIDKLNVNYNILNKKIDDLIKKQHDDIIELIDKLI 1033
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1390 QRLQeaEEAVEAVNAKCSSLEKTKHRLQNeiEDLMADVERSNaaaaaldkkqrnfDKILSEWKQKFEESQTELEASQKEA 1469
Cdd:PTZ00440 1034 KEKG--KEIEEKVDQYISLLEKMKTKLSS--FHFNIDIKKYK-------------NPKIKEEIKLLEEKVEALLKKIDEN 1096
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1470 RSlstELFKLKNayeESLEHLETFKRENKNlqeeildLTEQLGASQKSI----HELEKVRKQLDAEKLELQAALEEAEAS 1545
Cdd:PTZ00440 1097 KN---KLIEIKN---KSHEHVVNADKEKNK-------QTEHYNKKKKSLekiyKQMEKTLKELENMNLEDITLNEVNEIE 1163
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1546 LEHEegKILrAQLEFNQVKADYERKLAEKDE------EIEQSKRNHLRVVDSLQTSLDAeTRSRNEALRLKKKMEGDLNE 1619
Cdd:PTZ00440 1164 IEYE--RIL-IDHIVEQINNEAKKSKTIMEEiesykkDIDQVKKNMSKERNDHLTTFEY-NAYYDKATASYENIEELTTE 1239
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1620 MEIQLSHANRTaaeaqKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEE--LRAMVEQSERARKLA 1697
Cdd:PTZ00440 1240 AKGLKGEANRS-----TNVDELKEIKLQVFSYLQQVIKENNKMENALHEIKNMYEFLISIDSEkiLKEILNSTKKAEEFS 1314
|
890 900 910
....*....|....*....|....*....|....*..
gi 2163567613 1698 EQELIEASERVQLLhsqntslinqkKKMEADISQLQT 1734
Cdd:PTZ00440 1315 NDAKKELEKTDNLI-----------KQVEAKIEQAKE 1340
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1671-1926 |
6.95e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.57 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1671 RRNNLLqSELEELRAMVEQSERarklaeqeLIEA--SERVQLLHSQNTSLINQKKKMEAD-ISQLQTEVEEAIQEcRNAE 1747
Cdd:PTZ00108 996 RKEYLL-GKLERELARLSNKVR--------FIKHviNGELVITNAKKKDLVKELKKLGYVrFKDIIKKKSEKITA-EEEE 1065
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1748 EKAKKAITDAAMMAEELKKEQD------------TSAHLERMKKNMEQTVKDLQ-LRLDEAEQLALKGGKKQLQKLEVRV 1814
Cdd:PTZ00108 1066 GAEEDDEADDEDDEEELGAAVSydyllsmpiwslTKEKVEKLNAELEKKEKELEkLKNTTPKDMWLEDLDKFEEALEEQE 1145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1815 RELENELEAEQKrnAESIKGLRKSERRVKELSYQTEEDRKNMVrlqDLVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKV 1894
Cdd:PTZ00108 1146 EVEEKEIAKEQR--LKSKTKGKASKLRKPKLKKKEKKKKKSSA---DKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNS 1220
|
250 260 270
....*....|....*....|....*....|..
