|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 1479.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVAALGETPAKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDH 338
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 419 QNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 499 ILEQEEYKREGIDWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHLGKSPNFQKPRPDKKRKY 578
Cdd:cd14927 401 ILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 579 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDSASEHKIGGKEKRKKAASFQTVSQL 658
Cdd:cd14927 481 EAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEDPKSGVKEKRKKAASFQTVSQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 659 HKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPHAI 738
Cdd:cd14927 561 HKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAI 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 1591544934 739 PDDTFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14927 641 PDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-774 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1342.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVAALGetpakKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASS-----KKKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDH 338
Cdd:cd01377 156 TGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd01377 236 AFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 419 QNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd01377 316 QNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 499 ILEQEEYKREGIDWTFIDFGLDLQACIDLIEKP-LGIMSILEEECMFPKATDNSFKAKMYDNHLGKSPNFQKPrpdKKRK 577
Cdd:cd01377 396 VLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKP---KPKK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 578 YEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDSasehkiGGKEKRKKAASFQTVSQ 657
Cdd:cd01377 473 SEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGG------GGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 658 LHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPHA 737
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*..
gi 1591544934 738 IPDDtFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd01377 627 IPKG-FDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 1171.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVAALGETPAKKGqgpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLG---------ALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKpELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDH 338
Cdd:cd14929 152 RGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd14929 231 AMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 419 QNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14929 311 QNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 499 ILEQEEYKREGIDWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHLGKSPNFQKPRPDKKrKY 578
Cdd:cd14929 391 VLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKK-KF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 579 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDSASEHkigGKEKRKKAASFQTVSQL 658
Cdd:cd14929 470 EAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQF---GEKKRKKGASFQTVASL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 659 HKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPHAI 738
Cdd:cd14929 547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTF 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 1591544934 739 PDDTFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14929 627 PKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-774 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 1147.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 100 SVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 180 SGAGKTVNTKRVIQYFAIVAALGEtPAKKGQgpaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGD-LAKKKD---SKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDHA 339
Cdd:cd14913 158 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 420 NVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14913 318 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 500 LEQEEYKREGIDWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHLGKSPNFQKPRPDKKRKyE 579
Cdd:cd14913 398 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRA-E 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDSASEHKiggKEKRKKAASFQTVSQLH 659
Cdd:cd14913 477 AHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKK---KVAKKKGSSFQTVSALF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 660 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPHAIP 739
Cdd:cd14913 554 RENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIP 633
|
650 660 670
....*....|....*....|....*....|....*
gi 1591544934 740 DDTFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14913 634 EGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-774 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 1104.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 100 SVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 180 SGAGKTVNTKRVIQYFAIVAALGETpAKKGQGPATktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDR-SKKDQTPGK---GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDHA 339
Cdd:cd14917 158 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14917 238 FDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 420 NVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14917 318 NVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 500 LEQEEYKREGIDWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHLGKSPNFQKPRpDKKRKYE 579
Cdd:cd14917 398 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPR-NIKGKPE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDSASEHkigGKEKRKKAASFQTVSQLH 659
Cdd:cd14917 477 AHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEK---GKGKAKKGSSFQTVSALH 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 660 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPHAIP 739
Cdd:cd14917 554 RENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 633
|
650 660 670
....*....|....*....|....*....|....*
gi 1591544934 740 DDTFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14917 634 EGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-774 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 1069.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 100 SVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 180 SGAGKTVNTKRVIQYFAIVAALGETPAKKGqgpATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKKEN---PNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDHA 339
Cdd:cd14916 159 GKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 420 NVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 500 LEQEEYKREGIDWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHLGKSPNFQKPRpDKKRKYE 579
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPR-NVKGKQE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDSASEHKigGKEKRKKAASFQTVSQLH 659
Cdd:cd14916 478 AHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGK--GKGGKKKGSSFQTVSALH 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 660 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPHAIP 739
Cdd:cd14916 556 RENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 635
|
650 660 670
....*....|....*....|....*....|....*
gi 1591544934 740 DDTFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14916 636 EGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-774 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 1049.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 100 SVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 180 SGAGKTVNTKRVIQYFAIVAALGEtpaKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGD---KKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDHA 339
Cdd:cd14923 159 GKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14923 239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 420 NVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 500 LEQEEYKREGIDWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHLGKSPNFQKPRPdKKRKYE 579
Cdd:cd14923 399 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKP-AKGKAE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDSASEhkiGGKEK--RKKAASFQTVSQ 657
Cdd:cd14923 478 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDS---GGSKKggKKKGSSFQTVSA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 658 LHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPHA 737
Cdd:cd14923 555 VFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASA 634
|
650 660 670
....*....|....*....|....*....|....*..
gi 1591544934 738 IPDDTFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14923 635 IPEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-774 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1038.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 87 IEDMAMLTHLNEASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 167 RNRENQSMLITGESGAGKTVNTKRVIQYFAIVAalgetpakkGQGPATKtGGTLEDQIIEANPAMEAFGNAKTLRNDNSS 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVS---------GSGSAGN-VGRLEEQILQSNPILEAFGNAKTVRNNNSS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 247 RFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVsSNPYDYHFCSQ-GVTTVE 325
Cdd:pfam00063 151 RFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRL-TNPKDYHYLSQsGCYTID 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 326 NLDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLH 405
Cdd:pfam00063 230 GIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 406 PRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINF 484
Cdd:pfam00063 310 RRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLdVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 485 TNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNHlGK 563
Cdd:pfam00063 390 VNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 564 SPNFQKPRPdkkrKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENY-IGSDSASEHKIGG 642
Cdd:pfam00063 468 HPHFQKPRL----QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYeTAESAAANESGKS 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 643 KEKRKKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRIL 722
Cdd:pfam00063 544 TPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRIT 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 723 YAEFKRRYRILNPHAIPDDtFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:pfam00063 624 FQEFVQRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-774 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 1031.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 101 VLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 181 GAGKTVNTKRVIQYFAIVAALGEtpakKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTG 260
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGE----KKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 261 KLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDHAM 340
Cdd:cd14918 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 341 DILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQN 420
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 421 VEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFIL 500
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 501 EQEEYKREGIDWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHLGKSPNFQKPRPdKKRKYEA 580
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKV-VKGKAEA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 581 HFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDSASEHKIGGKekrKKAASFQTVSQLHK 660
Cdd:cd14918 478 HFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAK---KKGSSFQTVSALFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 661 ENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPHAIPD 740
Cdd:cd14918 555 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE 634
|
650 660 670
....*....|....*....|....*....|....
gi 1591544934 741 DTFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14918 635 GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-774 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 1028.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 100 SVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 180 SGAGKTVNTKRVIQYFAIVAALGETpaKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDHA 339
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14915 240 VDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 420 NVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 500 LEQEEYKREGIDWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHLGKSPNFQKPRPdKKRKYE 579
Cdd:cd14915 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENyiGSDSASEHKIGGKEKRKKAASFQTVSQLH 659
Cdd:cd14915 479 AHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG--GQTAEAEGGGGKKGGKKKGSSFQTVSALF 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 660 KENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPHAIP 739
Cdd:cd14915 557 RENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 636
|
650 660 670
....*....|....*....|....*....|....*
gi 1591544934 740 DDTFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14915 637 EGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-774 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 1024.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 100 SVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 180 SGAGKTVNTKRVIQYFAIVAALGETpaKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDHA 339
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14910 240 IEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 420 NVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14910 320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 500 LEQEEYKREGIDWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHLGKSPNFQKPRPdKKRKYE 579
Cdd:cd14910 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKP-AKGKVE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLAclyeNYIGSDSASEHKIGGKEK--RKKAASFQTVSQ 657
Cdd:cd14910 479 AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLA----LLFSGAAAAEAEEGGGKKggKKKGSSFQTVSA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 658 LHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPHA 737
Cdd:cd14910 555 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 634
|
650 660 670
....*....|....*....|....*....|....*..
gi 1591544934 738 IPDDTFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14910 635 IPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-774 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 1021.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 100 SVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 180 SGAGKTVNTKRVIQYFAIVAALGETpaKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEK--KKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDHA 339
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14912 240 IDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 420 NVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 500 LEQEEYKREGIDWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHLGKSPNFQKPRPdKKRKYE 579
Cdd:cd14912 400 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKV-VKGKAE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 580 AHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYEnyiGSDSASEHKIGGKEK---RKKAASFQTVS 656
Cdd:cd14912 479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFS---GAQTAEGASAGGGAKkggKKKGSSFQTVS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 657 QLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPH 736
Cdd:cd14912 556 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 635
|
650 660 670
....*....|....*....|....*....|....*...
gi 1591544934 737 AIPDDTFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14912 636 AIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 1016.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVAALGETpAKKGQGpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQ-SSDGKG-------SLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDH 338
Cdd:cd14934 153 TGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd14934 233 AFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 419 QNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14934 313 QNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 499 ILEQEEYKREGIDWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHLGKSPNFQKPRPDKKRKY 578
Cdd:cd14934 393 VLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKGP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 579 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYEnyigsdsaSEHKIGGKEKRKKAASFQTVSQL 658
Cdd:cd14934 473 EAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFK--------EEEAPAGSKKQKRGSSFMTVSNF 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 659 HKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPHAI 738
Cdd:cd14934 545 YREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVI 624
|
650 660 670
....*....|....*....|....*....|....*.
gi 1591544934 739 PDDtFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14934 625 PQG-FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 1008.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVAALGETPakkgqgPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTD------EAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDH 338
Cdd:cd14909 155 TGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd14909 235 AFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 419 QNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMF 498
Cdd:cd14909 315 RNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 499 ILEQEEYKREGIDWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHLGKSPNFQKPRPDKKRKY 578
Cdd:cd14909 395 VLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 579 EAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDSASEHKIGGkeKRKKAASFQTVSQL 658
Cdd:cd14909 475 AAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGG--RGKKGGGFATVSSA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 659 HKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPHAI 738
Cdd:cd14909 553 YKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGI 632
|
650 660 670
....*....|....*....|....*....|....*.
gi 1591544934 739 PDDTfvDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14909 633 QGEE--DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-786 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 997.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 80 NPPKYDMIEDMAMLTHLNEASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIAD 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 160 NAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAIVAAlgetpakkgqgpATKTGGTLEDQIIEANPAMEAFGNAKT 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG------------SNTEVGSVEDQILESNPILEAFGNAKT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 240 LRNDNSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQ 319
Cdd:smart00242 149 LRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 320 GVT-TVENLDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEA-DGTESADKASYLMGVSSA 397
Cdd:smart00242 228 GGClTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTvKDKEELSNAAELLGVDPE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 398 DLIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSF 477
Cdd:smart00242 308 ELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 478 EQLCINFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKM 556
Cdd:smart00242 388 EQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 557 YdNHLGKSPNFQKPRpdkkRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSdsas 636
Cdd:smart00242 467 N-QHHKKHPHFSKPK----KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSN---- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 637 ehkiggKEKRKKaasFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKG 716
Cdd:smart00242 538 ------AGSKKR---FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAG 608
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 717 FPNRILYAEFKRRYRILNPHAIPDDTFvDSRKAVEKLLASLDIDHSQYRFGHTKVFFKAGLLGHLEELRD 786
Cdd:smart00242 609 FPYRLPFDEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1123 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 873.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 36 RAWIPDEKEAYIEIEIKELSGDKVIV----ETKDGRTLTVK--DCDIQQMNPPKYDMIEDMAMLTHLNEASVLYNLRRRY 109
Cdd:COG5022 11 GCWIPDEEKGWIWAEIIKEAFNKGKVteegKKEDGESVSVKkkVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 110 AAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGESGAGKTVNTK 189
Cdd:COG5022 91 NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 190 RVIQYFAIVaalgetpakkgQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDI 269
Cdd:COG5022 171 RIMQYLASV-----------TSSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 270 YLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQG-VTTVENLDDGQELMATDHAMDILGFLPD 348
Cdd:COG5022 240 YLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQ-NPKDYIYLSQGgCDKIDGIDDAKEFKITLDALKTIGIDEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 349 EKYGCYKIVGAIMHFGNMKFKqKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVTYAV 428
Cdd:COG5022 319 EQDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 429 GALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKRE 508
Cdd:COG5022 398 DSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 509 GIDWTFIDFgLDLQACIDLIEK--PLGIMSILEEECMFPKATDNSFKAKMYDN-HLGKSPNFQKPR-PDKKrkyeahFEL 584
Cdd:COG5022 478 GIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRfRDNK------FVV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 585 VHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYigsdsasehkiggkEKRKKAASFQTVSQLHKENLN 664
Cdd:COG5022 551 KHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE--------------ENIESKGRFPTLGSRFKESLN 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 665 KLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPHAIPDDTF- 743
Cdd:COG5022 617 SLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYt 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 744 --VDSRKAVEKLLASLDIDHSQYRFGHTKVFFKAGLLGHLEELRDERLAKVLTLLQAAARGKIMRMELLRMMERRDALMI 821
Cdd:COG5022 697 wkEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQV 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 822 IQWNIRAFNAVKHWPWMKLFFKIKPLLKSAATEKELASLKEELAKLKEALEKsEVKRKELEERQVSLIQEKNDLSLQLQA 901
Cdd:COG5022 777 IQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKR-EKKLRETEEVEFSLKAEVLIQKFGRSL 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 902 EQDNLADAEDRCDLLIKTKIQLEAKVKEIMERLEDEEEMSAtVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHAten 981
Cdd:COG5022 856 KAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISS-LKLVNLELESEIIELKKSLSSDLIENLEFKTELIA--- 931
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 982 KVKNLIEEMAALDETILKLTKEKKALQeahqqtlddLQAEEDKvntLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKR 1061
Cdd:COG5022 932 RLKKLLNNIDLEEGPSIEYVKLPELNK---------LHEVESK---LKETSEEYEDLLKKSTILVREGNKANSELKNFKK 999
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1591544934 1062 KLEGDLKLSmesvMDLENDKQQLEEK---------LKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQART 1123
Cdd:COG5022 1000 ELAELSKQY----GALQESTKQLKELpvevaelqsASKIISSESTELSILKPLQKLKGLLLLENNQLQARY 1066
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-774 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 829.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRR-SEAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 178 GESGAGKTVNTKRVIQYFAIVAalgetpaKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALS-------GSGSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHF----CSQGVTTVENLDDGQEL 333
Cdd:cd00124 154 PTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylNSSGCDRIDGVDDAEEF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 334 MATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREE--QAEADGTESADKASYLMGVSSADLIKGLLHPRVKVG 411
Cdd:cd00124 234 QELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 412 NEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQ--YFIGVLDIAGFEIFELNSFEQLCINFTNEKL 489
Cdd:cd00124 314 GETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 490 QQFFNHHMFILEQEEYKREGIDWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNHLGKSPNFQ 568
Cdd:cd00124 394 QQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 569 KPRPDKKrkyeaHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSnkllaclyenyigsdsasehkiggkekrkk 648
Cdd:cd00124 473 KKRKAKL-----EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS------------------------------ 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 649 aasfqtvsqLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKR 728
Cdd:cd00124 518 ---------QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLK 588
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1591544934 729 RYRILNPHAIPDDtFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd00124 589 RYRILAPGATEKA-SDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 789.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVAAL----GETPAKKGQGPATKTGGtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 254
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgSGAVPHPAVNPAVLIGE-LEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 255 HFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS-----QKKPELLDmllvssNPYDYHFCSQGVTTVENLDD 329
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAgatpeQREKFILD------DVKSYAFLSNGSLPVPGVDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 330 GQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVK 409
Cdd:cd14911 234 YAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 410 VGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEK 488
Cdd:cd14911 314 VGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLdRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 489 LQQFFNHHMFILEQEEYKREGIDWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHlGKSPNFQ 568
Cdd:cd14911 394 LQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFM 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 569 KprpdKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENY----IGSDSASEHKIGgke 644
Cdd:cd14911 473 K----TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAeivgMAQQALTDTQFG--- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 645 KRKKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYA 724
Cdd:cd14911 546 ARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQ 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1591544934 725 EFKRRYRILNPHAIPDDtFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14911 626 EFRQRYELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 772.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVAAlgetpAKKGQGPATkTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVAS-----SHKGRKDHN-IPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPEL-LDMLLVSSNpyDYHFCSQGVTTVENLDDGQELMATD 337
Cdd:cd14920 155 TGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 338 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVK 417
Cdd:cd14920 233 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 418 GQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLyTSLPRQ--YFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNH 495
Cdd:cd14920 313 AQTKEQADFAVEALAKATYERLFRWLVHRINKAL-DRTKRQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 496 HMFILEQEEYKREGIDWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMyDNHLGKSPNFQKPRp 572
Cdd:cd14920 392 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPR- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 573 dkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYEN---YIGSD---SASEHKIGGKEKR 646
Cdd:cd14920 470 --QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrIVGLDqvtGMTETAFGSAYKT 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 647 KKAAsFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEF 726
Cdd:cd14920 548 KKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1591544934 727 KRRYRILNPHAIPdDTFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14920 627 RQRYEILTPNAIP-KGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 724.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVAALGETpaKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKT--KKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPyDYHFCSQGVTTVENLDDGQELMATDH 338
Cdd:cd14932 159 NGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYS-KYRFLSNGNVTIPGQQDKELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 419 QNVEQVTYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHM 497
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALdKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 498 FILEQEEYKREGIDWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMYdNHLGKSPNFQKPrpdK 574
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKP---K 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 575 KRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENY---IGSDSA---SEHKIGGKEKRKk 648
Cdd:cd14932 474 KLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdriVGLDKVagmGESLHGAFKTRK- 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 649 aASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKR 728
Cdd:cd14932 553 -GMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1591544934 729 RYRILNPHAIPDDtFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14932 632 RYEILTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 699.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVAAlgetpAKKGQGPATKTgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVAS-----SHKGKKDTSIT-GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELL-DMLLVSSNpyDYHFCSQGVTTVENLDDGQELMATD 337
Cdd:cd14921 155 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 338 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVK 417
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 418 GQNVEQVTYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHH 496
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKALdKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 497 MFILEQEEYKREGIDWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMYDNHlGKSPNFQKPrpd 573
Cdd:cd14921 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKP--- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 574 KKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENY---IGSDS---ASEHKIGGKEKRK 647
Cdd:cd14921 469 KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdriVGLDQmakMTESSLPSASKTK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 648 KAAsFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFK 727
Cdd:cd14921 549 KGM-FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1591544934 728 RRYRILNPHAIPDDtFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14921 628 QRYEILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-774 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 683.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVAALGETpaKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKT--KKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVsSNPYDYHFCSQGVTTVENLDDGQELMATDH 338
Cdd:cd15896 159 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLL-ENYNNYRFLSNGNVTIPGQQDKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 419 QNVEQVTYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHM 497
Cdd:cd15896 318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALdKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 498 FILEQEEYKREGIDWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMYDNHlGKSPNFQKPrpdK 574
Cdd:cd15896 398 FILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKP---K 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 575 KRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENY---IGSDS-ASEHKIGGKEKRKKAA 650
Cdd:cd15896 474 KLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVdriVGLDKvSGMSEMPGAFKTRKGM 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 651 sFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRY 730
Cdd:cd15896 554 -FRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1591544934 731 RILNPHAIPDDtFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd15896 633 EILTPNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 681.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVAALGETPAKKGqgpatkTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPG------VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYdYHFCSQGVTTvenlDDGQE---LMA 335
Cdd:cd14930 155 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSS----SPGQErelFQE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 336 TDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 415
Cdd:cd14930 230 TLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 416 VKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSlPRQ--YFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFF 493
Cdd:cd14930 310 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRS-PRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 494 NHHMFILEQEEYKREGIDWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMYDNHlGKSPNFQKP 570
Cdd:cd14930 389 NHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 571 RpdkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLY---ENYIGSDSASEHKIGGKEKRK 647
Cdd:cd14930 468 R---HLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRP 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 648 KAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFK 727
Cdd:cd14930 545 RRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFR 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1591544934 728 RRYRILNPHAIPDDtFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14930 625 QRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-774 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 681.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVAAlgETPAKKGQgpatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVAS--SHKSKKDQ-------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsnPYD-YHFCSQGVTTVENLDDGQELMATD 337
Cdd:cd14919 152 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLE--PYNkYRFLSNGHVTIPGQQDKDMFQETM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 338 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVK 417
Cdd:cd14919 230 EAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 418 GQNVEQVTYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHH 496
Cdd:cd14919 310 AQTKEQADFAIEALAKATYERMFRWLVLRINKALdKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 497 MFILEQEEYKREGIDWTFIDFGLDLQACIDLIEKPL---GIMSILEEECMFPKATDNSFKAKMYDNHlGKSPNFQKPrpd 573
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKP--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 574 KKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENY---IGSDSA---SEHKIGGKEKRK 647
Cdd:cd14919 466 KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriIGLDQVagmSETALPGAFKTR 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 648 KAAsFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFK 727
Cdd:cd14919 546 KGM-FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFR 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1591544934 728 RRYRILNPHAIPDDtFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14919 625 QRYEILTPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-774 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 679.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 100 SVLYNLRRRYA-AWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVaalgetpakkgQGPATKTGGTlEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATV-----------GGSSSGETQV-EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQK-KPELLDMLLVSSNpyDYHFCSQG-VTTVENLDDGQELMAT 336
Cdd:cd01380 150 NYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKELHLGSAE--DFFYTNQGgSPVIDGVDDAAEFEET 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 337 DHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVV 416
Cdd:cd01380 228 RKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 417 KGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLP--RQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFN 494
Cdd:cd01380 308 KPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 495 HHMFILEQEEYKREGIDWTFIDFgLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHLGK-SPNFQKPRPD 573
Cdd:cd01380 388 QHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 574 KKRkyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNkllaclyenyigsdsasehkiggkekRKKaasfq 653
Cdd:cd01380 467 NTA-----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN--------------------------RKK----- 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 654 TVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRIL 733
Cdd:cd01380 511 TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVL 590
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1591544934 734 NPHAipDDTFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd01380 591 LPSK--EWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-774 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 650.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 100 SVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 180 SGAGKTVNTKRVIQYFAIVAalgetpakkgqGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVS-----------GGSESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVENLDDGQELMATDHA 339
Cdd:cd01378 151 GEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 340 MDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADgTESADKASYLMGVSSADLIKGLLHPRVKVGNEY---VV 416
Cdd:cd01378 231 MKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 417 KGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQ-YFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFfnh 495
Cdd:cd01378 310 VPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQI--- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 496 hmFIL-----EQEEYKREGIDWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFP-KATDNSFKAKMydNHLGKSPNFQ 568
Cdd:cd01378 387 --FIEltlkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL--NQLFSNHPHF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 569 KPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDSasehkiggkEKRKK 648
Cdd:cd01378 462 ECPSGHFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDS---------KKRPP 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 649 AASFQTvsqlhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKR 728
Cdd:cd01378 533 TAGTKF-----KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLE 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1591544934 729 RYRILNPHAIPDDTFvDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd01378 608 RYKLLSPKTWPAWDG-TWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-774 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 648.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVAalgetpakkGQgpatktGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAIS---------GQ------HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVsSNPYDYHFCSQG-VTTVENLDDGQELMATD 337
Cdd:cd01381 146 NGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLEL-GDASDYYYLTQGnCLTCEGRDDAAEFADIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 338 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQRE--EQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 415
Cdd:cd01381 225 SAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 416 VKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYF---IGVLDIAGFEIFELNSFEQLCINFTNEKLQQF 492
Cdd:cd01381 305 VSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 493 FNHHMFILEQEEYKREGIDWTFIDFgLDLQACIDLI-EKPLGIMSILEEECMFPKATDNSFKAKMYDNHlGKSPNFQKPr 571
Cdd:cd01381 385 FVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 572 pdkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSdsasehkigGKEKRKKAas 651
Cdd:cd01381 462 ---KSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISM---------GSETRKKS-- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 652 fQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYR 731
Cdd:cd01381 528 -PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYR 606
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1591544934 732 ILNPhAIPDDTFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd01381 607 VLVP-GIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-774 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 624.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 100 SVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 180 SGAGKTVNTKRVIQYFAIVaalgetpakkgqgpaTKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAV---------------TNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDAS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS--QKKPELLDMLLVSSnPYDYHFCSQ-GVTTVENLDDGQELMAT 336
Cdd:cd14883 147 GHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAgaKHSKELKEKLKLGE-PEDYHYLNQsGCIRIDNINDKKDFDHL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 337 DHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAE-ADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 415
Cdd:cd14883 226 RLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 416 VKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNH 495
Cdd:cd14883 306 EIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 496 HMFILEQEEYKREGIDWTFIDFGlDLQACIDLIEK-PLGIMSILEEECMFPKATDNSFKAKMYDNHlGKSPNFQKPrpdK 574
Cdd:cd14883 386 YVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKP---D 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 575 KRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLA--CLYENYIGSDSASEHKIGGKEKRKKAASF 652
Cdd:cd14883 461 RRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKelFTYPDLLALTGLSISLGGDTTSRGTSKGK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 653 QTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRI 732
Cdd:cd14883 541 PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLC 620
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1591544934 733 LNPHAIPDDTfVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14883 621 LDPRARSADH-KETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-774 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 620.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 100 SVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYkGKRRSEaPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY-RQKLLD-SPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 180 SGAGKTVNTKRVIQYfaiVAALGetpakkgqgpatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd01383 80 SGAGKTETAKIAMQY---LAALG------------GGSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQ-GVTTVENLDDGQELMATDH 338
Cdd:cd01383 145 GKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQsNCLTIDGVDDAKKFHELKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 339 AMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKG 418
Cdd:cd01383 224 ALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 419 QNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTS-LPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHM 497
Cdd:cd01383 304 LTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGkRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 498 FILEQEEYKREGIDWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMyDNHLGKSPNFQKPRpdkkr 576
Cdd:cd01383 384 FKLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER----- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 577 kyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDSASE--HKIGGKEKRKkaasfQT 654
Cdd:cd01383 457 --GGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASRKALplTKASGSDSQK-----QS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 655 VSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILN 734
Cdd:cd01383 530 VATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLL 609
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1591544934 735 PHAIPDDTfvDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd01383 610 PEDVSASQ--DPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-774 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 580.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 178 GESGAGKTVNTKRVIQYFAIVAalgetpakkgqGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG-----------GRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQGVT-TVENLDDGQELMAT 336
Cdd:cd01384 150 DAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLK-DPKQFHYLNQSKCfELDGVDDAEEYRAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 337 DHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKqkqreEQAEADGTESADKASY--------LMGVSSADLIKGLLHPRV 408
Cdd:cd01384 229 RRAMDVVGISEEEQDAIFRVVAAILHLGNIEFS-----KGEEDDSSVPKDEKSEfhlkaaaeLLMCDEKALEDALCKRVI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 409 KVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEK 488
Cdd:cd01384 304 VTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 489 LQQFFNHHMFILEQEEYKREGIDWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNhLGKSPNF 567
Cdd:cd01384 384 LQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 568 QKPrpdkKRKYEAhFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDSasehkiggkekrK 647
Cdd:cd01384 462 SKP----KLSRTD-FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGT------------S 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 648 KAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFK 727
Cdd:cd01384 525 SSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1591544934 728 RRYRILNPHAipDDTFVDSRKAVEKLLASLDIDhsQYRFGHTKVFFK 774
Cdd:cd01384 605 DRFGLLAPEV--LKGSDDEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-774 |
5.51e-174 |
|
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: 543.98 E-value: 5.51e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVAalGETpakkgqgpatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVA--GST-------------NGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnpyDYHFCSQ-GVTTVENLDDGQELMATD 337
Cdd:cd14872 146 RGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSA---AYGYLSLsGCIEVEGVDDVADFEEVV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 338 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASY---LMGVSSADLIKGLLHPRVKvgney 414
Cdd:cd14872 223 LAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLME----- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 415 vVKGQNV-------EQVTYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTN 486
Cdd:cd14872 298 -IKGCDPtripltpAQATDACDALAKAAYSRLFDWLVKKINESMrPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 487 EKLQQFFNHHMFILEQEEYKREGIDWTFIDFgLDLQACIDLIEK-PLGIMSILEEECMFPKATDNSFKAKMYDNHLGKSp 565
Cdd:cd14872 377 EKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 566 NFQkprPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDSASEHKIGGKEK 645
Cdd:cd14872 455 TFV---YAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGDQKTSKVTLGGQFR 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 646 RKkaasfqtvsqlhkenLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAE 725
Cdd:cd14872 532 KQ---------------LSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHER 596
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1591544934 726 FKRRYRILnPHAIPDDTFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14872 597 FLKRYRFL-VKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-774 |
6.25e-173 |
|
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: 541.07 E-value: 6.25e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 178 GESGAGKTVNTKRVIQYfaIVAALGETpakkgqgpatktGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd01382 81 GESGAGKTESTKYILRY--LTESWGSG------------AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLvssnpydyhfcsqgvtTVENLDDGQELMATD 337
Cdd:cd01382 147 EKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 338 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREE----QAEADGTESADKASYLMGVSSADLIKGLLHpRVKVGNE 413
Cdd:cd01382 211 KAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSgggcNVKPKSEQSLEYAAELLGLDQDELRVSLTT-RVMQTTR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 414 YVVKGQ------NVEQVTYAVGALAKATYDRMFKWLVGRINRtlytSLPRQ---YFIGVLDIAGFEIFELNSFEQLCINF 484
Cdd:cd01382 290 GGAKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQ----CIPFEtssYFIGVLDIAGFEYFEVNSFEQFCINY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 485 TNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNHLgK 563
Cdd:cd01382 366 CNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK-N 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 564 SPNFQKPRPDKKRKY------EAhFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDSase 637
Cdd:cd01382 444 HFRLSIPRKSKLKIHrnlrddEG-FLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNK--- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 638 hkiGGKEKRKKaASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGF 717
Cdd:cd01382 520 ---DSKQKAGK-LSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGF 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1591544934 718 PNRILYAEFKRRYRILNPHAIPDdtfVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd01382 596 PSRTSFHDLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-774 |
5.54e-167 |
|
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: 525.50 E-value: 5.54e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 178 GESGAGKTVNTKRVIQYFAIVAAlgetpakkGQGPATKTggtledQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG--------GLNDSTIK------KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDmLLVSSNPYDYHFcSQGVTTVENLDDGQELMATD 337
Cdd:cd14903 147 KNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERL-FLDSANECAYTG-ANKTIKIEGMSDRKHFARTK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 338 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAE--ADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 415
Cdd:cd14903 225 EALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 416 VKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNH 495
Cdd:cd14903 305 TVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 496 HMFILEQEEYKREGIDWTFIDFgLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHLGKSPNFQKPRPDKk 575
Cdd:cd14903 385 DVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSR- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 576 rkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDSA--SEHKIGGKEKRKKAASFQ 653
Cdd:cd14903 463 ----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAasTSLARGARRRRGGALTTT 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 654 TVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRIL 733
Cdd:cd14903 539 TVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF 618
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1591544934 734 NPHAipDDTFVDSRKAVEKLLASLDIDH-SQYRFGHTKVFFK 774
Cdd:cd14903 619 LPEG--RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-774 |
4.04e-166 |
|
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: 523.18 E-value: 4.04e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLR----NRENQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 174 MLITGESGAGKTVNTKRVIQYFAIVAAlGETPAKKGQGPAT-----KTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITS-GFAQGASGEGEAAseaieQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 249 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQGVTTVENLD 328
Cdd:cd14890 160 GKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQ-TPVEYFYLRGECSSIPSCD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 329 DGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGT-ESADKASYLMGVSSADLIKGLLHPR 407
Cdd:cd14890 239 DAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTlQSLKLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 408 VKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNE 487
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 488 KLQQFFNHHMFILEQEEYKREGIDWTFIDFGlDLQACIDLIE-KPLGIMSIL------------EEECMFPKATDNSFKA 554
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFitlddcwrfkgeEANKKFVSQLHASFGR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 555 KMYDNHLGKS----PNFQKPRPDKKRkyeaHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLlaclyenyi 630
Cdd:cd14890 478 KSGSGGTRRGssqhPHFVHPKFDADK----QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSI--------- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 631 gsdsasehkiggkekRKKAASFQTVSQLHkenlnKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGI 710
Cdd:cd14890 545 ---------------REVSVGAQFRTQLQ-----ELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAI 604
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1591544934 711 RICRKGFPNRILYAEFKRRYRILNPHAipddtfvDSRKAVEKLLAS-LDIDHSQYRFGHTKVFFK 774
Cdd:cd14890 605 QIRQQGFALREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKmLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-774 |
5.92e-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: 516.06 E-value: 5.92e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 100 SVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 180 SGAGKTVNTKRVIQYfaiVAALGETPAKkgqgpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd01379 82 SGAGKTESANLLVQQ---LTVLGKANNR-----------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIM----SQKKpeLLDMLLVSSNPYDY-HFCSQGVTTVENLDDGQE-L 333
Cdd:cd01379 148 GAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYaglaEDKK--LAKYKLPENKPPRYlQNDGLTVQDIVNNSGNREkF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 334 MATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQ----AEADGTESADKASYLMGVSSADLIKGLLHPRVK 409
Cdd:cd01379 226 EEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 410 VGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLY---TSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTN 486
Cdd:cd01379 306 TRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKpdrSASDEPLSIGILDIFGFENFQKNSFEQLCINIAN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 487 EKLQQFFNHHMFILEQEEYKREGIDWTFIDFG-----LDLqacidLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHl 561
Cdd:cd01379 386 EQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEdnrplLDM-----FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI- 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 562 gKSPNFQKPRPDkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLAclyenyigsdsasehkig 641
Cdd:cd01379 460 -KSKYYWRPKSN-----ALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 642 gkekrkkaasfQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRI 721
Cdd:cd01379 516 -----------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRI 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1591544934 722 LYAEFKRRYRILNPHAipDDTFVDSRKAVEKLLASLDIDHsqYRFGHTKVFFK 774
Cdd:cd01379 585 LFADFLKRYYFLAFKW--NEEVVANRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-774 |
1.48e-163 |
|
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: 516.55 E-value: 1.48e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSeAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSIS-KSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 178 GESGAGKTVNTKRVIQYFAIVAALGEtpakkgqgpatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF- 256
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDI-----------KKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFs 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 257 --------GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS-----------------------QKKPELLDML 305
Cdd:cd14888 149 klkskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 306 LVSS-NPYDYHFCSqGVTTVENLDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQA---EADG 381
Cdd:cd14888 229 SFEPhLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASC 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 382 TESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQYF 460
Cdd:cd14888 308 TDDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIgYSKDNSLLF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 461 IGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGlDLQACIDLI-EKPLGIMSILE 539
Cdd:cd14888 388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLD 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 540 EECMFPKATDNSFKAKMYDNHLGKSpnfqkpRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSN 619
Cdd:cd14888 467 EECFVPGGKDQGLCNKLCQKHKGHK------RFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKN 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 620 KLLACLYENYIGSdsaseHKIGGKEKRKkaasFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLH 699
Cdd:cd14888 541 PFISNLFSAYLRR-----GTDGNTKKKK----FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNE 611
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1591544934 700 QLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPhaipddtfvdsrkavekllASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14888 612 QLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN-------------------GEGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-772 |
8.33e-163 |
|
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: 513.95 E-value: 8.33e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAY------KGKRRSEAPPHIYSIADNAYNDMLRNRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 171 --NQSMLITGESGAGKTVNTKRVIQYFAIVAAlgetpaKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS------ATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 249 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKP-ELLDMLLVSSNPYDYHFCSQGVTTVENL 327
Cdd:cd14901 155 GKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSdELHALGLTHVEEYKYLNSSQCYDRRDGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 328 DDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTES-ADKASYLMGVSSADLIKGLLHP 406
Cdd:cd14901 235 DDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLAnVRAACDLLGLDMDVLEKTLCTR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 407 RVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTL-YTSLPRQY-FIGVLDIAGFEIFELNSFEQLCINF 484
Cdd:cd14901 315 EIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaYSESTGASrFIGIVDIFGFEIFATNSLEQLCINF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 485 TNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNhLGK 563
Cdd:cd14901 395 ANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 564 SPNFQKprpDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLAclyenyigsdsasehkiggk 643
Cdd:cd14901 473 HASFSV---SKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS-------------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 644 ekrkkaasfQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILY 723
Cdd:cd14901 530 ---------STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPH 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1591544934 724 AEFKRRYRILNPHAIPDDTFVDSRKAVEKLLASLDI----DHSQYRFGHTKVF 772
Cdd:cd14901 601 DAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSElnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-774 |
9.96e-163 |
|
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: 515.00 E-value: 9.96e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYfaiVAALgetpAKKGQGPATktggtlEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01385 81 ESGSGKTESTNFLLHH---LTAL----SQKGYGSGV------EQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSqKKPELLDMLLVSSNPYDYHFCSQGVT-TVENLDDGQELMATD 337
Cdd:cd01385 148 NGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLA-GASEEERKELHLKQPEDYHYLNQSDCyTLEGEDEKYEFERLK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 338 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQK--QREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 415
Cdd:cd01385 227 QAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 416 VKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTL----YTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQ 491
Cdd:cd01385 307 ILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 492 FFNHHMFILEQEEYKREGIDWTFIDFgLDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKmYDNHLGKSPNFQKP 570
Cdd:cd01385 387 YFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 571 rpdkkRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLaclyENYIGSDSASEH------------ 638
Cdd:cd01385 465 -----QVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFV----RELIGIDPVAVFrwavlraffram 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 639 ---KIGGKEKRKKAASFQTVSQ---------LHKE------------NLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDA 694
Cdd:cd01385 536 aafREAGRRRAQRTAGHSLTLHdrttksllhLHKKkkppsvsaqfqtSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDD 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 695 FLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPHAIpddtfVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd01385 616 ELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGL-----ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-774 |
1.29e-159 |
|
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: 505.44 E-value: 1.29e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVAALGETPakkgqgpatktggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNL--------------VTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-E 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS------QKKPELLDmllvssnPYDYHFCSQGVTT-VENLDDGQ 331
Cdd:cd01387 146 GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAglpaqlRQKYGLQE-------AEKYFYLNQGGNCeIAGKSDAD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 332 ELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQRE---EQAEADGTESADKASYLMGVSSADLIKGLLHPRV 408
Cdd:cd01387 219 DFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 409 KVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEK 488
Cdd:cd01387 299 ETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANEN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 489 LQQFFNHHMFILEQEEYKREGIDWTFIDFgLDLQACIDLI-EKPLGIMSILEEECMFPKATDNSFKAKMYDNHlGKSPNF 567
Cdd:cd01387 379 LQYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELY 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 568 QKPRPDkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIG-SDSASEHKIGGKEKR 646
Cdd:cd01387 457 SKPRMP-----LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAqTDKAPPRLGKGRFVT 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 647 KKAASfQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEF 726
Cdd:cd01387 532 MKPRT-PTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVF 610
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1591544934 727 KRRYRILNPHAIPDDTFVDSRKAVEKLLASLDIDhSQYRFGHTKVFFK 774
Cdd:cd01387 611 IDRYRCLVALKLPRPAPGDMCVSLLSRLCTVTPK-DMYRLGATKVFLR 657
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
854-1931 |
2.61e-157 |
|
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: 513.57 E-value: 2.61e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 854 EKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEIMER 933
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 934 LEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALQEAHQQ 1013
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1014 TLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSMESVMDLENDKQQLEEKLKKKDF 1093
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1094 EMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRGDVARELEELSERLEESGGATSAQIEINK 1173
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1174 KRETDILKLRRDLEEAMLHHEATTAGLRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKASA 1253
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1254 EKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQNVEELKKQLEEENKA 1333
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1334 KNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTKYETDAiQRTEELEESKKKLAVRLQEAEEAVE 1413
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1414 ASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELFKLK 1493
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1494 NSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLEL 1573
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1574 NQIKADVDRKLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLRKKMEGDLNEMEVQLNHANRLASESQKLLRN 1653
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1654 LQVQIKDVQLELDETIHQNEELKEQVAVTERRNNLLASEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTSLIN 1733
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1734 QKKKLENDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIAL 1813
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1814 KGGKKQVQKLEARVKELENELESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKRQAEEA 1893
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 1591544934 1894 EDQANTNLSKYRKLQHELDDAEERADMAETQVTKLRVR 1931
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-774 |
4.49e-157 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 498.17 E-value: 4.49e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 178 GESGAGKTVNTKRVIQYfaiVAALGETPAKKGQGPATKTggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14873 81 GESGAGKTESTKLILKF---LSVISQQSLELSLKEKTSC---VEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNIC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQ-GVTTVENLDDGQELMAT 336
Cdd:cd14873 155 QKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLST-PENYHYLNQsGCVEDKTISDQESFREV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 337 DHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFkqkqreeqAEADGTESADK-----ASYLMGVSSADLIKGLLHPRVKVG 411
Cdd:cd14873 234 ITAMEVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 412 NEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSlPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQ 491
Cdd:cd14873 306 GEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGK-EDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 492 FFNHHMFILEQEEYKREGIDWTFIDFgLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHlGKSPNFQKPR 571
Cdd:cd14873 385 YFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 572 PDkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYigSDSASEHKIGGKEKRKKAas 651
Cdd:cd14873 463 VA-----VNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHV--SSRNNQDTLKCGSKHRRP-- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 652 fqTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYR 731
Cdd:cd14873 534 --TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYK 611
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1591544934 732 ILNPHAIPDDtfvDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14873 612 VLMRNLALPE---DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-774 |
3.56e-155 |
|
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: 493.12 E-value: 3.56e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKG--KRRSEAPPHIYSIADNAYNDMLRNR----EN 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 172 QSMLITGESGAGKTVNTKRVIQYFAIVAALGETPAKKGQgpATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKF 251
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKG--AANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 252 IRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKpELLDMLLVSSNPYDYHFCSQG-VTTVENLDDG 330
Cdd:cd14892 159 IQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGnCVEVDGVDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 331 QELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQ--KQREEQAEADGTESADKASYLMGVSSADLIKGLLhPRV 408
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLV-TQT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 409 KVGNeyvvKGQNVE------QVTYAVGALAKATYDRMFKWLVGRINR----------TLYTSLPRQYFIGVLDIAGFEIF 472
Cdd:cd14892 317 TSTA----RGSVLEikltarEAKNALDALCKYLYGELFDWLISRINAchkqqtsgvtGGAASPTFSPFIGILDIFGFEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 473 ELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGlDLQACIDLIEK-PLGIMSILEEECMFP-KATDN 550
Cdd:cd14892 393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 551 SFKAKMYDNHLGKSPNFQKPRPDKKrkyeaHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNkllaclyenyi 630
Cdd:cd14892 472 QLLTIYHQTHLDKHPHYAKPRFECD-----EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK----------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 631 gsdsasehkiggkekrkkaasFQTvsqlhkeNLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGI 710
Cdd:cd14892 536 ---------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVV 587
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1591544934 711 RICRKGFPNRILYAEFKRRYRIL---------NPHAIPDDTfvdSRKAVEKLLASLdIDHSQYRFGHTKVFFK 774
Cdd:cd14892 588 RIRREGFPIRRQFEEFYEKFWPLarnkagvaaSPDACDATT---ARKKCEEIVARA-LERENFQLGRTKVFLR 656
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-774 |
3.96e-145 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 464.55 E-value: 3.96e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKR-RSEAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 178 GESGAGKTVNTKRVIQYFAIVaalgeTPAKKGQgpatktggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKL-----SPSDDSD---------LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVsSNPYDYHFCSQGVTTVENLDDGQEL---- 333
Cdd:cd14897 147 ENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELeyyr 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 334 -MATDHA--MDILGFLPDEKYGCYKIVGAIMHFGNMKFkqkqrEEQAEADGTESADK-----ASYLMGVSSADLIKGLLH 405
Cdd:cd14897 226 qMFHDLTniMKLIGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALIS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 406 PRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYF-----IGVLDIAGFEIFELNSFEQL 480
Cdd:cd14897 301 NVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 481 CINFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGlDLQACIDLI-EKPLGIMSILEEECMFPKATDNSFKAKMyDN 559
Cdd:cd14897 381 CINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 560 HLGKSPNFQKPRPDKkrkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIgsdsasehk 639
Cdd:cd14897 459 YCGESPRYVASPGNR-----VAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSYF--------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 640 iggkekrkkaasfqtvsqlhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPN 719
Cdd:cd14897 525 --------------------KRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPI 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1591544934 720 RILYAEFKRRYRILNPHaiPDDTFVDSRKAVEKLLASLDIdhSQYRFGHTKVFFK 774
Cdd:cd14897 585 RIKYEDFVKRYKEICDF--SNKVRSDDLGKCQKILKTAGI--KGYQFGKTKVFLK 635
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-737 |
3.34e-141 |
|
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: 453.61 E-value: 3.34e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 100 SVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLP------------VYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLR 167
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPglyssdtmakylLSFEARSSSTRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 168 NR----ENQSMLITGESGAGKTVNTKRVIQYFAIVAAlgetPAKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRND 243
Cdd:cd14900 82 GLngvmSDQSILVSGESGSGKTESTKFLMEYLAQAGD----NNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRND 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 244 NSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLdmllvSSNPYdyhfcsqgvtt 323
Cdd:cd14900 158 NSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAAR-----KRDMY----------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 324 venlddgQELMAtdhAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTE-------SADKASYLMGVSS 396
Cdd:cd14900 222 -------RRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDlapssiwSRDAAATLLSVDA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 397 ADLIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTL-----YTSLPRQYFIGVLDIAGFEI 471
Cdd:cd14900 292 TKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 472 FELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGlDLQACIDLI-EKPLGIMSILEEECMFPKATDN 550
Cdd:cd14900 372 FPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECVMPKGSDT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 551 SFKAKMYdNHLGKSPNFQKPRPDKKRkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKssnkllaclyenyi 630
Cdd:cd14900 451 TLASKLY-RACGSHPRFSASRIQRAR---GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVY-------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 631 gsdsasehkiGGKekrkkaasfqtvsqlHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGI 710
Cdd:cd14900 513 ----------GLQ---------------FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAV 567
|
650 660 670
....*....|....*....|....*....|.