gi 2163567613 1895 QHELDEAEERADMAESQVNKLRARSRDIGAKK 1926
Cdd:PTZ00108 1221 SGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSK 1252
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1568-1844 |
7.10e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.58 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1568 ERKLAEKDEEIEQSKR-NHLRVVDSLQTSLDAetrsrnealrlkkkmegdLNEMEIqlshanrTAAEAQKQVKALQGYLK 1646
Cdd:PRK10929 25 EKQITQELEQAKAAKTpAQAEIVEALQSALNW------------------LEERKG-------SLERAKQYQQVIDNFPK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1647 DTQ------LQLDDVVRAnedLKENIAIVERRNNLLQSE---LEELRAMVEQSERARKLAE-------------QELIEA 1704
Cdd:PRK10929 80 LSAelrqqlNNERDEPRS---VPPNMSTDALEQEILQVSsqlLEKSRQAQQEQDRAREISDslsqlpqqqtearRQLNEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1705 SERVQLLHSQNTSLinqkkkMEADISQLQteveeaiqecrnAEEKAKKAITDaammaeELKkeqdtsahLERMKKNMEQT 1784
Cdd:PRK10929 157 ERRLQTLGTPNTPL------AQAQLTALQ------------AESAALKALVD------ELE--------LAQLSANNRQE 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1785 VKDLQLRLdeaeqlalkgGKKQLQKLEVRVRELENELEAEQKRNAEsiKGLRKSERRVKE 1844
Cdd:PRK10929 205 LARLRSEL----------AKKRSQQLDAYLQALRNQLNSQRQREAE--RALESTELLAEQ 252
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1676-1916 |
7.17e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1676 LQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAIT 1755
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1756 DAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQ---LRLDEAEQLALK--------GGKKQLQKLEVRVRELENELEAE 1824
Cdd:COG1340 93 ELDELRKELAELNKAGGSIDKLRKEIERLEWRQQtevLSPEEEKELVEKikelekelEKAKKALEKNEKLKELRAELKEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1825 QKRnaesikgLRKSERRVKELSYQTEEDRKNMVRLQDLVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKVQHELDEAEER 1904
Cdd:COG1340 173 RKE-------AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKE 245
|
250
....*....|..
gi 2163567613 1905 ADMAESQVNKLR 1916
Cdd:COG1340 246 LKKLRKKQRALK 257
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1004-1397 |
7.22e-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: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1004 DLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLE--GDL----KLAQESIMDLENDKQQLEERLKK 1077
Cdd:pfam05622 98 ELQHRNEELTSLAEEAQALKDEMDILRESSDKVKKLEATVETYKKKLEdlGDLrrqvKLLEERNAEYMQRTLQLEEELKK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1078 KdfelNTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEEaggatsvqLE 1157
Cdd:pfam05622 178 A----NALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRETNEE--------LR 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1158 LNKKQEAEFQKLRRDLEEATLQHEATAATLRKkhadsvAELSEQLDNLQRvKQKLEKEKSELklelddvnsnteqlikak 1237
Cdd:pfam05622 246 CAQLQQAELSQADALLSPSSDPGDNLAAEIMP------AEIREKLIRLQH-ENKMLRLGQEG------------------ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1238 tnlekmcrTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSrqleekeafinqltrgkltytQQLEDLKRQLEEE 1317
Cdd:pfam05622 301 --------SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQ---------------------QQVEELQKALQEQ 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1318 AkaknalahalqSAQHDCDLLREQYEEEMEAKTELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEE 1397
Cdd:pfam05622 352 G-----------SKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEDMKAMEE 420
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
964-1365 |
7.23e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.15 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 964 HATENKVKNLTEEMAGLDENITKLTKE-----KKILQEShQQALDDLQAEE--DKVNTLAKAKVKLEQQVDDLESSLEQE 1036
Cdd:NF033838 36 HAEEVRGGNNPTVTSSGNESQKEHAKEveshlEKILSEI-QKSLDKRKHTQnvALNKKLSDIKTEYLYELNVLKEKSEAE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1037 --KKIRMDLERAKRKLEGDLklaqesimdLENDKQQLEERLKKKDFELNTLNARIEDEQAISAQLQKKLKELQARieele 1114
Cdd:NF033838 115 ltSKTKKELDAAFEQFKKDT---------LEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAE----- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1115 eeleaertGRAKVEKLRSELLQElEETSERLEEAGGATSVQLELNKKQEAEFQKLRRDLEEATLQHEATAATLRKKHADS 1194
Cdd:NF033838 181 --------SDVEVKKAELELVKE-EAKEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1195 VAELSEQLDNLQRVKQKLEKEKSELKLELDDVNSNTEQLikAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAK 1274
Cdd:NF033838 252 NVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSV--GEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1275 ---------LQTENSELSRQLEEKEAfinQLTRGKLTYTQQLEDLKrQLEEEAKAKNALAHALQSAQHDcdllREQYEEE 1345
Cdd:NF033838 330 nyptntyktLELEIAESDVKVKEAEL---ELVKEEAKEPRNEEKIK-QAKAKVESKKAEATRLEKIKTD----RKKAEEE 401
|
410 420
....*....|....*....|
gi 2163567613 1346 MEAKTELQRALSKANSEVAQ 1365
Cdd:NF033838 402 AKRKAAEEDKVKEKPAEQPQ 421
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1376-1699 |
7.43e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1376 QRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMADVERSNAAAAALDKKQRNFDKILSEWKQKF 1455
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1456 EESQTELEASQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLEL 1535
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1536 QAALEEAEASLEHEEGKILRAQLEFNQVKADYERKLAEKDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKmeg 1615
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1616 DLNEMEIQLSHANRTAAEAQKQVKALQGYLKDTQLQLDDVVRANEDLKENIAIVERRNNLLQSELEELRAMVEQSERARK 1695
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLA 319
|
....
gi 2163567613 1696 LAEQ 1699
Cdd:COG4372 320 ALLE 323
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1466-1895 |
7.43e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1466 QKEARSLSTELFKLKNAYEESLEHLETFKRENKN---LQEEILDLTEQLGASQKSIHELEKVRKQLDAEKLELQAALEEA 1542
Cdd:COG5185 131 VALKDELIKVEKLDEIADIEASYGEVETGIIKDIfgkLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKES 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1543 EASLEHEEGKILRAQLEFNQVKAdYERKLAEKDEEIEQSKRNHLRVVDSLQTSLDAETRSRNEALRLKKKMEGDLNEMEI 1622
Cdd:COG5185 211 ETGNLGSESTLLEKAKEIINIEE-ALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1623 QLSHANRTAAEAQKQVKALQGYLkdtqlQLDDVVRANEDLKEniaiVERRNNLLQSELEELRAMVEQSERARKLAEQELI 1702
Cdd:COG5185 290 QFENTKEKIAEYTKSIDIKKATE-----SLEEQLAAAEAEQE----LEESKRETETGIQNLTAEIEQGQESLTENLEAIK 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1703 EASERVqllhsqntSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKAITDAAMMAEELKKEQDTSA-----HLERM 1777
Cdd:COG5185 361 EEIENI--------VGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIeelqrQIEQA 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1778 KKNMEQTVKDLQLRLDEAEQLALKGGKKQLQKLEVRVRELENELeaeQKRNAESIKGLRKSERRVKELSYQTEEDRKNMV 1857
Cdd:COG5185 433 TSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSV---RSKKEDLNEELTQIESRVSTLKATLEKLRAKLE 509
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2163567613 1858 R----LQDLVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKVQ 1895
Cdd:COG5185 510 RqlegVRSKLDQVAESLKDFMRARGYAHILALENLIPASELI 551
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1676-1844 |
7.51e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1676 LQSELEELRAMVEQSERARKLAEQELIEASERVQLLHSQNTSLINQKKKMEADISQLQT---EVEEAIQECRNAEEkakk 1752
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikKYEEQLGNVRNNKE---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1753 aitdaammAEELKKEQDTsahLERMKKNMEQTVKDLQLRLDEAEqlalkggkKQLQKLEVRVRELENELEAEQKRNAESI 1832
Cdd:COG1579 91 --------YEALQKEIES---LKRRISDLEDEILELMERIEELE--------EELAELEAELAELEAELEEKKAELDEEL 151
|
170
....*....|..