gi 1591544934 711 RICRKGFPNRILYAEFKRRYRIL----NPHA 737
Cdd:cd14900 568 RVARAGFPIRLLHDEFVARYFSLarakNRLL 598
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-774 |
3.35e-138 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 446.03 E-value: 3.35e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAA--WMIYTYSGLFCVTVNPYKWLPvytAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRE---NQS 173
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 174 MLITGESGAGKTVNTKRVIQYFAIVAALG----ETPAKKGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFG 249
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGkkasGQDIEQSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 250 KFIRIHFGPTG-KLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQ-GVTTVENL 327
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLS-PEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 328 DDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKA----SYLMGVSSADLIKGL 403
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEAlataAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 404 LHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTL---YTSLPrqyFIGVLDIAGFEIFEL-NSFEQ 479
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLghdPDPLP---YIGVLDIFGFESFETkNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 480 LCINFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGlDLQACIDLI-EKPLGIMSILEEECMFPKATDNSFKAKMYD 558
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 559 NHlGKSPNFqkPRPDKKRKYEAhFELVHYAGVVPYNIIGWLDKNKDPLNETvvacfqkssnkllaclYENYIgsdsaseh 638
Cdd:cd14891 473 TH-KRHPCF--PRPHPKDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPED----------------FEDLL-------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 639 kiggkekrKKAASFQTVSQlhkenlnKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFP 718
Cdd:cd14891 525 --------ASSAKFSDQMQ-------ELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLP 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 719 NRILYAEFKRRYRILNPHAI------PDDTFvdsrkaVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14891 590 TRVTYAELVDVYKPVLPPSVtrlfaeNDRTL------TQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-774 |
1.20e-137 |
|
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: 445.24 E-value: 1.20e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGK--------RRSEAPPHIYSIADNAYNDMLRNR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 170 ENQSMLITGESGAGKTVNTKRVIQYFAIVAALGETPAKKGQGP-----ATKTGGTLEDQIIEANPAMEAFGNAKTLRNDN 244
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTssiraTSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 245 SSRFGKFIRIHFG-PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYD-YHFCSQGV 321
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDrYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 322 T-TVENLDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQ--REEQAEADGTESADKASYLMGVSSAD 398
Cdd:cd14907 241 CyEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 399 LIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTL--YTSLPRQYF------IGVLDIAGFE 470
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpKDEKDQQLFqnkylsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 471 IFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIDWTF--IDFgLDLQACIDLIEK-PLGIMSILEEECMFPKA 547
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 548 TDNSFKAKMYDNHlGKSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYE 627
Cdd:cd14907 480 TDEKLLNKIKKQH-KNNSKLIFPNKINKDT----FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFS 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 628 NYIGSDSASEHKIGGKEKRKKaasfqTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVL 707
Cdd:cd14907 555 GEDGSQQQNQSKQKKSQKKDK-----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVL 629
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1591544934 708 EGIRICRKGFPNRILYAEFKRRYRILNphaipddtfvdsrkavekllasldidhSQYRFGHTKVFFK 774
Cdd:cd14907 630 ESIRVRKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-774 |
5.96e-137 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 442.81 E-value: 5.96e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 101 VLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDML----RNRENQSMLI 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 177 TGESGAGKTVNTKRVIQYFAIVAalgetpakkgqgpatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC---------------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 257 gPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI---MSQKKPELLDMLlvssNPYDYHFCSQGVTTVENLDD-GQE 332
Cdd:cd14889 148 -RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLL----DPGKYRYLNNGAGCKREVQYwKKK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 333 LMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREE-QAEADGTESADKASYLMGVSSADLIKGLLHPRVKVG 411
Cdd:cd14889 223 YDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 412 NEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLytsLPRQYF------IGVLDIAGFEIFELNSFEQLCINFT 485
Cdd:cd14889 303 GEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL---APKDDSsvelreIGILDIFGFENFAVNRFEQACINLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 486 NEKLQQFFNHHMFILEQEEYKREGIDWTFIDFgLDLQACIDL-IEKPLGIMSILEEECMFPKATDNSFKAKMyDNHLGKS 564
Cdd:cd14889 380 NEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 565 PNFQKPRpDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSD----------S 634
Cdd:cd14889 458 SYYGKSR-SKSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTgtlmpraklpQ 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 635 ASEHKIGGKEKRKKAASFqtvsqlhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICR 714
Cdd:cd14889 533 AGSDNFNSTRKQSVGAQF-------KHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRR 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 715 KGFPNRILYAEFKRRYRIL--NPhAIPDDtfvdsRKAVEKLLASLDIdhSQYRFGHTKVFFK 774
Cdd:cd14889 606 EGFSWRPSFAEFAERYKILlcEP-ALPGT-----KQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-726 |
7.11e-134 |
|
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: 436.25 E-value: 7.11e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYK--------GKRRSEAPPHIYSIADNAYNDMLRN- 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 169 RENQSMLITGESGAGKTVNTKRVIQYFAIVaalGETPAKKGQGPATKTggTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSV---GRDQSSTEQEGSDAV--EIGKRILQTNPILESFGNAQTIRNDNSSRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 249 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYDYH---FCSQGVTTV 324
Cdd:cd14902 156 GKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLgLQKGGKYELLnsyGPSFARKRA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 325 ENLDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESA---DKASYLMGVSSADLIK 401
Cdd:cd14902 236 VADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLET 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 402 GLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTL-------YTSLPRQYF--IGVLDIAGFEIF 472
Cdd:cd14902 316 LLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEInyfdsavSISDEDEELatIGILDIFGFESL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 473 ELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFPKATDNS 551
Cdd:cd14902 396 NRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGSNQA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 552 FKAKMYDNHLGkspnfqkprpdkkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLAclyenYIG 631
Cdd:cd14902 475 LSTKFYRYHGG----------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVV-----AIG 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 632 SDS--ASEHKIGGKEKRKKAASFQT--VSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVL 707
Cdd:cd14902 534 ADEnrDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVL 613
|
650
....*....|....*....
gi 1591544934 708 EGIRICRKGFPNRILYAEF 726
Cdd:cd14902 614 EAVRIARHGYSVRLAHASF 632
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-774 |
1.03e-132 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 430.90 E-value: 1.03e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 178 GESGAGKTVNTKRVIQYFAIVAAlgetpakkgqGPATKTggtlEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG----------GRKDKT----IAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNpYDYHFCSQGV--TTVENLDDGQELMA 335
Cdd:cd14904 147 GRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPN-CQYQYLGDSLaqMQIPGLDDAKLFAS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 336 TDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGtESADKASYLMGVSSADLIKGLLHPRVKVGNEYV 415
Cdd:cd14904 226 TQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNG-SQLSQVAKMLGLPTTRIEEALCNRSVVTRNESV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 416 VKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQY-FIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFN 494
Cdd:cd14904 305 TVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 495 HHMFILEQEEYKREGIDWTFIDFGlDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNH--LGKSPNFQKPRP 572
Cdd:cd14904 385 TDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 573 DKkrkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYenyiGSDSASEHKIGGKEKRKKAASF 652
Cdd:cd14904 464 KR-----TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF----GSSEAPSETKEGKSGKGTKAPK 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 653 QTVSQLhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRI 732
Cdd:cd14904 535 SLGSQF-KTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAI 613
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1591544934 733 LNPHAIPDDtfvDSRKAVEKLLASLDIDHS-QYRFGHTKVFFK 774
Cdd:cd14904 614 MFPPSMHSK---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
61-827 |
1.10e-127 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 422.52 E-value: 1.10e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 61 VETKDGRTLTVKDCDI----QQMNPPKYDmieDMAMLTHLNEASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTA 136
Cdd:PTZ00014 71 IDPPTNSTFEVKPEHAfnanSQIDPMTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 137 PVVAAYKGKRRSEA-PPHIYSIADNAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAivaalgetPAKKGQgpatk 215
Cdd:PTZ00014 148 DWIRRYRDAKDSDKlPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA--------SSKSGN----- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 216 TGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS 295
Cdd:PTZ00014 215 MDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 296 QKKPELLDML-LVSSNpyDYHFCSQGVTTVENLDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQRE 374
Cdd:PTZ00014 295 GANDEMKEKYkLKSLE--EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEG 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 375 EQAEA-----DGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINR 449
Cdd:PTZ00014 373 GLTDAaaisdESLEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 450 TLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGLDLQACIDLIE 529
Cdd:PTZ00014 453 TIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCG 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 530 KPLGIMSILEEECMFPKATDNSFKAKMYdNHLGKSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNET 609
Cdd:PTZ00014 533 KGKSVLSILEDQCLAPGGTDEKFVSSCN-TNLKNNPKYKPAKVDSNKN----FVIKHTIGDIQYCASGFLFKNKDVLRPE 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 610 VVACFQKSSNKLLACLYENyigsDSASEHKIGgkekRKKAASFQTVSQlhkenLNKLMTNLRSTQPHFVRCIIPNETKTP 689
Cdd:PTZ00014 608 LVEVVKASPNPLVRDLFEG----VEVEKGKLA----KGQLIGSQFLNQ-----LDSLMSLINSTEPHFIRCIKPNENKKP 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 690 GIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNpHAIPDDTFVDSRKAVEKLLASLDIDHSQYRFGHT 769
Cdd:PTZ00014 675 LDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD-LAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKT 753
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 770 KVFFKAGLLGHLEELRDERLAK---VLTLLQAAargkIMRMELLRMMERR-DALMIIQWNIR 827
Cdd:PTZ00014 754 MVFLKKDAAKELTQIQREKLAAwepLVSVLEAL----ILKIKKKRKVRKNiKSLVRIQAHLR 811
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-735 |
8.21e-123 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 403.91 E-value: 8.21e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYK--GKRRS---EAP----PHIYSIADNAYNDMLRN- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 169 RENQSMLITGESGAGKTVNTKRVIQYFAIVAAlGETPAKKGQGPATKtgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRF 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGN-GEEGAPNEGEELGK--LSIMDRVLQSNPILEAFGNARTLRNDNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 249 GKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIM------SQKKPELLDMLLVSSN-PYDYHFCSQG- 320
Cdd:cd14908 158 GKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggdeeEHEKYEFHDGITGGLQlPNEFHYTGQGg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 321 VTTVENLDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASY---LMGVSSA 397
Cdd:cd14908 238 APDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 398 DLIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQY--FIGVLDIAGFEIFELN 475
Cdd:cd14908 318 KLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrsSVGVLDIFGFECFAHN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 476 SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFP-KATDNSFK 553
Cdd:cd14908 398 SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 554 AKMYDNHLgksPNFQKPRPDKKR-------KYEAHFELVHYAGVVPYNI-IGWLDKNKDPLNETVVACFQKssnkllacl 625
Cdd:cd14908 477 SRLYETYL---PEKNQTHSENTRfeatsiqKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLFES--------- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 626 yenyigsdsasehkiggkekrkkaasfqtvSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNG 705
Cdd:cd14908 545 ------------------------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGG 594
|
650 660 670
....*....|....*....|....*....|
gi 1591544934 706 VLEGIRICRKGFPNRILYAEFKRRYRILNP 735
Cdd:cd14908 595 VLEAVRVARSGYPVRLPHKDFFKRYRMLLP 624
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
105-774 |
2.39e-122 |
|
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: 403.56 E-value: 2.39e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 105 LRRRYAAWMIYTYSGLFCVTVNPYKWLP-VYTapvVAAYKGKRR--SEAPPHIYSIADNAYNDMLR-------NRENQSM 174
Cdd:cd14895 7 LAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEMPgwTALPPHVFSIAEGAYRSLRRrlhepgaSKKNQTI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 175 LITGESGAGKTVNTKRVIQYFAIVAALGETPAKkgqgpATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 254
Cdd:cd14895 84 LVSGESGAGKTETTKFIMNYLAESSKHTTATSS-----SKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVRM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 255 HFGP-----TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYDYHFCSQGVTTV--EN 326
Cdd:cd14895 159 FFEGheldtSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELqLELLSAQEFQYISGGQCYQrnDG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 327 LDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESA------------------DKA 388
Cdd:cd14895 239 VRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqhlDIV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 389 SYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRIN----RTLYTSLPRQY----- 459
Cdd:cd14895 319 SKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNsaspQRQFALNPNKAankdt 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 460 --FIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGLDlQACIDLIE-KPLGIMS 536
Cdd:cd14895 399 tpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEqRPSGIFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 537 ILEEECMFPKATDNSFKAKMYdNHLGKSPNFQKPRPDKKrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQK 616
Cdd:cd14895 478 LLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASRTDQA---DVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGK 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 617 SSNKLLACLYENYIGSDSAsEHKIGGKEKRKKAASFQTV---SQLhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMD 693
Cdd:cd14895 554 TSDAHLRELFEFFKASESA-ELSLGQPKLRRRSSVLSSVgigSQF-KQQLASLLDVVQQTQTHYIRCIKPNDESASDQFD 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 694 AFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILnphaipddtfVDSRKAVE----KLLASLDIDHSQyrFGHT 769
Cdd:cd14895 632 MAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLL----------VAAKNASDatasALIETLKVDHAE--LGKT 699
|
....*
gi 1591544934 770 KVFFK 774
Cdd:cd14895 700 RVFLR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-774 |
1.77e-119 |
|
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: 392.99 E-value: 1.77e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVaalgetpakkGQGPATKTGGTLEDQIieanPAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL----------YQDQTEDRLRQPEDVL----PILESFGHAKTILNANASRFGQVLRLHL-Q 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSnPYDYHFCSQG-VTTVENLDDGQELMATD 337
Cdd:cd14896 146 HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQG-PETYYYLNQGgACRLQGKEDAQDFEGLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 338 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESAD--KASYLMGVsSADLIKGLLHPRVKVGN-EY 414
Cdd:cd14896 225 KALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVSSWAEihTAARLLQV-PPERLEGAVTHRVTETPyGR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 415 VVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLytSLPRQY----FIGVLDIAGFEIFELNSFEQLCINFTNEKLQ 490
Cdd:cd14896 304 VSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWL--APPGEAesdaTIGVVDAYGFEALRVNGLEQLCINLASERLQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 491 QFFNHHMFILEQEEYKREGIDWTFIDfGLDLQACIDLI-EKPLGIMSILEEECMFPKATDNSFKAKMYDNHlGKSPNFQK 569
Cdd:cd14896 382 LFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 570 PR---PDkkrkyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENyigsdsaSEHKIGGKEKR 646
Cdd:cd14896 460 PQlplPV--------FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE-------AEPQYGLGQGK 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 647 KKAAS-FQtvsqlhkENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAE 725
Cdd:cd14896 525 PTLASrFQ-------QSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQA 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1591544934 726 FKRRYRILNPHAIPDdtFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14896 598 FLARFGALGSERQEA--LSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-731 |
1.92e-116 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 387.14 E-value: 1.92e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYK-------GKRRSEA---PPHIYSIADNAYNDMLR 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 168 NRENQSMLITGESGAGKTVNTKRVIQYFAIVAALGETPAK---KGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDN 244
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTnseSISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 245 SSRFGKFIRIHF-GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQK----KPELLDMLLVSSNPYDYHFCSQ 319
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 320 GVTTV--ENLDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQ--KQREEQAEADGTESA---------- 385
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 386 DKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQY------ 459
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 460 ---------FIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGlDLQACIDLIE- 529
Cdd:cd14899 401 vddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFEh 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 530 KPLGIMSILEEECMFPKATDNSFKAKMYDNHLGKS--PNFqkpRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLN 607
Cdd:cd14899 480 RPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNshPHF---RSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFC 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 608 ETVVACFQKSSNKLLACLYENYIGSDSASEHKIGGKEKR-----KKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCII 682
Cdd:cd14899 557 ESAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRtrrraKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIK 636
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1591544934 683 PNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYR 731
Cdd:cd14899 637 PNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-774 |
2.86e-114 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 378.18 E-value: 2.86e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKG-KRRSEAPPHIYSIADNAYNDMLRNRENQSMLIT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 178 GESGAGKTVNTKRVIQYFAivaalgetPAKKGQgpatkTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA--------SAKSGN-----MDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS------QKKPELLDM---LLVSSNPYDyhfcsqgVTTVENLD 328
Cdd:cd14876 148 SEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKgadsemKSKYHLLGLkeyKFLNPKCLD-------VPGIDDVA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 329 DGQELMATDHAMdilGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADK-----ASYLMGVSSADLIKGL 403
Cdd:cd14876 221 DFEEVLESLKSM---GLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVDDAAAISNESLevfkeACSLLFLDPEALKREL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 404 LHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCIN 483
Cdd:cd14876 298 TVKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFIN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 484 FTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKMYDNhLGK 563
Cdd:cd14876 378 ITNEMLQKNFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKS 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 564 SPNFQKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIgsdsasehkiggK 643
Cdd:cd14876 457 NGKFKPAKVDSNIN----FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVV------------V 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 644 EKRKKAASFQTVSQLHKeNLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILY 723
Cdd:cd14876 521 EKGKIAKGSLIGSQFLK-QLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPF 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1591544934 724 AEFKRRYRILNPHAIPDDTfVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14876 600 EEFLYQFKFLDLGIANDKS-LDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-774 |
2.55e-108 |
|
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: 361.13 E-value: 2.55e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRS-----EAPPHIYSIADNAYNDMLRNRENQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 173 SMLITGESGAGKTVNTKRVIQYFAIvaalgetpakkgqGPATKTGgTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFI 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAY-------------GHSTSST-DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 253 RIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYdYHFCSQG-VTTVENLDDGQ 331
Cdd:cd14886 147 KLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASkCYDAPGIDDQK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 332 ELMATDHAMDILgFLPDEKYGCYKIVGAIMHFGNMKFKQKQR---EEQAEADGTESADKASYLMGVSSADLIKGLLHPRV 408
Cdd:cd14886 226 EFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 409 KVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEK 488
Cdd:cd14886 305 VINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANER 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 489 LQQFFNHHMFILEQEEYKREGIDWTFIDFGlDLQACIDLIEKP-LGIMSILEEECMFPKATDNSF----KAKMYDNHLGK 563
Cdd:cd14886 385 LQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFtsscKSKIKNNSFIP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 564 SPNFQkprpdkkrkyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDsasehkigGK 643
Cdd:cd14886 464 GKGSQ-----------CNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNED--------GN 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 644 EKRKKAASfqtvsqLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILY 723
Cdd:cd14886 525 MKGKFLGS------TFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTF 598
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 724 AEFKRRYRILNPHA-IPDDTFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14886 599 EEFFHRNKILISHNsSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-774 |
2.58e-108 |
|
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: 362.40 E-value: 2.58e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVAALGETPAKKgqgpatktggtleDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSV-------------EKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML----LVSSNpydyhfcSQGVTTVENLDDGQ--- 331
Cdd:cd01386 148 AGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELhlnqLAESN-------SFGIVPLQKPEDKQkaa 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 332 -ELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGN---MKFKQKQREEQAEadgTESADKASYLMGVSSADLIKGLLHPR 407
Cdd:cd01386 221 aAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFAR---PEWAQRAAYLLGCTLEELSSAIFKHH 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 408 VKVGNEYVVKGQNVEQVTY------------AVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELN 475
Cdd:cd01386 298 LSGGPQQSTTSSGQESPARsssggpkltgveALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 476 ------SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGLDLQACIDLIEKPL---------------GI 534
Cdd:cd01386 378 gsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPqqalvrsdlrdedrrGL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 535 MSILEEECMFPKATDNSFKAKMYdNHLGKSPNFQKPRPDKKRKYEAHFELVHYAGV--VPYNIIGWLDKNK-DPLNETVV 611
Cdd:cd01386 458 LWLLDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHSLLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNAT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 612 ACFQKSSNKLLAclyenyigsdsasehkiggkeKRKKAASFQTvsqlhKENLNKLMTNLRSTQPHFVRCIIPN------E 685
Cdd:cd01386 537 QLLQESQKETAA---------------------VKRKSPCLQI-----KFQVDALIDTLRRTGLHFVHCLLPQhnagkdE 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 686 TKTPG------IMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPH----AIPDDTFVDSRKAVEKLLA 755
Cdd:cd01386 591 RSTSSpaagdeLLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPltkkLGLNSEVADERKAVEELLE 670
|
730
....*....|....*....
gi 1591544934 756 SLDIDHSQYRFGHTKVFFK 774
Cdd:cd01386 671 ELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-735 |
7.82e-108 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 360.32 E-value: 7.82e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEA-PPHIYSIADNAYNDMLRNRE--NQSM 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 175 LITGESGAGKTVNTKRVIQYFAIVAALGETPAKKgqgpatKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESH------KIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 255 HFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS-QKKPELLDMLLVSSNPYDYhfcsqgVTTVENLDDGQEL 333
Cdd:cd14880 155 QLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKgASADERLQWHLPEGAAFSW------LPNPERNLEEDCF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 334 MATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQA---EADGTESADKASYLMGVSSADLIKGLLHPRVKV 410
Cdd:cd14880 229 EVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 411 GNEYVV--KGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPR-QYFIGVLDIAGFEIFELNSFEQLCINFTNE 487
Cdd:cd14880 309 GKQQQVfkKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 488 KLQQFFNHHMFILEQEEYKREGIDWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNHLGKSPN 566
Cdd:cd14880 389 KLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPC 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 567 FQKPRPDKkrkyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYEnyIGSDSASEHKIGGKekr 646
Cdd:cd14880 468 LGHNKLSR----EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFP--ANPEEKTQEEPSGQ--- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 647 KKAASFQTVSQLhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEF 726
Cdd:cd14880 539 SRAPVLTVVSKF-KASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNF 617
|
....*....
gi 1591544934 727 KRRYRILNP 735
Cdd:cd14880 618 VERYKLLRR 626
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-774 |
6.44e-106 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 354.89 E-value: 6.44e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMI-YTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEA-PPHIYSIADNAYNDM-LRNRENQSML 175
Cdd:cd14875 1 ATLLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLlPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 176 ITGESGAGKTVNTKRVIQYfaivaaLGETPAKKGQGPATKTggtLEDQIIE----ANPAMEAFGNAKTLRNDNSSRFGKF 251
Cdd:cd14875 81 ISGESGSGKTENAKMLIAY------LGQLSYMHSSNTSQRS---IADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 252 IRIHFGPT-GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTV------ 324
Cdd:cd14875 152 IKLYFDPTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 325 ENLDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESAdKASYLMGVSSADLIKGLL 404
Cdd:cd14875 232 KTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLRECFL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 405 hprVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLY--TSLPRQYFIGVLDIAGFEIFELNSFEQLCI 482
Cdd:cd14875 311 ---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpqGDCSGCKYIGLLDIFGFENFTRNSFEQLCI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 483 NFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGlDLQACIDLIE-KPLGIMSILEEECMFPKATDNSFKAKMYDNHL 561
Cdd:cd14875 388 NYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 562 GKSPNFQKPrpdkKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDsasehkig 641
Cdd:cd14875 467 NKSPYFVLP----KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLA-------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 642 gkeKRKkaasfQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRI 721
Cdd:cd14875 535 ---RRK-----QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRR 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1591544934 722 LYAEFKRRYRILNPHAiPDDTFVDSR--KAVEKLLAS----LDIDHSQYRFGHTKVFFK 774
Cdd:cd14875 607 PIEQFCRYFYLIMPRS-TASLFKQEKysEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-734 |
6.87e-106 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 356.60 E-value: 6.87e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRR-SEAPPHIYSIADNAYNDMLRNRENQSMLI 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 177 TGESGAGKTVNTKRVIQYfaivaaLGETPAKKGQGPAT--KTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 254
Cdd:cd14906 81 SGESGSGKTEASKTILQY------LINTSSSNQQQNNNnnNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 255 HFGPT-GKLASADIDIYLLEKSRvIFQQPGER--SYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGVTTVE------ 325
Cdd:cd14906 155 EFRSSdGKIDGASIETYLLEKSR-ISHRPDNInlSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISsfksqs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 326 ---------NLDDGQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQ---REEQAEADGTESADKASYLMG 393
Cdd:cd14906 234 snknsnhnnKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 394 VSSADLIKGLLHPRVKVGNEYVV--KGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTL-----------YTSLPRQYF 460
Cdd:cd14906 314 YIESVFKQALLNRNLKAGGRGSVycRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFnqntqsndlagGSNKKNNLF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 461 IGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFgLDLQACIDLIE-KPLGIMSILE 539
Cdd:cd14906 394 IGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 540 EECMFPKATDNSFKAK---MYDNhlgkspnfqKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQK 616
Cdd:cd14906 473 DECIMPKGSEQSLLEKynkQYHN---------TNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLA 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 617 SSNKLLACLYENYIGSDSASEhkiggkekrKKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFL 696
Cdd:cd14906 544 SSNFLKKSLFQQQITSTTNTT---------KKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVH 614
|
650 660 670
....*....|....*....|....*....|....*...
gi 1591544934 697 VLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILN 734
Cdd:cd14906 615 VLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIV 652
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-774 |
1.02e-91 |
|
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: 312.72 E-value: 1.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYtapvVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAivaalgetpakkgqgPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 258
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL---------------SGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPyDYHFCSQGVTTVENLDDGQE---LMA 335
Cdd:cd14937 142 YQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDfgnLMI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 336 TDHAMDilgfLPDEKYGCYKIVGAIMHFGNMKFKQ-----KQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKV 410
Cdd:cd14937 221 SFDKMN----MHDMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 411 GNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQ 490
Cdd:cd14937 297 ANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIH 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 491 QFFNHHMFILEQEEYKREGIDWTFIDFGLDlQACIDLIEKPLGIMSILEEECMFPKATDNSFkAKMYDNHLGKSPNFQKp 570
Cdd:cd14937 377 SIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYAS- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 571 rpdKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSDSASehkiggkekRKKAA 650
Cdd:cd14937 454 ---TKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLG---------RKNLI 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 651 SFQtvsqlHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRIcRKGFPNRILYAEFKRRY 730
Cdd:cd14937 522 TFK-----YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1591544934 731 RILNpHAIPDDTFVDSRKAVEKLLASlDIDHSQYRFGHTKVFFK 774
Cdd:cd14937 596 EYLD-YSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-774 |
1.07e-91 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 313.29 E-value: 1.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAY---KGKRRSEAPPHIYSIADNAYNDMLRNRENQSML 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 176 ITGESGAGKTVNTKRVIQYFAivaalgetpakkgqGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 255
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLT--------------CRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 256 FGPTGK-LASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQG----VTTVENLDDG 330
Cdd:cd14878 147 FCERKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLN-NLCAHRYLNQTmredVSTAERSLNR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 331 QELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKV 410
Cdd:cd14878 226 EKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 411 GNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTL-----YTSLPrQYFIGVLDIAGFEIFELNSFEQLCINFT 485
Cdd:cd14878 306 KGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdeQKSMQ-TLDIGILDIFGFEEFQKNEFEQLCVNMT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 486 NEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGLDLQACIDLI-EKPLGIMSILEEECMFPKATDNSFKAKMyDNHLGKS 564
Cdd:cd14878 385 NEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDFFfQKPSGFLSLLDEESQMIWSVEPNLPKKL-QSLLESS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 565 PNFQKPRPDKK-------RKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYIGSdsase 637
Cdd:cd14878 464 NTNAVYSPMKDgngnvalKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSKLVT----- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 638 hkiggkekrkkaasfqTVSQLHKeNLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGF 717
Cdd:cd14878 539 ----------------IASQLRK-SLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGY 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1591544934 718 PNRILYAEFKRRYRILNphaipdDTFVDSRK---AVEKL-LASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14878 602 PVRLSFSDFLSRYKPLA------DTLLGEKKkqsAEERCrLVLQQCKLQGWQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-737 |
4.02e-91 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 309.14 E-value: 4.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 100 SVLYNLRRRYAAWMIYTYSGLFCVTVNPYKwlPVYTAPVVAAYKgKRRSEAPPHIYSIADNAYNDMLRNrENQSMLITGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 180 SGAGKTVNTKRVIQYFAivaalgetpakkgqgPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgpT 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLV---------------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--D 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKpelldmLLVSSNPYDYHFCSQGVTTVENLDdgQELMATDHA 339
Cdd:cd14898 141 GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESIVQLS--EKYKMTCSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 340 MDILGFLPDEKYGcyKIVGAIMHFGNMKFKQkqrEEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQ 419
Cdd:cd14898 213 MKSLGIANFKSIE--DCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 420 NVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQyfIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFI 499
Cdd:cd14898 288 TLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 500 LEQEEYKREGIDWTFIDFgLDLQACIDLIEKPLGIMSILEEECMFPKATDNSFKAKM--YDNHLGKSpnfqkprpdkkrK 577
Cdd:cd14898 366 AKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNGFINT------------K 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 578 YEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVacfqksSNKLLAclyenyigsdsasehkigGKEKRKKAASFqtvsq 657
Cdd:cd14898 433 ARDKIKVSHYAGDVEYDLRDFLDKNREKGQLLIF------KNLLIN------------------DEGSKEDLVKY----- 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 658 lHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPHA 737
Cdd:cd14898 484 -FKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-774 |
1.10e-87 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 303.49 E-value: 1.10e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAA--------WMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 171 NQSMLITGESGAGKTVNTKRVIQYFAIVAALgetpaKKGQgpatkTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGK 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDR-----RHGA-----DSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 251 FIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQI-MSQKKPELLDMLLVSSNPYDYhfcsqgvttvenldd 329
Cdd:cd14887 151 MLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALcNAAVAAATQKSSAGEGDPEST--------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 330 gqELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGT--------ESADKASYLMGVSS----- 396
Cdd:cd14887 216 --DLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLtsvsvgceETAADRSHSSEVKClssgl 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 397 ---ADLIKGLLHPRVKVGNEYVVKGQN-------------------VEQVTYAVGALAKATYDRMFKWLVGRINRTLYTS 454
Cdd:cd14887 294 kvtEASRKHLKTVARLLGLPPGVEGEEmlrlalvsrsvretrsffdLDGAAAARDAACKNLYSRAFDAVVARINAGLQRS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 455 LPRQY--------------FIGVLDIAGFEIFE---LNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGI----DWT 513
Cdd:cd14887 374 AKPSEsdsdedtpsttgtqTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVfqnqDCS 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 514 FIDFGLDLQAC--------IDLIEKP--------------LGIMSILEEE-CMFPKATDNSFKAKMYDNHLGK----SPN 566
Cdd:cd14887 454 AFPFSFPLASTltsspsstSPFSPTPsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKniinSAK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 567 FQKPRPDKKRKyEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFqkssnklLAClyeNYIGSDSASEHKIGgkeKR 646
Cdd:cd14887 534 YKNITPALSRE-NLEFTVSHFACDVTYDARDFCRANREATSDELERLF-------LAC---STYTRLVGSKKNSG---VR 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 647 KKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEF 726
Cdd:cd14887 600 AISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVEL 679
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1591544934 727 KRRYRILNPHAIPDdtFVDSRKAVEKLLASLDIDHSQYRFGHTKVFFK 774
Cdd:cd14887 680 WRRYETKLPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-773 |
1.77e-75 |
|
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: 265.57 E-value: 1.77e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 96 LNEASVLYNLRRRYAAWMIYTY---SGLfcVTVNPYKWLPVYTAPVVAAYK-------GKRRSEAPPHIYSIADNAYNDM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 166 LRNRENQSMLITGESGAGKTVNTKRVIQYFAIVAAlgetPAKKGqgpaTKtggtLEDQIIEANPAMEAFGNAKTLRNDNS 245
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSS----HSKKG----TK----LSSQISAAEFVLDSFGNAKTLTNPNA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 246 SRFGKFIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYDYHFCSQGVTTV 324
Cdd:cd14879 147 SRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLgLDDPSDYALLASYGCHPLP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 325 ENL--DDG---QELMAtdhAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQ--REEQAEADGTESADKASYLMGVSSA 397
Cdd:cd14879 227 LGPgsDDAegfQELKT---ALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHegGEESAVVKNTDVLDIVAAFLGVSPE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 398 DLiKGLLHPRVKvgneYVVKgqnvEQVTY---AVGA------LAKATYDRMFKWLVGRINRTLytSLPRQY---FIGVLD 465
Cdd:cd14879 304 DL-ETSLTYKTK----LVRK----ELCTVfldPEGAaaqrdeLARTLYSLLFAWVVETINQKL--CAPEDDfatFISLLD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 466 IAGFEIF---ELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFgLDLQACIDLI-EKPLGIMSILEEE 541
Cdd:cd14879 373 FPGFQNRsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQ 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 542 C-MFPKATDNSFKAKMyDNHLGKSPNFQKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVAcfqkssnk 620
Cdd:cd14879 452 TrRMPKKTDEQMLEAL-RKRFGNHSSFIAVGNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVN-------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 621 LLAclyenyigsdSASEhkiggkekrkkaasfqtvsqlHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQ 700
Cdd:cd14879 523 LLR----------GATQ---------------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQ 571
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1591544934 701 LRCNGVLEGIRICRKGFPNRILYAEFKRRYrilnphaIPDDTFVDSRKAVEKLLASLDIDHSQYRFGHTKVFF 773
Cdd:cd14879 572 IRSLGLPELAARLRVEYVVSLEHAEFCERY-------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-725 |
3.83e-71 |
|
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: 253.68 E-value: 3.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEA-------PPHIYSIADNAYNDMLRNRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 171 NQSMLITGESGAGKTVNTKRVIQYFAIVaalgetpakkgQGPATKTggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGK 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI-----------QTDSQMT--ERIDKLIYINNILESMSNATTIKNNNSSRCGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 251 FIRIHF---------GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNPYDYHFCSQGV 321
Cdd:cd14884 148 INLLIFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 322 ------------TTVENLDDGQELMATD--------HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQkqreeqaeadg 381
Cdd:cd14884 228 shqkrsvkgtlrLGSDSLDPSEEEKAKDeknfvallHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA----------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 382 tesadkASYLMGVSSADLIKGLLHPRVKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPRQ--- 458
Cdd:cd14884 297 ------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDesd 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 459 ---------YFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDF--GLDLQACIDL 527
Cdd:cd14884 371 nediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVApsYSDTLIFIAK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 528 IEKPLGIMSILEEeCMFPKATDNSFK-----AKMY----DNHLGKSPNFQKPRPDKKRKYEAH-FELVHYAGVVPYNIIG 597
Cdd:cd14884 451 IFRRLDDITKLKN-QGQKKTDDHFFRyllnnERQQqlegKVSYGFVLNHDADGTAKKQNIKKNiFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 598 WLDKNKDPLNETVVACFQKSSNKLLaclyenyigsdsaSEHKIGGKEKrkkaaSFQTVSQLHKENLNKLMTNLRSTQPHF 677
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFL-------------REANNGGNKG-----NFLSVSKKYIKELDNLFTQLQSTDMYY 591
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1591544934 678 VRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAE 725
Cdd:cd14884 592 IRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-773 |
1.41e-70 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 250.80 E-value: 1.41e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 100 SVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAaykgkRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVGNPLTLTST-----RSSPLAPQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 180 SGAGKTVNTKRVI-QYFAIVAALGETPAKKgqgpatktggtledQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFgP 258
Cdd:cd14881 77 SGSGKTYASMLLLrQLFDVAGGGPETDAFK--------------HLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-T 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 259 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDML-LVSSNPYDYHFCSQGVTTVENLDDGQELMATD 337
Cdd:cd14881 142 DGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLhLDGYSPANLRYLSHGDTRQNEAEDAARFQAWK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 338 HAMDILG--FLpdekyGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKASyLMGVSSADLIKGLlHPRVKVGNEYV 415
Cdd:cd14881 222 ACLGILGipFL-----DVVRVLAAVLLLGNVQFIDGGGLEVDVKGETELKSVAA-LLGVSGAALFRGL-TTRTHNARGQL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 416 VKGQNVEQVTYAV-GALAKATYDRMFKWLVGRINrtlytSLPRQY----------FIGVLDIAGFEIFELNSFEQLCINF 484
Cdd:cd14881 295 VKSVCDANMSNMTrDALAKALYCRTVATIVRRAN-----SLKRLGstlgthatdgFIGILDMFGFEDPKPSQLEHLCINL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 485 TNEKLQQFFNHHMFILEQEEYKREGIDwTFIDFG-LDLQACIDLIEK-PLGIMSILEEECMfPKATDNSFKAKMYDNHLG 562
Cdd:cd14881 370 CAETMQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQ 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 563 kSPNFQKPRPDKKRKyeahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSnkllaCLYenyigsdsasehkigg 642
Cdd:cd14881 448 -NPRLFEAKPQDDRM----FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN-----CNF---------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 643 kekrkkaaSFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRIL 722
Cdd:cd14881 502 --------GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMR 573
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1591544934 723 YAEFKRRYRILNPHAIP---DDTFVDSRKAVEKLLASLDIDH-----SQYRFGHTKVFF 773
Cdd:cd14881 574 FKAFNARYRLLAPFRLLrrvEEKALEDCALILQFLEAQPPSKlssvsTSWALGKRHIFL 632
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-735 |
8.37e-67 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 239.39 E-value: 8.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 99 ASVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYkgkrrseappHIYSIADNAYNDMLRNRENQSMLI-T 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNAESIVfG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 178 GESGAGKTVNTKRVIQYfaivaaLGETPAKKgqgPATKTGGTLEDQIieanpamEAFGNAKTLRNDNSSRFGKFIRIHFG 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKY------LTSQPKSK---VTTKHSSAIESVF-------KSFGCAKTLKNDEATRFGCSIDLLYK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 258 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSSNpYDYHFCSQGVTTVENLDDGQELMATD 337
Cdd:cd14874 135 RNVLTGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL-QKFFYINQGNSTENIQSDVNHFKHLE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 338 HAMDILGFLPDEKYGCYKIVGAIMHFGNMKFKQKQR---EEQAEADGTESADK-ASYLMGVSSADLIKGLLhPRVKVGNE 413
Cdd:cd14874 214 DALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnvEQDVVEIGNMSEVKwVAFLLEVDFDQLVNFLL-PKSEDGTT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 414 YvvkgqNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLpRQYFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFF 493
Cdd:cd14874 293 I-----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPL-HTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 494 NHHMFILEQEEYKREGIDwtfIDFglDLQACID-------LIEKPLGIMSILEEECMFPKATDNSFKAKMYDNHLGKSpN 566
Cdd:cd14874 367 VKHSFHDQLVDYAKDGIS---VDY--KVPNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRS-S 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 567 FQKPRpdKKRKYEahFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENYigSDSASEHKIggkekr 646
Cdd:cd14874 441 YGKAR--NKERLE--FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY--SSNTSDMIV------ 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 647 kkaasfqTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEF 726
Cdd:cd14874 509 -------SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTF 581
|
....*....
gi 1591544934 727 KRRYRILNP 735
Cdd:cd14874 582 ARQYRCLLP 590
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-773 |
6.02e-65 |
|
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: 236.79 E-value: 6.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 102 LYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRR----------SEAPPHIYSIADNAYNDMLRNREN 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 172 QSMLITGESGAGKTVNTKRVIQYFAIVAAlGETPAKKGQGpATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKF 251
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGD-ETEPRPDSEG-ASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 252 IRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS--QKKPELLDMLLVSSNPYDYHFCSQGVTTVENLD- 328
Cdd:cd14893 162 ISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAgvQHDPTLRDSLEMNKCVNEFVMLKQADPLATNFAl 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 329 ---DGQELMATDHAMDIlgfLPDEKYGCYKIVGAIMHFGNMKF--KQKQREEQAEADGTESADKAS-YLMGVSSADLIKG 402
Cdd:cd14893 242 darDYRDLMSSFSALRI---RKNQRVEIVRIVAALLHLGNVDFvpDPEGGKSVGGANSTTVSDAQScALKDPAQILLAAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 403 LL--HPRV------------KVGNEYV--VKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLYTSLPR--------- 457
Cdd:cd14893 319 LLevEPVVldnyfrtrqffsKDGNKTVssLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksnivin 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 458 QYFIGVLDIAGFEIFE--LNSFEQLCINFTNEKLQQFFNHHMF-----ILEQEEYKREG--IDWTFIDFGLDLQACIDLI 528
Cdd:cd14893 399 SQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLainfsFLEDESQQVENrlTVNSNVDITSEQEKCLQLF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 529 E-KPLGIMSILEEECMFPKATDNSFKAKMY--DNHLG--KSPN----FQKPRPDKKRKYEAHFELVHYAGVVPYNIIGWL 599
Cdd:cd14893 479 EdKPFGIFDLLTENCKVRLPNDEDFVNKLFsgNEAVGglSRPNmgadTTNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 600 DKNKDPLNETVVACFQKSSNKLLACLYENYIGSDSASEHKIGGKEKRKKAASFQTVSQLHKENLN--------------K 665
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqadA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 666 LMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPHaipddtfvd 745
Cdd:cd14893 639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVCGH--------- 709
|
730 740 750
....*....|....*....|....*....|..
gi 1591544934 746 sRKAVEKLLASLD----IDHSQYRFGHTKVFF 773
Cdd:cd14893 710 -RGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-774 |
3.79e-64 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 231.94 E-value: 3.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 100 SVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 180 SGAGKTVNTKRVIQYFAIVaalgetpakkGQGPATKTGgtledQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYL----------GDGNRGATG-----RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGST 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 260 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMS--QKKPELLDMLLVSSNPYDYHFCSQGVTTV----------ENL 327
Cdd:cd14882 147 GKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEVPPSklkyrrddpeGNV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 328 DDGQELMATDHAMDilgFLPDEKYGCYKIVGAIMHFGNMKFKQKQREeqAEADGTESADKASYLMGVSSADLIKGLLHPR 407
Cdd:cd14882 227 ERYKEFEEILKDLD---FNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 408 VKVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINRTLytSLPR-----QYFIGVLDIAGFEIFELNSFEQLCI 482
Cdd:cd14882 302 LIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKM--SFPRavfgdKYSISIHDMFGFECFHRNRLEQLMV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 483 NFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGLDLQACIDLIEKPLGIMSILEEEcmfpkatdnsfKAKMYDNHLG 562
Cdd:cd14882 380 NTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDA-----------SRSCQDQNYI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 563 KSPNFQKPRPDKKRKYEAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQKSSNKLLACLYENyigsdsASEHKIgg 642
Cdd:cd14882 449 MDRIKEKHSQFVKKHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN------SQVRNM-- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 643 kekRKKAASFQTVSQlhkENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCNGVLEGIRICRKGFPNRIL 722
Cdd:cd14882 521 ---RTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIP 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 723 YAEFKRRYRILnphAIPDDTFVDSRKAVEKLLAsLDIDHSQYRFGHTKVFFK 774
Cdd:cd14882 595 FQEFLRRYQFL---AFDFDETVEMTKDNCRLLL-IRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
105-774 |
1.95e-60 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 221.50 E-value: 1.95e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 105 LRRRYAAWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRrsEAPPHIYSIADNAYNDMLRNRENQSMLITGESGAG 183
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 184 KTVNTKRVIQYFaIVAALGETPakkgqgpatktggTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPTGKLA 263
Cdd:cd14905 85 KSENTKIIIQYL-LTTDLSRSK-------------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 264 SADIDIYLLEKSRVIFQQPGERSYHIYYQIM---SQKKPELLDMLLVSSnpydYHFCSQGVT-TVENLDDGQELMATDHA 339
Cdd:cd14905 151 GAKLYSYFLDENRVTYQNKGERNFHIFYQFLkgiTDEEKAAYQLGDINS----YHYLNQGGSiSVESIDDNRVFDRLKMS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 340 MDILGFlPDEKYG-CYKIVGAIMHFGNMKFKQKQreEQAEADGTESADKASYLMGVSSADLIKGLLHPRVKVGNEYVvkg 418
Cdd:cd14905 227 FVFFDF-PSEKIDlIFKTLSFIIILGNVTFFQKN--GKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAV--- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 419 QNVEqvtyavgALAKATYDRMFKWLVGRINRTLYtslPRQY--FIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHH 496
Cdd:cd14905 301 ENRD-------SLARSLYSALFHWIIDFLNSKLK---PTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 497 MFILEQEEYKREGIDW-TFIDFGlDLQACIDLIEKplgIMSILEEECMFPKATDNSFKAKMyDNHLGKSPNFQKpRPDKk 575
Cdd:cd14905 371 VLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL-QNFLSRHHLFGK-KPNK- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 576 rkyeahFELVHYAGVVPYNIIGWLDKNKDP-------------------------LNETVVACFQ----KSSNK------ 620
Cdd:cd14905 444 ------FGIEHYFGQFYYDVRGFIIKNRDEilqrtnvlhknsitkylfsrdgvfnINATVAELNQmfdaKNTAKksplsi 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 621 ---LLACLYENYIGSDSASEHKIGGKEKRKKAASFQTVSQLHK--ENLNKLMTNlRSTQPHFVRCIIPNETKTPGIMDAF 695
Cdd:cd14905 518 vkvLLSCGSNNPNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTtySSTNKAINN-SNCDFHFIRCIKPNSKKTHLTFDVK 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 696 LVLHQLRCNGVLEGIRICRKGFP----NRILYAEF------KRRYRILNPHAIPDDTFVDSrkavekllasldIDHSQYR 765
Cdd:cd14905 597 SVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRFsfffqnQRNFQNLFEKLKENDINIDS------------ILPPPIQ 664
|
....*....
gi 1591544934 766 FGHTKVFFK 774
Cdd:cd14905 665 VGNTKIFLR 673
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-254 |
3.22e-55 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 189.86 E-value: 3.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 121 FCVTVNPYKWLPVYTAPVV-AAYKGKRRSEAPPHIYSIADNAYNDMLRNRENQSMLITGESGAGKTVNTKRVIQYFAIVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1591544934 200 ALGETPAK-KGQGPATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 254
Cdd:cd01363 81 FNGINKGEtEGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-772 |
1.62e-41 |
|
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: 165.01 E-value: 1.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 100 SVLYNLRRRYAAWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSE-APPHIYSIADNAYNDMLRNRENQSMLITG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 179 ESGAGKTVNTKRVIQYFAIVAALGETPAKKGQGPA---------TKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFG 249
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEednihneenTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 250 KFIRIHFgPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQIMSQKKPELLDMLLVSsNPYDYHFCSQGVTTVENLDD 329
Cdd:cd14938 162 KFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLK-NIENYSMLNNEKGFEKFSDY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 330 GQELMATDHAMDILGFLPDEKYGCYKIVGAIMHFGN-------------MKFKQKQRE----------EQAEADGTESAD 386
Cdd:cd14938 240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDENV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 387 K----ASYLMGVSSADLIKGLLHPRVkVGNEYVVKGQNVEQVTYAVGALAKATYDRMFKWLVGRINrTLYTSLPR----Q 458
Cdd:cd14938 320 KnlllACKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKIN-EKCTQLQNininT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 459 YFIGVLDIAGFEIFELNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIDWTFIDFGLDLQACIDLIEKPL--GIMS 536
Cdd:cd14938 398 NYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 537 ILEEECMfPKATDNSFKAKMYDNHLGKSPNFQKPRPDKKRKyeAHFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFQK 616
Cdd:cd14938 478 LLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNK--KTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 617 SSNKLLA--CLYENYIGSDSASEHKIGGKE-------KRKKAASFQTVSQLHKENLNKLMTNLRSTQPHFVRCIIPNETK 687
Cdd:cd14938 555 SENEYMRqfCMFYNYDNSGNIVEEKRRYSIqsalklfKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 688 TP-GIMDAFLVLHQLRCNGVLEGIRICRKGFPNRILYAEFKRRYRILNPhaipddtfvDSRKAVEKLLASLDIDHSQYRF 766
Cdd:cd14938 635 RElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMI 705
|
....*.