gi 2163567613 1833 KGLRKSERRVKE 1844
Cdd:COG1579 152 AELEAELEELEA 163
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1376-1559 |
7.74e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.51 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1376 QRTEELEEAKKKLAQRLQEA--EEAVEAVNAKCSSLEKTKHR----------LQNEIEDL---MADVE-RSNAAAAALDK 1439
Cdd:pfam09787 14 QKAARILQSKEKLIASLKEGsgVEGLDSSTALTLELEELRQErdllreeiqkLRGQIQQLrteLQELEaQQQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1440 KQRNFDKILSEWKQKFEESQTELEASQKEARSLSTELFKLKNAYEESLEHLETfkrenknlqeEILDLTEQLGASQKSI- 1518
Cdd:pfam09787 94 QLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREA----------EIEKLRNQLTSKSQSSs 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1519 --HELEKVRKQLDAEKLELQAALEE--AEAS-----LEHEEGKILRAQLE 1559
Cdd:pfam09787 164 sqSELENRLHQLTETLIQKQTMLEAlsTEKNslvlqLERMEQQIKELQGE 213
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
834-1189 |
7.89e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 834 LLKSAETEKEMQTMKEEFGHLKEALEKSE----ARRKELEEKMVSMLQEKNDLQLQVQAEQDNLADAEERCDqlIKNKIQ 909
Cdd:COG5185 235 LKGFQDPESELEDLAQTSDKLEKLVEQNTdlrlEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSID--IKKATE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 910 LEAKVKEMTERleeeeemNAELAAKKRKLEdecSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAgLDENITKLTK 989
Cdd:COG5185 313 SLEEQLAAAEA-------EQELEESKRETE---TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVE-LSKSSEELDS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 990 EKKILQESHQqalddlQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLERAKRKLEGDLKLAQESIMDLENDKQ 1069
Cdd:COG5185 382 FKDTIESTKE------SLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMR 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1070 QLEERLKKKdfelnTLNARIEDEQAISAQLQKKLKELQARIEELEEELEAERTGRAKVEKLRSELLQELEETSERLEEAG 1149
Cdd:COG5185 456 EADEESQSR-----LEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFM 530
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2163567613 1150 GATSVQLELNKKQEAEFQKLRRDLEEATLQHEATAATLRK 1189
Cdd:COG5185 531 RARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVI 570
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1520-1898 |
8.62e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1520 ELEKVRKQLDAEKLELQAALEEAEASLEHEEGKILRAQlEFNQVKADYERKLAEKDEEIEQSKRNHLRVVDS-------- 1591
Cdd:PRK10929 31 ELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAK-QYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNmstdaleq 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1592 --LQTS--LDAETRSRNEALRLKKKMEGDLNEMEIQLSHANRTAAEAQKQVKALQgylkdtqlqlddvvranedlKENIA 1667
Cdd:PRK10929 110 eiLQVSsqLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLG--------------------TPNTP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1668 IVERRNNLLQSELEELRAMVEQSERARKLA--EQELIEAseRVQLLHSQNTSLINQKKKMEADI-SQLQTEVEEAIQecr 1744
Cdd:PRK10929 170 LAQAQLTALQAESAALKALVDELELAQLSAnnRQELARL--RSELAKKRSQQLDAYLQALRNQLnSQRQREAERALE--- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1745 NAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMeqtvkdlqlrldeaEQLALKGGKKQLQKLEVRvRELENELEAE 1824
Cdd:PRK10929 245 STELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRM--------------DLIASQQRQAASQTLQVR-QALNTLREQS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1825 QKRNAESIKG--LRKSERRVKELSYQTEEDRkNMVRL-------QDLVDKLQLKVKAYKRQAEEAEEQANSNLAKFRKVQ 1895
Cdd:PRK10929 310 QWLGVSNALGeaLRAQVARLPEMPKPQQLDT-EMAQLrvqrlryEDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTQ 388
|
...