gi 1591544934 767 GHTKVF 772
Cdd:cd14938 706 GNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1184-1916 |
2.30e-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: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1184 RDLEEAMLHHEATTAGLRKKhadsvaELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKASAEKTCRLYEDQ 1263
Cdd:TIGR02168 216 KELKAELRELELALLVLRLE------ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1264 MNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQNVEELKKQLEEENKAKNALAHALQS 1343
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1344 SRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTKYEtDAIQRTEELEESKKKLAVRLQEAEeaVEASNAKCSSLE 1423
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE-RLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1424 KTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKCEECQAELETSQKESRSLST---------------- 1487
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllknqsglsgilgvls 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1488 ELFKLKNSYEETLE-----HLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMK-KGLEIEKSEIQAALEEAEGTLEH 1561
Cdd:TIGR02168 527 ELISVDEGYEAAIEaalggRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKgTEIQGNDREILKNIEGFLGVAKD 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1562 EESKTLRIQLELNQIKADVdrKLAEKEEEIDNLRRNHQRtlESMQATLDAE----------------------AKSRSEA 1619
Cdd:TIGR02168 607 LVKFDPKLRKALSYLLGGV--LVVDDLDNALELAKKLRP--GYRIVTLDGDlvrpggvitggsaktnssilerRREIEEL 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1620 VRLRKKMEGDLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTERRNNLLASEVEELRAL 1699
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1700 LEQNDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDD---AVQECRNAEEKAKKAITDAAMMAEE 1776
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneEAANLRERLESLERRIAATERRLED 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1777 LKKE-QDTSAHLERMKKNMEqtikDLQMRLDEAEqIALKGGKKQVQKLEARVKELENELESEQKKSQEYQKGVRKFERRI 1855
Cdd:TIGR02168 843 LEEQiEELSEDIESLAAEIE----ELEELIEELE-SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 1856 KELSYQGEEDKKNLVRMQELIDKLQAKVKS-YKRQAEEAEDQANTNLSKYRKLQHELDDAEE 1916
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQERLSEeYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1179-1929 |
8.63e-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: 123.24 E-value: 8.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1179 ILKLRRDLEEAMLHHEATTAGLrKKHADSVAELSEQIDSLQRVKQKLEK-----------ERSEAKMEVDDLASTVEQLS 1247
Cdd:TIGR02168 167 ISKYKERRKETERKLERTRENL-DRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1248 KGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQNVEELKKQL 1327
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1328 EEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTKYETdaiQRTE--ELEESKKKLAVRL 1405
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET---LRSKvaQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1406 QEAEEAVEasnakcsSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRnfDKVLAEWRQKCEECQAELETSQKESRSL 1485
Cdd:TIGR02168 403 ERLEARLE-------RLEDRRERLQQEIEELLKKLEEAELKELQAELEEL--EEELEELQEELERLEEALEELREELEEA 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1486 STELFKLKNSYEET---LEHLETIKRENKNLQEEITDL---SDQISQGAKTIHELEKMKKGLEIEKSE-----IQAAL-- 1552
Cdd:TIGR02168 474 EQALDAAERELAQLqarLDSLERLQENLEGFSEGVKALlknQSGLSGILGVLSELISVDEGYEAAIEAalggrLQAVVve 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1553 --EEAEGTLEH--EESKTLRIQLELNQIKADVDRKlaekeeeidnlrrNHQRTLESMQATLDAEAKSRSEAVRLRKKMEG 1628
Cdd:TIGR02168 554 nlNAAKKAIAFlkQNELGRVTFLPLDSIKGTEIQG-------------NDREILKNIEGFLGVAKDLVKFDPKLRKALSY 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1629 DLNEMEV--QLNHANRLASESQKLLRNlqVQIKDVQLELDETIHQNEELKEQVAVtERRNNL--LASEVEELRALLEQND 1704
Cdd:TIGR02168 621 LLGGVLVvdDLDNALELAKKLRPGYRI--VTLDGDLVRPGGVITGGSAKTNSSIL-ERRREIeeLEEKIEELEEKIAELE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1705 RARKLAEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTS 1784
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1785 AHLERMKKNMEQTIKDLQmrldeaeqialkggkKQVQKLEARVKELENELESEQKKSQEYQKGVRKFERRIKELSYQGEE 1864
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLK---------------EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1591544934 1865 DKKNLVRMQELIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELDDAEERADMAETQVTKLR 1929
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
984-1836 |
1.39e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 119.39 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 984 KNLIEEMAAldetILKLTKEKKalqEAHQQ---TLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLR------- 1053
Cdd:TIGR02168 158 RAIFEEAAG----ISKYKERRK---ETERKlerTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRelelall 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1054 -MDLERVKRKLE---GDLKLSMESVMDLENDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEE 1129
Cdd:TIGR02168 231 vLRLEELREELEelqEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1130 LEADRACRAKVEKQRGDVARELEELSERLEESGgATSAQIEINKKRETDILKLRRDLEEAMLHHEATTAGLRKKHADSVA 1209
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELE-EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1210 ELSEQIDSLQrvkqkleKERSEAKMEVDDLASTVEQLSKGKASAEKtcRLYEDQMNEAKAKVEELQRQLNETNSHRARAQ 1289
Cdd:TIGR02168 390 QLELQIASLN-------NEIERLEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQEELERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1290 AESSELSRKLEERE----ATVSQLQRSKNSFSQNVEELKKQLEEENKAKNALAHALQSSRHDcDLLREQYdeeqEAKAEL 1365
Cdd:TIGR02168 461 EALEELREELEEAEqaldAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGIL-GVLSELI----SVDEGY 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1366 QRALSKANGEVAQW-RTKYETDAIQRTEELEESKK--------------KLAVRLQEAEEAVEASNAKCSSLEKTKHRLQ 1430
Cdd:TIGR02168 536 EAAIEAALGGRLQAvVVENLNAAKKAIAFLKQNELgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLR 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1431 TEIEDL------VVDLERASAAAAALDKKQRNF----DKVLAEWRQkceecqaeleTSQKESRSLSTelfklknsyeetl 1500
Cdd:TIGR02168 616 KALSYLlggvlvVDDLDNALELAKKLRPGYRIVtldgDLVRPGGVI----------TGGSAKTNSSI------------- 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1501 ehLETiKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLELNQIkadv 1580
Cdd:TIGR02168 673 --LER-RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL---- 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1581 drklaekEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLRKKMEgdlnEMEVQLNHANRLASESQKLLRNLQVQIKD 1660
Cdd:TIGR02168 746 -------EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE----ELEAQIEQLKEELKALREALDELRAELTL 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1661 VQLELDETIHQNEELKEQVAVTERRNNLLASEVEELRALLEQndrarklAEHELLEATERVNLLHSQNTSLINQKKKLEN 1740
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-------LAAEIEELEELIEELESELEALLNERASLEE 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1741 DLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNMEQTIKDL----QMRLDEAEQIALKGg 1816
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE---LRLEGLEVRIDNLQERLseeySLTLEEAEALENKI- 963
|
890 900
....*....|....*....|
gi 1591544934 1817 KKQVQKLEARVKELENELES 1836
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
853-1739 |
4.20e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 114.38 E-value: 4.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 853 TEKELASLKEELAKLKEALeksevkrKELEERQVSL----------IQEKNDL-SLQLQAEQDNLADAEDRCDLLIKTKI 921
Cdd:TIGR02168 177 TERKLERTRENLDRLEDIL-------NELERQLKSLerqaekaeryKELKAELrELELALLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 922 QLEAKVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLt 1001
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1002 kekkalqeahQQTLDDLQAEedkVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEgdlklsmESVMDLENDK 1081
Cdd:TIGR02168 329 ----------ESKLDELAEE---LAELEEKLEELKEELESLEAELEELEAELEELESRLEELE-------EQLETLRSKV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1082 QQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARteeleeeleADRACRAKVEKQRGDVARELEELSERLEES 1161
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK---------LEEAELKELQAELEELEEELEELQEELERL 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1162 GGATSAQIEINKKRETDILKLRRDLEEAmlhheattaglrKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLAS 1241
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQL------------QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1242 TVEQLSKGKASAEKTCR-----LYEDQMNEAKAKVEELQrqlnETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSF 1316
Cdd:TIGR02168 528 LISVDEGYEAAIEAALGgrlqaVVVENLNAAKKAIAFLK----QNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGV 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1317 SQNVeelkkqLEEENKAKNALAHALQSSRHDCDL-----LREQYDEEqEAKAELQRALSKANGEVAQWRTKYETDAIQRT 1391
Cdd:TIGR02168 604 AKDL------VKFDPKLRKALSYLLGGVLVVDDLdnaleLAKKLRPG-YRIVTLDGDLVRPGGVITGGSAKTNSSILERR 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1392 EELEESKKKLAvrlqEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERasaaaaaLDKKQRNFDKVLAEWRQKCEEC 1471
Cdd:TIGR02168 677 REIEELEEKIE----ELEEKIAELEKALAELRKELEELEEELEQLRKELEE-------LSRQISALRKDLARLEAEVEQL 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1472 QAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAA 1551
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1552 LEEAEGTLeHEESKTLRiqlELNQIKADVDRKLAEKEEEIDNLrrnhQRTLESMQATLDAEAKSRSEAVRLRKKMEGDLN 1631
Cdd:TIGR02168 826 LESLERRI-AATERRLE---DLEEQIEELSEDIESLAAEIEEL----EELIEELESELEALLNERASLEEALALLRSELE 897
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1632 EMEVQLNHANRLASESQKLLRNLQVQIKDVQLELDET----IHQNEELKEQVAVT----ERRNNLLASEVEELRALLEQN 1703
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLevriDNLQERLSEEYSLTleeaEALENKIEDDEEEARRRLKRL 977
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 1591544934 1704 DRARK-------LAEHELLEATERVNLLHSQNTSLINQKKKLE 1739
Cdd:TIGR02168 978 ENKIKelgpvnlAAIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1268-1929 |
1.50e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 112.46 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1268 KAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKnsfsqnveelkkqleeenKAKNALahalqsSRHD 1347
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYK------------------ELKAEL------RELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1348 CDLLREQYDEEQEAKAELQRALSKANGEvaqwRTKYETDAIQRTEELEESKKKLAV---RLQEAEEAVEASNAKCSSLEK 1424
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEEE----LEELTAELQELEEKLEELRLEVSEleeEIEELQKELYALANEISRLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1425 TKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLE 1504
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1505 TIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLE--------LNQI 1576
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelqeelerLEEA 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1577 KADVDRKLAEKEEEIDNLRRNHQR------TLESMQATLDAEAKSRSEAVRLRKKMEG---------------------- 1628
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQlqarldSLERLQENLEGFSEGVKALLKNQSGLSGilgvlselisvdegyeaaieaa 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1629 -------------------------------------DLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQLE------- 1664
Cdd:TIGR02168 543 lggrlqavvvenlnaakkaiaflkqnelgrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyll 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1665 --------LDETIHQ-NEELKEQVAVT------------------------ERRNNL--LASEVEELRALLEQNDRARKL 1709
Cdd:TIGR02168 623 ggvlvvddLDNALELaKKLRPGYRIVTldgdlvrpggvitggsaktnssilERRREIeeLEEKIEELEEKIAELEKALAE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1710 AEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1789
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1790 MKKNMEQTIKDLQMRLDEAEQiALKGGKKQVQKLEARVKELENELESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKNL 1869
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALRE-ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1870 VRMQELIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELDDAEERADMAETQVTKLR 1929
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
851-1596 |
3.46e-23 |
|
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: 108.22 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 851 AATEKELASLKEELAKLKEALEKSEVKRKELEERQV-------SLIQEKNDLSLQLQAEQDNLAdaedrcdlliktkiQL 923
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLA--------------NL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 924 EAKVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKE 1003
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1004 KKALQEahqqtldDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLE--QEKKLRMDLERVKRKLEgdlklsmesvmDLENDK 1081
Cdd:TIGR02168 395 IASLNN-------EIERLEARLERLEDRRERLQQEIEELLKKLEeaELKELQAELEELEEELE-----------ELQEEL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1082 QQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRGDVareleelserlees 1161
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGIL-------------- 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1162 gGATSAQIEINKKRETDILK---------LRRDLEEAMLhheaTTAGLRKKHADSVA--ELSEQIDSLQRVKQKLEKERS 1230
Cdd:TIGR02168 523 -GVLSELISVDEGYEAAIEAalggrlqavVVENLNAAKK----AIAFLKQNELGRVTflPLDSIKGTEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1231 EAKMEV-DDLASTVEQLSKGKASAEKTCRLYEDqmneakakVEELQRQLNETNSH------------------RARAQAE 1291
Cdd:TIGR02168 598 EGFLGVaKDLVKFDPKLRKALSYLLGGVLVVDD--------LDNALELAKKLRPGyrivtldgdlvrpggvitGGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1292 SSELSRK--LEEREATVSQLQRSKNSFSQNVEELKKQLEEENKAKNALAHALQSSRHDCDLLREQYD---EEQEAKAELQ 1366
Cdd:TIGR02168 670 SSILERRreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArleAEVEQLEERI 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1367 RALSKANGEVAQWRTKYETDAIQRTEELEESKKK---LAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERA 1443
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1444 SAAAAALDKKQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQ 1523
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1591544934 1524 ISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLELnqiKADVDRKLAEKEEEIDNLRR 1596
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAL---ENKIEDDEEEARRRLKRLEN 979
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
847-1436 |
6.52e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.94 E-value: 6.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 847 LLKSAATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAK 926
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 927 VKEIMERLEDEEEmsatvlaKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKA 1006
Cdd:COG1196 304 IARLEERRRELEE-------RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1007 LQEAHQQTLDDLQAEEdkvntltKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSMESVMDLENDKQQLEE 1086
Cdd:COG1196 377 AEEELEELAEELLEAL-------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1087 KLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRGDVARELEELSERLEESGGATs 1166
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV- 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1167 aqieinkkRETDILKLRRDLEEAMLhheattAGLRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLAST-VEQ 1245
Cdd:COG1196 529 --------LIGVEAAYEAALEAALA------AALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAaLAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1246 LSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQNVEELKK 1325
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1326 QLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQwRTKYETDAIQRTEELEESKKKLAVRL 1405
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE-EQLEAEREELLEELLEEEELLEEEAL 753
|
570 580 590
....*....|....*....|....*....|.
gi 1591544934 1406 QEAEEAVEAsnakcSSLEKTKHRLQTEIEDL 1436
Cdd:COG1196 754 EELPEPPDL-----EELERELERLEREIEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
851-1536 |
1.90e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 102.44 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 851 AATEKELASLKEELAKLKEALEKSEVKRKELEERQvsliqekNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEI 930
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRL-------EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 931 MERLEDEEEMSATVLakKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKE---KKAL 1007
Cdd:TIGR02168 413 EDRRERLQQEIEELL--KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaqLQAR 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1008 QEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLklsmesVMDLENDKQQLEEK 1087
Cdd:TIGR02168 491 LDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAV------VVENLNAAKKAIAF 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1088 LKKKDF------------------EMNEMSTRIEDEQSLVNQLQKKIKELQ-------ARTEELEEELEADRacRAKVEK 1142
Cdd:TIGR02168 565 LKQNELgrvtflpldsikgteiqgNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllGGVLVVDDLDNALE--LAKKLR 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1143 QRGDVARELEELSERLEESGGATSAQIEINKKRETDILKLRRDLEEAmlhheattaglrkkhADSVAELSEQIDSLQRVK 1222
Cdd:TIGR02168 643 PGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEEL---------------EEKIAELEKALAELRKEL 707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1223 QKLEKERSEAKMEVDDLASTVEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEER 1302
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1303 EATVSQLQRSKNSFSQNVEELKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTK 1382
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1383 YETdAIQRTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDKK-QRNFDKVL 1461
Cdd:TIGR02168 868 IEE-LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRiDNLQERLS 946
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1462 AEWRQKCEECQAELETSQKESRSLSTELFKLKNSYEE-------TLEHLETIKRENKNLQEEITDLSDQISQGAKTIHEL 1534
Cdd:TIGR02168 947 EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
..
gi 1591544934 1535 EK 1536
Cdd:TIGR02168 1027 DR 1028
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
856-1679 |
1.28e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 99.76 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 856 ELASLKEELAKLKEALEKSEVKRKELEERQvSLIQEKNDlslQLQAEQDNLADAEDRCDLLiktKIQLEAKVKEIMERLE 935
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEELEEVEENIERLD-LIIDEKRQ---QLERLRREREKAERYQALL---KEKREYEGYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 936 DEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIE-EMAALDETILKLTKEKKALQEAHQQT 1014
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1015 LDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRmdlervkRKLEGDLKLSMESVMDLENDKQQLEEKLKKKDFE 1094
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR-------DKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1095 MNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELeadRACRAKVEKQRGDVARELEElserleesggATSAQIEInKK 1174
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEEL---ADLNAAIAGIEAKINELEEE----------KEDKALEI-KK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1175 RETDILKLRRDLEEAMLHHEATTAGLRKkhadsvaeLSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKASAE 1254
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDR--------VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVH 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1255 KTCR---LYEDQM---------NEAKAKV-------EELQRQLNETNSHRA------RAQAESSELSRKLEEREAT---- 1305
Cdd:TIGR02169 525 GTVAqlgSVGERYataievaagNRLNNVVveddavaKEAIELLKRRKAGRAtflplnKMRDERRDLSILSEDGVIGfavd 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1306 -VSQLQRSKNSFSQN------VEELKKQLEEENKAK-------------------NALAHALQSSRHDCDLLREQYDEEQ 1359
Cdd:TIGR02169 605 lVEFDPKYEPAFKYVfgdtlvVEDIEAARRLMGKYRmvtlegelfeksgamtggsRAPRGGILFSRSEPAELQRLRERLE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1360 EAKAELQRALSKAN---GEVAQWRTKYEtDAIQRTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDL 1436
Cdd:TIGR02169 685 GLKRELSSLQSELRrieNRLDELSQELS-DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKEL 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1437 VVDLERASAAAAALDKKQRNFDKVLAewRQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEE 1516
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1517 ITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLR-------IQLELNQIKADVDR------- 1582
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEleaqlreLERKIEELEAQIEKkrkrlse 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1583 ---KLAEKEEEIDNLRRNHQRTLESMQATLDAEaksrsEAVRLRKKMEGDLNEMEVQLNHANRLASESQKLLRNLQVQIK 1659
Cdd:TIGR02169 922 lkaKLEALEEELSEIEDPKGEDEEIPEEELSLE-----DVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRA 996
|
890 900
....*....|....*....|...
gi 1591544934 1660 DVQLE---LDETIHQNEELKEQV 1679
Cdd:TIGR02169 997 KLEEErkaILERIEEYEKKKREV 1019
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
852-1615 |
2.83e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 98.60 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 852 ATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLI-QEKNDLSLQLQAEQDNLADAED-------RCDLLIKTKIQL 923
Cdd:TIGR02169 191 LIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELlKEKEALERQKEAIERQLASLEEeleklteEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 924 EAKVKEIMERLED--EEEMSA------TVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDE 995
Cdd:TIGR02169 271 EQLLEELNKKIKDlgEEEQLRvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 996 TILKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSMESVM 1075
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1076 DLENDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRGDVareleels 1155
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS-------- 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1156 erlEESGGATSAQIEINKKRETDILKLRRDL---EEAMLHHEATTAGLRKKHA----DSVAElsEQIDSLQRVK------ 1222
Cdd:TIGR02169 503 ---EERVRGGRAVEEVLKASIQGVHGTVAQLgsvGERYATAIEVAAGNRLNNVvvedDAVAK--EAIELLKRRKagratf 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1223 ------QKLEKERSEAKME-----------------------------VDDLASTVEQL--------------------- 1246
Cdd:TIGR02169 578 lplnkmRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfgdtlvVEDIEAARRLMgkyrmvtlegelfeksgamtg 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1247 -SKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQnveelkk 1325
Cdd:TIGR02169 658 gSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ------- 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1326 qleEENKAKNALAHalqssrhdcdlLREQYDEEQEAKAELQRALSKANGEVAQwrtkYETDAIQRTEELEESKKKLavrl 1405
Cdd:TIGR02169 731 ---EEEKLKERLEE-----------LEEDLSSLEQEIENVKSELKELEARIEE----LEEDLHKLEEALNDLEARL---- 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1406 qeAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKCEECQAELETSQKESRSL 1485
Cdd:TIGR02169 789 --SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1486 STELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQ---AALEEAEGTLEHE 1562
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEeelSEIEDPKGEDEEI 946
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1591544934 1563 ESKTL---RIQLELNQIKADVDR-----KLAEKEEEIDNLRRNHqrtLESMQATLDAEAKS 1615
Cdd:TIGR02169 947 PEEELsleDVQAELQRVEEEIRAlepvnMLAIQEYEEVLKRLDE---LKEKRAKLEEERKA 1004
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
986-1825 |
7.42e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 97.06 E-value: 7.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 986 LIEEMAALDETILKLTKEKKALQEAHQQtLDDLQAEEDKVNtltkaqakleQQVDDLEGslEQEKKLR-MDLERVKRKLE 1064
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEEN-IERLDLIIDEKR----------QQLERLRR--EREKAERyQALLKEKREYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1065 GDLKLS-----MESVMDLENDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKEL----QARTEELEEELEADRA 1135
Cdd:TIGR02169 225 GYELLKekealERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeQLRVKEKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1136 C------------------RAKVEKQRGDVARELEELSERLEESGGATSAQIEINKKRETDILKLRRDLEEAmlhhEATT 1197
Cdd:TIGR02169 305 SlersiaekereledaeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV----DKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1198 AGLRKKHADSVAELSE----------QIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKASAEKTCRLYEDQMNEA 1267
Cdd:TIGR02169 381 AETRDELKDYREKLEKlkreinelkrELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1268 KAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQNVEELKKQLE------------------- 1328
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryata 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1329 ----EENKAKN-------------ALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTKYETD---AI 1388
Cdd:TIGR02169 541 ievaAGNRLNNvvveddavakeaiELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAfkyVF 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1389 QRT---EELEESKKKLA-VRLQEAE-EAVEASNA------KCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNF 1457
Cdd:TIGR02169 621 GDTlvvEDIEAARRLMGkYRMVTLEgELFEKSGAmtggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRI 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1458 DKVLAEWRQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKM 1537
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1538 KKglEIEKSEIQAALEEAEGTLEHEESKTLRIQLELNQIKADVDRKLAEKE------EEIDNLRRNHQRTLESMQATLDA 1611
Cdd:TIGR02169 781 LN--DLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEylekeiQELQEQRIDLKEQIKSIEKEIEN 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1612 EAKSRSEAVRLRKKMEGDLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTERRNNLLAS 1691
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1692 EVEELRALLEQNDRARKLAEhELLEATERVNLLHSQNTSLINQKKKLENDLSTLsnevddavQECRNAEEKAKKAITDAA 1771
Cdd:TIGR02169 939 PKGEDEEIPEEELSLEDVQA-ELQRVEEEIRALEPVNMLAIQEYEEVLKRLDEL--------KEKRAKLEEERKAILERI 1009
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1591544934 1772 MMAEELKKEQDTSAhLERMKKNMEQTIKDL-----QMRLDEAE-------QIALKGGKKQVQKLEA 1825
Cdd:TIGR02169 1010 EEYEKKKREVFMEA-FEAINENFNEIFAELsggtgELILENPDdpfagglELSAKPKGKPVQRLEA 1074
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1197-1896 |
7.49e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 97.06 E-value: 7.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1197 TAGLRKKHADSVAELSEQIDSLQRVKQKLEK-ERSEAKME--VDDLASTVEQLSKGKASAEK----TCRLYEDQMNEAKA 1269
Cdd:TIGR02169 151 SPVERRKIIDEIAGVAEFDRKKEKALEELEEvEENIERLDliIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1270 KVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQNVEELKKQLEEENKAKNALAHALQSS--RHD 1347
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASleRSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1348 CDLLREQYD-EEQEAKAELQRalSKANGEVAQWRTKYETDAIQR---TEELEESKKKLAV---RLQEAEEAVEASNAKCS 1420
Cdd:TIGR02169 311 AEKERELEDaEERLAKLEAEI--DKLLAEIEELEREIEEERKRRdklTEEYAELKEELEDlraELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1421 SLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELfklknsyEETL 1500
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL-------EQLA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1501 EHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIE----------------------------KSEIQAAL 1552
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrggraveevlkasiqgvhgtvaqlgsvGERYATAI 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1553 EEAEG------TLEHEESKTLRIQ------------LELNQIKAD-VDRKLAEKEEEID---NLRRNHQR---------- 1600
Cdd:TIGR02169 542 EVAAGnrlnnvVVEDDAVAKEAIEllkrrkagratfLPLNKMRDErRDLSILSEDGVIGfavDLVEFDPKyepafkyvfg 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1601 ---TLESMQA-----------TLDAE----------------------AKSRSEAVRLR---KKMEGDLNEMEVQLNHAN 1641
Cdd:TIGR02169 622 dtlVVEDIEAarrlmgkyrmvTLEGElfeksgamtggsraprggilfsRSEPAELQRLRerlEGLKRELSSLQSELRRIE 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1642 RLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTERRNNLLASEVEELRALLEQN-----DRARKLAEHELLE 1716
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELearieELEEDLHKLEEAL 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1717 ATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDavqecrnaeekakkaiTDAAMMAEELKKEQdtsahLERMKKNMEQ 1796
Cdd:TIGR02169 782 NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE----------------IEQKLNRLTLEKEY-----LEKEIQELQE 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1797 TIKDLQMRLDEAEQialkggkkQVQKLEARVKELENELESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKNLVRMQELI 1876
Cdd:TIGR02169 841 QRIDLKEQIKSIEK--------EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
810 820
....*....|....*....|
gi 1591544934 1877 DKLQAKVKSYKRQAEEAEDQ 1896
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEE 932
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1208-1836 |
9.29e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.54 E-value: 9.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1208 VAELSEQIDSLQRVKQKLEKERsEAKMEVDDLAstVEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRAR 1287
Cdd:COG1196 195 LGELERQLEPLERQAEKAERYR-ELKEELKELE--AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1288 AQAESSELSRKLEEREATVSQLQRSKNSfsqnveelkkqleeenkaknalahalqssrhdcdlLREQYDEEQEAKAELQR 1367
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELAR-----------------------------------LEQDIARLEERRRELEE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1368 ALSKANGEVAQWRTKYETDAiQRTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAA 1447
Cdd:COG1196 317 RLEELEEELAELEEELEELE-EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1448 AALDKKQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQG 1527
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1528 AKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLELNQIKADVDRKLAEKEEEIDNLrrnhqRTLESMQA 1607
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA-----ALAAALQN 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1608 TLDAEAKSRSEAVRLRKkmegdlnemEVQLNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTERRNN 1687
Cdd:COG1196 551 IVVEDDEVAAAAIEYLK---------AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1688 LLASEVEELRAL--------LEQNDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQECRNA 1759
Cdd:COG1196 622 LLGRTLVAARLEaalrravtLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1591544934 1760 EEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQKLEARVKELENELES 1836
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1331-1929 |
1.40e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.16 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1331 NKAKNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQwrtkyetdAIQRTEELEESKKKLAVRLQEAEE 1410
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEE--------LEAELAELEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1411 AVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELF 1490
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1491 KLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQ 1570
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1571 LELNQIKADVDRKLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLrkkmegdlnEMEVQLNHANRLASESQKL 1650
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL---------LLLLEAEADYEGFLEGVKA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1651 LRNLQVQiKDVQLELDETIHQNEELKEQVAVterrnnllASEVEELRALLEQNDRARKLAEHELLEATERVNLLHSqntS 1730
Cdd:COG1196 513 ALLLAGL-RGLAGAVAVLIGVEAAYEAALEA--------ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL---D 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1731 LINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQ 1810
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1811 IALKGGKKQVQKLEARVKELENELESEQKKSQEYQkgvrkfERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKRQA 1890
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELEL------EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
570 580 590
....*....|....*....|....*....|....*....
gi 1591544934 1891 EEAEDQANTNLSKYRKLQHELDDAEERADMAETQVTKLR 1929
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1170-1898 |
1.51e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 96.36 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1170 EINKKRETDILKLRRDLEEAMLHHEATTAGLRKKHADSVAELSE----QIDSLQRVKQKLEKERSEAKMEVDDLASTVEQ 1245
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEarkaEDAKRVEIARKAEDARKAEEARKAEDAKKAEA 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1246 LSKgkasAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRAR--AQAESSELSRKLEEREATVSQLQRSKNSFSQNVEEL 1323
Cdd:PTZ00121 1181 ARK----AEEVRKAEELRKAEDARKAEAARKAEEERKAEEARkaEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRK 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1324 KKQLEEENKAKNALAHALQSSRHDCDLLREqydEEQEAKAELQRALSKANGEVAQWRTKYETDAIQRTEELEESKKKLAV 1403
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKA---EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1404 RLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAaaaalDKKQRNFDKVLAEWRQKCEECQAELETSQKESR 1483
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE-----AKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1484 SLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEiEKSEIQAALEEAEGTLEHEE 1563
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE-EAKKADEAKKKAEEAKKADE 1487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1564 SKTlriQLELNQIKADVDRKLAEKEEEIDNLRRNHQ--------RTLESMQATLDAEAKSRSEAVRLRKKMEGDLNEMEV 1635
Cdd:PTZ00121 1488 AKK---KAEEAKKKADEAKKAAEAKKKADEAKKAEEakkadeakKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK 1564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1636 QLNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTERRNNLLASEVEELRALLEQNDRARKLAEHELL 1715
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1716 EATERVNLLHSQNTSLI---NQKKKLENDlstlsnevDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKK 1792
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIkaaEEAKKAEED--------KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1793 NMEQTIKDLQMRLDEAEQIALKGGKKQVQKLEARVKELENELESEQKKSQEYQKgvrKFERRIKELSYQGEEDKKNLVRM 1872
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA---EEIRKEKEAVIEEELDEEDEKRR 1793
|
730 740
....*....|....*....|....*.
gi 1591544934 1873 QElIDKLQAKVKSYKRQAEEAEDQAN 1898
Cdd:PTZ00121 1794 ME-VDKKIKDIFDNFANIIEGGKEGN 1818
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1211-1924 |
3.33e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 95.21 E-value: 3.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1211 LSEQIDSLQRVKQKLEKERSEAKMEVDDlASTVEQLSKGKAS--AEKTCRLYEDQMNEAKAKVEELQR---QLNETNSHR 1285
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKKKAED-ARKAEEARKAEDArkAEEARKAEDAKRVEIARKAEDARKaeeARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1286 ARAQAESSELSRKLEEREATVSQLQRSKNSFSQNVEELKKQLEEENKAKNALAHALQSSRhdcdllreqyDEEQEAKAEL 1365
Cdd:PTZ00121 1178 AEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKK----------DAEEAKKAEE 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1366 QRAlskaNGEVAQWRTKYETDAIQRTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDlvvdleraSA 1445
Cdd:PTZ00121 1248 ERN----NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE--------AK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1446 AAAALDKKQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELFKLKNSyeetlehletiKRENKNLQEEITDLSDQIS 1525
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-----------AEAAEKKKEEAKKKADAAK 1384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1526 QGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLElnqiKADVDRKLAEKEEEIDNLRRNHQRTLESM 1605
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK----KADEAKKKAEEAKKADEAKKKAEEAKKAE 1460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1606 QATLDAEAKSRSEAVRLRKKMEGDLNEMEVQLNHANRLASESQKLlrnlqvqikdvqlelDETIHQNEELKEqvaVTERR 1685
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA---------------AEAKKKADEAKK---AEEAK 1522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1686 NNLLASEVEELRALLEQNDRARKLAEHELLEATErvnLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQ-ECRNAEEKAK 1764
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEE---LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMK 1599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1765 KAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQI-ALKGGKKQVQKLEARVKELENELESEQKKSQE 1843
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1844 YQKGVRKFERRIKELSYQGEEDKKnlvrmqelIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELDDAEERADMAET 1923
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKK--------AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
|
.
gi 1591544934 1924 Q 1924
Cdd:PTZ00121 1752 D 1752
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
851-1734 |
3.58e-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: 94.86 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 851 AATEKELASLKEELAKLKEALEKSEVKRKELEErqvsliqekndlslQLQAEQDNLADAEdrcdlliKTKIQLEAKVKEI 930
Cdd:pfam01576 380 QALESENAELQAELRTLQQAKQDSEHKRKKLEG--------------QLQELQARLSESE-------RQRAELAEKLSKL 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 931 MERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETilkltkekkalqea 1010
Cdd:pfam01576 439 QSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQ-------------- 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1011 hqqtlddLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSMESVMDLENDKQQLEEKLKK 1090
Cdd:pfam01576 505 -------LEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNR 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1091 KDFEMNEMSTRIEDEQSLVNQLQKKIKEL-----QARTEELEEELEADRACRAKVEKqrgdvareleelserleesggat 1165
Cdd:pfam01576 578 LQQELDDLLVDLDHQRQLVSNLEKKQKKFdqmlaEEKAISARYAEERDRAEAEAREK----------------------- 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1166 saqieinkkrETDILKLRRDLEEAMlhheattaglrkkhadsvaelsEQIDSLQRVKQKLekerseaKMEVDDLASTVEQ 1245
Cdd:pfam01576 635 ----------ETRALSLARALEEAL----------------------EAKEELERTNKQL-------RAEMEDLVSSKDD 675
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1246 LSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRAR----AQAESSELSRKLEEREatvsqlqrsknsfsqnve 1321
Cdd:pfam01576 676 VGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRlevnMQALKAQFERDLQARD------------------ 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1322 elkkqleeenkaknalahalqssrhdcdllreqydeeqEAKAELQRALSKangEVAQWRTKYETDAIQRTEELeESKKKL 1401
Cdd:pfam01576 738 --------------------------------------EQGEEKRRQLVK---QVRELEAELEDERKQRAQAV-AAKKKL 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1402 AVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLErasaaaaaldkkqrnfdkvlaEWRQKCEECQAELETSQKE 1481
Cdd:pfam01576 776 ELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELE---------------------EARASRDEILAQSKESEKK 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1482 SRSLSTELFKLKnsyeetlEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEH 1561
Cdd:pfam01576 835 LKNLEAELLQLQ-------EDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTEL 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1562 EESKTLRIQLELNQIKADV--DRKLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAvrLRKKMEGDLNEMEVQLNH 1639
Cdd:pfam01576 908 LNDRLRKSTLQVEQLTTELaaERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKS--SIAALEAKIAQLEEQLEQ 985
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1640 ANRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTERRNNLLASEVEELRALLEQNDRARKLAEHELLEATE 1719
Cdd:pfam01576 986 ESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATE 1065
|
890
....*....|....*
gi 1591544934 1720 RVNLLHSQNTSLINQ 1734
Cdd:pfam01576 1066 SNESMNREVSTLKSK 1080
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
224-714 |
4.06e-18 |
|
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: 91.34 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 224 IIEANPAMEAFGNAKTLRNDNSSRFGKF--IRIHFGPTG---KLASADIDIYLLEKSRVIFQQ------PGERSYHIYYQ 292
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 293 IMSQ----------KKPELLDMLLVSSNPY----DYH---FCSQGVTTVENLDDGQELMatdHAMDILGFLPDEKYGCYK 355
Cdd:cd14894 329 MVAGvnafpfmrllAKELHLDGIDCSALTYlgrsDHKlagFVSKEDTWKKDVERWQQVI---DGLDELNVSPDEQKTIFK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 356 IVGAIMHFGNMKFKQKQREEQAEADGT---ESADKASYLMGVSSADLIKGLLHPR---VKVGNEYVVKGQNVEQVTYAVG 429
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 430 ALAKATYDRMFKWLVGRINRTLY----------------TSLPRQY-FIGVLDIAGFEIFELNSFEQLCINFTNEKL--- 489
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATKmsalstdgnkhqmdsnASAPEAVsLLKIVDVFGFEDLTHNSLDQLCINYLSEKLyar 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 490 -QQFF------NHHMFILEQEEykregiDWTFIdfgldlqacidlIEKPLGIMSILEEECMFPKATDNS----------F 552
Cdd:cd14894 566 eEQVIavayssRPHLTARDSEK------DVLFI------------YEHPLGVFASLEELTILHQSENMNaqqeekrnklF 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 553 KAKMYDNHLGKSPNFQKPRPDKKRKYEA-----HFELVHYAGVVPYNIIGWLDKNKDPLNETVVACFqKSSNKLLACLYE 627
Cdd:cd14894 628 VRNIYDRNSSRLPEPPRVLSNAKRHTPVllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGL-KTSNSSHFCRML 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 628 N---YIGSDSASEHKIGGKEKRKKAASFQTVSQLhKENLNKLMTNLRSTQPHFVRCIIPNETKTPGIMDAFLVLHQLRCN 704
Cdd:cd14894 707 NessQLGWSPNTNRSMLGSAESRLSGTKSFVGQF-RSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQ 785
|
570
....*....|
gi 1591544934 705 GVLEGIRICR 714
Cdd:cd14894 786 RLIRQMEICR 795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1390-1893 |
7.92e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 90.12 E-value: 7.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1390 RTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLqTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKCE 1469
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1470 ECQAELetsqKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEeitdlsdqISQGAKTIHELEKMKKGLEIEKSEIQ 1549
Cdd:PRK03918 325 GIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHELYEE--------AKAKKEELERLKKRLTGLTPEKLEKE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1550 -AALEEAEGTLEHEESKTLRIQLELNQIKADVDRKLAE---------------KEEEIDNLRRNHQRTLESMQATLdAEA 1613
Cdd:PRK03918 393 lEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKELLEEYTAELKRIEKEL-KEI 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1614 KSRSEAVRLRKKmegdlnEMEVQLNHANRLASESQ--KLLRNLQVQIKDVQLE-LDETIHQNEELKEQVAVTERRNNLLA 1690
Cdd:PRK03918 472 EEKERKLRKELR------ELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1691 SEVEELRALleqnDRARKLAEHELLEATERVNLLHSQNTSL-INQKKKLENDLSTLS------NEVDDAVQECRNAEEKA 1763
Cdd:PRK03918 546 KELEKLEEL----KKKLAELEKKLDELEEELAELLKELEELgFESVEELEERLKELEpfyneyLELKDAEKELEREEKEL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1764 KKAITDAAMMAEELkkeQDTSAHLERMKKNMEQtikdLQMRLDEAEQialKGGKKQVQKLEARVKELENELESEQKKSQE 1843
Cdd:PRK03918 622 KKLEEELDKAFEEL---AETEKRLEELRKELEE----LEKKYSEEEY---EELREEYLELSRELAGLRAELEELEKRREE 691
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1844 YQKGVRKFERRIKELSYQGEEDKKnLVRMQELIDKLQAKVKSYKRQAEEA 1893
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEK-LEKALERVEELREKVKKYKALLKER 740
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1236-1931 |
1.78e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 89.36 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1236 VDDLAStVEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQaESSELSRKLEEREATVsqlqrskns 1315
Cdd:TIGR02169 159 IDEIAG-VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYE--------- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1316 fsqnveelkkqleeenkaknaLAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTKYEtdaiQRTEELE 1395
Cdd:TIGR02169 228 ---------------------LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE----ELNKKIK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1396 ESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHR----LQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEW------- 1464
Cdd:TIGR02169 283 DLGEEEQLRVKEKIGELEAEIASLERSIAEKEReledAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLteeyael 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1465 RQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIE 1544
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1545 KSEIQAALEEAEGTLEHEESKTLRIQLELNQIKADVDRklaeKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLRK 1624
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR----VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1625 KMEG------DLNEMEVQLNHA------NRL----------ASESQKLLRNLQV---------QIKDVQLELDeTIHQN- 1672
Cdd:TIGR02169 519 SIQGvhgtvaQLGSVGERYATAievaagNRLnnvvveddavAKEAIELLKRRKAgratflplnKMRDERRDLS-ILSEDg 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1673 -----------EELKEQVAVTERRNNLLASEVEELRALLEQ--------------------NDRARKLA------EHELL 1715
Cdd:TIGR02169 598 vigfavdlvefDPKYEPAFKYVFGDTLVVEDIEAARRLMGKyrmvtlegelfeksgamtggSRAPRGGIlfsrsePAELQ 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1716 EATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNME 1795
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1796 QTIKDLQMRLDEAE-------------------------QIALKGGKKQVQKLEARVKELENEL-------ESEQKKSQE 1843
Cdd:TIGR02169 758 SELKELEARIEELEedlhkleealndlearlshsripeiQAELSKLEEEVSRIEARLREIEQKLnrltlekEYLEKEIQE 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1844 YQKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELDDAEERADMAET 1923
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
....*...
gi 1591544934 1924 QVTKLRVR 1931
Cdd:TIGR02169 918 RLSELKAK 925
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
861-1539 |
2.53e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.29 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 861 KEE-LAKLKEA---LEKSEVKRKELEeRQVSliqekndlSLQLQAEQ----DNLADAEDRCD--LLIKTKIQLEAKVKEI 930
Cdd:COG1196 174 KEEaERKLEATeenLERLEDILGELE-RQLE--------PLERQAEKaeryRELKEELKELEaeLLLLKLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 931 MERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALQEA 1010
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1011 HQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEgdlklsmesvmdlendkQQLEEKLKK 1090
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE-----------------EELEELAEE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1091 KDFEMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRGDVARELEELSERLEESGGATSAQIE 1170
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1171 INKK------------RETDILKLRRDLEEAML--HHEATTAGLRKKHADSVAELSEQIDSLQRVKQKLEKERSEAkmev 1236
Cdd:COG1196 468 LLEEaalleaalaellEELAEAAARLLLLLEAEadYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA---- 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1237 ddLASTVEQLSKGKASAEKTCRLYEDQMNEAKAKVEELqrqlnetNSHRARAQAESSELSRKLEEREATVSQLQRSKNSF 1316
Cdd:COG1196 544 --LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL-------DKIRARAALAAALARGAIGAAVDLVASDLREADAR 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1317 SQNVEELKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQwrtkyetdAIQRTEELEE 1396
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE--------AEAELEELAE 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1397 SKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLvvdLERASAAAAALDKKQRNFDKVLAEWRQKCEECQAELE 1476
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL---EEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1477 TSQKESRSLSTELFKLKN-------SYEETLEHLETIKRENKNLQEEITDLsdqisqgAKTIHELEKMKK 1539
Cdd:COG1196 764 ELERELERLEREIEALGPvnllaieEYEELEERYDFLSEQREDLEEARETL-------EEAIEEIDRETR 826
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1389-1917 |
2.62e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.03 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1389 QRTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKhrlqTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKC 1468
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1469 EECQaELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKgleiEKSEI 1548
Cdd:PRK03918 276 EELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK----KLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1549 QAALEEAEGTLEHEEsKTLRIQLELNQIKADVDRKLAEK-EEEIDNLRRNHQ------RTLESMQATLDAEAKSRSEAVR 1621
Cdd:PRK03918 351 EKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEeieeeiSKITARIGELKKEIKELKKAIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1622 LRKKMEGdlnemevQLNHANRLASESQK--LLRNLQVQIKDVQLELDETIHQNEELK------EQVAVTERRNNLLASEV 1693
Cdd:PRK03918 430 ELKKAKG-------KCPVCGRELTEEHRkeLLEEYTAELKRIEKELKEIEEKERKLRkelrelEKVLKKESELIKLKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1694 EELRALLEqndrarKLAEHELLEATERVNLLHSQNTSLInqkkKLENDLSTLSNEVDDAvqecrNAEEKAKKAITDAAMM 1773
Cdd:PRK03918 503 EQLKELEE------KLKKYNLEELEKKAEEYEKLKEKLI----KLKGEIKSLKKELEKL-----EELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1774 AEELKKEQdtsahLERMKKNMEQTIKDLQMRLDEAEQ-----IALKGGKKQVQKLEARVKELENELESEQKKSQEYQKGV 1848
Cdd:PRK03918 568 LEEELAEL-----LKELEELGFESVEELEERLKELEPfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1849 RKFERRIKELSYQ-GEEDKKNLVRMQELIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELDDAEER 1917
Cdd:PRK03918 643 EELRKELEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1009-1802 |
4.61e-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: 81.32 E-value: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1009 EAHQQTLDDLQAEEDKVNTLTKAQA-KLEQQVDDLEGSLEQ---EKKLRMDLERVKRKLEGDLKLSME-SVMDLENDKQQ 1083
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELHEKQKfYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLRNQLQnTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1084 LEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELeaDRACRAKVEKQRGDVARELEELSERLEESGG 1163
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEH--DSMSTMHFRSLGSAISKILRELDTEISYLKG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1164 ---ATSAQIEINKKRETDILKL-----RRDLEEAMLHHEATTAGLRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKME 1235
Cdd:pfam15921 239 rifPVEDQLEALKSESQNKIELllqqhQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQ 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1236 VDDLASTVEQLskgKASAEKTCRLYEDQmneakakVEELQRQLNETNSHRARAQAESSELSrklEEREATVSQLQRskns 1315
Cdd:pfam15921 319 LSDLESTVSQL---RSELREAKRMYEDK-------IEELEKQLVLANSELTEARTERDQFS---QESGNLDDQLQK---- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1316 FSQNVEELKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQeakAELQR--ALSKANGEVAQWRTKYETDAIqrtee 1393
Cdd:pfam15921 382 LLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRN---MEVQRleALLKAMKSECQGQMERQMAAI----- 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1394 leeskkklavrlQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVdlerasaAAAALDKKQRNFDKVLAEWRQKceecqa 1473
Cdd:pfam15921 454 ------------QGKNESLEKVSSLTAQLESTKEMLRKVVEELTA-------KKMTLESSERTVSDLTASLQEK------ 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1474 eletsQKESRSLSTELFKLKNSYEETLEHLETIKREN---KNLQEEITDLSDQISQGAKTI----HELEKMKKgLEIEKS 1546
Cdd:pfam15921 509 -----ERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEKDKVIeilrQQIENMTQ-LVGQHG 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1547 EIQAALEEAEGTLEHE-ESKTLRIQlELNQIKADVDRKLAEKEEEIDNlrrnhqrtLESMQATLDAEAKSRSEAVR-LRK 1624
Cdd:pfam15921 583 RTAGAMQVEKAQLEKEiNDRRLELQ-EFKILKDKKDAKIRELEARVSD--------LELEKVKLVNAGSERLRAVKdIKQ 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1625 KMEGDLNEMEVQLNHANRLASESQKLLRN--------------LQVQIKDVQLELDETIHQNEELK------------EQ 1678
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNSLSEDYEVLKRNfrnkseemetttnkLKMQLKSAQSELEQTRNTLKSMEgsdghamkvamgMQ 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1679 VAVTERRnnllaSEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQECRN 1758
Cdd:pfam15921 734 KQITAKR-----GQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVAN 808
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 1591544934 1759 AEEKAKKAITDAAMMAEELKKEQDTSAhleRMKKNMEQTIKDLQ 1802
Cdd:pfam15921 809 MEVALDKASLQFAECQDIIQRQEQESV---RLKLQHTLDVKELQ 849
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
920-1807 |
5.16e-15 |
|
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: 81.17 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 920 KIQLEAKVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILK 999
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1000 LTKEKKALQEAhqqtldDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSMESVMDLEN 1079
Cdd:pfam02463 248 DEQEEIESSKQ------EIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1080 DKQQLEEKLKKKDFEMNEmstriedeqslvnqlQKKIKELQARTEELEEELEADRACRAKVEKQRGDVARELEELSERLE 1159
Cdd:pfam02463 322 EKKKAEKELKKEKEEIEE---------------LEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1160 ESGGATSAQIEINKKRETDILKLRRDLEEAMLHHEATtagLRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDL 1239
Cdd:pfam02463 387 SSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKE---EKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1240 ASTVEQLSKGKASAEKTcrlyedqmNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVsqlqRSKNSFSQN 1319
Cdd:pfam02463 464 ELELKKSEDLLKETQLV--------KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGG----RIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1320 VEELKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTKYETDAIQRTEELEESKK 1399
Cdd:pfam02463 532 GDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1400 KLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDL--VVDLERASAAAAALDKKQRNFDKVLAEWRQKCEECQAELET 1477
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLrkGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1478 SQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEG 1557
Cdd:pfam02463 692 EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1558 TLEHEESKTLRIQLELNQIKADVDRKLAEKEEEIDNLRRNHQ--RTLESMQATLDAEAKSRSEAVRLRKKMEGDLNEMEV 1635
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEaeLLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKL 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1636 QLNHANRLASESQKLLRNLQVQIKDVQLElDETIHQNEELKEQVAVTERRnnllaSEVEELRALLEQNDRARKLAEHELL 1715
Cdd:pfam02463 852 AEEELERLEEEITKEELLQELLLKEEELE-EQKLKDELESKEEKEKEEKK-----ELEEESQKLNLLEEKENEIEERIKE 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1716 EATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNME 1795
Cdd:pfam02463 926 EAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
890
....*....|..
gi 1591544934 1796 QTIKDLQMRLDE 1807
Cdd:pfam02463 1006 KLIRAIIEETCQ 1017
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
32-76 |
5.32e-15 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 70.54 E-value: 5.32e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1591544934 32 DGKKRAWIPDEKEAYIEIEIKELSGDKVIVETKDGRTLTVKDCDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
852-1604 |
1.22e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.19 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 852 ATEKELASLKEELAKLKEALEKSEVKRKE--LEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLL-----IKTKIQLE 924
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEVRKAEelRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVkkaeeAKKDAEEA 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 925 AKVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEiTLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEK 1004
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK-KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAK 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1005 KALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEgDLKLSMESVMDLENDKQQL 1084
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD-AAKKKAEEKKKADEAKKKA 1400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1085 EEKLKKKD-FEMNEMSTRIEDEQSLVNQLQKKIKELQARteeleeeleADRACRAKVEKQRGDVARELEELSERLEESGG 1163
Cdd:PTZ00121 1401 EEDKKKADeLKKAAAAKKKADEAKKKAEEKKKADEAKKK---------AEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1164 ATSAQIEINKKRETDILKLRRDlEEAMLHHEATTAGLRKKHADSVAELSEQidslqrvKQKLEKERSEAKMEVDDLASTV 1243
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEAKKAEEA-------KKADEAKKAEEAKKADEAKKAE 1543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1244 EqlskgKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAqaessELSRKLEER--EATVSQLQRSKNSFSQNVE 1321
Cdd:PTZ00121 1544 E-----KKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA-----EEAKKAEEAriEEVMKLYEEEKKMKAEEAK 1613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1322 ELKKQLEEENKAKNAlahalQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTKYETDAiQRTEEL----EES 1397
Cdd:PTZ00121 1614 KAEEAKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkkaeEDE 1687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1398 KKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEdlvvdlERASAAAAALDKKQRNFDKVLAEWRQKCEECQAELET 1477
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA------EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH 1761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1478 SQKESRSLSTELFKLKNSY--EETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKglEIEKSEIQAALEEA 1555
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK--EMEDSAIKEVADSK 1839
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1591544934 1556 EGTLEhEESKTLRIQLELNQIKADVDRKLAEKEEEIDNLRRNHQRTLES 1604
Cdd:PTZ00121 1840 NMQLE-EADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA 1887
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1428-1935 |
2.61e-14 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 79.01 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1428 RLQTEIEDLVVDLERASAAAAALDKKQRNF-DKVLAEWRQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETI 1506
Cdd:pfam15921 78 RVLEEYSHQVKDLQRRLNESNELHEKQKFYlRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1507 KRENKNLQEeitDLSDQISQGAKTIHELEkmkkGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLElnQIKADVDRKLAE 1586
Cdd:pfam15921 158 KCLKEDMLE---DSNTQIEQLRKMMLSHE----GVLQEIRSILVDFEEASGKKIYEHDSMSTMHFR--SLGSAISKILRE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1587 KEEEIDNLRrNHQRTLESMQATLDAEAKSRSEAV--RLRKKMEGDLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQle 1664
Cdd:pfam15921 229 LDTEISYLK-GRIFPVEDQLEALKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQ-- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1665 ldetihqnEELKEQVAVTERRNNLLASEVEELRALLEQndrARKLAEHELLEATERVNLLHSQntslinqkkklendLST 1744
Cdd:pfam15921 306 --------EQARNQNSMYMRQLSDLESTVSQLRSELRE---AKRMYEDKIEELEKQLVLANSE--------------LTE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1745 LSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQialkggkkQVQKLE 1824
Cdd:pfam15921 361 ARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM--------EVQRLE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1825 ARVKELENELESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKR----------QAEEAE 1894
Cdd:pfam15921 433 ALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERtvsdltaslqEKERAI 512
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1895 DQANTNLSKYR--------KLQHELDDAEE-RADMAETQVTKLRVRTRDQ 1935
Cdd:pfam15921 513 EATNAEITKLRsrvdlklqELQHLKNEGDHlRNVQTECEALKLQMAEKDK 562
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1392-1925 |
2.63e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 78.52 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1392 EELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDK---VLAEWRQKC 1468
Cdd:TIGR04523 134 KENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELllsNLKKKIQKN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1469 EECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEI 1548
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1549 QAALEEAEGTLEHEESKTLRIQLELNQIK-ADVDRKLAEKEEEIDNLRRnhqrTLESMQATLDaeaKSRSEAVRLRKKME 1627
Cdd:TIGR04523 294 KSEISDLNNQKEQDWNKELKSELKNQEKKlEEIQNQISQNNKIISQLNE----QISQLKKELT---NSESENSEKQRELE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1628 GDLNEMEVQLNHANRLASESQkllrNLQVQIKDVQLELDETIHQNEELKEQVAVTERRNNLLASEVEELRALLEQNdrar 1707
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIK----NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN---- 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1708 klaEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQECrnaeEKAKKAITDAAMMAEELKKEqdtsahl 1787
Cdd:TIGR04523 439 ---NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL----EQKQKELKSKEKELKKLNEE------- 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1788 ermKKNMEQTIKDLQMRLDEAeqialkggKKQVQKLEARVKELENELES---------EQKKSQEYQKGVRKFERRIKEL 1858
Cdd:TIGR04523 505 ---KKELEEKVKDLTKKISSL--------KEKIEKLESEKKEKESKISDledelnkddFELKKENLEKEIDEKNKEIEEL 573
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1591544934 1859 SYQGEEDKKNLVRMQELIDKLQAKVK-------SYKRQAEEAEDQANTNLSKYRKLQHELDDAEERADMAETQV 1925
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQELIDQKEKEKKdlikeieEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
980-1679 |
2.63e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 78.52 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 980 ENKVKNLIEEMAALDETILKLTKEKKALQeahqqtlDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERV 1059
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLD-------KNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1060 KRKLEGDLKLSMESVMDLENDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELEadracraK 1139
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELN-------L 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1140 VEKQRgdvareleelserleesggatsaqieINKKRETDILKLRRDLEEAMLHHEATTAGLRKKHADSVAELSEQIDSLQ 1219
Cdd:TIGR04523 178 LEKEK--------------------------LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1220 RVKQKLEKERSEAKMEvddLASTVEQLSKGKASAEKTCRLYED---QMNEAKAKVEELQRQLNETNS-----HRARAQAE 1291
Cdd:TIGR04523 232 DNIEKKQQEINEKTTE---ISNTQTQLNQLKDEQNKIKKQLSEkqkELEQNNKKIKELEKQLNQLKSeisdlNNQKEQDW 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1292 SSELSRKLEEREatvSQLQRSKNSFSQNveelkkqleeeNKAKNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSK 1371
Cdd:TIGR04523 309 NKELKSELKNQE---KKLEEIQNQISQN-----------NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1372 ANGEVAQWRtkyetdaiQRTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALD 1451
Cdd:TIGR04523 375 LKKENQSYK--------QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1452 KKQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTI 1531
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1532 HELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKT--LRIQLELNQIKAD---VDRKLAEKEEEIDNLRRNhQRTLESMQ 1606
Cdd:TIGR04523 527 EKLESEKKEKESKISDLEDELNKDDFELKKENLEKeiDEKNKEIEELKQTqksLKKKQEEKQELIDQKEKE-KKDLIKEI 605
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1591544934 1607 ATLDAEAKSRSEAVRLRKKMEGDLNEMEVQLNHAnrlASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQV 1679
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK---KNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1475-1941 |
3.32e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1475 LETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEE 1554
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1555 AEGtLEHEESKTLRIQLELNQIKADVDRKLAEKEEEIDNLRRNHQRTLEsmqatLDAEAKSRSEAVRLRKKMEGDLNEME 1634
Cdd:PRK03918 240 IEE-LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-----LKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1635 VQLNHANRLASESQKLLRNLQ---VQIKDVQLELDETIHQNEELKEQVAVTERRNNLLAS-----------EVEELRALL 1700
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlkkrltglTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1701 EQNDRARKLAEHELLEATERVNLLHSQNTSL---INQKKKLENDLSTLSNEVDD------------AVQECRNAEEKAKK 1765
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELkkaIEELKKAKGKCPVCGRELTEehrkelleeytaELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1766 AITDAAMMAEELKKEQDTSAHLERMKKNMEQtIKDLQMRLDEAEQIALKGGKKQVQKLEARVKELENE---LESEQKKSQ 1842
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEiksLKKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1843 EYQKGVRKFERRIKELsyqgEEDKKNLVR---------MQELIDKLQAKVKSYKR--QAEEAEDQANTNLSKYRKLQHEL 1911
Cdd:PRK03918 553 ELKKKLAELEKKLDEL----EEELAELLKeleelgfesVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEEL 628
|
490 500 510
....*....|....*....|....*....|
gi 1591544934 1912 DDAEERADMAETQVTKLRVRTRDQGSKFAE 1941
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKKYSE 658
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1616-1922 |
5.33e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.05 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1616 RSEAVRLRKKMEGDLN-------EMEVQLNhanRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTERRNNL 1688
Cdd:COG1196 174 KEEAERKLEATEENLErledilgELERQLE---PLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1689 LASEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLENDLS--------------TLSNEVDDAVQ 1754
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArleerrreleerleELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1755 ECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKgGKKQVQKLEARVKELENEL 1834
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE-ALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1835 ESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELDDA 1914
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
....*...
gi 1591544934 1915 EERADMAE 1922
Cdd:COG1196 490 AARLLLLL 497
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
855-1866 |
1.14e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 77.01 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 855 KELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSL---QLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEIM 931
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSkeaQLESSREIVKSYENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 932 ErLEDEEEMSATVLAKKRKLEDECAELKKDIddLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALQEAH 1011
Cdd:TIGR00606 266 K-LDNEIKALKSRKKQMEKDNSELELKMEKV--FQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1012 -----QQTLDDLQAEEDKVNTLTKAQAKLEQQ----VDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSMESVMDLENDKQ 1082
Cdd:TIGR00606 343 tellvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKER 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1083 QLEEKLKKKDFEMNEMSTRIEDEQSL----VNQLQKKIKELQARTEELEEELEADRACRakveKQRGDVARELEELSERL 1158
Cdd:TIGR00606 423 LKQEQADEIRDEKKGLGRTIELKKEIlekkQEELKFVIKELQQLEGSSDRILELDQELR----KAERELSKAEKNSLTET 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1159 EEsggatsAQIEINKKRETDILKLRRDLEEAM--LHHEATTaglrKKHADSVAElsEQIDSLQRVKQKLEKERSEAKMEV 1236
Cdd:TIGR00606 499 LK------KEVKSLQNEKADLDRKLRKLDQEMeqLNHHTTT----RTQMEMLTK--DKMDKDEQIRKIKSRHSDELTSLL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1237 DDLASTvEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEE---REATVSQLQRSK 1313
Cdd:TIGR00606 567 GYFPNK-KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDvcgSQDEESDLERLK 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1314 NSFSQNveelkkqleEENKAKNALAHALQSSrhdcdLLREQYDEEQEAKAELQRALskangevaqwrtkyetdaiQRTEE 1393
Cdd:TIGR00606 646 EEIEKS---------SKQRAMLAGATAVYSQ-----FITQLTDENQSCCPVCQRVF-------------------QTEAE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1394 LEESKKKLAVRLQEAEEAVEasnakcsSLEKTKHRLQTEIEDLVVDLErasAAAAALDKKQRnfdkvlaewrqkceecqa 1473
Cdd:TIGR00606 693 LQEFISDLQSKLRLAPDKLK-------STESELKKKEKRRDEMLGLAP---GRQSIIDLKEK------------------ 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1474 ELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSdqisqgakTIHELEKMKKGLEIEKSEIQAALE 1553
Cdd:TIGR00606 745 EIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVT--------IMERFQMELKDVERKIAQQAAKLQ 816
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1554 EAEGTLEHEEsktlriqleLNQIKADVD---RKLAEKEEEIDNLRRNHQRTLESMQATLD---AEAKSRSEAVRLRKKME 1627
Cdd:TIGR00606 817 GSDLDRTVQQ---------VNQEKQEKQhelDTVVSKIELNRKLIQDQQEQIQHLKSKTNelkSEKLQIGTNLQRRQQFE 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1628 GDLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNEElkeqvavterRNNLLASEVEELRALLEQNDRAR 1707
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKET----------SNKKAQDKVNDIKEKVKNIHGYM 957
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1708 KLAEHELLEATERvnllhsqntslinQKKKLENDLSTLSNEVDDAVQECRNAEE--KAKKAITDAAMMAEELKKEQDTSA 1785
Cdd:TIGR00606 958 KDIENKIQDGKDD-------------YLKQKETELNTVNAQLEECEKHQEKINEdmRLMRQDIDTQKIQERWLQDNLTLR 1024
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1786 HLERMKKNMEQTIKDLqmrLDEAEQIALKGGKKQVQKLEARVKELENELESEQKKSQEYQKGVRKFERRIKELSYQGEED 1865
Cdd:TIGR00606 1025 KRENELKEVEEELKQH---LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEE 1101
|
.
gi 1591544934 1866 K 1866
Cdd:TIGR00606 1102 K 1102
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
854-1591 |
1.89e-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: 76.16 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 854 EKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLAdaedrcdlLIKTKIQLEAKVKEIMER 933
Cdd:pfam02463 278 EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK--------KEKEEIEELEKELKELEI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 934 LEDEEEmsaTVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALQEAHQQ 1013
Cdd:pfam02463 350 KREAEE---EEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1014 TLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSMESVMDLENDKQQLEEKLKKKDF 1093
Cdd:pfam02463 427 EELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKAR 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1094 EMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRGDVARELEELSERLEESGGATSAQIEINK 1173
Cdd:pfam02463 507 SGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPK 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1174 KRETDILKLRRDLEEAMLHHEATTAGLRKKHADSVAELSEqiDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKASA 1253
Cdd:pfam02463 587 LKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVE--GILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1254 EKTCRLyEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQNVEELKKQLEEENKA 1333
Cdd:pfam02463 665 KASLSE-LTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQ 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1334 KNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTKYETDAIQRTEELEESKKKLAVRLQEAEEAVE 1413
Cdd:pfam02463 744 KIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLL 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1414 ASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALD-------KKQRNFDKVLAEWRQKCEECQAELETSQKESRSLS 1486
Cdd:pfam02463 824 IEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEeitkeelLQELLLKEEELEEQKLKDELESKEEKEKEEKKELE 903
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1487 TELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKT 1566
Cdd:pfam02463 904 EESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEF 983
|
730 740
....*....|....*....|....*
gi 1591544934 1567 LRIQLELNQIKADVDRKLAEKEEEI 1591
Cdd:pfam02463 984 EEKEERYNKDELEKERLEEEKKKLI 1008
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
843-1695 |
3.81e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 75.39 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 843 KIKPLLKSAATEKELASLKEELAKLKEALEKSE----VKRKELEERQVSLIQEKNDLSLQLQAEQdnladaedrcDLLIK 918
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKKKEALKKLIEETENLAeliiDLEELKLQELKLKEQAKKALEYYQLKEK----------LELEE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 919 TKIQLEAKVKEIMERLEDEEEmsatvlaKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETIL 998
Cdd:pfam02463 224 EYLLYLDYLKLNEERIDLLQE-------LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 999 KLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVK---RKLEGDLKLSMESVM 1075
Cdd:pfam02463 297 ELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEeelEKLQEKLEQLEEELL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1076 DLENDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELEadracraKVEKQRGDVARELEELS 1155
Cdd:pfam02463 377 AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL-------EEEEESIELKQGKLTEE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1156 ERLEESGGATSAQIEINKKRETDILKLRRDLEEAMLHHEAttAGLRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKME 1235
Cdd:pfam02463 450 KEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELL--LSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISA 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1236 VDDLASTVEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNS 1315
Cdd:pfam02463 528 HGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQ 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1316 FSQNVEELKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTK-YETDAIQRTEEL 1394
Cdd:pfam02463 608 LDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKElLEIQELQEKAES 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1395 EESKKKlaVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKCEECQA- 1473
Cdd:pfam02463 688 ELAKEE--ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEe 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1474 ELETSQKESRSLSTELFKLKNSYEETLEHLEtiKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEiEKSEIQAALE 1553
Cdd:pfam02463 766 KSELSLKEKELAEEREKTEKLKVEEEKEEKL--KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKE-EELEELALEL 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1554 EAEGTLEHEESKTLRIQLELNQIKADVDRKLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLRKKMEGDLNEM 1633
Cdd:pfam02463 843 KEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEER 922
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1591544934 1634 EVQLNHANRLASESQKLLRNLQVQIKDVQLELDET-IHQNEELKEQVAVTERRNNLLASEVEE 1695
Cdd:pfam02463 923 IKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEeEERNKRLLLAKEELGKVNLMAIEEFEE 985
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
848-1429 |
5.07e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 74.77 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 848 LKSAATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNladAEDRCDLLIKTKIQLEAKV 927
Cdd:pfam15921 250 LKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTV 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 928 KEIMERLEDeeemsatvlaKKRKLEDECAELKKD--IDDLEITLAKVEKEKHATENkvKNLIEEMAALDETILKLTKEKK 1005
Cdd:pfam15921 327 SQLRSELRE----------AKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQLQKLLADLHKREKELS 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1006 ALQEAHQ-----------------QTLDDLQAEEDKVNTLTKA-----QAKLEQQVDDLEG---SLEQEKKLRMDLERVK 1060
Cdd:pfam15921 395 LEKEQNKrlwdrdtgnsitidhlrRELDDRNMEVQRLEALLKAmksecQGQMERQMAAIQGkneSLEKVSSLTAQLESTK 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1061 ---RKLEGDL---KLSMES----VMDLENDKQQLEEKLKKKDFEMNEMSTRIEdeqslvnqlqKKIKELQARTEELEEEL 1130
Cdd:pfam15921 475 emlRKVVEELtakKMTLESsertVSDLTASLQEKERAIEATNAEITKLRSRVD----------LKLQELQHLKNEGDHLR 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1131 EADRACRA----------KVEKQRGDVARELEELSERLEESGG--ATSAQI--EINKKR-ETDILKLRRDLEEAMLHH-E 1194
Cdd:pfam15921 545 NVQTECEAlklqmaekdkVIEILRQQIENMTQLVGQHGRTAGAmqVEKAQLekEINDRRlELQEFKILKDKKDAKIRElE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1195 ATTAGLRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKAS-------AEKTCRLYEDQMNEA 1267
Cdd:pfam15921 625 ARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNfrnkseeMETTTNKLKMQLKSA 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1268 KAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQNVEELKKQLEEENKAKNALAHALQSSRH- 1346
Cdd:pfam15921 705 QSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATe 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1347 ------DCDLLREQYDEEQEAKAELQRALSKANGEVAQWRtkyetDAIQRTEEleeskKKLAVRLQEAEEAVEASNAKCS 1420
Cdd:pfam15921 785 knkmagELEVLRSQERRLKEKVANMEVALDKASLQFAECQ-----DIIQRQEQ-----ESVRLKLQHTLDVKELQGPGYT 854
|
....*....
gi 1591544934 1421 SLEKTKHRL 1429
Cdd:pfam15921 855 SNSSMKPRL 863
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
849-1400 |
8.57e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.41 E-value: 8.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 849 KSAATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDlsLQLQAEQDNLAD-AEDRCDLLIKTKIQLEAKV 927
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE--AKKKAEEAKKADeAKKKAEEAKKKADAAKKKA 1338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 928 KEIMERLE--DEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKK 1005
Cdd:PTZ00121 1339 EEAKKAAEaaKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1006 ALQEAHQqtlddlQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGD-LKLSMESVMDLENDKQQL 1084
Cdd:PTZ00121 1419 KADEAKK------KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAEEAKKADEAKKKA 1492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1085 EEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQA--------RTEELEEELEADRACRAKVEKQRGDVARELEELSE 1156
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKaeeakkadEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA 1572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1157 RLEESGGATSAQI--EINKKRETDILKLRRDL-----EEAMLHHEATTAGLRKKHADSVAELSEQIDSLQ----RVKQKL 1225
Cdd:PTZ00121 1573 EEDKNMALRKAEEakKAEEARIEEVMKLYEEEkkmkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEaeekKKAEEL 1652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1226 EKERSEAKMEVDDLASTVEQlSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREAT 1305
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEE-DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1306 VSQLQRSKNSFSQNVEELKKQLEEENK----AKNALAHALQSSRHDCDLLREQYDEEQEA-KAELQRAL--SKANGEVAQ 1378
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKDEEEKKKiahlKKEEEKKAEEIRKEKEAVIEEELDEEDEKrRMEVDKKIkdIFDNFANII 1811
|
570 580
....*....|....*....|..
gi 1591544934 1379 WRTKYETDAIQRTEELEESKKK 1400
Cdd:PTZ00121 1812 EGGKEGNLVINDSKEMEDSAIK 1833
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1335-1927 |
2.07e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.87 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1335 NALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQwrtKYETDAIQRTEELEESKKKlAVRLQEAEEAVEA 1414
Cdd:PTZ00121 1061 EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAK---KTETGKAEEARKAEEAKKK-AEDARKAEEARKA 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1415 SNA-KCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELFKLK 1493
Cdd:PTZ00121 1137 EDArKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEE 1216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1494 NSYEETLEHLETIKR---------ENKNLQEEITDLSDQISQGAKTIH--------ELEKMKKGLEIEKSEIQAALEEAE 1556
Cdd:PTZ00121 1217 ARKAEDAKKAEAVKKaeeakkdaeEAKKAEEERNNEEIRKFEEARMAHfarrqaaiKAEEARKADELKKAEEKKKADEAK 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1557 GTLEHEESKTLRIQLELNQIKADVDRKLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLRKKMEGDlnemEVQ 1636
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA----EKK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1637 LNHANRLASESQKLLRNLQvQIKDVQLELDETIHQNEELKEQVAVTERRNNLL--ASEVEELRALLEQNDRARKlAEHEL 1714
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKK-KADEAKKKAEEDKKKADELKKAAAAKKKADEAKkkAEEKKKADEAKKKAEEAKK-ADEAK 1450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1715 LEATERVNllhSQNTSLINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKAitDAAMMAEELKKEQDTSAHLERMKKNM 1794
Cdd:PTZ00121 1451 KKAEEAKK---AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA--DEAKKAAEAKKKADEAKKAEEAKKAD 1525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1795 EQTIKDLQMRLDEAEQIALKGGKKQVQKLEaRVKELENELESEQKKSQEYQK--GVRKFE-------RRIKELSYQGEED 1865
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEEDKnmALRKAEeakkaeeARIEEVMKLYEEE 1604
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1591544934 1866 KKnlVRMQELIDKLQAKVKSYKRQAEEAEDQANTNLSKY----RKLQHELDDAEERADMAETQVTK 1927
Cdd:PTZ00121 1605 KK--MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKeaeeKKKAEELKKAEEENKIKAAEEAK 1668
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1213-1912 |
2.26e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 72.45 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1213 EQIDSLQRVKQKLEKErseakmevddlastVEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETnshraraQAES 1292
Cdd:pfam05483 71 ENSEGLSRLYSKLYKE--------------AEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQEL-------QFEN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1293 SELSRKLEEreatvsQLQRSKNSFSQNveelkkqleeenkaknalahalQSSRHDCDLLRE--------------QYDEE 1358
Cdd:pfam05483 130 EKVSLKLEE------EIQENKDLIKEN----------------------NATRHLCNLLKEtcarsaektkkyeyEREET 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1359 QEAKAELQRALSKANGEVAQWRTKYETDAIQRTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVV 1438
Cdd:pfam05483 182 RQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1439 DLERASAAAAALDKKQRNFDKVLAEWRQKCEECQAELETSQKE-SRSLSTElfklknsyeETLEhletikrenKNLQEEI 1517
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSlQRSMSTQ---------KALE---------EDLQIAT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1518 TDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLELNQIKADVDRKLAEKEEeIDNLRRN 1597
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEE-MTKFKNN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1598 HQRTLESMQATLDAEAKSRSEavrlRKKMEGDLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKE 1677
Cdd:pfam05483 403 KEVELEELKKILAEDEKLLDE----KKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKT 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1678 QVAVTERRNNLLASEVEELraLLEQndraRKLAEhellEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQECR 1757
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKL--LLEN----KELTQ----EASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRD 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1758 NAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAeqialkggKKQVQKLEARVKELENELESE 1837
Cdd:pfam05483 549 ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL--------KKQIENKNKNIEELHQENKAL 620
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1591544934 1838 QKKSQEYQKGVRKFERRIKELSYQGEEDKKnlvRMQELIDKLQAKVKSYKRQAE---EAEDQANTNLSKYRKLQHELD 1912
Cdd:pfam05483 621 KKKGSAENKQLNAYEIKVNKLELELASAKQ---KFEEIIDNYQKEIEDKKISEEkllEEVEKAKAIADEAVKLQKEID 695
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
842-1295 |
2.65e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 842 FKIKPLLKSAATEKELASLKEELAKLKEALEKSEVKRKELEE---------RQVSLIQEKNDLSLQLQAEQDNLADAEDR 912
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEElkkklkeleKRLEELEERHELYEEAKAKKEELERLKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 913 cdLLIKTKIQLEAKVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLE-----ITLAKVEKEKHATEN------ 981
Cdd:PRK03918 381 --LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkCPVCGRELTEEHRKElleeyt 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 982 -KVKNLIEEMAALDETILKLTKEKKALQEA---------HQQTLDDLQAEEDKVNTLTKaqAKLEQQVDDLEGSLEQEKK 1051
Cdd:PRK03918 459 aELKRIEKELKEIEEKERKLRKELRELEKVlkkeselikLKELAEQLKELEEKLKKYNL--EELEKKAEEYEKLKEKLIK 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1052 LRMDLERVKRKLegdlklsmESVMDLENDKQQLEEKLKKKDFEMNEMSTRIEDEQ-SLVNQLQKKIKELQARTEELEEEL 1130
Cdd:PRK03918 537 LKGEIKSLKKEL--------EKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELK 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1131 EADRACRAKVEKQRgdvareleelserlEESGGATSAQIEINKKrETDILKLRRDLEEA-MLHHEATTAGLRKKHadsvA 1209
Cdd:PRK03918 609 DAEKELEREEKELK--------------KLEEELDKAFEELAET-EKRLEELRKELEELeKKYSEEEYEELREEY----L 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1210 ELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKASAEKtcrlyedqMNEAKAKVEELQRQLNE-TNSHRARA 1288
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK--------LEKALERVEELREKVKKyKALLKERA 741
|
....*..
gi 1591544934 1289 QAESSEL 1295
Cdd:PRK03918 742 LSKVGEI 748
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1206-1900 |
4.66e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 4.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1206 DSVAELSEQIDSLQRVKQKLEKERSEAKM------EVDDLASTVEQLSKGKASAEKTcRLYEDQmneakAKVEELQRQLN 1279
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELlepireLAERYAAARERLAELEYLRAAL-RLWFAQ-----RRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1280 ETNSHRARAQAESSELSRKLEEREATVSQLQRsknsfsqnveelkkqleeenkaknalahalqssrhdcDLLREQYDEEQ 1359
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEA-------------------------------------QIRGNGGDRLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1360 EAKAELQRALSKANgEVAQWRTKYETDAIQRTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVD 1439
Cdd:COG4913 342 QLEREIERLERELE-ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1440 LERASAAAAALDKKQRNFDKVLAEWRQK-CEECQ---------AEL-ETSQKES----------RSLSTELFKLKNSYEE 1498
Cdd:COG4913 421 LRELEAEIASLERRKSNIPARLLALRDAlAEALGldeaelpfvGELiEVRPEEErwrgaiervlGGFALTLLVPPEHYAA 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1499 TLEHLETIKRENK-NLQEEITDLSDQISQGAKTIHELEKmkkgLEIEKSEIQAALE------------EAEGTLEHEE-- 1563
Cdd:COG4913 501 ALRWVNRLHLRGRlVYERVRTGLPDPERPRLDPDSLAGK----LDFKPHPFRAWLEaelgrrfdyvcvDSPEELRRHPra 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1564 ---------SKTL------RIQLELNQIKADVDRKLAEKEEEIDNLRRNH---QRTLESMQATLDAEAKSRSEAVRLRKK 1625
Cdd:COG4913 577 itragqvkgNGTRhekddrRRIRSRYVLGFDNRAKLAALEAELAELEEELaeaEERLEALEAELDALQERREALQRLAEY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1626 MEGDLNEMEVQ-----LNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTERRNNLLASEVEELRALL 1700
Cdd:COG4913 657 SWDEIDVASAEreiaeLEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1701 EQNDRARKLAEHELLEatERVNLLHSQNtSLINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKK--------------A 1766
Cdd:COG4913 737 EAAEDLARLELRALLE--ERFAAALGDA-VERELRENLEERIDALRARLNRAEEELERAMRAFNRewpaetadldadleS 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1767 ITDAAMMAEELkKEQDTSAHLERMK----KNMEQTIKDLQMRLDEAEQIAlkggKKQVQKLEARVKELE-NE-----LES 1836
Cdd:COG4913 814 LPEYLALLDRL-EEDGLPEYEERFKellnENSIEFVADLLSKLRRAIREI----KERIDPLNDSLKRIPfGPgrylrLEA 888
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1591544934 1837 EQKKSQEyqkgVRKFERRIKELS-----YQGEEDKKNLVRMQELIDKLqakvksykRQAEEAEDQANTN 1900
Cdd:COG4913 889 RPRPDPE----VREFRQELRAVTsgaslFDEELSEARFAALKRLIERL--------RSEEEESDRRWRA 945
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1260-1912 |
4.97e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 71.69 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1260 YEDQMNEAKAKVEELQRQLNETNSHRARAQ----AESSELSRKLE----EREATVSQLQRSKNSFSQNVEELKKQLEEEN 1331
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKQKfylrQSVIDLQTKLQemqmERDAMADIRRRESQSQEDLRNQLQNTVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1332 KAKNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALskANGEVAQWRTKYETDAIQRT-------------EELEESK 1398
Cdd:pfam15921 156 AAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL--VDFEEASGKKIYEHDSMSTMhfrslgsaiskilRELDTEI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1399 KKLAVRLQEAEEAVEASNAKCSS-LEKTKHRLQTEIEDLVVDLErasAAAAALDKKQrnfdkvlAEWRQKCEECQAELET 1477
Cdd:pfam15921 234 SYLKGRIFPVEDQLEALKSESQNkIELLLQQHQDRIEQLISEHE---VEITGLTEKA-------SSARSQANSIQSQLEI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1478 SQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEE-ITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAE 1556
Cdd:pfam15921 304 IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDkIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1557 GTLeHEESKTLRIQLELNQIKADVDrklAEKEEEIDNLRRN-HQRTLESMQatLDAEAKSrseavrLRKKMEGdlnEMEV 1635
Cdd:pfam15921 384 ADL-HKREKELSLEKEQNKRLWDRD---TGNSITIDHLRRElDDRNMEVQR--LEALLKA------MKSECQG---QMER 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1636 QLNhANRLASESQKLLRNLQVQIKDVQLELDETIhqnEELkeqvavTERRNNLLASE--VEELRALLEQNDRARKLAEHE 1713
Cdd:pfam15921 449 QMA-AIQGKNESLEKVSSLTAQLESTKEMLRKVV---EEL------TAKKMTLESSErtVSDLTASLQEKERAIEATNAE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1714 LLEATERVNLLHSQNTSLINQKKKLENdLSTLSNEVDDAVQECRNAEEKAKKAITDaamMAEELKKEQDTSAHLERMKKN 1793
Cdd:pfam15921 519 ITKLRSRVDLKLQELQHLKNEGDHLRN-VQTECEALKLQMAEKDKVIEILRQQIEN---MTQLVGQHGRTAGAMQVEKAQ 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1794 MEQTIKDLQMRLDEAEQIALKGGKKqVQKLEARVKELENELESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKNLVRMQ 1873
Cdd:pfam15921 595 LEKEINDRRLELQEFKILKDKKDAK-IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLS 673
|
650 660 670
....*....|....*....|....*....|....*....
gi 1591544934 1874 ELIDKLQakvKSYKRQAEEAEDQANTNLSKYRKLQHELD 1912
Cdd:pfam15921 674 EDYEVLK---RNFRNKSEEMETTTNKLKMQLKSAQSELE 709
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1641-1941 |
5.30e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1641 NRLASESQKLLRnlqvqIKDVQLELDETIhqnEELKEQVAVTER-----------RNNLLASEVEELRALLEQNDRARKL 1709
Cdd:COG1196 179 RKLEATEENLER-----LEDILGELERQL---EPLERQAEKAERyrelkeelkelEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1710 AEHELLEATERVNLLHSqntslinQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLER 1789
Cdd:COG1196 251 LEAELEELEAELAELEA-------ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1790 MKKNMEQTIKDLQMRLDEAEQiALKGGKKQVQKLEARVKELENELESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKNL 1869
Cdd:COG1196 324 ELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 1870 VRMQELIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELDDAEERADMAETQVTKLRVRTRDQGSKFAE 1941
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1496-1922 |
6.05e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.10 E-value: 6.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1496 YEETLEHLETIKRENKNLqEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEgtLEHEESKTLRIQLELNQ 1575
Cdd:COG4913 237 LERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1576 IKADVDRkLAEKEEEIDNLRRNHQ-RTLESMQATLDAEAKSRSEAVRLRKKMEGDLNEMEVQLNHA----NRLASESQKL 1650
Cdd:COG4913 314 LEARLDA-LREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeefAALRAEAAAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1651 LRNLQVQIKDVQLELDETI-------HQNEELKEQVAVTERRNNLLASEVEELRALLEQN-----DRARKLAehELLE-- 1716
Cdd:COG4913 393 LEALEEELEALEEALAEAEaalrdlrRELRELEAEIASLERRKSNIPARLLALRDALAEAlgldeAELPFVG--ELIEvr 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1717 --------ATERVnlLHSQNTSL-------------INQKK-----------------------------KLENDLSTLS 1746
Cdd:COG4913 471 peeerwrgAIERV--LGGFALTLlvppehyaaalrwVNRLHlrgrlvyervrtglpdperprldpdslagKLDFKPHPFR 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1747 NEVDDAVQE------CRNAEE--KAKKAITDAAMMAEELKK-EQDTSAHLER---MKKNMEQTIKDLQMRLDEAEQiALK 1814
Cdd:COG4913 549 AWLEAELGRrfdyvcVDSPEElrRHPRAITRAGQVKGNGTRhEKDDRRRIRSryvLGFDNRAKLAALEAELAELEE-ELA 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1815 GGKKQVQKLEARVKELEN---------ELESEQKKSQEYQKGVRKFERRIKELsyqgEEDKKNLVRMQELIDKLQAKVKS 1885
Cdd:COG4913 628 EAEERLEALEAELDALQErrealqrlaEYSWDEIDVASAEREIAELEAELERL----DASSDDLAALEEQLEELEAELEE 703
|
490 500 510
....*....|....*....|....*....|....*..
gi 1591544934 1886 YKRQAEEAEDQANTNLSKYRKLQHELDDAEERADMAE 1922
Cdd:COG4913 704 LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
843-1313 |
1.96e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 843 KIKPLLKSAATEKELASLKEELAKLKEALEKSEVKRKELEERqvsliqeKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQ 922
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKR-------LSRLEEEINGIEERIKELEEKEERLEELKKK 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 923 LEaKVKEIMERLEDEEEMSATVLAKKRKLEDECAELK-KDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLT 1001
Cdd:PRK03918 347 LK-ELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1002 KEKKALQEAHQQ--TLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSmeSVMDLEN 1079
Cdd:PRK03918 426 KAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI--KLKELAE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1080 DKQQLEEKLKKKDFE-MNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELEADRACRAKVEkqrgdvareleelserl 1158
Cdd:PRK03918 504 QLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD----------------- 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1159 eesggatsaqiEINKKRETDILKLRRDLEEAMLHHEATTAGLRKKHADSVaELSEQIDSLQRVKQKLEKERSEAKMEVDD 1238
Cdd:PRK03918 567 -----------ELEEELAELLKELEELGFESVEELEERLKELEPFYNEYL-ELKDAEKELEREEKELKKLEEELDKAFEE 634
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1591544934 1239 LASTVEQLSKGKASAEKTCRLY-EDQMNEAKAKVEELQRQLnetnshrARAQAESSELSRKLEEREATVSQLQRSK 1313
Cdd:PRK03918 635 LAETEKRLEELRKELEELEKKYsEEEYEELREEYLELSREL-------AGLRAELEELEKRREEIKKTLEKLKEEL 703
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1389-1835 |
1.48e-10 |
|
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: 65.87 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1389 QRTEELE-------ESKKKLAV---RLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFD 1458
Cdd:pfam05622 14 QRCHELDqqvsllqEEKNSLQQenkKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1459 KVLAEWRQKCEEcqaeLETSQKESRSLSTELFKLKNS-------------YEETLEHLETIKRENKNLQEEITDLSDQIS 1525
Cdd:pfam05622 94 KEVLELQHRNEE----LTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNAEYMQRTL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1526 QGAKTIHELEKMKKGLEIEKSEIQaaleEAEGTLEHEESKTLRIQLELNQIKADVDRKLAEKE----------EEIDNLR 1595
Cdd:pfam05622 170 QLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKErliierdtlrETNEELR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1596 RNHQRTLESMQATLDAEAKSRSEAVRLRKKMEGDLNEMEVQLNHANRLASESQKLlrNLQVQIKDVQLELDETIHQNEEL 1675
Cdd:pfam05622 246 CAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEG--SYRERLTELQQLLEDANRRKNEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1676 KEQVAVTERRNNLLASEVEEL-RALLEQNDRA-------RKLAEHelleaTERVNLLHSQNTSLINQKKKLENDLSTLSN 1747
Cdd:pfam05622 324 ETQNRLANQRILELQQQVEELqKALQEQGSKAedssllkQKLEEH-----LEKLHEAQSELQKKKEQIEELEPKQDSNLA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1748 EVDDAVQECRNaeekakkaitdaammaeelKKEQDTSAHLERMKKNMEQT---IKDLQMRLDEAEQIALKGGKKQVQKLE 1824
Cdd:pfam05622 399 QKIDELQEALR-------------------KKDEDMKAMEERYKKYVEKAksvIKTLDPKQNPASPPEIQALKNQLLEKD 459
|
490
....*....|.
gi 1591544934 1825 ARVKELENELE 1835
Cdd:pfam05622 460 KKIEHLERDFE 470
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
851-1104 |
1.54e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.63 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 851 AATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAE-----QDNLADAEDRCDLLIKTKIQLEA 925
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiQAELSKLEEEVSRIEARLREIEQ 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 926 KVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKK 1005
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1006 ALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEG-------------SLEQEKKLRMDLERVKRKLEGDLKLSME 1072
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDpkgedeeipeeelSLEDVQAELQRVEEEIRALEPVNMLAIQ 979
|
250 260 270
....*....|....*....|....*....|..
gi 1591544934 1073 SVMDLENDKQQLEEKLKKKDFEMNEMSTRIED 1104
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1451-1928 |
1.78e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1451 DKKQRNFDKVLAEWRQKCEECQAELET--SQKE-SRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQG 1527
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERyeEQREqARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1528 AKTIHELEKMKKGLEiekSEIQAALEEAEgtLEHEESKTLRIQLElnqikaDVDRKLAEKEEEIDNLRRNHQRTLESMQA 1607
Cdd:PRK02224 278 AEEVRDLRERLEELE---EERDDLLAEAG--LDDADAEAVEARRE------ELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1608 TLDAEAKSRSEAVRLRKKmegdlnemevqlnhANRLASESQKllrnlqvqikdvqleldetihqneelkEQVAVTERRnn 1687
Cdd:PRK02224 347 LREDADDLEERAEELREE--------------AAELESELEE---------------------------AREAVEDRR-- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1688 llaSEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLENDLSTlsneVDDAVQECRNAEEKAKkai 1767
Cdd:PRK02224 384 ---EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRT----ARERVEEAEALLEAGK--- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1768 tdaammAEELKKEQDTSAHLERMKKNMEQtIKDLQMRLDEAEQialkggkkQVQKLEARVKELEN--ELESEQKKSQEYQ 1845
Cdd:PRK02224 454 ------CPECGQPVEGSPHVETIEEDRER-VEELEAELEDLEE--------EVEEVEERLERAEDlvEAEDRIERLEERR 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1846 KGVrkfERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELDDAEERADMAETQV 1925
Cdd:PRK02224 519 EDL---EELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIR 595
|
...
gi 1591544934 1926 TKL 1928
Cdd:PRK02224 596 TLL 598
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
853-1281 |
2.14e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 853 TEKELASLKEELAKLKEALEKSEVKRKELEERqvslIQEKNDLSLQLQAEQDNLADAEDRCDLLIKT----KIQLEAKVK 928
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEE----VRDLRERLEELEEERDDLLAEAGLDDADAEAvearREELEDRDE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 929 EIMERLEDE-------EEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLT 1001
Cdd:PRK02224 325 ELRDRLEECrvaaqahNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1002 KEKKALQEAHQQTLDDLQAEEDKVNTLT-----------KAQAKLE------------------------QQVDDLEGSL 1046
Cdd:PRK02224 405 VDLGNAEDFLEELREERDELREREAELEatlrtarerveEAEALLEagkcpecgqpvegsphvetieedrERVEELEAEL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1047 EQekkLRMDLERVKRKLEG--DLKLSMESVMDLENDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARTE 1124
Cdd:PRK02224 485 ED---LEEEVEEVEERLERaeDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1125 ELEEELEADRACRAKVEKQRGDVARELEELSERLEESGGATSAQIEINKKRET------------DILKLRRD----LEE 1188
Cdd:PRK02224 562 EAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKrealaelnderrERLAEKRErkreLEA 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1189 AmlHHEATTAGLRKKHA----------DSVAELSEQIDSLQR----VKQKLEkERSEAKMEVDDLASTVEQLSKGKASAE 1254
Cdd:PRK02224 642 E--FDEARIEEAREDKEraeeyleqveEKLDELREERDDLQAeigaVENELE-ELEELRERREALENRVEALEALYDEAE 718
|
490 500
....*....|....*....|....*...
gi 1591544934 1255 KTCRLYEDQMNEAKAK-VEELQRQLNET 1281
Cdd:PRK02224 719 ELESMYGDLRAELRQRnVETLERMLNET 746
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1219-1857 |
2.85e-10 |
|
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: 65.51 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1219 QRVKQKLEKERSEAKMEVDDLASTVEQLSKGKA----SAEKTCRlYEDQMNEAKAKVEELQRQLNE--TNSHRARAQAES 1292
Cdd:pfam05483 130 EKVSLKLEEEIQENKDLIKENNATRHLCNLLKEtcarSAEKTKK-YEYEREETRQVYMDLNNNIEKmiLAFEELRVQAEN 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1293 S--ELSRKLEEREATVSQL----QRSKNSFSQNVEELKKQLEEENKAKNALAHALQSSRHDCDLLREQ---YDEEQEAKA 1363
Cdd:pfam05483 209 ArlEMHFKLKEDHEKIQHLeeeyKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKtklQDENLKELI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1364 ELQRALSKANGEVAQWRTKYETDAIQRTEELEESKKKLAVRLQEAEEAVEASNAKcssleKTKHRLQ-TEIEDLVVDLER 1442
Cdd:pfam05483 289 EKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKA-----KAAHSFVvTEFEATTCSLEE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1443 ASAAAAALDKKQRNFDKVLAEWRQKCeecQAELETSQKESRSLSTELFKLKN--SYEETL----EHLETIKRENKNLQEE 1516
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKK---SSELEEMTKFKNNKEVELEELKKilAEDEKLldekKQFEKIAEELKGKEQE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1517 ITDLsdqISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRI----------QLELNQIKADVDRKLAE 1586
Cdd:pfam05483 441 LIFL---LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELtahcdkllleNKELTQEASDMTLELKK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1587 KEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLRKKMEGDLNEMEVQLNhanrlASESQKLLRNLQVQIKDVQLELD 1666
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLD-----KSEENARSIEYEVLKKEKQMKIL 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1667 ETIHQNeeLKEQVavtERRNNLLASEVEELRALleqndRARKLAEHELLEATE-RVNLLHSQntsLINQKKKLENDLSTL 1745
Cdd:pfam05483 593 ENKCNN--LKKQI---ENKNKNIEELHQENKAL-----KKKGSAENKQLNAYEiKVNKLELE---LASAKQKFEEIIDNY 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1746 SNEVDD---AVQECRNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKKNMEQTIKDLQMRLDEaeqIALKGGKKQV 1820
Cdd:pfam05483 660 QKEIEDkkiSEEKLLEEVEKAKAIADEAVKLQKEIDKrcQHKIAEMVALMEKHKHQYDKIIEERDSE---LGLYKNKEQE 736
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1591544934 1821 QK-----LEARVKELENELESEQKKSQEYQKGVRKFERRIKE 1857
Cdd:pfam05483 737 QSsakaaLEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1538-1941 |
3.35e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1538 KKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQL-ELNQIKADVDRKLAEKEEEidnlRRNHQRTLESMQATLDAEAKSR 1616
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLnGLESELAELDEEIERYEEQ----REQARETRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1617 SEAVRLrkkmEGDLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNE-ELKEQVAVTERRNNLlASEVEE 1695
Cdd:PRK02224 251 EELETL----EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlDDADAEAVEARREEL-EDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1696 LRALLEQNDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDD---AVQECRNAEEKAKKAITDAAM 1772
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDrreEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1773 ----MAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIaLKGGK---------------------KQVQKLEARV 1827
Cdd:PRK02224 406 dlgnAEDFLEELREERDELREREAELEATLRTARERVEEAEAL-LEAGKcpecgqpvegsphvetieedrERVEELEAEL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1828 KELENELESEQKKsQEYQKGVRKFERRIKELsyqgEEDKKNLvrmQELIDKLQAKVKSYKRQAEEAEDQANtnlskyrKL 1907
Cdd:PRK02224 485 EDLEEEVEEVEER-LERAEDLVEAEDRIERL----EERREDL---EELIAERRETIEEKRERAEELRERAA-------EL 549
|
410 420 430
....*....|....*....|....*....|....