gi 2163567613 1896 HEL 1898
Cdd:PRK10929 389 REL 391
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1773-1894 |
9.08e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1773 HLERMKKNMEQTVKDLQLRLDEAEQLAlkggKKQLQKLEVRVRELENELEaEQKRNAESIKGLRKSERrvkelsyQTEED 1852
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELH----EKQKFYLRQSVIDLQTKLQ-EMQMERDAMADIRRRES-------QSQED 142
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2163567613 1853 RKNmvRLQDLVDKLQlkvkAYKRQAEEAEEQANSNLAKFRKV 1894
Cdd:pfam15921 143 LRN--QLQNTVHELE----AAKCLKEDMLEDSNTQIEQLRKM 178
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
935-1294 |
9.36e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 40.43 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 935 KRKLEDECSELKKDIDDLELSLAKVEKEKHATENKVKNLTEEMAGLDENITKLTKEKKILQ-----------------ES 997
Cdd:pfam15742 8 KYQQQEEVQQLRQNLQRLQILCTSAEKELRYERGKNLDLKQHNSLLQEENIKIKAELKQAQqklldstkmcssltaewKH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 998 HQQALDDLQAEEDKVNTLAKAKVKLEQQVDDLESSLEQEKKIRMDLeraKRKLEGDLKLAQESIMDLEndKQQLEERLKK 1077
Cdd:pfam15742 88 CQQKIRELELEVLKQAQSIKSQNSLQEKLAQEKSRVADAEEKILEL---QQKLEHAHKVCLTDTCILE--KKQLEERIKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1078 KDFELNTLNARIEDEQAISAQLQKKLKELQARIeeleeelEAERTGRAKVEKLRSELLQELEETSERLEeaggatsvQLE 1157
Cdd:pfam15742 163 ASENEAKLKQQYQEEQQKRKLLDQNVNELQQQV-------RSLQDKEAQLEMTNSQQQLRIQQQEAQLK--------QLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1158 LNKKQEAEFQKLRRDLEE--ATLQHEATAatLRKKHADSVAELSEQLDNL----QRVKQKLEKEKSELKLELDDVNSNTE 1231
Cdd:pfam15742 228 NEKRKSDEHLKSNQELSEklSSLQQEKEA--LQEELQQVLKQLDVHVRKYnekhHHHKAKLRRAKDRLVHEVEQRDERIK 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2163567613 1232 QLikaktnlekmcrttEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSELSRQLEEKEAFIN 1294
Cdd:pfam15742 306 QL--------------ENEIGILQQQSEKEKAFQKQVTAQNEILLLEKRKLLEQLTEQEELIK 354
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1202-1421 |
9.44e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.56 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1202 LDNLQRVKQKLEKEKSELKLelddVNSNTEQLIKAKTNLEKMCRTTEDQMNEHRSKLEEAQRTVTDLSTQRAKLQTENSE 1281
Cdd:pfam15905 58 SLELKKKSQKNLKESKDQKE----LEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1282 LSRQLEEKEAFINQLTRGKLTYTQQLEDLKRQLEEEAKAKNALAHA------LQSAQHDC-----------DLLREQYEE 1344
Cdd:pfam15905 134 LTRVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQegmegkLQVTQKNLehskgkvaqleEKLVSTEKE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1345 EMEAKTELQR------ALSKANSEVAQWR---TKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHR 1415
Cdd:pfam15905 214 KIEEKSETEKlleyitELSCVSEQVEKYKldiAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEE 293
|
....*.
gi 2163567613 1416 LQNEIE 1421
Cdd:pfam15905 294 LLREYE 299
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1686-1911 |
9.99e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 40.71 E-value: 9.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1686 MVEQSERARKLAEQELIEasERVQLLHSQNTSLINQKKKMEADISQLQTEVEEAIQECRNAEEKAKKaitdaamMAEELK 1765
Cdd:pfam15709 309 MESEEERSEEDPSKALLE--KREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEK-------MREELE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163567613 1766 KEQDTSAHLERMKKnmeQTVKDLQLRLDEAEqlalKGGKKQLQKLEVRVRELENE-----LEAEQKRNAESIKGLRKSER 1840
Cdd:pfam15709 380 LEQQRRFEEIRLRK---QRLEEERQRQEEEE----RKQRLQLQAAQERARQQQEEfrrklQELQRKKQQEEAERAEAEKQ 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2163567613 1841 RVKELSYQTEEDRKnmvRLQDLVDKLQLKvkaYKRQAEEAEEQAnsnlakfrkvqheLDEAEERADMAESQ 1911
Cdd:pfam15709 453 RQKELEMQLAEEQK---RLMEMAEEERLE---YQRQKQEAEEKA-------------RLEAEERRQKEEEA 504
|
|
| |