gi 1591544934 1908 QHELDDAEERADMAETQVTKLRVRTRDQGSKFAE 1941
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
848-1064 |
3.61e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 65.04 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 848 LKSAATEKELASLKEELAKLKEALEKSEVKRKELEERQ--VSLIQEKNDLSLQLQAEQDNLADAEDRcdlliktKIQLEA 925
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAE-------LAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 926 KVKEIMERLEDEEEMSATVLAkkrklEDECAELKKDIDDLEITLAkvEKEKHATEN--KVKNLIEEMAALdetilkltke 1003
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL---------- 303
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1591544934 1004 KKALQEAHQQTLDDLQAEedkVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLE 1064
Cdd:COG3206 304 RAQLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
839-1535 |
4.47e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 65.07 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 839 KLFFKIKPLLKSAATEKELASLKEELAKLKEALEKSEVKR--KELEERQVSLIQEKNDLSLQLQAEQDNLADAE------ 910
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhhtttr 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 911 DRCDLLIKTKIQLEAKVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDID-------DLEITLAKVEKEKHATENKV 983
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 984 KNLIEEMAALDETILKLTKekkalQEAHQQTLDDLQAEEDKVNT----LTKAQAKLEQQVDDLEGS-------LEQEKKL 1052
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCG-----SQDEESDLERLKEEIEKSSKqramLAGATAVYSQFITQLTDEnqsccpvCQRVFQT 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1053 RMDLERVKRKLEGDLKLSmesvmdlENDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELEA 1132
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLA-------PDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQR 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1133 DRACRAKVEKQRGDVareleelserleesggatSAQIEINKKRETDILKLRRDLEEamlhheatTAGLRKKHADSVAELs 1212
Cdd:TIGR00606 763 LKNDIEEQETLLGTI------------------MPEEESAKVCLTDVTIMERFQME--------LKDVERKIAQQAAKL- 815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1213 eQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKgkasaektcrLYEDQmneaKAKVEELQRQLNETNSHR---ARAQ 1289
Cdd:TIGR00606 816 -QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK----------LIQDQ----QEQIQHLKSKTNELKSEKlqiGTNL 880
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1290 AESSELSRKLEEREATVSQLQRSKNSFSQNVEELKKQLEEENKAKNALAHALQSSRhdcdllREQYDEEQEAKAELQRAL 1369
Cdd:TIGR00606 881 QRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSN------KKAQDKVNDIKEKVKNIH 954
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1370 SkangevaqwrtkYETDAIQRTEELEESKKKlavrlqEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAA 1449
Cdd:TIGR00606 955 G------------YMKDIENKIQDGKDDYLK------QKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERW 1016
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1450 LDKKQrnfdkVLAEWRQKCEECQAELETSQKESRSLstELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAK 1529
Cdd:TIGR00606 1017 LQDNL-----TLRKRENELKEVEEELKQHLKEMGQM--QVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKK 1089
|
....*.
gi 1591544934 1530 TIHELE 1535
Cdd:TIGR00606 1090 ELREPQ 1095
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
847-1599 |
4.56e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 64.99 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 847 LLKSAATEKELaslkeeLAKLkEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDnlaDAEDRCDLLIKTKIQLEAK 926
Cdd:TIGR00618 158 LKAKSKEKKEL------LMNL-FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTL---CTPCMPDTYHERKQVLEKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 927 VKEIMERLEDEEEMSA------TVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATE--NKVKNLIEEMAALDE--- 995
Cdd:TIGR00618 228 LKHLREALQQTQQSHAyltqkrEAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINraRKAAPLAAHIKAVTQieq 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 996 ---TILKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSme 1072
Cdd:TIGR00618 308 qaqRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQ-- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1073 svMDLENDKQQLEEKLKKKDFEMNEMSTrIEDEQSLVNQLQKKIKELQARTEELEEELEADR---ACRAKVEKQRGDVAR 1149
Cdd:TIGR00618 386 --QQKTTLTQKLQSLCKELDILQREQAT-IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAaaiTCTAQCEKLEKIHLQ 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1150 ELEELSERLEESggatSAQIEINKKRETDILKLR-----------RDLEEAMLHHEATTAGL----------------RK 1202
Cdd:TIGR00618 463 ESAQSLKEREQQ----LQTKEQIHLQETRKKAVVlarllelqeepCPLCGSCIHPNPARQDIdnpgpltrrmqrgeqtYA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1203 KHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLskgKASAEKTCRLyedqmneakakVEELQRQLNETN 1282
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRS---KEDIPNLQNI-----------TVRLQDLTEKLS 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1283 SHRARAQAESSELSRKLEEREAT--VSQLQRSKnSFSQNVEELKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQE 1360
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLqdVRLHLQQC-SQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQ 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1361 AKAELQRALSKANGEVAQWRTKyetdaiqrTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEdlvvDL 1440
Cdd:TIGR00618 684 KMQSEKEQLTYWKEMLAQCQTL--------LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELM----HQ 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1441 ERASAAAAALDKKQRNFDKVLAEWR-QKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKR-ENKNLQEEIT 1518
Cdd:TIGR00618 752 ARTVLKARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEE 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1519 DLSDQISQGAKTIHELEKMKKGLEiEKSEIQAALEEAEGTLEHEESKTLRIQLELNQIKADVDRKLAEKEEEIDNLRRNH 1598
Cdd:TIGR00618 832 QFLSRLEEKSATLGEITHQLLKYE-ECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLAN 910
|
.
gi 1591544934 1599 Q 1599
Cdd:TIGR00618 911 Q 911
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1416-1913 |
5.11e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.66 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1416 NAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELFKLKNS 1495
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1496 YEETLehLETIKRENKNLQEEITDLSDQISQGAKTIHEL-------EKMKKGLEIEKSEIQAALEEAEGTLEheesktlr 1568
Cdd:TIGR04523 304 KEQDW--NKELKSELKNQEKKLEEIQNQISQNNKIISQLneqisqlKKELTNSESENSEKQRELEEKQNEIE-------- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1569 iqlelnqikaDVDRKLAEKEEEIDNLRrNHQRTLESMQATLDAEAKSRSEAVrlrKKMEGDLNEMEVQLNHANRLASESQ 1648
Cdd:TIGR04523 374 ----------KLKKENQSYKQEIKNLE-SQINDLESKIQNQEKLNQQKDEQI---KKLQQEKELLEKEIERLKETIIKNN 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1649 KLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTERrnnllasEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQN 1728
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR-------SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1729 TSLINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKaitdaamMAEELKKEQdtsahLERMKKNMEQTIKDLqmrldEA 1808
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK-------DDFELKKEN-----LEKEIDEKNKEIEEL-----KQ 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1809 EQIALKGGKKQVQKLearVKELENELESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKR 1888
Cdd:TIGR04523 576 TQKSLKKKQEEKQEL---IDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
490 500
....*....|....*....|....*
gi 1591544934 1889 QAEEAEDQANTNLSKYRKLQHELDD 1913
Cdd:TIGR04523 653 TIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
854-1490 |
5.13e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 854 EKELASLKEELAKLKEALEK-----SEVKR--KELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAK 926
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKfikrtENIEEliKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 927 VKEIMERLEDEEEMSatvlAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKnLIEEMAALDETILKLTKEKKA 1006
Cdd:PRK03918 244 EKELESLEGSKRKLE----EKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1007 LQE---AHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGS---LEQEKKLRMDLERVKRKLEGDLKLSMESVMD-LEN 1079
Cdd:PRK03918 319 LEEeinGIEERIKELEEKEERLEELKKKLKELEKRLEELEERhelYEEAKAKKEELERLKKRLTGLTPEKLEKELEeLEK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1080 DKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKkikelqarteeleeeleADRAC----RAKVEKQRGDVARELEELS 1155
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKK-----------------AKGKCpvcgRELTEEHRKELLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1156 ERLEESGGATSAQIEINKKRETDILKLRRDLEEamlhheattagLRKKHadsvaELSEQIDSLQRVKQKLEKERSEAKME 1235
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESE-----------LIKLK-----ELAEQLKELEEKLKKYNLEELEKKAE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1236 vddLASTVEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRK-LEEREATVSQLQRSKN 1314
Cdd:PRK03918 526 ---EYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPFYN 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1315 SFsqnveelkkqleeeNKAKNAlAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTKYEtdaiqrteel 1394
Cdd:PRK03918 603 EY--------------LELKDA-EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS---------- 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1395 EESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVlAEWRQKCEECQAE 1474
Cdd:PRK03918 658 EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERV-EELREKVKKYKAL 736
|
650
....*....|....*..
gi 1591544934 1475 L-ETSQKESRSLSTELF 1490
Cdd:PRK03918 737 LkERALSKVGEIASEIF 753
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1293-1918 |
5.26e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 64.99 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1293 SELSRKLEEREATVSQLQRSKNSFSQNVEELKKQLEE-ENKAKNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSK 1371
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKlKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1372 ANGEVAQWRTKYETDAIQRTEELEESKKKLAvrlqEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALD 1451
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENK----EEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1452 KKQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEItdlsdqisQGAKTI 1531
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERL--------SSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1532 HELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLELNQIKADVDRKLAEKEEEIDNLRRNHQRTLESMQATLDA 1611
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1612 EAKSRSEAVRLRKKMEGDLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQL-------ELDETIHQNEELKEQVAVTER 1684
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIisahgrlGDLGVAVENYKVAISTAVIVE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1685 RNNL---LASEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQECRNAEE 1761
Cdd:pfam02463 553 VSATadeVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDT 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1762 KAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKggKKQVQKLEARVKELENELESEQKKS 1841
Cdd:pfam02463 633 ELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA--ESELAKEEILRRQLEIKKKEQREKE 710
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1591544934 1842 QEYQKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELDDAEERA 1918
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK 787
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1340-1881 |
5.53e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1340 ALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRtkyetdaiQRTEELEESKKKLAVRLQEAEEAVEASNAKC 1419
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR--------EELETLEAEIEDLRETIAETEREREELAEEV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1420 SSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELFKLKNSYEET 1499
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1500 LEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLE--HEESKTLRIQLElnqik 1577
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDelREREAELEATLR----- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1578 aDVDRKLAEKEE--EIDNLRRNHQRTLESMQA-TLDAEAKSRSEAVRLRKKMEGDLNEMEVQLNHANRLAsESQKLLRNL 1654
Cdd:PRK02224 437 -TARERVEEAEAllEAGKCPECGQPVEGSPHVeTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1655 QVQIKDVQLELDETIHQNEELKEQVAVTERRNNLLASEVEELRalleqnDRARKlAEHELLEATERVNLLHSQNTSLINQ 1734
Cdd:PRK02224 515 EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKR------EAAAE-AEEEAEEAREEVAELNSKLAELKER 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1735 KKKLeNDLSTLSNEVDDAVQECRNAEEKAKkaitDAAMMAEELKkeqdtsahlERMKKNMEQtIKDLQMRLDEAeqiALK 1814
Cdd:PRK02224 588 IESL-ERIRTLLAAIADAEDEIERLREKRE----ALAELNDERR---------ERLAEKRER-KRELEAEFDEA---RIE 649
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1591544934 1815 GGKKQVQKLEARVKELENELESEQKKSQEYQKGVRKFERRIKELsyqgEEDKKNLVRMQELIDKLQA 1881
Cdd:PRK02224 650 EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL----EELRERREALENRVEALEA 712
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
912-1680 |
6.18e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 64.60 E-value: 6.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 912 RCDLLIKTKIQLEAKVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDI----DDLEITLAKVEKEKHATENKVKNLI 987
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 988 EEMAALDETILKLTKEKKALQEAH--QQTLDDLQAEEDKVNTLTKAQAKLEQqvddlegsleqekklRMDLERVKRKLEG 1065
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAVLEETQE---------------RINRARKAAPLAA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1066 DLKLSMESVMDLENDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQA----RTEELEEELEADRACRAKVE 1141
Cdd:TIGR00618 298 HIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeihiRDAHEVATSIREISCQQHTL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1142 KQRgDVARELEELSERLEESGGATSAQIEINKKRETDILKLRRDLEEAMLHHEATTAGLRKKHADSVAELSEQIDSLQRV 1221
Cdd:TIGR00618 378 TQH-IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1222 KQKLEKERSEAKMEVDDLASTVEQLSKgkaSAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAqAESSELSRKLEE 1301
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQTKEQIHL---QETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDI-DNPGPLTRRMQR 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1302 REATVSQLQRSknsfsqnveelkkqleeenkaknalahaLQSSRHDCDLLREQYDEEQEAKAELQRALSKangeVAQWRT 1381
Cdd:TIGR00618 533 GEQTYAQLETS----------------------------EEDVYHQLTSERKQRASLKEQMQEIQQSFSI----LTQCDN 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1382 KYetdaiqrTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLErasaaaaaldkkQRNFDKVL 1461
Cdd:TIGR00618 581 RS-------KEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH------------LQQCSQEL 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1462 AEWRQKCEECQAELETSQKESRSLSTELFKlknsyEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGL 1541
Cdd:TIGR00618 642 ALKLTALHALQLTLTQERVREHALSIRVLP-----KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY 716
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1542 EIEKSEIQAALEEAEGTLEHEESKTLRIQLELNQikadvDRKLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEA-V 1620
Cdd:TIGR00618 717 DREFNEIENASSSLGSDLAAREDALNQSLKELMH-----QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFfN 791
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1591544934 1621 RLRKKMEGDLNEMEVQLNH----------------ANRLASESQKLLRN--LQVQIKDVQLELDETIHQNEELKEQVA 1680
Cdd:TIGR00618 792 RLREEDTHLLKTLEAEIGQeipsdedilnlqcetlVQEEEQFLSRLEEKsaTLGEITHQLLKYEECSKQLAQLTQEQA 869
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
851-1334 |
6.95e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 851 AATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSL---QLQAEQDNLADAEDRCDLLIKTKIQLEAKV 927
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESlegSKRKLEEKIRELEERIEELKKEIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 928 KEIMERLEDEEEMSATV------LAKKRKLEDECAELKKDIDDLEITLAKVEK---EKHATENKVKNLIEEMAALDETIL 998
Cdd:PRK03918 283 KELKELKEKAEEYIKLSefyeeyLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEERHE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 999 KLTKEKKALQEAHQ-------QTLDDLQAE-----------EDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVK 1060
Cdd:PRK03918 363 LYEEAKAKKEELERlkkrltgLTPEKLEKEleelekakeeiEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCG 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1061 RKLEGDLKLSM-----ESVMDLENDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQ--KKIKELQARTEELEEELEAD 1133
Cdd:PRK03918 443 RELTEEHRKELleeytAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNLEELEK 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1134 RA-----CRAKVEKQRGDVARELEELSerleesggatsaQIEINKKRETDILKLRRDLEE--AMLHHEattagLRKKHAD 1206
Cdd:PRK03918 523 KAeeyekLKEKLIKLKGEIKSLKKELE------------KLEELKKKLAELEKKLDELEEelAELLKE-----LEELGFE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1207 SVAELSEQIDSLqrvkQKLEKERSEAKMEVDDLASTVEQLSKGKASAEKTcrlyEDQMNEAKAKVEELQRQLNETNS--- 1283
Cdd:PRK03918 586 SVEELEERLKEL----EPFYNEYLELKDAEKELEREEKELKKLEEELDKA----FEELAETEKRLEELRKELEELEKkys 657
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1591544934 1284 --HRARAQAESSELSRKLEEREATVSQLQRSKNSFSQNVEELKKQLEEENKAK 1334
Cdd:PRK03918 658 eeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK 710
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
854-1675 |
7.42e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 64.30 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 854 EKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQ-------------------LQAEQDNL---ADAED 911
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQadrhqehirardsliqslaTRLELDGFergPFSER 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 912 RCDLLIKTKIQ-LEAKVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAK-------VEKEKHATENKV 983
Cdd:TIGR00606 391 QIKNFHTLVIErQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKkqeelkfVIKELQQLEGSS 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 984 KNLIEEMAALDETILKLTK-EKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKL---RMDLERV 1059
Cdd:TIGR00606 471 DRILELDQELRKAERELSKaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLtkdKMDKDEQ 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1060 KRKLEGDLKLSMESVMDLENDKQQLEEKLKKKDFEMNEMSTRIEDeqslvnqLQKKIKELQARTEELEEELEADRACRAK 1139
Cdd:TIGR00606 551 IRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAK-------LNKELASLEQNKNHINNELESKEEQLSS 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1140 VEKQRGDVARELEElserleesggatsaqieinkkrETDILKLRRDLEEAMlHHEATTAGLRKKHADSVAELSEQIDSLQ 1219
Cdd:TIGR00606 624 YEDKLFDVCGSQDE----------------------ESDLERLKEEIEKSS-KQRAMLAGATAVYSQFITQLTDENQSCC 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1220 RVKQKLEKERSEAKMEVDDLASTVEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNetnshraRAQAESSELSRKL 1299
Cdd:TIGR00606 681 PVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIID-------LKEKEIPELRNKL 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1300 EEREatvSQLQRSKNSFSQNVEELKKQLEEENKAKNALAhalqssrhDCDLLREQYDEEQEAKAELQRALSKANGeVAQW 1379
Cdd:TIGR00606 754 QKVN---RDIQRLKNDIEEQETLLGTIMPEEESAKVCLT--------DVTIMERFQMELKDVERKIAQQAAKLQG-SDLD 821
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1380 RTKYETDaiQRTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDK 1459
Cdd:TIGR00606 822 RTVQQVN--QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQS 899
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1460 VLAEWRQKCEEcQAELETSQKESRSLSTELFKLKNSYEETLE-HLETIKRENKNLQEEITDLSDQISQGAktihelEKMK 1538
Cdd:TIGR00606 900 LIREIKDAKEQ-DSPLETFLEKDQQEKEELISSKETSNKKAQdKVNDIKEKVKNIHGYMKDIENKIQDGK------DDYL 972
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1539 KGLEIEKSEIQAALEEAEGTLE--HEESKTLRIQLELNQIKADV------DRKLAEKEEEIDNLRRNHQRTLESMQAT-L 1609
Cdd:TIGR00606 973 KQKETELNTVNAQLEECEKHQEkiNEDMRLMRQDIDTQKIQERWlqdnltLRKRENELKEVEEELKQHLKEMGQMQVLqM 1052
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1610 DAEAKSRSEAVRLRKKME----GDLNEMEVQLNHANRLASESQklLRNLQVQIKDVQLELDETIHQNEEL 1675
Cdd:TIGR00606 1053 KQEHQKLEENIDLIKRNHvlalGRQKGYEKEIKHFKKELREPQ--FRDAEEKYREMMIVMRTTELVNKDL 1120
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1168-1717 |
8.01e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1168 QIEINKKRETDILKLRRDLEEAMLHHEATTAGLRKKHADSVAELSE----QIDSLQRVKQKLEKERSEAKMEVDDLASTV 1243
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1244 EQLskgKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQN---- 1319
Cdd:COG4913 369 AAL---GLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARllal 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1320 -------------------------------------------------------------------------VEELKKQ 1326
Cdd:COG4913 446 rdalaealgldeaelpfvgelievrpeeerwrgaiervlggfaltllvppehyaaalrwvnrlhlrgrlvyerVRTGLPD 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1327 LEEENKAKNALAHALQSSRHDC-----DLLREQYD----EEQEAKAELQRALSKAnGEVAQWRTKYE------------- 1384
Cdd:COG4913 526 PERPRLDPDSLAGKLDFKPHPFrawleAELGRRFDyvcvDSPEELRRHPRAITRA-GQVKGNGTRHEkddrrrirsryvl 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1385 -TDAIQRTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQteiedlvvDLERASAAAAALDKKQRNfdkvLAE 1463
Cdd:COG4913 605 gFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ--------RLAEYSWDEIDVASAERE----IAE 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1464 WRQKceecQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQgAKTIHElekmkkglEI 1543
Cdd:COG4913 673 LEAE----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE-LQDRLE--------AA 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1544 EKSEIQAALEEAEGTLEHE--ESKTLRIQLELNQIKADVDRKLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVR 1621
Cdd:COG4913 740 EDLARLELRALLEERFAAAlgDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLA 819
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1622 LRKKMEGD-LNEMEVQLnhANRLASESQKLLRNLQVQIKDVQLELDETIHQ-NEELKE---------QVAVTERRNnlla 1690
Cdd:COG4913 820 LLDRLEEDgLPEYEERF--KELLNENSIEFVADLLSKLRRAIREIKERIDPlNDSLKRipfgpgrylRLEARPRPD---- 893
|
650 660
....*....|....*....|....*..
gi 1591544934 1691 SEVEELRALLEQNDRARKLAEHELLEA 1717
Cdd:COG4913 894 PEVREFRQELRAVTSGASLFDEELSEA 920
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1164-1913 |
8.14e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 64.30 E-value: 8.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1164 ATSAQIEINKKRETDILKLRRDLEEAMLhheattaglrkkhaDSVAELSEQIDSLQRVKQKLEKERSEAKME-VDDLAST 1242
Cdd:TIGR00606 234 ESSREIVKSYENELDPLKNRLKEIEHNL--------------SKIMKLDNEIKALKSRKKQMEKDNSELELKmEKVFQGT 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1243 VEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQ--LQRSKNSFSQNV 1320
Cdd:TIGR00606 300 DEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRArdSLIQSLATRLEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1321 EELKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTKYETDAIQRTEELEESKKK 1400
Cdd:TIGR00606 380 DGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFV 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1401 L------------------AVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLA 1462
Cdd:TIGR00606 460 IkelqqlegssdrileldqELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEM 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1463 EWRQKCEECQAELETSQKESRSLSTEL--FKLKNSYEETLEHLetiKRENKNLQEEITDLSDQISQGAKTIHELEKMKKG 1540
Cdd:TIGR00606 540 LTKDKMDKDEQIRKIKSRHSDELTSLLgyFPNKKQLEDWLHSK---SKEINQTRDRLAKLNKELASLEQNKNHINNELES 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1541 LEIEKSEIQAALEEAEGTlEHEESKTLRIQLELNQIKADVdRKLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAV 1620
Cdd:TIGR00606 617 KEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQR-AMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQ 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1621 RLRKKMEGDLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTERRNNLLASEVEELRALL 1700
Cdd:TIGR00606 695 EFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLL 774
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1701 EQNDRARKLAEHELLEAT--ERVNLLHSQNTSLINQKKKlENDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELK 1778
Cdd:TIGR00606 775 GTIMPEEESAKVCLTDVTimERFQMELKDVERKIAQQAA-KLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQ 853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1779 KEQDTSAHLE----RMKKNMEQTIKDLQMRLDEAEQIALKggKKQVQKLEARVKELENE-LESEQKKSQEYQKGVRKFER 1853
Cdd:TIGR00606 854 DQQEQIQHLKsktnELKSEKLQIGTNLQRRQQFEEQLVEL--STEVQSLIREIKDAKEQdSPLETFLEKDQQEKEELISS 931
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1591544934 1854 riKELSYQGEEDKKNLVR---------MQELIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELDD 1913
Cdd:TIGR00606 932 --KETSNKKAQDKVNDIKekvknihgyMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINE 998
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1473-1910 |
1.11e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.50 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1473 AELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAAL 1552
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1553 EEAEGTLEHEESKTLRIQlELNQIKADVDRKLAEKEEEIDNLRRN---HQRTLESMQATLDAEAKSRSEAVRLRKKMEGD 1629
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLK-KKIQKNKSLESQISELKKQNNQLKDNiekKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1630 LNEMEVQLNHANRLASESQKLLRNLQVQI------------KDVQLELDETIHQNEELKEQVAVTERRNNLLASEVEELR 1697
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEIsdlnnqkeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1698 ALLEQNDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKaitdaammaeel 1777
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK------------ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1778 kkeqdtsahLERMKKNMEQTIKDL-QMRLDEAEQIalKGGKKQVQKLEARVKELENELESEQKKsqeyqkgVRKFERRIK 1856
Cdd:TIGR04523 417 ---------LQQEKELLEKEIERLkETIIKNNSEI--KDLTNQDSVKELIIKNLDNTRESLETQ-------LKVLSRSIN 478
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1591544934 1857 ELSYQGEEDKKNLVRMQELIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHE 1910
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1578-1934 |
1.13e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1578 ADVDRKLAEKEEEIDNLRRNHQR---TLESMQATLDAEAKSRSEAVR---LRKKME--------GDLNEMEVQLNHANRL 1643
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAERyqaLLKEKReyegyellKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1644 ASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQV-AVTERRNNLLASEVEELRALLEQNDRARKLAEHELLEATERVN 1722
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1723 LLHSQNTSLINQKKKLENDLST-------LSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDtsaHLERMKKNME 1795
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEerkrrdkLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE---KLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1796 QTIKDLQMRLDEAEQIALKGG--KKQVQKLEARVKELENELESEQKKsqeyqkgVRKFERRIKELsyqgeedkknlvrmq 1873
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELAdlNAAIAGIEAKINELEEEKEDKALE-------IKKQEWKLEQL--------------- 460
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1591544934 1874 elidklQAKVKSYKRQAEEAEdqantnlSKYRKLQHELDDAEERADMAETQVTKLRVRTRD 1934
Cdd:TIGR02169 461 ------AADLSKYEQELYDLK-------EEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
867-1546 |
1.31e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.50 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 867 LKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLiKTKIQ-LEAKVKEIMERLEDEEEMSATVL 945
Cdd:TIGR04523 24 YKNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNS-NNKIKiLEQQIKDLNDKLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 946 AKKRKLEDECAELKKDIDDLEITLAKVEKEKHATE-------NKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDL 1018
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1019 QAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRK---LEGDLKLSMESVMDLENDKQQLEEKLKKKDFEM 1095
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1096 NEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELEAdracrAKVEKQRGDVARELEelserleesggatsaQIEINKKR 1175
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD-----LNNQKEQDWNKELKS---------------ELKNQEKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1176 ETDILKLRRDLEEAMLHHEATTAGLRKKHADSVAE---LSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKAS 1252
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESEnseKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1253 AEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQNVEELKKQLEEENK 1332
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1333 AKNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKangevaqwrtkyetdAIQRTEELEESKKKLAVRLQEAEEAV 1412
Cdd:TIGR04523 483 NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS---------------LKEKIEKLESEKKEKESKISDLEDEL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1413 EA--SNAKCSSLEKTKHRLQTEIEDLVVD----LERASAAAAALDKKQRNFDKV---LAEWRQKCEECQAELETSQKESR 1483
Cdd:TIGR04523 548 NKddFELKKENLEKEIDEKNKEIEELKQTqkslKKKQEEKQELIDQKEKEKKDLikeIEEKEKKISSLEKELEKAKKENE 627
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1591544934 1484 SLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKS 1546
Cdd:TIGR04523 628 KLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELS 690
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
847-1064 |
1.34e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 847 LLKSAATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAK 926
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 927 VKEIMERLEDEEEMSATVLAK--KRKLEDECAEL--KKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTK 1002
Cdd:COG4942 92 IAELRAELEAQKEELAELLRAlyRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 1003 EKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLE 1064
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1205-1429 |
1.39e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1205 ADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSH 1284
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1285 RARAQAESSELSRKLEEREAT-----------VSQLQRSKNSFSQNVEELKKQLEEENKAKNALAHALQSSRHDCDLLRE 1353
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1591544934 1354 QYDEEQEAKAELQRALSKANGEVAQWRTKYETDAiQRTEELEESKKKLAVRLQ--EAEEAVEASNAKCSSLEKTKHRL 1429
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIArlEAEAAAAAERTPAAGFAALKGKL 255
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1100-1634 |
1.69e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1100 TRIEDEQSLVNQLQKKIKELQARTEELEeeleadracraKVEKQRGDVAReleelserleesggatsaQIEINKKRETDI 1179
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLE-----------KFIKRTENIEE------------------LIKEKEKELEEV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1180 LKLRRDLEEAMLHHEATTAGLRK------KHADSVAELSEQIDSLQRVKQKLE-------KERSEAKMEVDDLASTVEQL 1246
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKevkeleELKEEIEELEKELESLEGSKRKLEekireleERIEELKKEIEELEEKVKEL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1247 SKGKASAEKTCRLYE--DQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQNVEELK 1324
Cdd:PRK03918 286 KELKEKAEEYIKLSEfyEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1325 KQLEEENKAKNalaHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTKyETDAIQRTEELEESKKKLAV- 1403
Cdd:PRK03918 366 EAKAKKEELER---LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE-IKELKKAIEELKKAKGKCPVc 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1404 ----RLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDK--KQRNFDKVLAEWRQKCEECQAE-LE 1476
Cdd:PRK03918 442 grelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEeLE 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1477 TSQKESRSLSTELFKLK----------NSYEETLEHLETIKRENKNLQEEITDLSDQISQ-GAKTIHELEKMKKGLE--- 1542
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKgeikslkkelEKLEELKKKLAELEKKLDELEEELAELLKELEElGFESVEELEERLKELEpfy 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1543 ---IEKSEIQAALEEAEGTLEHEESKTLRIQLELNQIKADVDRKLAE--------KEEEIDNLRRNH---QRTLESMQAT 1608
Cdd:PRK03918 602 neyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEleelekkySEEEYEELREEYlelSRELAGLRAE 681
|
570 580
....*....|....*....|....*.
gi 1591544934 1609 LDAEAKSRSEAVRLRKKMEGDLNEME 1634
Cdd:PRK03918 682 LEELEKRREEIKKTLEKLKEELEERE 707
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1350-1696 |
2.18e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 62.22 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1350 LLREQYDEEQEAKAELQRALSKANGEVAQWRTKYETDaiqrTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRL 1429
Cdd:pfam07888 31 LLQNRLEECLQERAELLQAQEAANRQREKEKERYKRD----REQWERQRRELESRVAELKEELRQSREKHEELEEKYKEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1430 QT------------------------EIEDLVVDL-ERASAAAAALDKKQRNFDKVLAEWRQKCEE---CQAELETSQKE 1481
Cdd:pfam07888 107 SAsseelseekdallaqraahearirELEEDIKTLtQRVLERETELERMKERAKKAGAQRKEEEAErkqLQAKLQQTEEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1482 SRSLSTELFKLKNSYEETLEHLETikrenknLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEh 1561
Cdd:pfam07888 187 LRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGE- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1562 eesktlriqlELNQIKADVDRKLAEKeeeidnlrrnHQRTLESMQATL---DAEAKSRSEAVRLRKKMEGDLNEMEVQLN 1638
Cdd:pfam07888 259 ----------ELSSMAAQRDRTQAEL----------HQARLQAAQLTLqlaDASLALREGRARWAQERETLQQSAEADKD 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 1639 HANRLASESQKLLRNLQ-------------VQIKDVQL-ELDETIHQNEELKEQVAVTERRNNLLASEVEEL 1696
Cdd:pfam07888 319 RIEKLSAELQRLEERLQeermereklevelGREKDCNRvQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1466-1685 |
2.67e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1466 QKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEK 1545
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1546 SEIQAALEEAEGTLeHEESKTLRIQLELNQIKADvdrKLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLRKK 1625
Cdd:COG4942 100 EAQKEELAELLRAL-YRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1626 MEGDLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTERR 1685
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1266-1924 |
7.25e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 61.01 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1266 EAKAKVEELQRQL-NETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQ-NVEELKKQLEEENKAKNALAhaLQS 1343
Cdd:pfam12128 283 ETSAELNQLLRTLdDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDaDIETAAADQEQLPSWQSELE--NLE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1344 SRHDCdLLREQYDEEQEAKAELQRALSKANGEVAqwRTKYETDAIQRTEELEESKKKLAVRLQEAEEAVEASNAKcSSLE 1423
Cdd:pfam12128 361 ERLKA-LTGKHQDVTAKYNRRRSKIKEQNNRDIA--GIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGK-LEFN 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1424 KTKHRLQTEIEDLVVDLERASAAAAALdKKQRNFDkvlaewrQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHL 1503
Cdd:pfam12128 437 EEEYRLKSRLGELKLRLNQATATPELL-LQLENFD-------ERIERAREEQEAANAEVERLQSELRQARKRRDQASEAL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1504 ETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLELN--QIKADVD 1581
Cdd:pfam12128 509 RQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNlyGVKLDLK 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1582 R-KLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLRKKMEgdlnEMEVQLNHANRLASESQKLLRNLQVQikd 1660
Cdd:pfam12128 589 RiDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELE----KASREETFARTALKNARLDLRRLFDE--- 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1661 vqleldetiHQNEELKEQVAVTERRnnllASEVEELRALleqnDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLEn 1740
Cdd:pfam12128 662 ---------KQSEKDKKNKALAERK----DSANERLNSL----EAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVV- 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1741 dLSTLSNEVdDAVQECRNAEEKAKKAITDA--AMMAEELKK---EQDTSAHLERMKKNMEQTIKDLQMRLDEAeqialkg 1815
Cdd:pfam12128 724 -EGALDAQL-ALLKAAIAARRSGAKAELKAleTWYKRDLASlgvDPDVIAKLKREIRTLERKIERIAVRRQEV------- 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1816 gkkqvqkleARVKELENELESEQKksQEYQKGVRKFERRIKELsyqgeedKKNLVRMQELIDKLQAKVKSYKRQAEEAED 1895
Cdd:pfam12128 795 ---------LRYFDWYQETWLQRR--PRLATQLSNIERAISEL-------QQQLARLIADTKLRRAKLEMERKASEKQQV 856
|
650 660
....*....|....*....|....*....
gi 1591544934 1896 QANTNLSKYRKLQHELDDAEERADMAETQ 1924
Cdd:pfam12128 857 RLSENLRGLRCEMSKLATLKEDANSEQAQ 885
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1209-1746 |
8.13e-09 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 60.52 E-value: 8.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1209 AELSEQIDSLQRVKQKLEKERSEAKMEVDDLAStveqlskgKASAEKTCRLYE-DQMNEAKAKVEELQRQLNETNSHRaR 1287
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEK--------KASALKRQLDREsDRNQELQKRIRLLEKREAEAEEAL-R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1288 AQAESS--------ELSRKLEEREATVSQLQRSKNSFSQNVEELKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQ 1359
Cdd:pfam05557 73 EQAELNrlkkkyleALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1360 EAKAELQRALSKAngevaqwrtkyeTDAIQRTEELEeskKKLAVRLQEAEEaVEASNAKCSS---LEKTKHRLQTEIEDL 1436
Cdd:pfam05557 153 QLRQNLEKQQSSL------------AEAEQRIKELE---FEIQSQEQDSEI-VKNSKSELARipeLEKELERLREHNKHL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1437 VVDLERASAAAAALDKKQRNFDKVlaewrqkcEECQAELETSQKESRSLSTEL---FKLKNSYEETLEHLETIKRENKNL 1513
Cdd:pfam05557 217 NENIENKLLLKEEVEDLKRKLERE--------EKYREEAATLELEKEKLEQELqswVKLAQDTGLNLRSPEDLSRRIEQL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1514 QEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQlelnqikadvdRKLAEKEEEIDN 1593
Cdd:pfam05557 289 QQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ-----------RRVLLLTKERDG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1594 LRRNhqrtLESMQATLDAEAKSRSEAVRLRK------KMEGDLNEMEVQLNHANRLASESQKLLRNLQVQIK-------- 1659
Cdd:pfam05557 358 YRAI----LESYDKELTMSNYSPQLLERIEEaedmtqKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQalrqqesl 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1660 ----DVQLELDETIHQNEELKEQVAVTERRNNLLASEVE--ELRALLEQND-RARKLAEHELLEATER----VNLLHSQN 1728
Cdd:pfam05557 434 adpsYSKEEVDSLRRKLETLELERQRLREQKNELEMELErrCLQGDYDPKKtKVLHLSMNPAAEAYQQrknqLEKLQAEI 513
|
570
....*....|....*...
gi 1591544934 1729 TSLINQKKKLENDLSTLS 1746
Cdd:pfam05557 514 ERLKRLLKKLEDDLEQVL 531
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1212-1912 |
9.40e-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: 60.75 E-value: 9.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1212 SEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLnETNSHRARAQAE 1291
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR-EAQEEQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1292 SSELSRKLEEREATVSQLQRSKnsfsqnveelkkqlEEENKAKNALAHALQSSR-HDCDLLREQ-YDEEQEAKAELQRAL 1369
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVLEETQ--------------ERINRARKAAPLAAHIKAvTQIEQQAQRiHTELQSKMRSRAKLL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1370 SKANGEVAQWRTKYETDAIQRTEELEESKKKlavrlQEAEEAVEASNAKCSSLEKTkHRLQTEIEDLVVDLERASAAAAA 1449
Cdd:TIGR00618 328 MKRAAHVKQQSSIEEQRRLLQTLHSQEIHIR-----DAHEVATSIREISCQQHTLT-QHIHTLQQQKTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1450 LDKKQRNFDKVLAEWRQKCEEcQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQgAK 1529
Cdd:TIGR00618 402 LDILQREQATIDTRTSAFRDL-QGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQT-KE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1530 TIHELEKMKKGLEIEKSEIQAALE-EAEGTLEHEESKtlriqlelnQIKADVDRKLAEKEEEIDNLRRNHQRTLESMQAT 1608
Cdd:TIGR00618 480 QIHLQETRKKAVVLARLLELQEEPcPLCGSCIHPNPA---------RQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1609 LDAEaksrseavrlRKKMEGDLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTERRNNL 1688
Cdd:TIGR00618 551 LTSE----------RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1689 LASEVEELRALLEQNDRARKLAEHELLEATERVNLL-----HSQNTSLINQKKKLENDLSTLSNEVDDAVQECRNAEEKA 1763
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTqervrEHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLA 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1764 KKaitdAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQKLEARVKELEN---ELESEQKK 1840
Cdd:TIGR00618 701 QC----QTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNnneEVTAALQT 776
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 1841 SQEYQKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELD 1912
Cdd:TIGR00618 777 GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEIT 848
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
854-1436 |
9.59e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 9.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 854 EKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEIMER 933
Cdd:TIGR02169 377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 934 LEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKV---KNLIEEMAALDETILKLTKEKKALQEA 1010
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVrggRAVEEVLKASIQGVHGTVAQLGSVGER 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1011 HQQTL--------------DDLQAEEdKVNTLTKAQA---------KLEQQVDDLEGSLEQ------------EKKLR-- 1053
Cdd:TIGR02169 537 YATAIevaagnrlnnvvveDDAVAKE-AIELLKRRKAgratflplnKMRDERRDLSILSEDgvigfavdlvefDPKYEpa 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1054 -----------MDLERVKR--------KLEGDL-------------KLSMESVMDLENDK-QQLEEKLKKKDFEMNEMST 1100
Cdd:TIGR02169 616 fkyvfgdtlvvEDIEAARRlmgkyrmvTLEGELfeksgamtggsraPRGGILFSRSEPAElQRLRERLEGLKRELSSLQS 695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1101 RIEDEQSLVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRGDVARELEelserleesggatsaqiEINKKRETDIL 1180
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS-----------------SLEQEIENVKS 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1181 KLRrDLEEAMLHHEATTAGLRKKHADSVAELS-EQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKASAEKTC-- 1257
Cdd:TIGR02169 759 ELK-ELEARIEELEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIqe 837
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1258 -----RLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQNVEELKkqleeenk 1332
Cdd:TIGR02169 838 lqeqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE-------- 909
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1333 aknalahalqssrhdcdllrEQYDEEQEAKAELQRALSKANGEVAQ-----WRTKYETDAIQRTEELEESKKKLAVRLQE 1407
Cdd:TIGR02169 910 --------------------AQIEKKRKRLSELKAKLEALEEELSEiedpkGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
|
650 660 670
....*....|....*....|....*....|....*.
gi 1591544934 1408 -------AEEAVEASNAKCSSLEKTKHRLQTEIEDL 1436
Cdd:TIGR02169 970 lepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1508-1924 |
1.03e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1508 RENKNLQEEITDLSDQISQgaktIHELEKMKKGLEIEKSEIQAALEEAEGtlEHEESKTLRIQLELNQIKADVDRKLAEK 1587
Cdd:COG4717 71 KELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELRE--ELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1588 EEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLRKKMEGDLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQLELDE 1667
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1668 TIHQNEELKEQVAVTERRNNLLASEVE-----ELRALLEQNDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLENDL 1742
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLlliaaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1743 STLsnevdDAVQECRNAEEKAKKAITDAAMMAEELKKEqdtsaHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQK 1822
Cdd:COG4717 305 EEL-----QALPALEELEEEELEELLAALGLPPDLSPE-----ELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1823 LEARVK-ELENELESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKNLVRMQEliDKLQAKVKSYKRQAEEAEDQANTNL 1901
Cdd:COG4717 375 LLAEAGvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELR 452
|
410 420
....*....|....*....|...
gi 1591544934 1902 SKYRKLQHELDDAEERADMAETQ 1924
Cdd:COG4717 453 EELAELEAELEQLEEDGELAELL 475
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1208-1603 |
1.12e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1208 VAELSEQIDSLQRVK---QKLEKERSEAKMEVDDLASTVEQLSKGKASAEKTCRLYED--QMNEAKAKVEELQRQLNETN 1282
Cdd:COG4717 73 LKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1283 shraRAQAESSELSRKLEEREATVSQLQRSKNsfsqnveelkkqlEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAK 1362
Cdd:COG4717 153 ----ERLEELRELEEELEELEAELAELQEELE-------------ELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1363 AELQRALSKANGEVAQWRTKYETDAI-QRTEELEESKKKLAVRL------------------------------------ 1405
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALeERLKEARLLLLIAAALLallglggsllsliltiagvlflvlgllallflllar 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1406 --QEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKCEecQAELETSQKESR 1483
Cdd:COG4717 296 ekASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1484 SLsteLFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKM--KKGLEIEKSEIQAALEEAEGTLEH 1561
Cdd:COG4717 374 AL---LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEE 450
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1591544934 1562 EESKTLRIQLELNQIKAdvDRKLAEKEEEIDNLRRNHQRTLE 1603
Cdd:COG4717 451 LREELAELEAELEQLEE--DGELAELLQELEELKAELRELAE 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
849-1123 |
1.26e-08 |
|
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: 60.46 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 849 KSAATEKELASLKEELAKLKEALEKsevkrkeleerqvsliqekndLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVK 928
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDE---------------------LRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 929 EIMERLEDEEEMSAtvlakkrKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALQ 1008
Cdd:TIGR02168 842 DLEEQIEELSEDIE-------SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1009 eahqqtlDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSL-EQEKKLRMDLERVKRKLEGDLKLSMESVMDLENDKQQL--- 1084
Cdd:TIGR02168 915 -------RELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpv 987
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1591544934 1085 ----EEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQART 1123
Cdd:TIGR02168 988 nlaaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
849-1053 |
1.65e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 849 KSAATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQekndlSLQLQAEQDNLADAEDRCDlliktkiqleakvk 928
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-----LAEYSWDEIDVASAEREIA-------------- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 929 EIMERLEDEEEMSATVlakkRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALQ 1008
Cdd:COG4913 672 ELEAELERLDASSDDL----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1591544934 1009 EAHqqtLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQ-EKKLR 1053
Cdd:COG4913 748 RAL---LEERFAAALGDAVERELRENLEERIDALRARLNRaEEELE 790
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1583-1841 |
2.08e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1583 KLAEKEEEIDNLrrnhQRTLESMQATLDAEAKSRSEAVRLRKKMEGDLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQ 1662
Cdd:COG4942 21 AAAEAEAELEQL----QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1663 LELDEtihQNEELKEQVAVTERrnnllASEVEELRALLEQNDrarklaeheLLEATERVNLLHSQNTSLINQKKKLENDL 1742
Cdd:COG4942 97 AELEA---QKEELAELLRALYR-----LGRQPPLALLLSPED---------FLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1743 STLsnevddavQECRNAEEKAKKAITDAAMMAEELKKEqdtsahLERMKKNMEQTIKDLQMRLDEAEQiALKGGKKQVQK 1822
Cdd:COG4942 160 AEL--------AALRAELEAERAELEALLAELEEERAA------LEALKAERQKLLARLEKELAELAA-ELAELQQEAEE 224
|
250
....*....|....*....
gi 1591544934 1823 LEARVKELENELESEQKKS 1841
Cdd:COG4942 225 LEALIARLEAEAAAAAERT 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
898-1311 |
2.46e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 898 QLQAEQDNLADAEDRCDLLIKTKIQ-LEAKVKEimerLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEK 976
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKeLEEELKE----AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 977 hatenKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLegSLEQEKKLRMDL 1056
Cdd:COG4717 126 -----QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1057 ERVKRkLEGDLKLSMESVMDLENDKQQLEEKLK--KKDFEMNEMSTRIEDEQSL-------------------------- 1108
Cdd:COG4717 199 EELEE-LQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEARLLlliaaallallglggsllsliltiag 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1109 ------------VNQLQKKIKELQARTEELEEELEADRACRAKVEKQRGDVARELEELSERLEESggatSAQIEINKKRE 1176
Cdd:COG4717 278 vlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLEL----LDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1177 TDILKLRRDLEEAMLHHEATtAGLRKKHADSVAELSEQIDSLQRvKQKLEKERSEAKMEVDDLASTVEQLSKGKASAEkt 1256
Cdd:COG4717 354 REAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEE-- 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1591544934 1257 crlYEDQMNEAKAKVEELQRQLNETNSHRARAQAE------SSELSRKLEEREATVSQLQR 1311
Cdd:COG4717 430 ---LEEELEELEEELEELEEELEELREELAELEAEleqleeDGELAELLQELEELKAELRE 487
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
932-1148 |
2.63e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 932 ERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALQEah 1011
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1012 qqtldDLQAEEDKVNTLTKAQAKLEQQ-----------VDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSMESVMDLEND 1080
Cdd:COG4942 98 -----ELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1591544934 1081 KQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRGDVA 1148
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
848-1185 |
3.77e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 848 LKSAATEKELAslkEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKV 927
Cdd:PTZ00121 1462 AKKKAEEAKKA---DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 928 KEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKvknlIEEMAALDETILKLTKEKKAL 1007
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR----IEEVMKLYEEEKKMKAEEAKK 1614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1008 QEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDlKLSMESVMDLENDKQQLEEK 1087
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED-KKKAEEAKKAEEDEKKAAEA 1693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1088 LKKKDFE---MNEMSTRIEDEQSLVNQLQK-----KIKELQARTEELEEELEADRACRAKVEKQRgdVARELEELSERLE 1159
Cdd:PTZ00121 1694 LKKEAEEakkAEELKKKEAEEKKKAEELKKaeeenKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK--IAHLKKEEEKKAE 1771
|
330 340
....*....|....*....|....*.
gi 1591544934 1160 ESGGATSAQIEINKKRETDILKLRRD 1185
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1479-1928 |
5.22e-08 |
|
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: 58.29 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1479 QKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQI-SQGAKTIHELEKMKKGLEIekSEIQAALEEAEG 1557
Cdd:pfam10174 122 QSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLqSKGLPKKSGEEDWERTRRI--AEAEMQLGHLEV 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1558 TLEHEESKTLRIQLEL---NQIKADVDRKLA------EKEEEIDNLRRNHqRTLESMQATLDAEAKSRSEavrlrkKMEG 1628
Cdd:pfam10174 200 LLDQKEKENIHLREELhrrNQLQPDPAKTKAlqtvieMKDTKISSLERNI-RDLEDEVQMLKTNGLLHTE------DREE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1629 DLNEMEVQLNHANRLASESQKLLRNLQ---VQIKDVQLELDETIHQN-------EELKEQVAVTERRNNLLASEVEELRA 1698
Cdd:pfam10174 273 EIKQMEVYKSHSKFMKNKIDQLKQELSkkeSELLALQTKLETLTNQNsdckqhiEVLKESLTAKEQRAAILQTEVDALRL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1699 LLEQNDRARKLAEHELLEATERVNLLHSQNTSL----------INQ-KKKLENdlstLSNEVDDAVQECRNAEEKAKKAI 1767
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLkdmldvkerkINVlQKKIEN----LQEQLRDKDKQLAGLKERVKSLQ 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1768 TDAAMMAEELKKEQDTSAHLERMKKNM-EQTIKDLQMRLDEAEQI--ALKGGKKQVQKLEARVKELENELESEQKKSQEY 1844
Cdd:pfam10174 429 TDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESLkkENKDLKEKVSALQPELTEKESSLIDLKEHASSL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1845 QKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQakvksykrQAEEAEDQANTNLSKYRKLQHELDDAEERADMAETQ 1924
Cdd:pfam10174 509 ASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAE 580
|
....
gi 1591544934 1925 VTKL 1928
Cdd:pfam10174 581 VERL 584
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1534-1815 |
5.86e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 58.00 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1534 LEKMKKG--LEIEKSEIQAALEEAEGTLEheesKTLRIQLELNQIK---ADVDRKLAEKEEEIDNLrrnhqrtlesmQAT 1608
Cdd:PRK11281 45 LDALNKQklLEAEDKLVQQDLEQTLALLD----KIDRQKEETEQLKqqlAQAPAKLRQAQAELEAL-----------KDD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1609 LDAEAKSRSEAVRLRkKMEGDLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVA-------- 1680
Cdd:PRK11281 110 NDEETRETLSTLSLR-QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKggkvggka 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1681 -VTERRNNLLAseveELRALLEQNDRARKLAE-----HELLEA-----TERVNLLHSQNTSL---INQKKKlendlsTLS 1746
Cdd:PRK11281 189 lRPSQRVLLQA----EQALLNAQNDLQRKSLEgntqlQDLLQKqrdylTARIQRLEHQLQLLqeaINSKRL------TLS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1747 NEVddaVQECRNAEEKAKkaITDAAMMAEELKKEQDTSAHL-ERMKKNMEQTIKDLQMR--LDEA--------EQI-ALK 1814
Cdd:PRK11281 259 EKT---VQEAQSQDEAAR--IQANPLVAQELEINLQLSQRLlKATEKLNTLTQQNLRVKnwLDRLtqsernikEQIsVLK 333
|
.
gi 1591544934 1815 G 1815
Cdd:PRK11281 334 G 334
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1494-1935 |
6.77e-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: 57.72 E-value: 6.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1494 NSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLEl 1573
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1574 nqIKADVDRKLAeKEEEIDNLRRNHQRTLESMQATLdaeaksrseaVRLRKKmEGDLNEMEVQLNHANRLASESQKLLRN 1653
Cdd:TIGR04523 112 --IKNDKEQKNK-LEVELNKLEKQKKENKKNIDKFL----------TEIKKK-EKELEKLNNKYNDLKKQKEELENELNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1654 LQVQIKDVQLELDETIHQNEELKEQVAVTE---RRNNLLASEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTS 1730
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLELLLSNLKkkiQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1731 LINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKAITDAammaEELK--KEQDTSAHLERMKKNMEQTIKDLQMRLDEA 1808
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI----SDLNnqKEQDWNKELKSELKNQEKKLEEIQNQISQN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1809 EQI------ALKGGKKQVQKLEARVKELENELESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAK 1882
Cdd:TIGR04523 334 NKIisqlneQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1591544934 1883 VKSYKRQAEEAEDQANTNLSKYRKLQHELDDAEERADMAETQVTKLRVRTRDQ 1935
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1335-1933 |
7.19e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.60 E-value: 7.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1335 NALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTKYE--TDAIQRTEELEESKKKLAVRLQEAEEAV 1412
Cdd:PRK01156 186 DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDMKNRYESEIKTAESDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1413 EASNAKCSSLEKTKHRLQtEIEDLVVDLERASAAAAALDKKQrnfdkvLAEWRQKCEECQAELETSQKESRSLStELFKL 1492
Cdd:PRK01156 266 SMELEKNNYYKELEERHM-KIINDPVYKNRNYINDYFKYKND------IENKKQILSNIDAEINKYHAIIKKLS-VLQKD 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1493 KNSYEETlehletiKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLE 1572
Cdd:PRK01156 338 YNDYIKK-------KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1573 LNQIKADVDR---KLAEKEEEIDNLRRNHQRTLESMqATLDAEAKSRSEAVRLRKKMEGDLnemevqLNHANRLASESQK 1649
Cdd:PRK01156 411 LNEINVKLQDissKVSSLNQRIRALRENLDELSRNM-EMLNGQSVCPVCGTTLGEEKSNHI------INHYNEKKSRLEE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1650 LLRNLQVQIKDVqleldetihqNEELKEQVAVTERrnnLLASEVEELrallEQNDRARKLAEHELleatervnllhsqnt 1729
Cdd:PRK01156 484 KIREIEIEVKDI----------DEKIVDLKKRKEY---LESEEINKS----INEYNKIESARADL--------------- 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1730 slinqkKKLENDLSTLsnevddavqecRNAEEKAKKAITDAAMMAEELKKEQDTSaHLERMKKNMEQTIKDLQMRLDEAe 1809
Cdd:PRK01156 532 ------EDIKIKINEL-----------KDKHDKYEEIKNRYKSLKLEDLDSKRTS-WLNALAVISLIDIETNRSRSNEI- 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1810 qialkggKKQVQKLEARVKELENELESEQKKSQEYqkgVRKFERRIKELsyqgeEDKKNLVR-MQELIDKLQAKVKSYKR 1888
Cdd:PRK01156 593 -------KKQLNDLESRLQEIEIGFPDDKSYIDKS---IREIENEANNL-----NNKYNEIQeNKILIEKLRGKIDNYKK 657
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1591544934 1889 QAEEAED----------QANTNLSKYRKLQHELDDAeeRADMAETQVTKLRVRTR 1933
Cdd:PRK01156 658 QIAEIDSiipdlkeitsRINDIEDNLKKSRKALDDA--KANRARLESTIEILRTR 710
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
843-1025 |
8.21e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 55.32 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 843 KIKPLLKSAATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRcdlliktkiq 922
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 923 lEAKVKEIMERLEDEEEMSAtvlakkrkLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTK 1002
Cdd:COG1579 75 -IKKYEEQLGNVRNNKEYEA--------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
170 180
....*....|....*....|...
gi 1591544934 1003 EKKALQEAHQQTLDDLQAEEDKV 1025
Cdd:COG1579 146 ELDEELAELEAELEELEAEREEL 168
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
950-1908 |
1.11e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 57.37 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 950 KLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLT---------KEKKALQEAHQQTLDDLQA 1020
Cdd:TIGR01612 1108 KYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVAdkaisnddpEEIEKKIENIVTKIDKKKN 1187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1021 EEDKVNTLTKAQAKLEQQvddlEGSLEQEKKLRMD---------LERV---KRKLEGDLKlSMESVM-DLENDKQQLEEK 1087
Cdd:TIGR01612 1188 IYDEIKKLLNEIAEIEKD----KTSLEEVKGINLSygknlgklfLEKIdeeKKKSEHMIK-AMEAYIeDLDEIKEKSPEI 1262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1088 LKKKDFEMNemstrIEDEQSLVNQLQKKIKELQARTEeleeeleadracraKVEKQRGDVAREleelserleesggatSA 1167
Cdd:TIGR01612 1263 ENEMGIEMD-----IKAEMETFNISHDDDKDHHIISK--------------KHDENISDIREK---------------SL 1308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1168 QIEINKKRETDILKLRRDLE----EAMLHHEATTAGLRK----KHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDL 1239
Cdd:TIGR01612 1309 KIIEDFSEESDINDIKKELQknllDAQKHNSDINLYLNEianiYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKS 1388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1240 ASTVEQLSKGkaSAEKTCR------LYEDQMNEAKAKVEELQRQL------NETNSHRARAQAESSELSRKLEEREATVS 1307
Cdd:TIGR01612 1389 EKLIKKIKDD--INLEECKskiestLDDKDIDECIKKIKELKNHIlseesnIDTYFKNADENNENVLLLFKNIEMADNKS 1466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1308 Q--LQRSKNSFSQ----NVEELKKQLEEENKAKN-ALAHALQSSRHDcdLLREQYdeeqeaKAELQRALSKANG-EVAQW 1379
Cdd:TIGR01612 1467 QhiLKIKKDNATNdhdfNINELKEHIDKSKGCKDeADKNAKAIEKNK--ELFEQY------KKDVTELLNKYSAlAIKNK 1538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1380 RTKYETDAIQRTEELEESKKKLAVRLQEAEEaveasnaKCSSLEKTKHRlqteIEDLVVDLERASAAAAALDKKQRNFDK 1459
Cdd:TIGR01612 1539 FAKTKKDSEIIIKEIKDAHKKFILEAEKSEQ-------KIKEIKKEKFR----IEDDAAKNDKSNKAAIDIQLSLENFEN 1607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1460 VL---AEWRQKCEECQAELETSQKESRSLS-----TELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTI 1531
Cdd:TIGR01612 1608 KFlkiSDIKKKINDCLKETESIEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIE 1687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1532 HELEKMKKGLEI------------EKSEIQAALEEAEGTLEHEESKTLRIQLElnqiKADVDRKLAEKEEEID------- 1592
Cdd:TIGR01612 1688 IDVDQHKKNYEIgiiekikeiaiaNKEEIESIKELIEPTIENLISSFNTNDLE----GIDPNEKLEEYNTEIGdiyeefi 1763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1593 ---NLRRNHQRTLESMQATLDAEAKSRSEA-------VRLRKKMEGDLNEMEVqlNHANRLASESQKLLRNLQVQIKDVQ 1662
Cdd:TIGR01612 1764 elyNIIAGCLETVSKEPITYDEIKNTRINAqneflkiIEIEKKSKSYLDDIEA--KEFDRIINHFKKKLDHVNDKFTKEY 1841
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1663 LELDETIHQNEELKEQVAVTERRNNLL--ASEVEEL------RALLEQNDRARKLAEHeLLEATERVNlLHSQNTSLINQ 1734
Cdd:TIGR01612 1842 SKINEGFDDISKSIENVKNSTDENLLFdiLNKTKDAyagiigKKYYSYKDEAEKIFIN-ISKLANSIN-IQIQNNSGIDL 1919
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1735 KKKLEND-LSTLSNEVDDAVQECRNAEEKAK---------KAITDAAMMAEEL-KKEQDTsahLERMKKNMEQTIKdlqM 1803
Cdd:TIGR01612 1920 FDNINIAiLSSLDSEKEDTLKFIPSPEKEPEiytkirdsyDTLLDIFKKSQDLhKKEQDT---LNIIFENQQLYEK---I 1993
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1804 RLDEAEQIALKGGKKQVQKLEARVKEL---ENELESEQKKSQEYQKGVRKFER-RIKELSYQGEEDKKNLV------RMQ 1873
Cdd:TIGR01612 1994 QASNELKDTLSDLKYKKEKILNDVKLLlhkFDELNKLSCDSQNYDTILELSKQdKIKEKIDNYEKEKEKFGidfdvkAME 2073
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|..
gi 1591544934 1874 EL-------IDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQ 1908
Cdd:TIGR01612 2074 EKfdndikdIEKFENNYKHSEKDNHDFSEEKDNIIQSKKKLK 2115
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1349-1936 |
1.64e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1349 DLLREQYD--EEQEAKAELQRALSKANGEVAQWrtkyetDAIQRTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTK 1426
Cdd:TIGR02169 194 DEKRQQLErlRREREKAERYQALLKEKREYEGY------ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1427 HRLQTEIEDLVVDLERA-SAAAAALDKKQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLET 1505
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1506 IKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAegtleheesktlriQLELNQIKADVDRKLA 1585
Cdd:TIGR02169 348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL--------------KREINELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1586 EKEEEIDNLRRNHQR--TLESMQATLDAEAKSRSEAVrlrKKMEGDLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQL 1663
Cdd:TIGR02169 414 ELQRLSEELADLNAAiaGIEAKINELEEEKEDKALEI---KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1664 ELDETIHQNEELKEQVAVTERRNNLLASEVEELRALLEQ----------------NDRARKLAEHELLEATERVNLLHSQ 1727
Cdd:TIGR02169 491 ELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQlgsvgeryataievaaGNRLNNVVVEDDAVAKEAIELLKRR 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1728 NTSL-----INQKKKLENDLSTLSNE--VDDAVQ--ECRNAEEKA-KKAITDAAMMAE-ELKKEQDTSAHL-----ERMK 1791
Cdd:TIGR02169 571 KAGRatflpLNKMRDERRDLSILSEDgvIGFAVDlvEFDPKYEPAfKYVFGDTLVVEDiEAARRLMGKYRMvtlegELFE 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1792 KNMEQTIKDLQMRLDEAEQIALKGgkkQVQKLEARVKELENELESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKNLVR 1871
Cdd:TIGR02169 651 KSGAMTGGSRAPRGGILFSRSEPA---ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ 727
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1591544934 1872 MQELIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELDDAEERADMAETQVTKLRVRTRDQG 1936
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR 792
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1424-1858 |
1.84e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1424 KTKHRLQTEIEDLVVDLERASAAAAALDKKQRNfdkvLAEWRQKCEECQAELETSQKESRSLSTELfklknSYEETLEHL 1503
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEE----LEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1504 ETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLELNQIKADVDRK 1583
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1584 LAEKEEEIDNLRRNHQRTLESMQATLDAEAKSR------SEAVRLRKKMEGDLNEMEVQLNHANRLA---------SESQ 1648
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEarllllIAAALLALLGLGGSLLSLILTIAGVLFLvlgllallfLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1649 KLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTERRNNLLASEVEEL----RALLEQNDRARKLAEHELLEA--TERVN 1722
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELldriEELQELLREAEELEEELQLEEleQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1723 LLHSQNTS----------LINQKKKLENDLSTLSNEVDDAvqecrNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKK 1792
Cdd:COG4717 375 LLAEAGVEdeeelraaleQAEEYQELKEELEELEEQLEEL-----LGELEELLEALDEEELEEELEELEEELEELEEELE 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1591544934 1793 NMEQTIKDLQMRLDEAEqialkgGKKQVQKLEARVKELENELESEQKKSQEYQKGVRKFERRIKEL 1858
Cdd:COG4717 450 ELREELAELEAELEQLE------EDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
826-1318 |
2.28e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.88 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 826 IRAFNAVKHWPWMKLFFKIKPLLKSAATEKELASLKEELAKLKEALEKSEVKRKELE--------ERQVSLIQEKNDLSL 897
Cdd:pfam05483 147 IKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRvqaenarlEMHFKLKEDHEKIQH 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 898 QLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEIMERLEDEEEmSATVLAKKRKLEDE-CAELKKDIDDLEITLAKVEKEK 976
Cdd:pfam05483 227 LEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRD-KANQLEEKTKLQDEnLKELIEKKDHLTKELEDIKMSL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 977 HATENKVKNLIEEMAALDETILKLTKEKKALQEA--HQQTLDDLQAEEDKVNTLTKAQA-KLEQQvdDLEGSLEQEKKLR 1053
Cdd:pfam05483 306 QRSMSTQKALEEDLQIATKTICQLTEEKEAQMEElnKAKAAHSFVVTEFEATTCSLEELlRTEQQ--RLEKNEDQLKIIT 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1054 MDLERVKRKLEGDLKLSMESVMDLENDKQQLEEKLK----KKDFEmnEMSTRIE-DEQSLVNQLQKKIKELQARTEELEE 1128
Cdd:pfam05483 384 MELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKlldeKKQFE--KIAEELKgKEQELIFLLQAREKEIHDLEIQLTA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1129 ELEADRACRAKVEKQRGDV-----------ARELEELSERLEESGGATSAQIEI---------NKKRETDILKLRRDLEE 1188
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKTELekeklknieltAHCDKLLLENKELTQEASDMTLELkkhqediinCKKQEERMLKQIENLEE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1189 amlhheaTTAGLRkkhadsvaelseqiDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKASAEKTCRLYEDQMNEAK 1268
Cdd:pfam05483 542 -------KEMNLR--------------DELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLK 600
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1269 AKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQ 1318
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ 650
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1627-1864 |
2.30e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1627 EGDLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTERRNNLLASEVEELRALLEQndRA 1706
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--RA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1707 RKLAEHELLEATERVnLLHSQNTS-LINQkkklENDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTsa 1785
Cdd:COG3883 93 RALYRSGGSVSYLDV-LLGSESFSdFLDR----LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE-- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1591544934 1786 hLERMKKNMEQTIKDLQMRLDEAEQialkggkkQVQKLEARVKELENELESEQKKSQEYQKGVRKFERRIKELSYQGEE 1864
Cdd:COG3883 166 -LEAAKAELEAQQAEQEALLAQLSA--------EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1754-1941 |
2.46e-07 |
|
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: 56.22 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1754 QECRNAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQMRLDEAEQialkggkkQVQKLEARVKELENE 1833
Cdd:TIGR02168 216 KELKAELRELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEELRLEVSELEEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1834 LESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELDD 1913
Cdd:TIGR02168 283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE 362
|
170 180
....*....|....*....|....*...
gi 1591544934 1914 AEERADMAETQVTKLRVRTRDQGSKFAE 1941
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETLRSKVAQ 390
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1458-1941 |
2.77e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1458 DKVLAEWRQKCEECQAELETSQKESRSLSTELFKLknsyEETLEHLETIKRENKNLQEEitdlsdqiSQGAKTIHELEKM 1537
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKA----EEARKAEDARKAEEARKAED--------AKRVEIARKAEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1538 KKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLELNQIKAdvdRKLAEKEEEIDNLRRnhqrtlesmqatldAEAKSRS 1617
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEA---ARKAEEERKAEEARK--------------AEDAKKA 1226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1618 EAVR----LRKKMEGDLNEMEVQLNHANRLASESQKL-LRNLQVQIKDVQLELDETIHQNEELKEqvaVTERRNNLLASE 1692
Cdd:PTZ00121 1227 EAVKkaeeAKKDAEEAKKAEEERNNEEIRKFEEARMAhFARRQAAIKAEEARKADELKKAEEKKK---ADEAKKAEEKKK 1303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1693 VEELRALLEQN---DRARKLAEhellEATERVNLLHSQntslINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKAITD 1769
Cdd:PTZ00121 1304 ADEAKKKAEEAkkaDEAKKKAE----EAKKKADAAKKK----AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1770 AAMMAEELKKEQDTSAHLERMKKNMEQTIKdlqmrldEAEQIAlkggkkqvQKLEARVKELENELESEQKKSQEYQKGVR 1849
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKK-------KADELK--------KAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1850 KFERRIKELSYQGEEDKKnlvrMQELIDKLQAKVKS--YKRQAEEAE--DQANTNLSKYRKLQHELDDAEERADMAETQV 1925
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKK----AEEAKKKAEEAKKAdeAKKKAEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
490
....*....|....*.
gi 1591544934 1926 TKLRVRTRDQGSKFAE 1941
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEE 1532
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1434-1868 |
3.27e-07 |
|
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: 55.45 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1434 EDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKCEECQAELETSQKEsrsLSTELFKLKNsyEETLEHLETIKRENKNL 1513
Cdd:pfam13166 89 EESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDE---CWKKIKRKKN--SALSEALNGFKYEANFK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1514 QEEITDLSDQISQgAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLeheesktlrIQLELNQIKADVDRKLAEKEEEIDN 1593
Cdd:pfam13166 164 SRLLREIEKDNFN-AGVLLSDEDRKAALATVFSDNKPEIAPLTFNV---------IDFDALEKAEILIQKVIGKSSAIEE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1594 LRRNH------QRTLESMQATLDAEAKSRSEAVRLRKKMEGDL--NEMEVQLNHANRLASESQKLLRNLQVQIKDVqlel 1665
Cdd:pfam13166 234 LIKNPdladwvEQGLELHKAHLDTCPFCGQPLPAERKAALEAHfdDEFTEFQNRLQKLIEKVESAISSLLAQLPAV---- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1666 DETIHQNEELKEQVAVTERRNNLLASEVEELRALLEQNdRARKLAEHELLEATErvnllhsqNTSLINQKKKLENDLSTL 1745
Cdd:pfam13166 310 SDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAK-RKDPFKSIELDSVDA--------KIESINDLVASINELIAK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1746 SNEVDDavqecrNAEEKAKKAITD-AAMMAEELKKEQDTsahLERMKKNMEQTIKDLQMRLDEAEqialkggkKQVQKLE 1824
Cdd:pfam13166 381 HNEITD------NFEEEKNKAKKKlRLHLVEEFKSEIDE---YKDKYAGLEKAINSLEKEIKNLE--------AEIKKLR 443
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1591544934 1825 ARVKELENELESEQKKSQEYQKGVRKFERRIKELSYqgEEDKKN 1868
Cdd:pfam13166 444 EEIKELEAQLRDHKPGADEINKLLKAFGFGELELSF--NEEGKG 485
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
948-1533 |
3.39e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 948 KRKLEDECAELKKDIDDLEITLAKVEKekhaTENKVKNLiEEMAALDETILKLtKEKKALQEAHQQTLDDLQAEEdKVNT 1027
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALED----AREQIELL-EPIRELAERYAAA-RERLAELEYLRAALRLWFAQR-RLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1028 LTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDL-KLSMESVMDLENDKQQLEEKLKKKDFEMNEMSTRIE--- 1103
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAalg 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1104 -----DEQSLVNqLQKKIKELQARTEELEEELEADRAcRAKVEKQRGDVAREleelserleesggATSAQIEINKKRETD 1178
Cdd:COG4913 373 lplpaSAEEFAA-LRAEAAALLEALEEELEALEEALA-EAEAALRDLRRELR-------------ELEAEIASLERRKSN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1179 I----LKLRRDLEEAM------------------------------LHHEATTAGLRKKHADSVAELSEQIDSLQRVK-Q 1223
Cdd:COG4913 438 IparlLALRDALAEALgldeaelpfvgelievrpeeerwrgaiervLGGFALTLLVPPEHYAAALRWVNRLHLRGRLVyE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1224 KLEKERSEAKMEVDDLASTVEQLSkgkaSAEKTCRLY-EDQMNEAKA-----KVEELQRQ--------LNETNSHRARAQ 1289
Cdd:COG4913 518 RVRTGLPDPERPRLDPDSLAGKLD----FKPHPFRAWlEAELGRRFDyvcvdSPEELRRHpraitragQVKGNGTRHEKD 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1290 AESSELSR---------KLEEREATVSQLQRSKNSFSQNVEELKKQLEEENKAKNALAHALQSSRHDCDLlrEQYDEEQE 1360
Cdd:COG4913 594 DRRRIRSRyvlgfdnraKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV--ASAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1361 AKAELQRALSKANGEVaqwrtkyetdaiqrtEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDL 1440
Cdd:COG4913 672 ELEAELERLDASSDDL---------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1441 ERASAAAAA-----LDKK--QRNFDKVLAEWRqkcEECQAELETSQKESRSLSTELFKLKNSY----------------- 1496
Cdd:COG4913 737 EAAEDLARLelralLEERfaAALGDAVERELR---ENLEERIDALRARLNRAEEELERAMRAFnrewpaetadldadles 813
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1591544934 1497 -EETLEHLETIKRE-------------NKNLQEEITDLSDQISQGAKTIHE 1533
Cdd:COG4913 814 lPEYLALLDRLEEDglpeyeerfkellNENSIEFVADLLSKLRRAIREIKE 864
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
925-1537 |
5.06e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 925 AKVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEK 1004
Cdd:PRK02224 216 AELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEER 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1005 KALqeahqqtLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEkklRMDLERVKRKLEGdlklsmesvmdLENDKQQL 1084
Cdd:PRK02224 296 DDL-------LAEAGLDDADAEAVEARREELEDRDEELRDRLEEC---RVAAQAHNEEAES-----------LREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1085 EEKLKKKDFEMNEMSTRIEDeqslvnqlqkkikelqarteeleeeleadraCRAKVEKQRGDVARELeelserleesgga 1164
Cdd:PRK02224 355 EERAEELREEAAELESELEE-------------------------------AREAVEDRREEIEELE------------- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1165 tsAQIEINKKRETDILKLRRDLEEAMLHHEATTAGLRKKHADSVAELSEQIDSLQRVKQKLEKER-SEAKMEVDDlASTV 1243
Cdd:PRK02224 391 --EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcPECGQPVEG-SPHV 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1244 EQLSKGKASAEKtcrlYEDQMNEAKAKVEELQRQLNetnshRARAQAESSELSRKLEEREATVSQLQRSKNSfsqNVEEL 1323
Cdd:PRK02224 468 ETIEEDRERVEE----LEAELEDLEEEVEEVEERLE-----RAEDLVEAEDRIERLEERREDLEELIAERRE---TIEEK 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1324 KKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTKYE-----TDAIQRTEELEESK 1398
Cdd:PRK02224 536 RERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTllaaiADAEDEIERLREKR 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1399 KKLAVRLQEAEEAVEASNAKCSSLEKTKHrlQTEIEDLVVDLERASAAAAALDKKqrnfdkvLAEWRQKCEECQAE---L 1475
Cdd:PRK02224 616 EALAELNDERRERLAEKRERKRELEAEFD--EARIEEAREDKERAEEYLEQVEEK-------LDELREERDDLQAEigaV 686
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 1476 ETSQKESRSLSTELFKLknsyEETLEHLETIKRENKNLQEEITDLSDQISQgaKTIHELEKM 1537
Cdd:PRK02224 687 ENELEELEELRERREAL----ENRVEALEALYDEAEELESMYGDLRAELRQ--RNVETLERM 742
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1399-1890 |
5.42e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1399 KKLAVRLQEAEEAVEASNAkcssLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFdkvlaEWRQKCEECQAELETS 1478
Cdd:COG4717 74 KELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKLLQLL-----PLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1479 QKESRSLSTELfklkNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKtiHELEKMKKGLEieksEIQAALEEAEGT 1558
Cdd:COG4717 145 PERLEELEERL----EELRELEEELEELEAELAELQEELEELLEQLSLATE--EELQDLAEELE----ELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1559 LEheesktlRIQLELNQIKADVDRKLAEKEEEidnlrrNHQRTLESMQATLDAEAKSRSEAVRLRKKMEGDLNEMEVQLN 1638
Cdd:COG4717 215 LE-------EAQEELEELEEELEQLENELEAA------ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1639 HANRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTERRNNLLASEVEELRALLEQNDRARKLaEHELLEAT 1718
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL-LREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1719 ERVNLLHSQNtsliNQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLErmKKNMEQTI 1798
Cdd:COG4717 361 EELQLEELEQ----EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD--EEELEEEL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1799 KDLQMRLDEAEQiALKGGKKQVQKLEARVKELENELESEQKKSQEYQKgvrkfERRIKELsyqgEEDKKNLVRMQELIDK 1878
Cdd:COG4717 435 EELEEELEELEE-ELEELREELAELEAELEQLEEDGELAELLQELEEL-----KAELREL----AEEWAALKLALELLEE 504
|
490
....*....|..
gi 1591544934 1879 LQAKVKSYKRQA 1890
Cdd:COG4717 505 AREEYREERLPP 516
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
922-1307 |
6.53e-07 |
|
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: 54.13 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 922 QLEAKVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLT 1001
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1002 KEKKAL---QEAHQQTLDDLqaeEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSMESVMDLE 1078
Cdd:pfam07888 115 EEKDALlaqRAAHEARIREL---EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1079 NDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRGDVARELEELserl 1158
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQR---- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1159 eesggaTSAQIEINKKR-ETDILKLR-RDLEEAMLHHEATTAGLRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEV 1236
Cdd:pfam07888 268 ------DRTQAELHQARlQAAQLTLQlADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER 341
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1591544934 1237 DDLASTVEQlskgkasaEKTCRLYedQMNEAKAKVEELQRQLNETNSHRARAQAESSEL---SRKLEEREATVS 1307
Cdd:pfam07888 342 EKLEVELGR--------EKDCNRV--QLSESRRELQELKASLRVAQKEKEQLQAEKQELleyIRQLEQRLETVA 405
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1507-1740 |
7.88e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1507 KRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLELNQIKADvdrkLAE 1586
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE----LEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1587 KEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLRKKMegdlnemevqlnhaNRLASESQKLLRNLQVQIKDVQLELD 1666
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL--------------KYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1591544934 1667 ETIHQNEELKEQVAVTERRNNLLASEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLEN 1740
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
656-683 |
9.05e-07 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 50.81 E-value: 9.05e-07
10 20
....*....|....*....|....*...
gi 1591544934 656 SQLHKENLNKLMTNLRSTQPHFVRCIIP 683
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1359-1590 |
9.55e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1359 QEAKAELQRALSKANGEVAQwrtkyetdAIQRTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVV 1438
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAE--------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1439 DLERASAAaaaLDKKQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEIT 1518
Cdd:COG4942 91 EIAELRAE---LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 1519 DLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLELNQIKADVDRKLAEKEEE 1590
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
843-1243 |
9.69e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 843 KIKPLLKSAATEKELASLKEELAKLKEALEKSEVKRKELEERQVSliqekndlslQLQAEQDNLADAEDRCDLLIKTKiq 922
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE----------EAKKAEEDKNMALRKAEEAKKAE-- 1590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 923 lEAKVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDiddlEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTK 1002
Cdd:PTZ00121 1591 -EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1003 EKKALQEAHQQTLDDLQAEEDKvntltkaqAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSMESVMDLENDKQ 1082
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDE--------KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1083 QLEEKLKKKDfemnemSTRIEDEQSLVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRGDVARELEELSERLEE-S 1161
Cdd:PTZ00121 1738 EAEEDKKKAE------EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANiI 1811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1162 GGATSAQIEINKKRETDILKLR---------RDLEEAMLHHEATTAGLRKKHADSVAELSEQIDSLQRVKQKLEKERSEA 1232
Cdd:PTZ00121 1812 EGGKEGNLVINDSKEMEDSAIKevadsknmqLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
410
....*....|.
gi 1591544934 1233 KMEVDDLASTV 1243
Cdd:PTZ00121 1892 KIDKDDIEREI 1902
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1475-1837 |
1.31e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 53.15 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1475 LETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAAL-- 1552
Cdd:pfam19220 36 IEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELrd 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1553 -----EEAEGTL--EHEESKTLRIQLELNQIKADV-DRKLAEKEEEIDNLRRNHQRtlesmqatldAEAKSRseavRLRK 1624
Cdd:pfam19220 116 ktaqaEALERQLaaETEQNRALEEENKALREEAQAaEKALQRAEGELATARERLAL----------LEQENR----RLQA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1625 KMEgdlnEMEVQLNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNE----ELKEQVAVTERRNNLLASEVEELRALL 1700
Cdd:pfam19220 182 LSE----EQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAEREraeaQLEEAVEAHRAERASLRMKLEALTARA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1701 EQNDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQEcRNAEEKAKKAITD-AAMMAEELKk 1779
Cdd:pfam19220 258 AATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQ-FQEMQRARAELEErAEMLTKALA- 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1591544934 1780 eqDTSAHLERMkknmEQTIKDLQMRLDEAEQIALKggkkQVQKLEARVKELENELESE 1837
Cdd:pfam19220 336 --AKDAALERA----EERIASLSDRIAELTKRFEV----ERAALEQANRRLKEELQRE 383
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1664-1941 |
1.52e-06 |
|
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: 53.53 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1664 ELDETIHQNEELKEQVAVTERRNNLLASEVEELRALLeQNDRARKLAEHELLEATERVNLlhsqnTSLINQKKKLENDLS 1743
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERL-RREREKAERYQALLKEKREYEG-----YELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1744 TLSNEVDDAVQEcrnaeekakkaITDAAMMAEELKKEqdtSAHLERMKKNMEQTIKDLqmrlDEAEQIALKGG----KKQ 1819
Cdd:TIGR02169 241 AIERQLASLEEE-----------LEKLTEEISELEKR---LEEIEQLLEELNKKIKDL----GEEEQLRVKEKigelEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1820 VQKLEARVKELENELESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKRQAEEAEDQANT 1899
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1591544934 1900 NLSKYRKLQHELDDAEERADMAETQVTKLRVRTRDQGSKFAE 1941
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
977-1233 |
1.53e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 977 HATENKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSL----EQEKKL 1052
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1053 RMDLERVKRKLEGDLKlsmesVMDLENDKQQLEEKLKKKDFemNEMSTRIEDEQSLVNQLQKKIKELQARteeleeelea 1132
Cdd:COG4942 96 RAELEAQKEELAELLR-----ALYRLGRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRAD---------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1133 dracRAKVEKQRGDVAreleelserleesggatsAQIEINKKRETDILKLRRDLEEAMLHHEATTAGLRKK---HADSVA 1209
Cdd:COG4942 159 ----LAELAALRAELE------------------AERAELEALLAELEEERAALEALKAERQKLLARLEKElaeLAAELA 216
|
250 260
....*....|....*....|....
gi 1591544934 1210 ELSEQIDSLQRVKQKLEKERSEAK 1233
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAA 240
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1535-1913 |
1.69e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 53.37 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1535 EKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLELNQIKA----DVDRKLAEKEEEIDNLRRNHQRTLESMQATLD 1610
Cdd:PLN02939 48 KKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTssddDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1611 AEAKSRSEAVRLRKKMEGDLNEMEVQ-LNHANRLASESQKLlrnlQVQIKDVQLELDETIHQNEELKEQVAVTErrnnLL 1689
Cdd:PLN02939 128 FQLEDLVGMIQNAEKNILLLNQARLQaLEDLEKILTEKEAL----QGKINILEMRLSETDARIKLAAQEKIHVE----IL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1690 ASEVEELRALLEQNDRARKLAEHELleaTERVNLLHSQNTSLinqkkklENDLSTLSNEVDdavqecrnaeekakkaitd 1769
Cdd:PLN02939 200 EEQLEKLRNELLIRGATEGLCVHSL---SKELDVLKEENMLL-------KDDIQFLKAELI------------------- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1770 aammaeELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQKLEARVKELENELESEQKKSQEYQ---K 1846
Cdd:PLN02939 251 ------EVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAAlvlD 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1591544934 1847 GVRKFERRIKELSYQGEEdkKNLVRMQ-ELIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELDD 1913
Cdd:PLN02939 325 QNQDLRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQD 390
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1255-1711 |
1.86e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1255 KTCRLYEDQMNEAKAKVEELQRQLNEtnshRARAQAESSELSRKLEEREATVSQLQRSKNSFSQNVEELKKQLEEenkak 1334
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL----- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1335 nalaHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTKYETDAIQRTEELEESKKKLAVRLQEAEEAVEA 1414
Cdd:COG4717 135 ----EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1415 SNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAAldKKQRNFDKVLAEwrqkceecQAELETSQKESRSLSTELFKLKN 1494
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEERL--KEARLLLLIAAA--------LLALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1495 SYEETLEHLETI-KRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHeesktlrIQLEL 1573
Cdd:COG4717 281 LVLGLLALLFLLlAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE-------LQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1574 NQIKAdvdrklAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLRKKMEGDLNEMEVQLNHANRLASESQKLL-- 1651
Cdd:COG4717 354 REAEE------LEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALde 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1652 RNLQVQIKDVQLELDETIHQNEELKEQVAVTERRNNLLASEVEELRALLEQNDRARKLAE 1711
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
967-1168 |
2.79e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 967 ITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSL 1046
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1047 E------QEKKLRMD-----------------LERVKRKLEGDLKLsmesVMDLENDKQQLEEKLKKKDFEMNEMSTRIE 1103
Cdd:COG3883 89 GeraralYRSGGSVSyldvllgsesfsdfldrLSALSKIADADADL----LEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1591544934 1104 DEQSLVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRGDVARELEELSERLEESGGATSAQ 1168
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1064-1319 |
3.02e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1064 EGDLKLSMESVMDLENDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARteeleeeleADRAcRAKVEKQ 1143
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---------IAEA-EAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1144 RGDVAREleelserleesggATSAQIEINKKRETDILKLRRDLEEAMlhheaTTAGLRKKHADSVAELseqIDSLQRVKQ 1223
Cdd:COG3883 85 REELGER-------------ARALYRSGGSVSYLDVLLGSESFSDFL-----DRLSALSKIADADADL---LEELKADKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1224 KLEKERSEAKMEVDDLASTVEQLSKGKASAEKtcrlyedQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEERE 1303
Cdd:COG3883 144 ELEAKKAELEAKLAELEALKAELEAAKAELEA-------QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
250
....*....|....*.
gi 1591544934 1304 ATVSQLQRSKNSFSQN 1319
Cdd:COG3883 217 AAAAAAAAAAAAAAAA 232
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
852-1062 |
3.90e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 852 ATEKELASLKEELAKLKEALEKSEVKRK------ELEERQVSLIQEKNDLS-LQLQAEQDNLADAEDRCDLLIKTKIQLE 924
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREqiellePIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 925 AKVKEIMERLEDEEEMSATVLAKKRKLEDECAELK-KDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKE 1003
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1591544934 1004 KKALQEAHQQTLDDLQAEEDKvntLTKAQAKLEQQVDDLEgslEQEKKLRMDLERVKRK 1062
Cdd:COG4913 382 FAALRAEAAALLEALEEELEA---LEEALAEAEAALRDLR---RELRELEAEIASLERR 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1387-1620 |
3.92e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1387 AIQRTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQ 1466
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1467 KCEECQAELE----TSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLE 1542
Cdd:COG4942 98 ELEAQKEELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1543 IEKSEIQ---AALEEAegtleheesktlriQLELNQIKADVDRKLAEKEEEIDNLRRNhQRTLESMQATLDAEAKSRSEA 1619
Cdd:COG4942 178 ALLAELEeerAALEAL--------------KAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAER 242
|
.
gi 1591544934 1620 V 1620
Cdd:COG4942 243 T 243
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
843-1121 |
4.32e-06 |
|
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: 51.61 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 843 KIKPLLKSAAtekELASLKEELAKLKEALEKS-------EVKRKELEE-----RQVSLIQEKNDLSLQ--LQAEQDNLAD 908
Cdd:pfam05622 102 RNEELTSLAE---EAQALKDEMDILRESSDKVkkleatvETYKKKLEDlgdlrRQVKLLEERNAEYMQrtLQLEEELKKA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 909 AEDRCDL-LIKTKIQ-LEAKVKEIM---ERLEDE----EEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHA- 978
Cdd:pfam05622 179 NALRGQLeTYKRQVQeLHGKLSEESkkaDKLEFEykklEEKLEALQKEKERLIIERDTLRETNEELRCAQLQQAELSQAd 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 979 -----TENKVKNLIEEM--AALDETILKLTKEKKALQEAH-----------QQTLDDLQAEEDKVNT-LTKAQAK---LE 1036
Cdd:pfam05622 259 allspSSDPGDNLAAEImpAEIREKLIRLQHENKMLRLGQegsyrerltelQQLLEDANRRKNELETqNRLANQRileLQ 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1037 QQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSMESVMDLENDKQQLEEKlkkkdfemnemstriedEQSLVNQLQKKI 1116
Cdd:pfam05622 339 QQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEEL-----------------EPKQDSNLAQKI 401
|
....*
gi 1591544934 1117 KELQA 1121
Cdd:pfam05622 402 DELQE 406
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1467-1859 |
4.43e-06 |
|
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: 51.43 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1467 KCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIK----RENKNLQEEITDLSDQISQGAKTIHELEKMKKGLE 1542
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDReqweRQRRELESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1543 IEKSEIQaalEEAEGTLEHEESKTLRIqLELNQIKADVDRKLAEKEEEID----------NLRRNHQRTLESMQATLDAe 1612
Cdd:pfam07888 108 ASSEELS---EEKDALLAQRAAHEARI-RELEEDIKTLTQRVLERETELErmkerakkagAQRKEEEAERKQLQAKLQQ- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1613 akSRSEAVRLRKKMEGDLNEMEVQLNHANRLASESQKLLRNL-QVQIKDVQLELdeTIHQNEELKEQVAVTERRNNLLAs 1691
Cdd:pfam07888 183 --TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLtTAHRKEAENEA--LLEELRSLQERLNASERKVEGLG- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1692 evEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVD---DAVQECRNAEEKAKKAIT 1768
Cdd:pfam07888 258 --EELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEadkDRIEKLSAELQRLEERLQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1769 DAAMMAEELKKEqdtsahLERMKknmeqtikdlqmrldEAEQIALKGGKKQVQKLEARVKELENELESEQKKSQEYQKGV 1848
Cdd:pfam07888 336 EERMEREKLEVE------LGREK---------------DCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYI 394
|
410
....*....|.
gi 1591544934 1849 RKFERRIKELS 1859
Cdd:pfam07888 395 RQLEQRLETVA 405
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1688-1918 |
4.84e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1688 LLASEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKAI 1767
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1768 TDAAMMAEELKKEQDTSAHLER-MKKNMEQTIKDLQMRLDEAEQIA---------LKGGKKQVQKLEARVKELENELESE 1837
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRaLYRLGRQPPLALLLSPEDFLDAVrrlqylkylAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1838 QKKSQEYQKGVRKFERRIKELSyqgeedkKNLVRMQELIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELDDAEER 1917
Cdd:COG4942 170 EAERAELEALLAELEEERAALE-------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
.
gi 1591544934 1918 A 1918
Cdd:COG4942 243 T 243
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1351-1628 |
6.11e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 50.30 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1351 LREQYDEEQEAKAELQRALSKANGEVAQWRTKYETDAIQRteeleeskkklavrlQEAEEAVEASNAKCSSLEKTKHRLQ 1430
Cdd:pfam00038 59 LRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLR---------------TSAENDLVGLRKDLDEATLARVDLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1431 TEIEDLVVDLERAsaaaaaldkkQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHL-----ET 1505
Cdd:pfam00038 124 AKIESLKEELAFL----------KKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNreeaeEW 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1506 IKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESktlRIQLELNQIKadvdRKLA 1585
Cdd:pfam00038 194 YQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEE---RYELQLADYQ----ELIS 266
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1591544934 1586 EKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLRKKMEG 1628
Cdd:pfam00038 267 ELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEG 309
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1757-1898 |
7.99e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1757 RNAEEKAKKAITDAAMMAEELKKEQDTSA---------HLERMKKNMEQTIKDLQMRLDEAEQI---ALKGGKKQVQKLE 1824
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAkeeihklrnEFEKELRERRNELQKLEKRLLQKEENldrKLELLEKREEELE 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1591544934 1825 ARVKELENELESEQKKSQEYQKGVRKFERRIKELS-YQGEEDKKNLvrMQELIDKLQAKVKSYKRQAE-EAEDQAN 1898
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQELERISgLTAEEAKEIL--LEKVEEEARHEAAVLIKEIEeEAKEEAD 187
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
946-1122 |
8.26e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 946 AKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKvKNLIEEMAALDETILKLTKEKKALQEAHQQtLDDLQAEEDKV 1025
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVASAEREIAELEAE-LERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1026 NTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSMESVMDLENDKQQ-----LEEKLKKKDFE------ 1094
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralLEERFAAALGDaverel 767
|
170 180
....*....|....*....|....*...
gi 1591544934 1095 MNEMSTRIEDEQSLVNQLQKKIKELQAR 1122
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELERAMRA 795
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
907-1168 |
9.52e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 907 ADAEDRCDLLIKTKIQLEAKVKEIMERLED-EEEMSATVlAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKN 985
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDAlQAELEELN-EEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 986 LIEEMAALDETILKLTkekkALQEAhqQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKlrmdlervkrkleg 1065
Cdd:COG3883 91 RARALYRSGGSVSYLD----VLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA-------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1066 dlklsmesvmDLENDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRG 1145
Cdd:COG3883 151 ----------ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
250 260
....*....|....*....|...
gi 1591544934 1146 DVARELEELSERLEESGGATSAQ 1168
Cdd:COG3883 221 AAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
855-1273 |
9.54e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 9.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 855 KELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQD--NLADAEDRCDLLIKTKIQLEAKVKEIME 932
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 933 RLEDEEEMSATVLAKKRKLEDECAEL----KKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALQ 1008
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1009 EAHQ------------------QTLDDLQAEEDKV---------------NTLTKAQAKLEQQVDDLEGSLEQEKKLRMD 1055
Cdd:COG4717 241 LEERlkearlllliaaallallGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1056 LERVKRKLEGDLKLSMESVMDLENDKQQLEEKLKKKdfemnemstRIEDEQSLVNQLQKKIKELQARTEELEEELEADRA 1135
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREA---------EELEEELQLEELEQEIAALLAEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1136 crAKVEKQRGDVARELEELSERLEESGGATSAQIEINKKR-ETDILKLRRDLEEAmlhheattaglrkkhADSVAELSEQ 1214
Cdd:COG4717 392 --EQAEEYQELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEEL---------------EEELEELREE 454
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1591544934 1215 IDSLQRVKQKLEKER--SEAKMEVDDLASTVEQLSKGKASAektcRLYEDQMNEAKAKVEE 1273
Cdd:COG4717 455 LAELEAELEQLEEDGelAELLQELEELKAELRELAEEWAAL----KLALELLEEAREEYRE 511
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1733-1934 |
9.71e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1733 NQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQia 1812
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1813 lkggkkqvqKLEARVKELENELESEQKKSQEY-------QKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKS 1885
Cdd:COG4942 98 ---------ELEAQKEELAELLRALYRLGRQPplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1591544934 1886 YKRQAEEAEDQANTNLSKYRKLQHELDDAEERADMAETQVTKLRVRTRD 1934
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1671-1902 |
9.98e-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: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1671 QNEELKEQVAVTERRNNLLASEVEELRALLEQNDRARK--LAEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNE 1748
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1749 VDdAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNMEQTIKDLQMRLDEAEQIALKGGKK 1818
Cdd:COG3206 242 LA-ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1819 QVQKLEARVKELENELESEQKKSQEYQKGvrkfERRIKELsyqgEEDKKNLvrmQELIDKLQAKVKsykrQAEEAEDQAN 1898
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPEL----EAELRRL----EREVEVA---RELYESLLQRLE----EARLAEALTV 385
|
....
gi 1591544934 1899 TNLS 1902
Cdd:COG3206 386 GNVR 389
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
851-1033 |
1.14e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 851 AATEKELASLKEELAKLKEALEKSEvkrKELEERQVSLIQEKNDLSLQLQAEQ---------------DNLADAEDRCDL 915
Cdd:COG3883 47 EELNEEYNELQAELEALQAEIDKLQ---AEIAEAEAEIEERREELGERARALYrsggsvsyldvllgsESFSDFLDRLSA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 916 LiktkIQLEAKVKEIMERLEDEEEMSAtvlAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDE 995
Cdd:COG3883 124 L----SKIADADADLLEELKADKAELE---AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA 196
|
170 180 190
....*....|....*....|....*....|....*...
gi 1591544934 996 TILKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAQA 1033
Cdd:COG3883 197 QLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
926-1541 |
1.27e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 926 KVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDEtilkltkekk 1005
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS---------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1006 alqeahqqTLDDLQAEEDKVNTLTKAQAKLEQqvdDLEGSLEQEKKLRMDLERVKRKLEGDLKLSMESVMDLENDKQQLE 1085
Cdd:PRK01156 240 --------ALNELSSLEDMKNRYESEIKTAES---DLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1086 EKlkkkdfemNEMSTRIEDEQSLVNQLQKKIKELQarteeleeeleADRACRAKVEKQRGDVARELEELSERLEESGGAT 1165
Cdd:PRK01156 309 NK--------KQILSNIDAEINKYHAIIKKLSVLQ-----------KDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1166 SAQIEINKKRET---DILKLRRDLEEAMLHHEATTAGLRKKHAD---SVAELSEQIDSLQRVKQKLEkersEAKMEVDDL 1239
Cdd:PRK01156 370 KSIESLKKKIEEyskNIERMSAFISEILKIQEIDPDAIKKELNEinvKLQDISSKVSSLNQRIRALR----ENLDELSRN 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1240 ASTVEQLSK--------GKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSEL-SRKLEEREATVSQLQ 1310
Cdd:PRK01156 446 MEMLNGQSVcpvcgttlGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLeSEEINKSINEYNKIE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1311 RSKNSFSQNVEELKKQLEEENKAKNALAhalQSSRHDCDLLREQYDEEQEAKAElqralskangevaqwRTKYETDAIQ- 1389
Cdd:PRK01156 526 SARADLEDIKIKINELKDKHDKYEEIKN---RYKSLKLEDLDSKRTSWLNALAV---------------ISLIDIETNRs 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1390 RTEELEESKKKLAVRLQEAEEAVEASNakcSSLEKTKHRLQTEIEDL---VVDLERASAAAAALDKKQRNFDKVLAEwrq 1466
Cdd:PRK01156 588 RSNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLnnkYNEIQENKILIEKLRGKIDNYKKQIAE--- 661
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1591544934 1467 kCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGL 1541
Cdd:PRK01156 662 -IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAI 735
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1232-1418 |
1.30e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1232 AKMEVDDLASTVEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQ--- 1308
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1309 -LQRSKNSFS---------------QNVEELKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKA 1372
Cdd:COG3883 94 aLYRSGGSVSyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1591544934 1373 NGEVAQWRTKYETDAIQRtEELEESKKKLAVRLQEAEEAVEASNAK 1418
Cdd:COG3883 174 EAQQAEQEALLAQLSAEE-AAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
931-1491 |
1.32e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 50.14 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 931 MERLEDEEEM-SATVLAKKRKLEDECAELKkdiddleiTLAKVEKEKHATENKVKNLIEEMAALDETILKLT-KEKKALQ 1008
Cdd:pfam07111 75 LRRLEEEVRLlRETSLQQKMRLEAQAMELD--------ALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSqRELEEIQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1009 EAHQQTLDDL-QAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKK-----------LRMDLERVKRKLEGDLKLsMESVMD 1076
Cdd:pfam07111 147 RLHQEQLSSLtQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKqlaeaqkeaelLRKQLSKTQEELEAQVTL-VESLRK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1077 LENDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELEADRACRAKvEKQRGDVARELEELSe 1156
Cdd:pfam07111 226 YVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTR-KIQPSDSLEPEFPKK- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1157 rleesggatsAQIEINKKRETdILKLRRDLEEAMLHHEATTAGLRkkhaDSVAELSEQIDS-------LQRVKQ----KL 1225
Cdd:pfam07111 304 ----------CRSLLNRWREK-VFALMVQLKAQDLEHRDSVKQLR----GQVAELQEQVTSqsqeqaiLQRALQdkaaEV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1226 EKERSEAK---MEVDDLASTVEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETnshRARAQAESSELSRKLEER 1302
Cdd:pfam07111 369 EVERMSAKglqMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQA---VARIPSLSNRLSYAVRKV 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1303 EaTVSQLQRSKNSFSQNVEELKKQLEEENKAKNALAHALQSSRHDcdllREQYDEEQEAKAEL-QRALSKANGEVAQWRT 1381
Cdd:pfam07111 446 H-TIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREE----RNRLDAELQLSAHLiQQEVGRAREQGEAERQ 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1382 KYETDAIQRTEELEESKKKLA---VRLQEAEEAVEASNAKCSSL--EKTKHR------LQTEIEDLVVDL-ERASAAAAA 1449
Cdd:pfam07111 521 QLSEVAQQLEQELQRAQESLAsvgQQLEVARQGQQESTEEAASLrqELTQQQeiygqaLQEKVAEVETRLrEQLSDTKRR 600
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1591544934 1450 LDKKQRNFDKVLAEWRQKCEECQAELETSQkESRSLSTELFK 1491
Cdd:pfam07111 601 LNEARREQAKAVVSLRQIQHRATQEKERNQ-ELRRLQDEARK 641
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1459-1841 |
1.46e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.46 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1459 KVLAEWRQKCEECQAElETSQKESRSLSTE--LFKLKNS--YEETLEHLETIKRENKNLQEE---ITDLSDQISQGAKTI 1531
Cdd:COG5022 830 KKLRETEEVEFSLKAE-VLIQKFGRSLKAKkrFSLLKKEtiYLQSAQRVELAERQLQELKIDvksISSLKLVNLELESEI 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1532 HELEKMKKGLEIEKSEIQaaLEEAEGTLEHEESKTLRIQLELNQIKADVDRKLAEKEEEIDNLRRNHQRTLESMQATLDA 1611
Cdd:COG5022 909 IELKKSLSSDLIENLEFK--TELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVRE 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1612 EAKSRSEAVRLRKKMEGDLNEMEVqlnhanrlASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTE-RRNNLLA 1690
Cdd:COG5022 987 GNKANSELKNFKKELAELSKQYGA--------LQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKlKGLLLLE 1058
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1691 SEVEELRALLEQNDRARKLAEHELLEATERVN---------LLHSQNTSLINQKKKLENDLSTLSNevddaVQECRNAEE 1761
Cdd:COG5022 1059 NNQLQARYKALKLRRENSLLDDKQLYQLESTEnllktinvkDLEVTNRNLVKPANVLQFIVAQMIK-----LNLLQEISK 1133
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1762 KAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQKLEARVKELENELESEQKKS 1841
Cdd:COG5022 1134 FLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKI 1213
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
923-1520 |
1.69e-05 |
|
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: 50.22 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 923 LEAKVKEIMERLEDEEEMSATVLAKKRKledecaELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTK 1002
Cdd:pfam12128 263 LHFGYKSDETLIASRQEERQETSAELNQ------LLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLD 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1003 EKKALQEAHQQTLDDLQAE----EDKVNTLTKAQAKLEQQVDDLEGSLEQEkkLRMDLERVKRKL----EGDLKLSMESV 1074
Cdd:pfam12128 337 ADIETAAADQEQLPSWQSElenlEERLKALTGKHQDVTAKYNRRRSKIKEQ--NNRDIAGIKDKLakirEARDRQLAVAE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1075 MDLENDKQQLEEKLKKKDFEMNE----MSTRIEDEQSLVNQ--------LQKKIK---------ELQARTEELEEELEAD 1133
Cdd:pfam12128 415 DDLQALESELREQLEAGKLEFNEeeyrLKSRLGELKLRLNQatatpellLQLENFderierareEQEAANAEVERLQSEL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1134 RACRAKVEKQR---GDVARELEELSERLEEsggatsAQIEINKKRETDILKLRRD--LEEAMLHHEATTAGLRKKHADSV 1208
Cdd:pfam12128 495 RQARKRRDQASealRQASRRLEERQSALDE------LELQLFPQAGTLLHFLRKEapDWEQSIGKVISPELLHRTDLDPE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1209 AELSEQIDSLQRVKQKLEKERSEAKMEV---DDLASTVEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQlnETNSHR 1285
Cdd:pfam12128 569 VWDGSVGGELNLYGVKLDLKRIDVPEWAaseEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASRE--ETFART 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1286 ARAQAEsSELSRKLEEREATVSQLQRSKNSFSQNVeelKKQLEEENKAKNALAHALQssrhdcDLLREQYDEEQEAKAEL 1365
Cdd:pfam12128 647 ALKNAR-LDLRRLFDEKQSEKDKKNKALAERKDSA---NERLNSLEAQLKQLDKKHQ------AWLEEQKEQKREARTEK 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1366 QRALSKANGEvaqwrTKYETDAIQrtEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASA 1445
Cdd:pfam12128 717 QAYWQVVEGA-----LDAQLALLK--AAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAV 789
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1591544934 1446 AAAaldKKQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDL 1520
Cdd:pfam12128 790 RRQ---EVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSEN 861
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1544-1916 |
1.70e-05 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 50.06 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1544 EKSEIQAALEEAEGTLEHEESKTlrIQLELNQIKADVDRKLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLR 1623
Cdd:pfam13166 90 ESIEIQEKIAKLKKEIKDHEEKL--DAAEANLQKLDKEKEKLEADFLDECWKKIKRKKNSALSEALNGFKYEANFKSRLL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1624 KKMEGDLNEMEVQLNHANRLASESQKLLRNLQ--VQIKDVQLELDeTIHQNEELKEQVAVTE------RRNNLLASEVEE 1695
Cdd:pfam13166 168 REIEKDNFNAGVLLSDEDRKAALATVFSDNKPeiAPLTFNVIDFD-ALEKAEILIQKVIGKSsaieelIKNPDLADWVEQ 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1696 LRALLEQN-------------DRARKLAEHELLEATERVNLLHSQNTSLINQKKKLEN------DLSTLSNEVDDAVQEC 1756
Cdd:pfam13166 247 GLELHKAHldtcpfcgqplpaERKAALEAHFDDEFTEFQNRLQKLIEKVESAISSLLAqlpavsDLASLLSAFELDVEDI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1757 RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQtIKDLQMRLDEaeQIALKggKKQVQKLEARVKELENELE- 1835
Cdd:pfam13166 327 ESEAEVLNSQLDGLRRALEAKRKDPFKSIELDSVDAKIES-INDLVASINE--LIAKH--NEITDNFEEEKNKAKKKLRl 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1836 --SEQKKS--QEYQKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKRQAEEaedqANTNLSKYRKLQHEL 1911
Cdd:pfam13166 402 hlVEEFKSeiDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADE----INKLLKAFGFGELEL 477
|
....*
gi 1591544934 1912 DDAEE 1916
Cdd:pfam13166 478 SFNEE 482
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
853-1283 |
2.19e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 853 TEKELASLKEELAKLKEALEKsevKRKELEERQVSLIQEKNDLS--------LQLQAEQDNLADAEDRCDLLIKTKIQLE 924
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSE---KQKELEQNNKKIKELEKQLNqlkseisdLNNQKEQDWNKELKSELKNQEKKLEEIQ 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 925 AKVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEK 1004
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1005 KALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSMESVMDLENDKQQL 1084
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1085 EEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELqarteeleeeleadracRAKVEKqrgdvareleelserleesgga 1164
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSL-----------------KEKIEK---------------------- 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1165 tsAQIEINKKrETDILKLRRDLEEamLHHEATTAGLRKkhadSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVE 1244
Cdd:TIGR04523 529 --LESEKKEK-ESKISDLEDELNK--DDFELKKENLEK----EIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKK 599
|
410 420 430
....*....|....*....|....*....|....*....
gi 1591544934 1245 QLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNS 1283
Cdd:TIGR04523 600 DLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1352-1636 |
2.83e-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: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1352 REQYDEEQEAKAELQRALSKANGEVAQWRTKY---ETDAIQRTEELE----ESKKKLAVRLQEAEEAVEASnaKCSSLEK 1424
Cdd:pfam17380 305 KEEKAREVERRRKLEEAEKARQAEMDRQAAIYaeqERMAMERERELErirqEERKRELERIRQEEIAMEIS--RMRELER 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1425 TKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKCEEcqaELETSQKESRSLStelfklknsyEETLEHLE 1504
Cdd:pfam17380 383 LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE---QEEARQREVRRLE----------EERAREME 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1505 TIKRENKNLQEEITDLSDQISQGAKTIHELEKMKK----GLEIEKSEIQAALEEAEGTLEHEESKTLRIQLEL----NQI 1576
Cdd:pfam17380 450 RVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRdrkrAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMeerqKAI 529
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1577 KADVDRKLAEKEEEIDNLRRNHQRTLESMQATldAEAKSRSEAVRLRKKMEGDLNEMEVQ 1636
Cdd:pfam17380 530 YEEERRREAEEERRKQQEMEERRRIQEQMRKA--TEERSRLEAMEREREMMRQIVESEKA 587
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1262-1481 |
3.09e-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: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1262 DQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQNVEELKKQLEEENKAKNALAHAL 1341
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1342 QSSRHD-CDLLREQYDEEQEAKAELqrALSKANGEVAQWRTKYETDAIQ----RTEELEESKKKLAVRLQEAEEAVEAsn 1416
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAParreQAEELRADLAELAALRAELEAERAE-- 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1591544934 1417 akcssLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKCEECQAELETSQKE 1481
Cdd:COG4942 176 -----LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1622-1928 |
3.43e-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: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1622 LRKKMEGDLNEMEVQLNHANRLASESQKLLRnLQVQIKDV---QLEL-DETIHQNE---ELKEQVAVTERRNNLLASEVE 1694
Cdd:TIGR01612 546 LKESYELAKNWKKLIHEIKKELEEENEDSIH-LEKEIKDLfdkYLEIdDEIIYINKlklELKEKIKNISDKNEYIKKAID 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1695 eLRALLEQN----DRARKLAEHELLEATERVNLLHSQNTSLINQKkkLENDLSTLSNEVDDAVQE--CRNAEEKAKKAIT 1768
Cdd:TIGR01612 625 -LKKIIENNnayiDELAKISPYQVPEHLKNKDKIYSTIKSELSKI--YEDDIDALYNELSSIVKEnaIDNTEDKAKLDDL 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1769 DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQKLEARVKELENELESEQKKSQEYQKGV 1848
Cdd:TIGR01612 702 KSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAKEKDEL 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1849 RKFERRIKELSYQ-----------GEEDKKNLVRMQELIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELDDAEER 1917
Cdd:TIGR01612 782 NKYKSKISEIKNHyndqinidnikDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEK 861
|
330
....*....|.
gi 1591544934 1918 ADMAETQVTKL 1928
Cdd:TIGR01612 862 IDSEHEQFAEL 872
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
854-1053 |
3.48e-05 |
|
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: 48.91 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 854 EKELASLKEELAKLKEALEKSEVKRKELEErqvsliqEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEIMER 933
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLEK-------EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 934 LEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALD------------------- 994
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEdpkgedeeipeeelsledv 956
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 995 -ETILKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLR 1053
Cdd:TIGR02169 957 qAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
846-1010 |
3.60e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 846 PLLKSAATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEA 925
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 926 KVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDL-------EITLAKVEKEKHATENKVKNLIEEMAALDETIL 998
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaIEEYEELEERYDFLSEQREDLEEARETLEEAIE 819
|
170
....*....|...
gi 1591544934 999 KLTKEKK-ALQEA 1010
Cdd:COG1196 820 EIDRETReRFLET 832
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1593-1892 |
3.66e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1593 NLRRNHQRTLESMQATLDAE---AKSRSEAVRLRKKMEgDLNEMEVQLNHANRLASESQKLLRN---LQVQIKDVQLELD 1666
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRrqlAAEQYRLVEMARELA-ELNEAESDLEQDYQAASDHLNLVQTalrQQEKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1667 ETihqNEELKEQVAVTErrnnLLASEVEELRALLEQN----DRARK-LAEH-ELLEATERVNLLHSQNTSLINQKKKLeN 1740
Cdd:PRK04863 359 EL---EERLEEQNEVVE----EADEQQEENEARAEAAeeevDELKSqLADYqQALDVQQTRAIQYQQAVQALERAKQL-C 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1741 DLSTLSNE-VDDAVQECRNAEekakKAITDAAMMAEElkKEQDTSAHLERMKKNME---------------QTIKDLQMR 1804
Cdd:PRK04863 431 GLPDLTADnAEDWLEEFQAKE----QEATEELLSLEQ--KLSVAQAAHSQFEQAYQlvrkiagevsrseawDVARELLRR 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1805 LDEAEQIAlkggkKQVQKLEARVKELENELESEQ----------KKSQ-------EYQKGVRKFERRIKELSYQGEEDKK 1867
Cdd:PRK04863 505 LREQRHLA-----EQLQQLRMRLSELEQRLRQQQraerllaefcKRLGknlddedELEQLQEELEARLESLSESVSEARE 579
|
330 340
....*....|....*....|....*
gi 1591544934 1868 NLVRMQELIDKLQAKVKSYKRQAEE 1892
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRLAARAPA 604
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1164-1571 |
3.79e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1164 ATSAQIEINKKRETDILKLRRDLEEAMLHHEATTAGLRKKhadsvAELSEQIDSLQRVKQKLEkERSEAKMEVDDLASTV 1243
Cdd:COG4717 99 ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE-----AELAELPERLEELEERLE-ELRELEEELEELEAEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1244 EQLSKGKASAEKTCRLY-EDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREA---------TVSQLQRSK 1313
Cdd:COG4717 173 AELQEELEELLEQLSLAtEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENeleaaaleeRLKEARLLL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1314 NSFSQNVEELKKQLEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANG------EVAQWRTKYETDA 1387
Cdd:COG4717 253 LIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALeeleeeELEELLAALGLPP 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1388 IQRTEELEESKKKLAvRLQEAEEAVEASNAkcsslEKTKHRLQTEIEDL-----VVDLERASAAAAALDKKQrnfdkvla 1462
Cdd:COG4717 333 DLSPEELLELLDRIE-ELQELLREAEELEE-----ELQLEELEQEIAALlaeagVEDEEELRAALEQAEEYQ-------- 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1463 EWRQKCEECQAELETSQKESRSLSTELfklknSYEETLEHLETIKRENKNLQEEITDLSDQIsqgAKTIHELEKMKKGLE 1542
Cdd:COG4717 399 ELKEELEELEEQLEELLGELEELLEAL-----DEEELEEELEELEEELEELEEELEELREEL---AELEAELEQLEEDGE 470
|
410 420
....*....|....*....|....*....
gi 1591544934 1543 IekSEIQAALEEAEGTLEHEESKTLRIQL 1571
Cdd:COG4717 471 L--AELLQELEELKAELRELAEEWAALKL 497
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1395-1617 |
4.20e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1395 EESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAaaaLDKKQRNFDKVLAEWRQKCEECQAE 1474
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE---IDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1475 LETSQKESRSLSTELFKLK-NSYEETLEHLETIKRENKNLQEEITDLSDQISqgaktihELEKMKKGLEIEKSEIQAALE 1553
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLGsESFSDFLDRLSALSKIADADADLLEELKADKA-------ELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1591544934 1554 EAEGTLEHEESKTLRIQLELNQIKADVDRKLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRS 1617
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
851-1010 |
4.33e-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: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 851 AATEKELASLKEELAKLKEALEKsevKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDL--------------L 916
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEA---QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYlkylaparreqaeeL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 917 IKTKIQLEAKVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKdiddleiTLAKVEKEKHATENKVKNLIEEMAALDET 996
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK-------LLARLEKELAELAAELAELQQEAEELEAL 228
|
170
....*....|....
gi 1591544934 997 ILKLTKEKKALQEA 1010
Cdd:COG4942 229 IARLEAEAAAAAER 242
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1774-1909 |
4.82e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1774 AEELKKEQDTSAHLERMKKNMEQTIKDLQmrldeaeqialkggkKQVQKLEARVKELENELESEQKKSQEYQKGVRKFER 1853
Cdd:COG2433 391 PEEEPEAEREKEHEERELTEEEEEIRRLE---------------EQVERLEAEVEELEAELEEKDERIERLERELSEARS 455
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1591544934 1854 RIKElsyQGEEDKKnLVRMQELIDKLQAKVKSYKRQAEEAEDQANTnLSKYRKLQH 1909
Cdd:COG2433 456 EERR---EIRKDRE-ISRLDREIERLERELEEERERIEELKRKLER-LKELWKLEH 506
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
847-1122 |
5.00e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 847 LLKSAAT-EKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAE--DRC--DLLiktki 921
Cdd:PRK04863 284 HLEEALElRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEkiERYqaDLE----- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 922 QLEAKVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDL-------------------------------EITLA 970
Cdd:PRK04863 359 ELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYqqaldvqqtraiqyqqavqalerakqlcglpDLTAD 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 971 KVEKEKHATENKVKNLIEEMAALdETILKLTKE-----KKALQ------------EAHQQTLDDLQAEEDKVNTLTKAQA 1033
Cdd:PRK04863 439 NAEDWLEEFQAKEQEATEELLSL-EQKLSVAQAahsqfEQAYQlvrkiagevsrsEAWDVARELLRRLREQRHLAEQLQQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1034 kLEQQVDDLEGSLEQEKklrmDLERVKRKLEGDLKLSMESVMDLENDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQ 1113
Cdd:PRK04863 518 -LRMRLSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQ 592
|
....*....
gi 1591544934 1114 KKIKELQAR 1122
Cdd:PRK04863 593 ARIQRLAAR 601
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1569-1911 |
6.87e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.93 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1569 IQLELNQIKADVDR--------KLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLRKK--------------- 1625
Cdd:pfam06160 65 IEELLFEAEELNDKyrfkkakkALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKyrelrktllanrfsy 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1626 ------MEGDLNEMEVQLNHANRLASESQkllrnlQVQIKDVQLELDETIHQNEELKEQV-AVTERRNNLLASEVEELRA 1698
Cdd:pfam06160 145 gpaideLEKQLAEIEEEFSQFEELTESGD------YLEAREVLEKLEEETDALEELMEDIpPLYEELKTELPDQLEELKE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1699 ----LLEQNdraRKLAEHELLEATERVNLLHSQNTSLINQK--KKLENDLSTLSNEVDdAVQECRNAEEKAKKaitdaam 1772
Cdd:pfam06160 219 gyreMEEEG---YALEHLNVDKEIQQLEEQLEENLALLENLelDEAEEALEEIEERID-QLYDLLEKEVDAKK------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1773 maeELKKEQDT-SAHLERMKKNMEQTIKDLQM-----RLDEAEQIALKGGKKQVQKLEARVKELENELESEQKKSQEYQK 1846
Cdd:pfam06160 288 ---YVEKNLPEiEDYLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQE 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1591544934 1847 GVRKFERRIKElsyqgeedkknlvrmqelIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHEL 1911
Cdd:pfam06160 365 ELEEILEQLEE------------------IEEEQEEFKESLQSLRKDELEAREKLDEFKLELREI 411
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1596-1771 |
7.81e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1596 RNHQRTLESMQAtLDAEAKsrsEAVRLRKKMEGDLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNEEL 1675
Cdd:COG1579 3 PEDLRALLDLQE-LDSELD---RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1676 KEQVAvtERRNNllasevEELRAL---LEQNDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDA 1752
Cdd:COG1579 79 EEQLG--NVRNN------KEYEALqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170
....*....|....*....
gi 1591544934 1753 VQECRNAEEKAKKAITDAA 1771
Cdd:COG1579 151 LAELEAELEELEAEREELA 169
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
854-1023 |
8.85e-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: 47.20 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 854 EKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKvkeiMER 933
Cdd:pfam07888 79 ESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE----LER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 934 LEDEEEMSatvLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEkkaLQEAHQQ 1013
Cdd:pfam07888 155 MKERAKKA---GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK---LTTAHRK 228
|
170
....*....|
gi 1591544934 1014 TLDDLQAEED 1023
Cdd:pfam07888 229 EAENEALLEE 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1694-1917 |
9.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1694 EELRALLEQNDRARKlAEHELLEATERVNLLhsqntslinqkkkleNDLSTLSNEVDDAVQECRNAEE-----KAKKAIT 1768
Cdd:COG4913 225 EAADALVEHFDDLER-AHEALEDAREQIELL---------------EPIRELAERYAAARERLAELEYlraalRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1769 DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAE-QIALKGGkkqvqkleARVKELENELESEQKKSQEYQKG 1847
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEaQIRGNGG--------DRLEQLEREIERLERELEERERR 360
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1591544934 1848 VRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKRQAEEAEDQANTNLSK----YRKLQHELDDAEER 1917
Cdd:COG4913 361 RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDlrreLRELEAEIASLERR 434
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
843-1098 |
9.07e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 843 KIKPLLKSAATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQ 922
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 923 LEAKVKEIMERLEDEEEMsATVLAKKRKLEDECAELKKDIDDLEiTLAKVEKEKHATENKVKNLIEEmaALDETILKLTK 1002
Cdd:PRK02224 577 LNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREALA-ELNDERRERLAEKRERKRELEA--EFDEARIEEAR 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1003 EKKALQEAHQQTLDdlqaeeDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEgDLKLSMESVMDLENDKQ 1082
Cdd:PRK02224 653 EDKERAEEYLEQVE------EKLDELREERDDLQAEIGAVENELEELEELRERREALENRVE-ALEALYDEAEELESMYG 725
|
250 260
....*....|....*....|.
gi 1591544934 1083 QLEEKLKKKDFE-----MNEM 1098
Cdd:PRK02224 726 DLRAELRQRNVEtlermLNET 746
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1657-1927 |
9.65e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1657 QIKDVQLELDETIHQNEELKEQVAVTERRNNLLASEVEELRALL-EQNDRARKLAEhELLEATERVNLLHSQNTSLINQK 1735
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRdELNAQVKELRE-EAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1736 KKLENDLSTLSNEVDDAVQEcRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIAlkg 1815
Cdd:COG1340 81 DELNEKLNELREELDELRKE-LAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKAL--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1816 gkkqvqKLEARVKELENELESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKRQAEEAED 1895
Cdd:COG1340 157 ------EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHE 230
|
250 260 270
....*....|....*....|....*....|..
gi 1591544934 1896 QANTNLSKYRKLQHELDDAEERADMAETQVTK 1927
Cdd:COG1340 231 EIIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
860-1302 |
1.04e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.51 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 860 LKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLiktkiqlEAKVKEIMERLEDEEe 939
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL-------QTEVDALRLRLEEKE- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 940 msaTVLAKKRK----LEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALQEAHQQ-- 1013
Cdd:pfam10174 359 ---SFLNKKTKqlqdLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNtd 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1014 ----TLDDLQAEEDKVNTLTKAQAKLEQQVDDLEgsLEQEKKLRMDLERVKRKLEGDLKLSMESVMDLENDKQQLEEKLK 1089
Cdd:pfam10174 436 taltTLEEALSEKERIIERLKEQREREDRERLEE--LESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGL 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1090 KKDFEMN----EMSTRIEDEQSLVNQLQKkikelqARTEELEEELEADRACRAKVEKQrgDVARELEElserleesggAT 1165
Cdd:pfam10174 514 KKDSKLKsleiAVEQKKEECSKLENQLKK------AHNAEEAVRTNPEINDRIRLLEQ--EVARYKEE----------SG 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1166 SAQIEINkkRETDILklrRDLEEAMLHHEATTAGLRKKHADSVAELSEQIDSLQRVKQKLEKERS----EAKMEVDDLAS 1241
Cdd:pfam10174 576 KAQAEVE--RLLGIL---REVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAqlleEARRREDNLAD 650
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1591544934 1242 TVE--QLSKGKASAEKTcrlyEDQMNEAKAKVEELQRQLNETNSHRARAQAESselSRKLEER 1302
Cdd:pfam10174 651 NSQqlQLEELMGALEKT----RQELDATKARLSSTQQSLAEKDGHLTNLRAER---RKQLEEI 706
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1184-1560 |
1.36e-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: 47.25 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1184 RDLEEAMLHHEATtAGLRKKHADSVAELSEQIDSLQRVKQKL-EKERSEAKMEvDDLASTVEQLSK---GKASAEKTCRl 1259
Cdd:COG3096 275 RHANERRELSERA-LELRRELFGARRQLAEEQYRLVEMARELeELSARESDLE-QDYQAASDHLNLvqtALRQQEKIER- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1260 YEDQMNEAKAKVEELQRQLNETNSHRARAQAEsselsrkLEEREATVSQLQRSKNSFSQNVEELKKQLEEENKAKNALAH 1339
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEAR-------LEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEK 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1340 AlqssRHDCDL--------------LREQYDEEQEAKAELQRALSKANGEVAQWRTKYE-----TDAIQRTEELEESKKK 1400
Cdd:COG3096 425 A----RALCGLpdltpenaedylaaFRAKEQQATEEVLELEQKLSVADAARRQFEKAYElvckiAGEVERSQAWQTAREL 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1401 L--AVRLQEAEEAVEASNAKCSSLEKTKHRLQteiedlvvDLERASAAAAALDKKQRN----FDKVLAEWRQKCEECQAE 1474
Cdd:COG3096 501 LrrYRSQQALAQRLQQLRAQLAELEQRLRQQQ--------NAERLLEEFCQRIGQQLDaaeeLEELLAELEAQLEELEEQ 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1475 LETSQKESRSLSTELFKLKNSYEEtLEHLETIKREnknLQEEITDLSDQISQGAKTIHEL-EKMKKGLE------IEKSE 1547
Cdd:COG3096 573 AAEAVEQRSELRQQLEQLRARIKE-LAARAPAWLA---AQDALERLREQSGEALADSQEVtAAMQQLLErereatVERDE 648
|
410
....*....|...
gi 1591544934 1548 IQAALEEAEGTLE 1560
Cdd:COG3096 649 LAARKQALESQIE 661
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1584-1924 |
1.40e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 46.61 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1584 LAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLRKKMEgdlnemevQLNHANRLASESQKLLRNLQVQIKDVQL 1663
Cdd:pfam05622 2 LSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLD--------QLESGDDSGTPGGKKYLLLQKQLEQLQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1664 EL--------DETIHqNEELKEQVAVTERRNNLLASEVEELRALLEQNDrarklaehELLEATERVNLLHSQNTSLinqK 1735
Cdd:pfam05622 74 ENfrletardDYRIK-CEELEKEVLELQHRNEELTSLAEEAQALKDEMD--------ILRESSDKVKKLEATVETY---K 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1736 KKLEnDLSTLSNEVddavqecRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNmeqtIKDLQMRLDEAEQIALK- 1814
Cdd:pfam05622 142 KKLE-DLGDLRRQV-------KLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQ----VQELHGKLSEESKKADKl 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1815 --GGKKQVQKLEARVKELEN---------ELESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKNLV--RMQELIDKLQA 1881
Cdd:pfam05622 210 efEYKKLEEKLEALQKEKERliierdtlrETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMpaEIREKLIRLQH 289
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1591544934 1882 KVKSYKRQAEEAEDQantnlsKYRKLQHELDDAEERADMAETQ 1924
Cdd:pfam05622 290 ENKMLRLGQEGSYRE------RLTELQQLLEDANRRKNELETQ 326
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
862-1114 |
1.42e-04 |
|
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: 47.02 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 862 EELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEIMERLEDEEEMS 941
Cdd:pfam05483 408 EELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKN 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 942 ATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAE 1021
Cdd:pfam05483 488 IELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1022 EDK-----------VNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKL--EGDLKLSMESVMDLENDKQQLEEKL 1088
Cdd:pfam05483 568 LDKseenarsieyeVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALkkKGSAENKQLNAYEIKVNKLELELAS 647
|
250 260 270
....*....|....*....|....*....|..
gi 1591544934 1089 KKKDFE--MNEMSTRIED----EQSLVNQLQK 1114
Cdd:pfam05483 648 AKQKFEeiIDNYQKEIEDkkisEEKLLEEVEK 679
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
982-1467 |
1.45e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 982 KVKNLIEEMAALDETIlkltKEKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLE------GSLEQEKKLRMD 1055
Cdd:COG4717 65 KPELNLKELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllqllPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1056 LERVKRKLEgDLKLSMESVMDLENDKQQLEEKLKKKDFEMNEMSTRI-EDEQSLVNQLQKKIKELQARTEELEEELEADR 1134
Cdd:COG4717 141 LAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1135 ACRAKVEKQRGDVARELEELSERLEESGGATSAQIeinkkretdiLKLRRDLEEAMLHHEATTAGLRKKHADSVAELSEQ 1214
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARLLLLI----------AAALLALLGLGGSLLSLILTIAGVLFLVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1215 IDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSE 1294
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1295 LSRKLEEREATVSqlqrSKNSFSQNVEELkkqleeenkaknalahalqssrhdcdllrEQYDEEQEAKAELQRALSKANG 1374
Cdd:COG4717 370 QEIAALLAEAGVE----DEEELRAALEQA-----------------------------EEYQELKEELEELEEQLEELLG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1375 EVAQWRTKYETDAI-QRTEELEESKKKLAVRLQEAEEAVEASNAKCSSLEK--TKHRLQTEIEDLVVDLERASAAAAALD 1451
Cdd:COG4717 417 ELEELLEALDEEELeEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEWAALK 496
|
490
....*....|....*.
gi 1591544934 1452 KKQRNFDKVLAEWRQK 1467
Cdd:COG4717 497 LALELLEEAREEYREE 512
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
841-1122 |
1.47e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 46.77 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 841 FFKIKPLLKSA-----ATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEkndlslqLQAEQDNLADAEDrcdl 915
Cdd:pfam06160 81 FKKAKKALDEIeelldDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKT-------LLANRFSYGPAID---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 916 liktkiQLEAKVKEIMERLED-EEEMSAT--VLAKK--RKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEM 990
Cdd:pfam06160 150 ------ELEKQLAEIEEEFSQfEELTESGdyLEAREvlEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREM 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 991 A----ALDEtiLKLTKEKKALQEAHQQTLDDLqaEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGD 1066
Cdd:pfam06160 224 EeegyALEH--LNVDKEIQQLEEQLEENLALL--ENLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDY 299
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1591544934 1067 LKlsmesvmDLENDKQQLEEKLK--KKDFEMNemstriEDEQSLVNQLQKKIKELQAR 1122
Cdd:pfam06160 300 LE-------HAEEQNKELKEELErvQQSYTLN------ENELERVRGLEKQLEELEKR 344
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
781-1060 |
1.51e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 781 LEELRDERLAKVLTLLQAAARGKIMRMELLRMMERRDALMIIQwnirafnavkhwpwmKLFFKIkplLKSAATEKELASL 860
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA---------------EYSWDE---IDVASAEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 861 KEELAKLKEA---LEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLiktKIQLEAKVKEIMERLEDE 937
Cdd:COG4913 674 EAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL---QDRLEAAEDLARLELRAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 938 -EEMSATVLAKKRkLEDECAELKKDIDDLEITLAKVEKE--------KHATENKVKNLIEEMAALDETILKLT------- 1001
Cdd:COG4913 751 lEERFAAALGDAV-ERELRENLEERIDALRARLNRAEEEleramrafNREWPAETADLDADLESLPEYLALLDrleedgl 829
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1591544934 1002 -----KEKKALQEAHQQTLDDLQAEedkvntLTKAQAKLEQQVDDLEGSLEQ-----EKKLRMDLERVK 1060
Cdd:COG4913 830 peyeeRFKELLNENSIEFVADLLSK------LRRAIREIKERIDPLNDSLKRipfgpGRYLRLEARPRP 892
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1495-1624 |
1.57e-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: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1495 SYEETLEHL--ETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESKTLRIQLE 1572
Cdd:COG2433 377 SIEEALEELieKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE 456
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 1573 LNQiKADVDRKLAEKEEEIDNLRrnhqRTLESMQATLDaEAKSRSEavRLRK 1624
Cdd:COG2433 457 ERR-EIRKDREISRLDREIERLE----RELEEERERIE-ELKRKLE--RLKE 500
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1646-1848 |
1.63e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1646 ESQKLLRNLQvqikDVQLELDETIHQNEELKEQVAVTERRNNLLASEVEELRALLEQNDRARKLAEHELLEATERVNLLH 1725
Cdd:COG1579 4 EDLRALLDLQ----ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1726 SQNTSLINQKkklenDLSTLSNEVDDAVQECRNAEEKAKkaitdAAMMAEELKKEQdtsahlermKKNMEQTIKDLQMRL 1805
Cdd:COG1579 80 EQLGNVRNNK-----EYEALQKEIESLKRRISDLEDEIL-----ELMERIEELEEE---------LAELEAELAELEAEL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1591544934 1806 DEAEQialkggkkqvqKLEARVKELENELESEQKKSQEYQKGV 1848
Cdd:COG1579 141 EEKKA-----------ELDEELAELEAELEELEAEREELAAKI 172
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1464-1916 |
1.80e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.97 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1464 WRQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIheleKMKKGLEI 1543
Cdd:TIGR01612 556 WKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDKNEYIKKAI----DLKKIIEN 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1544 EKSEI-QAALEEAEGTLEHEESKTL---RIQLELNQI-KADVDRKLAE-----KEEEIDNLRrnHQRTLESMQATLDAEA 1613
Cdd:TIGR01612 632 NNAYIdELAKISPYQVPEHLKNKDKiysTIKSELSKIyEDDIDALYNElssivKENAIDNTE--DKAKLDDLKSKIDKEY 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1614 KS----RSEAVRLR-KKMEGDLNEM-EVQLNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTERRNN 1687
Cdd:TIGR01612 710 DKiqnmETATVELHlSNIENKKNELlDIIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKIS 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1688 LLASEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLENDlstLSNEVDDAVQECRNAEEKAKKAI 1767
Cdd:TIGR01612 790 EIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDD---FLNKVDKFINFENNCKEKIDSEH 866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1768 TDAAMMAEELKKE--QDTSAHLERMKKNMEQTIKDLQMRLDEAEQialkgGKKQVQKLEARVKELENELESEQKKSQEYQ 1845
Cdd:TIGR01612 867 EQFAELTNKIKAEisDDKLNDYEKKFNDSKSLINEINKSIEEEYQ-----NINTLKKVDEYIKICENTKESIEKFHNKQN 941
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1846 KGVRKFERRIK--------ELSYQGEEDKKNLVRMQELiDKL--QAKVKSYKRQAEEA-----EDQANTNLSKYRKLQHE 1910
Cdd:TIGR01612 942 ILKEILNKNIDtikesnliEKSYKDKFDNTLIDKINEL-DKAfkDASLNDYEAKNNELikyfnDLKANLGKNKENMLYHQ 1020
|
....*.
gi 1591544934 1911 LDDAEE 1916
Cdd:TIGR01612 1021 FDEKEK 1026
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1672-1868 |
1.83e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1672 NEELKEQVAVTERRNNLLASEVEELRALLeqndRARKLAEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVdd 1751
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEEL----KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1752 AVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQKLEARVKELE 1831
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|....*..
gi 1591544934 1832 NELESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKN 1868
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1193-1911 |
1.99e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.58 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1193 HEATTAGLRKKHADSVAELSEQIDS-----LQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKASAEKTCRLYEDQMNEA 1267
Cdd:TIGR01612 723 HLSNIENKKNELLDIIVEIKKHIHGeinkdLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINID 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1268 KAKVEELQRQLNETNSHRARAQAESSELSRKLEERE-------ATVSQLQRSKNSFSQNVEELKKQ-LEEENKAKNALA- 1338
Cdd:TIGR01612 803 NIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKfmkddflNKVDKFINFENNCKEKIDSEHEQfAELTNKIKAEISd 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1339 ---HALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTKYET-------------------DAIQRTEELEE 1396
Cdd:TIGR01612 883 dklNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKICENTKESiekfhnkqnilkeilnkniDTIKESNLIEK 962
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1397 SKKK-----LAVRLQEAEEAVeaSNAKCSSLEKTKHRLQTEIEDLVVDL--ERASAAAAALDKKQR---NFDKVLAEWRQ 1466
Cdd:TIGR01612 963 SYKDkfdntLIDKINELDKAF--KDASLNDYEAKNNELIKYFNDLKANLgkNKENMLYHQFDEKEKatnDIEQKIEDANK 1040
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1467 KCEECQAELETS------------QKESRSLSTELFKLK-------NSYEETLEHL---ETIKRENKNLQEEITDLSDQI 1524
Cdd:TIGR01612 1041 NIPNIEIAIHTSiyniideiekeiGKNIELLNKEILEEAeinitnfNEIKEKLKHYnfdDFGKEENIKYADEINKIKDDI 1120
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1525 ----SQGAKTIHELEKMKKGLEIEKSEIQAALEE----AEGTLEHEESKtlRIQLELNQIKADVDRKLAEKEE------E 1590
Cdd:TIGR01612 1121 knldQKIDHHIKALEEIKKKSENYIDEIKAQINDledvADKAISNDDPE--EIEKKIENIVTKIDKKKNIYDEikkllnE 1198
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1591 IDNLRRNhQRTLESMQATLDAEAKSRSEAV-----RLRKKMEGDLNEMEVQLNHANRLASESQKLLRNLQVQIkDVQLEL 1665
Cdd:TIGR01612 1199 IAEIEKD-KTSLEEVKGINLSYGKNLGKLFlekidEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEM-DIKAEM 1276
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1666 DETIHQNEELKEQVAVTERRNNLLASEVEELRALLEQNDRARKLAEhelLEATERVNLLHSQ-NTSLINQK-KKLENDLS 1743
Cdd:TIGR01612 1277 ETFNISHDDDKDHHIISKKHDENISDIREKSLKIIEDFSEESDIND---IKKELQKNLLDAQkHNSDINLYlNEIANIYN 1353
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1744 TLS----NEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDlqmrldeaeqialkggkKQ 1819
Cdd:TIGR01612 1354 ILKlnkiKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDD-----------------KD 1416
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1820 VQKLEARVKELENELESEQ-------KKSQEYQKGV-----------RKFERRIKELSYQGEEDKK-NLVRMQELIDklq 1880
Cdd:TIGR01612 1417 IDECIKKIKELKNHILSEEsnidtyfKNADENNENVlllfkniemadNKSQHILKIKKDNATNDHDfNINELKEHID--- 1493
|
810 820 830
....*....|....*....|....*....|.
gi 1591544934 1881 aKVKSYKRQAEEAEDQANTNLSKYRKLQHEL 1911
Cdd:TIGR01612 1494 -KSKGCKDEADKNAKAIEKNKELFEQYKKDV 1523
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1072-1293 |
2.05e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1072 ESVMDLENDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELEADRA-----------CRAKV 1140
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAelaelekeiaeLRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1141 EKQRGDVAreleELSERLEESGGATSAQIEINKKRETDILKLRRDLEEAMLHHEATTAGLRKKhadsVAELSEQIDSLQR 1220
Cdd:COG4942 100 EAQKEELA----ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1591544934 1221 VKQKLEKERSEAKMEVDDLASTVEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESS 1293
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1450-1625 |
2.53e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1450 LDKKQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNL--QEEITDLSDQISQG 1527
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1528 AKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEESktlriqlELNQIKADVDRKLAEKEEEIDNLRRnhQRtlESMQA 1607
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEA-------ELEEKKAELDEELAELEAELEELEA--ER--EELAA 170
|
170
....*....|....*...
gi 1591544934 1608 TLDAEAKSRSEAVRLRKK 1625
Cdd:COG1579 171 KIPPELLALYERIRKRKN 188
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
853-1091 |
2.60e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 853 TEKELASLKEE---LAKLKEALEKSEVKRKELEERQVSliqeknDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKE 929
Cdd:PRK01156 488 IEIEVKDIDEKivdLKKRKEYLESEEINKSINEYNKIE------SARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLE 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 930 IME--RLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKE----KHATENKVKNLIEEMAALDETIlKLTKE 1003
Cdd:PRK01156 562 DLDskRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGfpddKSYIDKSIREIENEANNLNNKY-NEIQE 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1004 KKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSMESVMDLENDKQQ 1083
Cdd:PRK01156 641 NKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
....*...
gi 1591544934 1084 LEEKLKKK 1091
Cdd:PRK01156 721 INETLESM 728
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
847-1121 |
2.73e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 847 LLKSAATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLslqLQAEQDNLADAEDrcdlLIKTKIQLEAK 926
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL---VNAGSERLRAVKD----IKQERDQLLNE 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 927 VKEIMERLEDEEEMSATVlakKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNlieeMAALDETILKLTKEKKA 1006
Cdd:pfam15921 662 VKTSRNELNSLSEDYEVL---KRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS----MEGSDGHAMKVAMGMQK 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1007 LQEAHQQTLDDLQAeedKVNTLTKAQAKLEQQVDDLEgslEQEKKLRMDLERV---KRKLEGDLKLSMESVMDLENDKQQ 1083
Cdd:pfam15921 735 QITAKRGQIDALQS---KIQFLEEAMTNANKEKHFLK---EEKNKLSQELSTVateKNKMAGELEVLRSQERRLKEKVAN 808
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1591544934 1084 LEEKLKKKDFEMNEMSTRI--EDEQSLVNQLQKK--IKELQA 1121
Cdd:pfam15921 809 MEVALDKASLQFAECQDIIqrQEQESVRLKLQHTldVKELQG 850
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
847-1120 |
3.29e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 847 LLKSAATEKELASLKEELAKLKEALEKSEVKRKELEerqvsliQEKNDLslqlqaeQDNLADAEDRCDLLIKTKIQLEAK 926
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQ-------QERDEL-------ADEIASGASGKSALQDEKRRLEAR 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 927 VKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETIlkLTKEKKA 1006
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTV--KSKFKSS 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1007 LqeahqqtlddlqaeedkvntltkaqAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDLKLSMESVMDLENDKQQLEE 1086
Cdd:pfam01576 969 I-------------------------AALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKD 1023
|
250 260 270
....*....|....*....|....*....|....
gi 1591544934 1087 KLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQ 1120
Cdd:pfam01576 1024 QAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQ 1057
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
978-1148 |
3.32e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 978 ATENKVKNLIEeMAALDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLrmdLE 1057
Cdd:COG1579 1 AMPEDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR---IK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1058 RVKRKLEG--------DLKLSMESvmdLENDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEE 1129
Cdd:COG1579 77 KYEEQLGNvrnnkeyeALQKEIES---LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170
....*....|....*....
gi 1591544934 1130 LEADracRAKVEKQRGDVA 1148
Cdd:COG1579 154 LEAE---LEELEAEREELA 169
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
985-1187 |
3.48e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 985 NLIEEMAALDETILKLTKE----KKALQEAhQQTLDDLQAEEDKVNTLTKAQAkLEQQVDDLEGSLEQEKKLRMDLERVK 1060
Cdd:COG3206 165 NLELRREEARKALEFLEEQlpelRKELEEA-EAALEEFRQKNGLVDLSEEAKL-LLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1061 RKLEGDLKLSMESVMDLENDK--QQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKELQARTEELEEELEADRACRA 1138
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1591544934 1139 KVEKQRGDVARELEElserleesggATSAQIEINKKRETDILKLRRDLE 1187
Cdd:COG3206 323 EALQAREASLQAQLA----------QLEARLAELPELEAELRRLEREVE 361
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
906-1050 |
3.98e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 906 LADAEDRCDLLIK-TKIQLEAKVKEIMerLEDEEEmsatVLAKKRKLEDECAELKKDIDDLEITLAK----VEKEKHATE 980
Cdd:PRK12704 33 IKEAEEEAKRILEeAKKEAEAIKKEAL--LEAKEE----IHKLRNEFEKELRERRNELQKLEKRLLQkeenLDRKLELLE 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 981 NKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQaeedKVNTLTKAQAKlEQQVDDLEGSLEQEK 1050
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE----RISGLTAEEAK-EILLEKVEEEARHEA 171
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1710-1918 |
4.15e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1710 AEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDT-SAHLE 1788
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1789 RMKKNMEQT-----------IKDLQMRLD------EAEQIALKGGKKQVQKLEARVKELENELESEQKKSQEYQKGVRKF 1851
Cdd:COG3883 94 ALYRSGGSVsyldvllgsesFSDFLDRLSalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1591544934 1852 ERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELDDAEERA 1918
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1461-1737 |
4.33e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1461 LAEWRQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKG 1540
Cdd:COG4372 61 LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1541 LEIEKSEIQAALEEAEGTLEHEESKTLRIQLELNQIkadvdrKLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAV 1620
Cdd:COG4372 141 LQSEIAEREEELKELEEQLESLQEELAALEQELQAL------SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1621 RLRKKMEGDLNEMEVQLNHANRLASESQKLLRNLQVQIKDVQLELDEtihqnEELKEQVAVTERRNNLLASEVEELRALL 1700
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE-----ELELAILVEKDTEEEELEIAALELEALE 289
|
250 260 270
....*....|....*....|....*....|....*..
gi 1591544934 1701 EQNDRARKLAEHELLEATERVNLLHSQNTSLINQKKK 1737
Cdd:COG4372 290 EAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
923-1122 |
4.35e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 923 LEAKVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDI----DDLEITLAKVEKEKHATENKVKNLIEEMAALDETIL 998
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIkaeiEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 999 KLTKEKKALQEAH-----QQTLDD----LQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLE---GD 1066
Cdd:PHA02562 273 QFQKVIKMYEKGGvcptcTQQISEgpdrITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKIStnkQS 352
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1591544934 1067 LKLSMESVMDLENDKQQLEEKLKKKDfemNEMSTRIEDEQSLVNQLQKKIKELQAR 1122
Cdd:PHA02562 353 LITLVDKAKKVKAAIEELQAEFVDNA---EELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
926-1119 |
4.41e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 926 KVKEIMERLEDEeeMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEkhatenkVKNLIEEMAALDETILKLTKEKK 1005
Cdd:PRK05771 54 KLSEALDKLRSY--LPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1006 ALQ--EAHQQTLDDLQAEED---KVNTLTKAQAKLEQQVDDLEGSLEqekklrmdlerVKRKLEGDLKLsmesVMDLEND 1080
Cdd:PRK05771 125 RLEpwGNFDLDLSLLLGFKYvsvFVGTVPEDKLEELKLESDVENVEY-----------ISTDKGYVYVV----VVVLKEL 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 1081 KQQLEEKLKKKDFE-------------MNEMSTRIEDEQSLVNQLQKKIKEL 1119
Cdd:PRK05771 190 SDEVEEELKKLGFErleleeegtpselIREIKEELEEIEKERESLLEELKEL 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1761-1933 |
4.46e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1761 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIalkggkKQVQKLEARVKELENELESEQKK 1840
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1841 SQEYQKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAK----VKSYKRQAEEAEDQANTNLSKYRKLQHELDDAEE 1916
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAteeeLQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170
....*....|....*..
gi 1591544934 1917 RADMAETQVTKLRVRTR 1933
Cdd:COG4717 228 ELEQLENELEAAALEER 244
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
841-1122 |
4.66e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 841 FFKIKPLLKSA-----ATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEkndlslqLQAEQDNLADAEDrcdl 915
Cdd:PRK04778 100 FRKAKHEINEIeslldLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKS-------LLANRFSFGPALD---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 916 liktkiQLEAKVKEIMERLEDEEEMSAT---VLAKK--RKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKN----L 986
Cdd:PRK04778 169 ------ELEKQLENLEEEFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 987 IEEMAALDEtiLKLTKEKKALQEAHQQTLDDLqaEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKRKLEGD 1066
Cdd:PRK04778 243 VEEGYHLDH--LDIEKEIQDLKEQIDENLALL--EELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDF 318
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1591544934 1067 LKLSMEsvmdlENDKQQLEEKLKKKDFEMNEmstrieDEQSLVNQLQKKIKELQAR 1122
Cdd:PRK04778 319 LEHAKE-----QNKELKEEIDRVKQSYTLNE------SELESVRQLEKQLESLEKQ 363
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
847-1344 |
7.37e-04 |
|
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: 44.71 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 847 LLKSAATEKE---------LASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLI 917
Cdd:pfam05483 244 LLLIQITEKEnkmkdltflLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAT 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 918 KTKIQLEAKVKEIMERLEDEE--------EMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEE 989
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKaahsfvvtEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 990 MAALDETILKLTKEKKALQEAHQ--QTLDDLQAEEDKVNTLTKAQaklEQQVDDLEGSLEQEKKLRMDLERVKRKLEGDL 1067
Cdd:pfam05483 404 EVELEELKKILAEDEKLLDEKKQfeKIAEELKGKEQELIFLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1068 KLSMESVMDLENDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVN----QLQKKIKELQARTEELEEELEADRACRAKVEKQ 1143
Cdd:pfam05483 481 EKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIInckkQEERMLKQIENLEEKEMNLRDELESVREEFIQK 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1144 RGDVARELEELSERLEESGGATSAQIEINKKRETDILKLRRDLEEAMLHHEATTAGLRKKHADSVAElSEQIDSLQRVKQ 1223
Cdd:pfam05483 561 GDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAE-NKQLNAYEIKVN 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1224 KLEKERSEAKMEVDDLAST---------------VEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQrQLNETNSHRARA 1288
Cdd:pfam05483 640 KLELELASAKQKFEEIIDNyqkeiedkkiseeklLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMV-ALMEKHKHQYDK 718
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 1289 QAES--SEL----SRKLEEREATVSqLQRSKNSFSQNVEELKKQLEEENKAKNALAHALQSS 1344
Cdd:pfam05483 719 IIEErdSELglykNKEQEQSSAKAA-LEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKEN 779
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
854-1061 |
7.41e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 854 EKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNL--ADAEDRCDLLIKTKIQLEAKVKEIM 931
Cdd:PRK01156 528 RADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIdiETNRSRSNEIKKQLNDLESRLQEIE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 932 ERLEDEEEMSATVLakkRKLEDECAELKKDIDDLEITLAKVEKEKHATEN------KVKNLIEEMAALDETILKLTKEKK 1005
Cdd:PRK01156 608 IGFPDDKSYIDKSI---REIENEANNLNNKYNEIQENKILIEKLRGKIDNykkqiaEIDSIIPDLKEITSRINDIEDNLK 684
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1591544934 1006 ALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMDLERVKR 1061
Cdd:PRK01156 685 KSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLKR 740
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1800-1929 |
7.43e-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: 43.37 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1800 DLQMRLDEAEQiALKGGKKQVQKLEARVKELENELESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKNL--VRMQELID 1877
Cdd:COG1579 14 ELDSELDRLEH-RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNKEYE 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 1878 KLQAKVKSYKRQAEEAEDQANTNLSKYRKLQHELDDAEERADMAETQVTKLR 1929
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK 144
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1757-1920 |
7.43e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1757 RNAEEKAKKAITDAAMMAEELKKEqdtsahLERMKKNMEQTIKDLQMRL-DEAEQiALKGGKKQVQKLEARVKE----LE 1831
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKE------AEAIKKEALLEAKEEIHKLrNEFEK-ELRERRNELQKLEKRLLQkeenLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1832 NELESEQKKSQEYQKGVRKFERRIKELSYQGEEdkknlvrMQELIDKLQAKVKSY---------KRQAEEAEDQANTNLS 1902
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEE-------LEELIEEQLQELERIsgltaeeakEILLEKVEEEARHEAA 172
|
170
....*....|....*...
gi 1591544934 1903 KYRKLQHEldDAEERADM 1920
Cdd:PRK12704 173 VLIKEIEE--EAKEEADK 188
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1472-1730 |
7.47e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1472 QAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKnlqeeITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAA 1551
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1552 LEEAEGTLEheESKTLRIQLELNQIKADVDRKLAEKEEEIDNLRRNHQRTLESMQAtldaeaksrseavrLRKKMEgDLN 1631
Cdd:COG3206 242 LAALRAQLG--SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA--------------LRAQIA-ALR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1632 EmevqlnhanRLASESQKLLRNLQVQIKDVQleldetiHQNEELKEQVAVTERRNNLLASEVEELRALLEQNDRARKLAE 1711
Cdd:COG3206 305 A---------QLQQEAQRILASLEAELEALQ-------AREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYE 368
|
250
....*....|....*....
gi 1591544934 1712 hELLEATERVNLLHSQNTS 1730
Cdd:COG3206 369 -SLLQRLEEARLAEALTVG 386
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
773-1118 |
8.09e-04 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 44.55 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 773 FKAGLLGHLEELRDERLAKVLTLLQAaarGKIMrMELLRMMERRDALM-----IIQWNIRAFNAVKHWPWMKLFF----K 843
Cdd:pfam15818 5 FKTSLLEALEELRMRREAETQYEEQI---GKII-VETQELKWQKETLQnqketLAKQHKEAMAVFKKQLQMKMCAleeeK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 844 IKPLLKSAATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQL 923
Cdd:pfam15818 81 GKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLHLLAKEDHHKQLNEIEKYYATITGQFGLVKENHGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 924 EAKVKEIMerledeeEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVE---KEKHATEN--------KVKNLIEEMAA 992
Cdd:pfam15818 161 EQNVQEAI-------QLNKRLSALNKKQESEICSLKKELKKVTSDLIKSKvtcQYKMGEENinltikeqKFQELQERLNM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 993 LDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEgslEQEKKLRMDLERVKRKlegdLKLSME 1072
Cdd:pfam15818 234 ELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALK---ENNQTLERDNELQREK----VKENEE 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1591544934 1073 SVMDLENDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQKKIKE 1118
Cdd:pfam15818 307 KFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQE 352
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
848-1116 |
8.16e-04 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 44.38 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 848 LKSAATEKELASLKEELAKLKEALEKSEVKR----KELEERQVSLIQEKNDLSLQLQAEQDnladaEDRCDLLIKTKIQL 923
Cdd:pfam18971 596 FNKAVAEAKSTGNYDEVKKAQKDLEKSLRKRehleKEVEKKLESKSGNKNKMEAKAQANSQ-----KDEIFALINKEANR 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 924 EAKVKEIMERLEdeeemsatvlAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKnliEEMAALDETI--LKLT 1001
Cdd:pfam18971 671 DARAIAYTQNLK----------GIKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAE---ETLKALKGSVkdLGIN 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1002 KEKKALQEAHQQTLDDLQAEEDK-VNTLTKAQAKLEQQVDDLEGSLEQEKKL-RMDLERVKRKLEGDLKLSMESVMDLEN 1079
Cdd:pfam18971 738 PEWISKVENLNAALNEFKNGKNKdFSKVTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKN 817
|
250 260 270
....*....|....*....|....*....|....*....
gi 1591544934 1080 -DKQQLEEKLKK-KDFEMNEMStriEDEQSLVNQLQKKI 1116
Cdd:pfam18971 818 fSKEQLAQQAQKnEDFNTGKNS---ELYQSVKNSVNKTL 853
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1640-1911 |
8.54e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1640 ANRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVAVT-----ERRNNLLA---------SEVEE-LRALLEQND 1704
Cdd:PRK04778 103 AKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLkdlyrELRKSLLAnrfsfgpalDELEKqLENLEEEFS 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1705 RARKLAEH-ELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKA---ITDAAMMAE--ELK 1778
Cdd:PRK04778 183 QFVELTESgDYVEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEgyhLDHLDIEKEiqDLK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1779 KE-QDTSAHLERMK-KNMEQTIKDLQMRLD------EAEQIA-------LKGGKKQVQKLEARVKELENELESEQKK--- 1840
Cdd:PRK04778 263 EQiDENLALLEELDlDEAEEKNEEIQERIDqlydilEREVKArkyveknSDTLPDFLEHAKEQNKELKEEIDRVKQSytl 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1841 SQEYQKGVRKFERRIKELSYQGEEDKKNLV-----------RMQEL------IDKLQAKVKSYKRQAEEAEDQANTNLSK 1903
Cdd:PRK04778 343 NESELESVRQLEKQLESLEKQYDEITERIAeqeiayselqeELEEIlkqleeIEKEQEKLSEMLQGLRKDELEAREKLER 422
|
....*...
gi 1591544934 1904 YRKLQHEL 1911
Cdd:PRK04778 423 YRNKLHEI 430
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1623-1884 |
1.06e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1623 RKKMEGDLNEMEVqLNHANRLaseSQKLLRNLQVQIKDVQLELDetiHQNEELKEQVAVTERRNNLLASEVEELRALLEQ 1702
Cdd:PHA02562 152 RRKLVEDLLDISV-LSEMDKL---NKDKIRELNQQIQTLDMKID---HIQQQIKTYNKNIEEQRKKNGENIARKQNKYDE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1703 NDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAvqecrNAEEKAKKAITDAAMMAEELKKEQD 1782
Cdd:PHA02562 225 LVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQF-----QKVIKMYEKGGVCPTCTQQISEGPD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1783 TSAHLERMKKNMEQTIKDLQMRLDEAEQIalkggKKQVQKLEARVKELENELESEQKKSQEYQKGVRKFERRIKELSYQG 1862
Cdd:PHA02562 300 RITKIKDKLKELQHSLEKLDTAIDELEEI-----MDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEF 374
|
250 260
....*....|....*....|....*.
gi 1591544934 1863 EEDKKNLVRMQ----ELIDKLQAKVK 1884
Cdd:PHA02562 375 VDNAEELAKLQdeldKIVKTKSELVK 400
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
849-1006 |
1.06e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 849 KSAATEKELASL--KEELAKLKEALEK-SEVKRKELEERQVSLIQEKNDLslqlqaeqdnladaEDRCDLLIKTKIQLEA 925
Cdd:PRK12704 49 KEAEAIKKEALLeaKEEIHKLRNEFEKeLRERRNELQKLEKRLLQKEENL--------------DRKLELLEKREEELEK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 926 KVKEIMERLEDEEEMSATVLAKKRKLEDE---CAELKKDiDDLEITLAKVEKE-KHATENKVKNlIEEMAaldetilKLT 1001
Cdd:PRK12704 115 KEKELEQKQQELEKKEEELEELIEEQLQElerISGLTAE-EAKEILLEKVEEEaRHEAAVLIKE-IEEEA-------KEE 185
|
....*
gi 1591544934 1002 KEKKA 1006
Cdd:PRK12704 186 ADKKA 190
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1582-1917 |
1.19e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1582 RKLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLRKKMEGDLNEMEVQLNHANRLASESQKLLRNLQVQIKDV 1661
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1662 QLELDETIHQNEELKEQVAVTERRNNLLASEVEELRALLEQNDRARKLAEHELLEATERVNLLHSQNTSLINQKKKLEND 1741
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1742 LSTLsnEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQ 1821
Cdd:COG4372 166 LAAL--EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1822 KLEARVKELENELESE-QKKSQEYQKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKRQAEEAEDQANTN 1900
Cdd:COG4372 244 LEEDKEELLEEVILKEiEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330
....*....|....*..
gi 1591544934 1901 LSKYRKLQHELDDAEER 1917
Cdd:COG4372 324 LAKKLELALAILLAELA 340
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1497-1882 |
1.37e-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: 43.85 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1497 EETLEHLETIKRE-----NKNLQEEITDLSDQISQGAKT-IHELEKMKKGLEIEK-SEIQAALEEAEGTLEHEESKTLRI 1569
Cdd:NF033838 61 KEVESHLEKILSEiqkslDKRKHTQNVALNKKLSDIKTEyLYELNVLKEKSEAELtSKTKKELDAAFEQFKKDTLEPGKK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1570 QLELNQIKADVDRKL-AEKEEEIDNLRRNHQRTLESMQATLDAEAKsRSEAVRLRKKMEGDLNEMEVQLNHANrlaSESQ 1648
Cdd:NF033838 141 VAEATKKVEEAEKKAkDQKEEDRRNYPTNTYKTLELEIAESDVEVK-KAELELVKEEAKEPRDEEKIKQAKAK---VESK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1649 KLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTErrnNLLASEVEELRAlleqndRARKLAEHELLEATERVNLLHSQN 1728
Cdd:NF033838 217 KAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEK---NVATSEQDKPKR------RAKRGVLGEPATPDKKENDAKSSD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1729 TSLinqkkkLENDLSTLSNEVDDAVQECRNAEEKAKKAITDaammaeelKKEQDTSAHLERMKKNMEQTIKDLQMRLDEA 1808
Cdd:NF033838 288 SSV------GEETLPSPSLKPEKKVAEAEKKVEEAKKKAKD--------QKEEDRRNYPTNTYKTLELEIAESDVKVKEA 353
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1591544934 1809 EQIALKGGKKQVQKlEARVKELENELESEQKKSQEYQKgvrkferrIKELSYQGEEDKKnlvRMQELIDKLQAK 1882
Cdd:NF033838 354 ELELVKEEAKEPRN-EEKIKQAKAKVESKKAEATRLEK--------IKTDRKKAEEEAK---RKAAEEDKVKEK 415
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
843-1048 |
1.54e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 843 KIKPLLKSAATEKELASLKEELAKLKEALEKSEVKRKELEERQvsLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQ 922
Cdd:COG4913 250 QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 923 LEAKVKEI-MERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEkhatenkvknLIEEMAALDETILKLT 1001
Cdd:COG4913 328 LEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE----------FAALRAEAAALLEALE 397
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1591544934 1002 KEKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQ 1048
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1194-1437 |
1.58e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1194 EATTAGLRKKHADSVAELSEQIDSLQRVKQKLE--KERSEA---------KMEVDDLASTVEQLSKGKASAEKTcRLYED 1262
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDqlKEQLQLlnkllpqanLLADETLADRLEELREELDAAQEA-QAFIQ 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1263 QMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQL----QRSKN-SFSQNVEELKKQLEEENKAKNAL 1337
Cdd:COG3096 914 QHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALsevvQRRPHfSYEDAVGLLGENSDLNEKLRARL 993
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1338 AHALQSSRHDCDLLREQYDEEQEAKAELQRALSKAngevaqwRTKYET--DAIQRTEELE-----ESKKKLAVRLQEAEE 1410
Cdd:COG3096 994 EQAEEARREAREQLRQAQAQYSQYNQVLASLKSSR-------DAKQQTlqELEQELEELGvqadaEAEERARIRRDELHE 1066
|
250 260
....*....|....*....|....*..
gi 1591544934 1411 AVEASNAKCSSLEKTKHRLQTEIEDLV 1437
Cdd:COG3096 1067 ELSQNRSRRSQLEKQLTRCEAEMDSLQ 1093
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
915-1085 |
1.63e-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: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 915 LLIKTKIQLEAK----------VKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITL-AKVEKEKHATENKV 983
Cdd:smart00787 120 QLVKTFARLEAKkmwyewrmklLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALeEELRQLKQLEDELE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 984 KNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKL-RMDLERVKRK 1062
Cdd:smart00787 200 DCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFtFKEIEKLKEQ 279
|
170 180
....*....|....*....|...
gi 1591544934 1063 LEGDLKLSMESVMDLENDKQQLE 1085
Cdd:smart00787 280 LKLLQSLTGWKITKLSGNTLSMT 302
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1690-1917 |
1.64e-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: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1690 ASEVEELRALLEQ--NDRARKLAEH--ELLEATERVNLLHSQNTSLINQKKKLENDLSTLsnevddavqecRNAEEKAKK 1765
Cdd:pfam05557 1 RAELIESKARLSQlqNEKKQMELEHkrARIELEKKASALKRQLDRESDRNQELQKRIRLL-----------EKREAEAEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1766 AITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAeqiaLKGGKKQVQKLEARVKELENELESEQKKSQEYQ 1845
Cdd:pfam05557 70 ALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNE----LSELRRQIQRAELELQSTNSELEELQERLDLLK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 1846 KGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQakvkSYKRQAEEAEDqANTNLSKYRKLQHELDDAEER 1917
Cdd:pfam05557 146 AKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQ----SQEQDSEIVKN-SKSELARIPELEKELERLREH 212
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1266-1896 |
1.69e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.50 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1266 EAKAKVEELQRQLNETNSHRARAQAESSELSrkleereatVSQLQRSKNSFSQN-VEELKKQLEEENKAKNALAHALQSS 1344
Cdd:TIGR01612 693 EDKAKLDDLKSKIDKEYDKIQNMETATVELH---------LSNIENKKNELLDIiVEIKKHIHGEINKDLNKILEDFKNK 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1345 RHDCDLLREQY----DEEQEAKAELQRALSKANGEVAQWRTKyETDAIQRTEELEESKKKLAVRLQEAEEAV-EASNAKC 1419
Cdd:TIGR01612 764 EKELSNKINDYakekDELNKYKSKISEIKNHYNDQINIDNIK-DEDAKQNYDKSKEYIKTISIKEDEIFKIInEMKFMKD 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1420 SSLEKTkhrlqteieDLVVDLERASAAAaaLDKKQRNFDKVLAEWRQKCEECQ-AELETSQKESRSLSTELfklKNSYEE 1498
Cdd:TIGR01612 843 DFLNKV---------DKFINFENNCKEK--IDSEHEQFAELTNKIKAEISDDKlNDYEKKFNDSKSLINEI---NKSIEE 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1499 TLEHLETIKREN------KNLQEEI-------TDLSDQISQGAKTIHELEKMKKG--------LEIEKSEIQAALEEAeg 1557
Cdd:TIGR01612 909 EYQNINTLKKVDeyikicENTKESIekfhnkqNILKEILNKNIDTIKESNLIEKSykdkfdntLIDKINELDKAFKDA-- 986
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1558 TLEHEESKTLRIQLELNQIKAdvdrklaekeeeidNLRRNHQRTLESMqatLDAEAKSrseavrlrkkmegdLNEMEVQL 1637
Cdd:TIGR01612 987 SLNDYEAKNNELIKYFNDLKA--------------NLGKNKENMLYHQ---FDEKEKA--------------TNDIEQKI 1035
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1638 NHANRLASESQKLLrnlQVQIKDVQLELDETIHQNEELKEQVAVTERRNNLLA-SEVEELRALLEQNDRARKlaehelle 1716
Cdd:TIGR01612 1036 EDANKNIPNIEIAI---HTSIYNIIDEIEKEIGKNIELLNKEILEEAEINITNfNEIKEKLKHYNFDDFGKE-------- 1104
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1717 atervnllhsQNTSLINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKnMEQ 1796
Cdd:TIGR01612 1105 ----------ENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDPEE-IEK 1173
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1797 TIKDLQMRLDEAEQIAlkggkKQVQKLEARVKELENE---LESEQKKSQEYQKGVRK-FERRIkelsyqgEEDKKNLVRM 1872
Cdd:TIGR01612 1174 KIENIVTKIDKKKNIY-----DEIKKLLNEIAEIEKDktsLEEVKGINLSYGKNLGKlFLEKI-------DEEKKKSEHM 1241
|
650 660
....*....|....*....|....
gi 1591544934 1873 QELIDKLQAKVKSYKRQAEEAEDQ 1896
Cdd:TIGR01612 1242 IKAMEAYIEDLDEIKEKSPEIENE 1265
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
1463-1577 |
1.97e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 42.41 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1463 EWRQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKmKKGLE 1542
Cdd:COG4026 132 ELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLK-KRLLE 210
|
90 100 110
....*....|....*....|....*....|....*
gi 1591544934 1543 IEKseIQAALEEAEGTLEHEESKTLRIQLELNQIK 1577
Cdd:COG4026 211 VFS--LEELWKELFPEELPEEDFIYFATENLKPGK 243
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
1488-1697 |
2.11e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 42.32 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1488 ELFKLKNSYEETLEHLETikrENKNLQEEITDLSdqisqgaktiHELEKMKKGLEI-----EKSEIQAALEEAEGTLEHE 1562
Cdd:pfam04849 91 SLLKQNSVLTERNEALEE---QLGSAREEILQLR----------HELSKKDDLLQIysndaEESETESSCSTPLRRNESF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1563 ESKTLRIQLELNQikadvdRKLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLRKKMEGDLNEMEVQLNHANR 1642
Cdd:pfam04849 158 SSLHGCVQLDALQ------EKLRGLEEENLKLRSEASHLKTETDTYEEKEQQLMSDCVEQLSEANQQMAELSEELARKME 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1591544934 1643 LASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVAVTERRNNLLASEVEELR 1697
Cdd:pfam04849 232 ENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQLTSELQELQ 286
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1728-1925 |
2.22e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.01 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1728 NTSLINQKKKLENDLSTLSNEVDDAvqecrnaeEKAKKAITDAAMMAEEL-KKEQDTSAHLERMKKNMEQTIKDLQMRLD 1806
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENAHKIQI--------EILEKELSSLAQETEELqKKATQTLAKAQQVNAESERTLGHAKELAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1807 EAEQIAlkggkKQVQKLEARVKEL-ENELESEQKKSQEYQKGVRKF--ERRIKELSYQGEEDKKNLVRMQELIDKLQAKV 1883
Cdd:pfam06008 90 AIKNLI-----DNIKEINEKVATLgENDFALPSSDLSRMLAEAQRMlgEIRSRDFGTQLQNAEAELKAAQDLLSRIQTWF 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1591544934 1884 KSYKRQAEEAEDQANTNLSKYrklQHELDDAEERADMAETQV 1925
Cdd:pfam06008 165 QSPQEENKALANALRDSLAEY---EAKLSDLRELLREAAAKT 203
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1356-1470 |
2.22e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1356 DEEQEAKAELQRALSKANGEVAQWRTKYETDAIQRTEELEESKKklavRLQEAEEAVEasnAKCSSLEKTKHRLQTEIED 1435
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEK----RLLQKEENLD---RKLELLEKREEELEKKEKE 118
|
90 100 110
....*....|....*....|....*....|....*
gi 1591544934 1436 LVVDLErasaaaaALDKKQRNFDKVLAEWRQKCEE 1470
Cdd:PRK12704 119 LEQKQQ-------ELEKKEEELEELIEEQLQELER 146
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
815-934 |
2.38e-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: 40.57 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 815 RRDALMIIQWNIRAFNAVK-HWPwmklffKIKPLLKSAATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQE-K 892
Cdd:cd21759 44 RREALIKIQKTVRGYLARKkHRP------RIKGLRKIRALEKQLKEMEEIASQLKKDKDKWTKQVKELKKEIDALIKKiK 117
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1591544934 893 NDlslqlqaEQDNLADAEDRCDlliktkiQLEAKVKEIMERL 934
Cdd:cd21759 118 TN-------DMITRKEIDKLYN-------ALVKKVDKQLAEL 145
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1038-1642 |
2.73e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1038 QVDDL-EGSLEQEKKLRMDLERVKRKLEGDLKLSmESVMDLE---NDKQQLEEKLKKKDFEMNEMSTRIEDEQSLVNQLQ 1113
Cdd:PRK01156 139 EMDSLiSGDPAQRKKILDEILEINSLERNYDKLK-DVIDMLRaeiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1114 KKIKELQArteelEEELEADRACRAKVEKQRgdvareleelserleesggaTSAQIEINKKRETDILKLRRDL---EEAM 1190
Cdd:PRK01156 218 KEIERLSI-----EYNNAMDDYNNLKSALNE--------------------LSSLEDMKNRYESEIKTAESDLsmeLEKN 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1191 LHHEATTAGLRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKmEVDDLASTVEQLSKGKASAEKtcrlYEDQMNEAKAK 1270
Cdd:PRK01156 273 NYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILS-NIDAEINKYHAIIKKLSVLQK----DYNDYIKKKSR 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1271 VEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQNVEELKKQLEEENKAKNALAHALQSSRHDCDL 1350
Cdd:PRK01156 348 YDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSS 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1351 LREQYDEEQEAKAELQRALSKANGE--VAQWRTKYETDAIQR-TEELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKH 1427
Cdd:PRK01156 428 LNQRIRALRENLDELSRNMEMLNGQsvCPVCGTTLGEEKSNHiINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKE 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1428 RLQTE-----------IEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQ-KCEECQAELETSQKESRSLSteLFKLKNS 1495
Cdd:PRK01156 508 YLESEeinksineynkIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDLDSKRTSWLNALAVIS--LIDIETN 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1496 YEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQ---AALEEAEGTLEHEESKTLRIQlE 1572
Cdd:PRK01156 586 RSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQenkILIEKLRGKIDNYKKQIAEID-S 664
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1573 LNQIKADVDRKLAEKEEEIDNLRRnhqrtlesmqaTLDAEAKSRSEAVRLRKKMEGDLNEMEVQLNHANR 1642
Cdd:PRK01156 665 IIPDLKEITSRINDIEDNLKKSRK-----------ALDDAKANRARLESTIEILRTRINELSDRINDINE 723
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
843-975 |
2.89e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 41.61 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 843 KIKPLLKSAATE---KELASLKEELAKLKEaleksevKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKT 919
Cdd:pfam15294 118 KLEPLNEGGGSAllhMEIERLKEENEKLKE-------RLKTLESQATQALDEKSKLEKALKDLQKEQGAKKDVKSNLKEI 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1591544934 920 KiQLEAKVKEIMERLEDEEEMSAtvlAKKRKLEDECAELKKDIDDLEITLAKVEKE 975
Cdd:pfam15294 191 S-DLEEKMAALKSDLEKTLNAST---ALQKSLEEDLASTKHELLKVQEQLEMAEKE 242
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1570-1931 |
2.97e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.89 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1570 QLELNQIKADVDRKLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSR-----SEAVRLRKKMEGDLNEmEVQLNHANRLA 1644
Cdd:NF041483 82 QIQADQLRADAERELRDARAQTQRILQEHAEHQARLQAELHTEAVQRrqqldQELAERRQTVESHVNE-NVAWAEQLRAR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1645 SESQKllRNLqvqIKDVQLELDETIHQNEELKEQVAVTERRNnlLASEVEELRALLEQN-DRARKLAEHEL-------LE 1716
Cdd:NF041483 161 TESQA--RRL---LDESRAEAEQALAAARAEAERLAEEARQR--LGSEAESARAEAEAIlRRARKDAERLLnaastqaQE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1717 ATERVNLLHSQNTSLINQKKKLENDLSTLS----NEVDDAVQECRNAEEKAKKAITDAA---MMAEELKKEQDTSAHLER 1789
Cdd:NF041483 234 ATDHAEQLRSSTAAESDQARRQAAELSRAAeqrmQEAEEALREARAEAEKVVAEAKEAAakqLASAESANEQRTRTAKEE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1790 MKKNMEQTIKDLQMRLDEAEQiALKGGKKQVQKLEARVKELENELESEQKKSQeyqkgVRKFERRIKELSYQGEEDKKNL 1869
Cdd:NF041483 314 IARLVGEATKEAEALKAEAEQ-ALADARAEAEKLVAEAAEKARTVAAEDTAAQ-----LAKAARTAEEVLTKASEDAKAT 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1591544934 1870 VRmqelidklqAKVKSYKRQAEEAEDQANTNLSKYRKLQHEL-----DDAEE-RADMAETQVTKLRVR 1931
Cdd:NF041483 388 TR---------AAAEEAERIRREAEAEADRLRGEAADQAEQLkgaakDDTKEyRAKTVELQEEARRLR 446
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1495-1917 |
3.46e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1495 SYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTI----HELEKMKKGLEiEKSEIQAALEEAEGTLEHEESKTLRIQ 1570
Cdd:TIGR00606 204 EHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVksyeNELDPLKNRLK-EIEHNLSKIMKLDNEIKALKSRKKQME 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1571 LELNQIKADVDRKLAEKEEEIDNLRRNHQRTLESMQATLDAEAKSRSEAVRLRKKMEGDLNEMEVQLNHANRLAS--ESQ 1648
Cdd:TIGR00606 283 KDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADrhQEH 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1649 KLLRNLQVQIKDVQLELDETIHQ---NEELKEQVAVTERRNNLLASEVEELRALLEQNDRARKLAehelleATERVNLLH 1725
Cdd:TIGR00606 363 IRARDSLIQSLATRLELDGFERGpfsERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQ------ADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1726 SQNTSLINQKKKLENDLSTLSNevddAVQECRNAEEKAKKAITdaamMAEELKKEQdtsAHLERMKKNMEQTIKDLQMRL 1805
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKF----VIKELQQLEGSSDRILE----LDQELRKAE---RELSKAEKNSLTETLKKEVKS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1806 DEAEQIALKggkKQVQKLEARVKELENELESEQKKSQEYQKGVRKFERrIKELSYQGEEDKKNLV----RMQELIDKLQA 1881
Cdd:TIGR00606 506 LQNEKADLD---RKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQ-IRKIKSRHSDELTSLLgyfpNKKQLEDWLHS 581
|
410 420 430
....*....|....*....|....*....|....*.
gi 1591544934 1882 KVKSyKRQAEEAEDQANTNLSKYRKLQHELDDAEER 1917
Cdd:TIGR00606 582 KSKE-INQTRDRLAKLNKELASLEQNKNHINNELES 616
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1784-1923 |
3.46e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1784 SAHLERMKKNMEQTIKDLQMRLDEAEQIALKGGKKQVQKL----EARVKELENELESEQKKSQEYQKGVRKFERRIKELS 1859
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLrnefEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1591544934 1860 YQGEEDKKNLVRMQELIDKLQAKVksykrqaEEAEDQANTNLSKYRKLQHE------LDDAEE--RADMAET 1923
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEEL-------EELIEEQLQELERISGLTAEeakeilLEKVEEeaRHEAAVL 174
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1412-1935 |
3.61e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1412 VEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAAlDKKQRNFDKVLAEW-RQKCEECQAELETSQKESRSLSTELF 1490
Cdd:pfam10174 235 IEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREE-EIKQMEVYKSHSKFmKNKIDQLKQELSKKESELLALQTKLE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1491 KLKNSYEETLEHLETIK-------RENKNLQEEITDLSDQISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEGTLEHEE 1563
Cdd:pfam10174 314 TLTNQNSDCKQHIEVLKesltakeQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKE 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1564 SKTLRIQLELNQIKadvdRKLAEKEEEIDNLRRNHQrTLESMQATLDAEAKSRSEAVrlrkkmegdlnemevqlnhanrl 1643
Cdd:pfam10174 394 RKINVLQKKIENLQ----EQLRDKDKQLAGLKERVK-SLQTDSSNTDTALTTLEEAL----------------------- 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1644 aSESQKLLRNLQVQI----KDVQLELDETIHQNEELKEQVAVTERrnnllaseveelralleqndrarklaehELLEATE 1719
Cdd:pfam10174 446 -SEKERIIERLKEQReredRERLEELESLKKENKDLKEKVSALQP----------------------------ELTEKES 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1720 RVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKA--ITDAAMMAEELkkeQDTSAHLErmkknmeqt 1797
Cdd:pfam10174 497 SLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAhnAEEAVRTNPEI---NDRIRLLE--------- 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1798 iKDLQMRLDEAeqialkgGKKQ--VQKLEARVKELENELESEQKKSQEYQKgvrKFERRIKEL--------SYQGEEDKK 1867
Cdd:pfam10174 565 -QEVARYKEES-------GKAQaeVERLLGILREVENEKNDKDKKIAELES---LTLRQMKEQnkkvanikHGQQEMKKK 633
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1591544934 1868 NLVRMQE-LIDKLQAKVKSYKRQAEEAedqantnLSKYRKLQHELDDAEERadMAETQV---------TKLRVRTRDQ 1935
Cdd:pfam10174 634 GAQLLEEaRRREDNLADNSQQLQLEEL-------MGALEKTRQELDATKAR--LSSTQQslaekdghlTNLRAERRKQ 702
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1544-1785 |
3.83e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1544 EKSEIQAALEEAEGTLEHEESKTLRIQLELNQIKADVDR---KLAEKEEEIDNLRRNhqrtLESMQATLDAEAKSRSEAV 1620
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNElqaELEALQAEIDKLQAE----IAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1621 RLRKKMEGDLNEMEVQLNhanrlASESQKLLRNLQV--QIKDVQLE-LDETIHQNEELKEQVAvterrnnLLASEVEELR 1697
Cdd:COG3883 93 RALYRSGGSVSYLDVLLG-----SESFSDFLDRLSAlsKIADADADlLEELKADKAELEAKKA-------ELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1698 ALLEQNDRARKLAEHELLEATERVNllhsqntSLINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKAITDAAMMAEEL 1777
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLA-------QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
....*...
gi 1591544934 1778 KKEQDTSA 1785
Cdd:COG3883 234 AAAAAAAA 241
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1694-1914 |
3.85e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.17 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1694 EELRALLEQNDRAR---KLAEHELLEATERVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQECRNAEEKAKKAITDA 1770
Cdd:pfam00261 1 KKMQQIKEELDEAEerlKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1771 AMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAE------QIALKGGKKQVQKLEARVKELENELE--------- 1835
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVArklvvvEGDLERAEERAELAESKIVELEEELKvvgnnlksl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1836 --SEQKKSQ---EYQKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKrqaeeaedqantnlSKYRKLQHE 1910
Cdd:pfam00261 161 eaSEEKASEredKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEK--------------EKYKAISEE 226
|
....
gi 1591544934 1911 LDDA 1914
Cdd:pfam00261 227 LDQT 230
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1392-1837 |
3.95e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.94 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1392 EELEESKKKLAVRLQEAEEAVEASNAKCSSLEKTKHrlqtEIEDLVVDLERASaaaaaLDKKQRNFDKVLAEWRQKceec 1471
Cdd:pfam05701 42 LELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKR----LIEELKLNLERAQ-----TEEAQAKQDSELAKLRVE---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1472 QAELETSQKESRSLSTELFKLKNSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIH-------ELEKMKKGLEIE 1544
Cdd:pfam05701 109 EMEQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEeavsaskEIEKTVEELTIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1545 KSEIQAALEEAEGTLEHEESKTLRIQLELNQIKADVDRKLAEKEEEIDNLRrnhqrtlESMQATLDAEAKSrSEAVRLRK 1624
Cdd:pfam05701 189 LIATKESLESAHAAHLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRLN-------QQLLSAKDLKSKL-ETASALLL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1625 KMEGDLNE-MEVQLNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVavterrnNLLASEVEELRALLEQn 1703
Cdd:pfam05701 261 DLKAELAAyMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEV-------NCLRVAAASLRSELEK- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1704 drarklaehellEATERVNLLHSQNTSLINqkkklendLSTLSNEVDDAVQECRNAEEKAKKAitdAAMMAEELKKEQDT 1783
Cdd:pfam05701 333 ------------EKAELASLRQREGMASIA--------VSSLEAELNRTKSEIALVQAKEKEA---REKMVELPKQLQQA 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1591544934 1784 SAHLERMKKNMEQTIKDLQMRLDEAEQIalKGGKKQVQ-KLEARVKELENELESE 1837
Cdd:pfam05701 390 AQEAEEAKSLAQAAREELRKAKEEAEQA--KAAASTVEsRLEAVLKEIEAAKASE 442
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
988-1097 |
4.01e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 988 EEMAALDETILKLTKEKKAL----QEAHQQTLDDLQAEEdkvntltkaqAKLEQQVDDLEGSLEQEKKLRMDLERVKRKL 1063
Cdd:COG0542 411 EELDELERRLEQLEIEKEALkkeqDEASFERLAELRDEL----------AELEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|....
gi 1591544934 1064 EGDLklsmESVMDLENDKQQLEEKLKKKDFEMNE 1097
Cdd:COG0542 481 EQRY----GKIPELEKELAELEEELAELAPLLRE 510
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1239-1470 |
4.10e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1239 LASTVEQLSKGKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQ 1318
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1319 NVEELKKQLEEENKA-KNALAHALQSSRHDCDLLREQydeeQEAKAELQRALsKANGEVAQWRTKYETDAIQRTEELEES 1397
Cdd:COG4942 91 EIAELRAELEAQKEElAELLRALYRLGRQPPLALLLS----PEDFLDAVRRL-QYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1591544934 1398 KKKLAVRLQEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKCEE 1470
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1418-1578 |
4.35e-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: 41.54 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1418 KCSSLEKTKHRLQTEIEDLVVDLERasaaaaaLDKKQRNFDKVLAEWRQKCEECQAELETSQKESRSL----STELFKLK 1493
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKL-------LMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELedcdPTELDRAK 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1494 NSYEETLEHLETIKRENKNLQEEITDLSDQISQGAKTIHELEKmkkgleiEKSEIQAALEEAEGTLEHEESKtlrIQLEL 1573
Cdd:smart00787 211 EKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT-------EIAEAEKKLEQCRGFTFKEIEK---LKEQL 280
|
....*
gi 1591544934 1574 NQIKA 1578
Cdd:smart00787 281 KLLQS 285
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
898-1145 |
4.44e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.60 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 898 QLQAEQDNLADAEdrcdlliKTKIQLEAKVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKH 977
Cdd:PRK11637 48 QLKSIQQDIAAKE-------KSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 978 ATEnkvKNLIEEMAAL--------DETILKLTKEKKA---------LQEAHQQTLDDLQaeedkvntltKAQAKLEQQVD 1040
Cdd:PRK11637 121 AQE---RLLAAQLDAAfrqgehtgLQLILSGEESQRGerilayfgyLNQARQETIAELK----------QTREELAAQKA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1041 DLEGSLEQEKKLRMDLERVKRKLEGDLKLSMESVMDLEN----DKQQLEEkLKkkdfemnemstriEDEQSLVNQLQKKI 1116
Cdd:PRK11637 188 ELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESslqkDQQQLSE-LR-------------ANESRLRDSIARAE 253
|
250 260
....*....|....*....|....*....
gi 1591544934 1117 KELQARTEELEEELEADRAcRAKVEKQRG 1145
Cdd:PRK11637 254 REAKARAEREAREAARVRD-KQKQAKRKG 281
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
948-1065 |
4.48e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.20 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 948 KRKLEDECAELKKDIDDLEITLAKVEKE----KHATENKVKNLIEEMAALDEtilKLTKEKKALQEAHqqtLDDLQAEED 1023
Cdd:cd22656 116 KKTIKALLDDLLKEAKKYQDKAAKVVDKltdfENQTEKDQTALETLEKALKD---LLTDEGGAIARKE---IKDLQKELE 189
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1591544934 1024 KVNTLTKAQAK-----LEQQVDDLEGSLEQEKKLRMDLERVKRKLEG 1065
Cdd:cd22656 190 KLNEEYAAKLKakideLKALIADDEAKLAAALRLIADLTAADTDLDN 236
|
|
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
849-1019 |
4.51e-03 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 42.06 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 849 KSAATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLiqeknDLSLQLQAEQDNLADAEDRCDlliktkiQLEAKVK 928
Cdd:PRK11519 261 KSEEASKSLAFLAQQLPEVRSRLDVAENKLNAFRQDKDSV-----DLPLEAKAVLDSMVNIDAQLN-------ELTFKEA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 929 EIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDdleiTLAKVEKEkhatenkvknlieemaaldetILKLTKEKKALQ 1008
Cdd:PRK11519 329 EISKLYTKEHPAYRTLLEKRKALEDEKAKLNGRVT----AMPKTQQE---------------------IVRLTRDVESGQ 383
|
170
....*....|.
gi 1591544934 1009 EAHQQTLDDLQ 1019
Cdd:PRK11519 384 QVYMQLLNKQQ 394
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
1814-1902 |
4.53e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 41.57 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1814 KGGKKQVQKLEARVKELENELESEQKKSQEYQ-------KGVRKFERRIKELSYQGEEDKKNLVRMQ---ELIDKLQAKV 1883
Cdd:smart00435 273 KTHEKSMEKLQEKIKALKYQLKRLKKMILLFEmisdlkrKLKSKFERDNEKLDAEVKEKKKEKKKEEkkkKQIERLEERI 352
|
90
....*....|....*....
gi 1591544934 1884 KSYKRQAEEAEDQANTNLS 1902
Cdd:smart00435 353 EKLEVQATDKEENKTVALG 371
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
928-1248 |
4.68e-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: 42.05 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 928 KEIMERLEDEEEMSATVLAKKRKLEDECAELKKDiddleitlaKVEKEKHATENKVKNLI-EEMAALDETILKLTKEKKA 1006
Cdd:pfam09731 121 KSEQEKEKALEEVLKEAISKAESATAVAKEAKDD---------AIQAVKAHTDSLKEASDtAEISREKATDSALQKAEAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1007 LQEAHQQTLDDLQAEEDKVN-TLTKAQAKLEQQVDDL---EGSLEQEKKLRMDLERVKRKLEGDlklSMESVMDLENDKQ 1082
Cdd:pfam09731 192 AEKLKEVINLAKQSEEEAAPpLLDAAPETPPKLPEHLdnvEEKVEKAQSLAKLVDQYKELVASE---RIVFQQELVSIFP 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1083 QLEEKLKK-KDFEMNEMSTRIEDEQSLVNQLQKKIKELQARteeleeeleADRACRAKVEKQRGDVARELEELSERLEES 1161
Cdd:pfam09731 269 DIIPVLKEdNLLSNDDLNSLIAHAHREIDQLSKKLAELKKR---------EEKHIERALEKQKEELDKLAEELSARLEEV 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1162 GGATSAQIEINKKREtdILKLRRDLEEAM---LHHEATTAGLRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDD 1238
Cdd:pfam09731 340 RAADEAQLRLEFERE--REEIRESYEEKLrteLERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNE 417
|
330
....*....|
gi 1591544934 1239 LASTVEQLSK 1248
Cdd:pfam09731 418 LLANLKGLEK 427
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
918-1250 |
4.72e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 918 KTKIQLEAKVKEIMERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETI 997
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 998 LKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQekklrmdLERVKRKLEGDLKLSMESVMDL 1077
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ-------LEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1078 ENDKQQLEEKLKKKDFEMNEMSTRiEDEQSLVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRGDVARELEELSER 1157
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEA-EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1158 LEESGGATSAQIEINKKRETDILKLRRDLEEAMLHHEATTAGLRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVD 1237
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330
....*....|...
gi 1591544934 1238 DLASTVEQLSKGK 1250
Cdd:COG4372 315 DALLAALLELAKK 327
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1103-1517 |
4.91e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1103 EDEQSLVNQLQKKIKELQARTEELEEELEADRACRAKVEKQRGDVARELEELSERLEESGGAT-----SAQIEINKKRET 1177
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPErleelEERLEELRELEE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1178 DILKLRRDLEEAMLHHEATTAGLRKKHADSVAELSEQIDSLQRVKQKLEKERSEAKMEVDDLASTVEQLSKGKASAEKTC 1257
Cdd:COG4717 164 ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1258 RLYEdqmneakakveelQRQLNETNSHRARAQAESSELSRKLEEREATV-----------SQLQRSKNSFSQNVEELKKQ 1326
Cdd:COG4717 244 RLKE-------------ARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallfLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1327 LEEENKAKNALAHALQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTKYETDAIQR--TEELEESKKKLAVR 1404
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1405 LQEAEEAVEASNAkcssLEKTKHRLQTEIEDLVVDLEraSAAAAALDKKQRNFDKVLAEWRQKCEECQAELETSQKESRS 1484
Cdd:COG4717 391 LEQAEEYQELKEE----LEELEEQLEELLGELEELLE--ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420 430
....*....|....*....|....*....|...
gi 1591544934 1485 LSTElfklkNSYEETLEHLETIKRENKNLQEEI 1517
Cdd:COG4717 465 LEED-----GELAELLQELEELKAELRELAEEW 492
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1479-1680 |
5.20e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1479 QKESRSLSTE-LFKLKNSYEETLEHLETIKRENKNLQEEITDLsdqISQGAKTIHELEKMKKGLEIEKSEIQAALEEAEG 1557
Cdd:PHA02562 204 IEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDELLNL---VMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKM 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1558 TLEHEESKTLRIQLElnqikaDVDRKLAEKEEEIDNLrrnhQRTLESMQATLDAEAKSRSEAVRLRKK---MEGDLNEME 1634
Cdd:PHA02562 281 YEKGGVCPTCTQQIS------EGPDRITKIKDKLKEL----QHSLEKLDTAIDELEEIMDEFNEQSKKlleLKNKISTNK 350
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1591544934 1635 VQLNHANRLASESQKLLRNLQVQIKDVQLELDETIHQNEELKEQVA 1680
Cdd:PHA02562 351 QSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKS 396
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1616-1882 |
5.53e-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: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1616 RSEAVRLRKKMEGDLNEMEVQLNHANRlasESQKLLRNLQVqikdVQLELDETIHQNEELKEQVAV--TERRNNLLASEV 1693
Cdd:pfam15905 89 RGEQDKRLQALEEELEKVEAKLNAAVR---EKTSLSASVAS----LEKQLLELTRVNELLKAKFSEdgTQKKMSSLSMEL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1694 EELRALLEQNDRARKLAEHEL---LEATERvNLLHSQNTsLINQKKKLendlstLSNEVDDAVQECRNaeEKAKKAITDA 1770
Cdd:pfam15905 162 MKLRNKLEAKMKEVMAKQEGMegkLQVTQK-NLEHSKGK-VAQLEEKL------VSTEKEKIEEKSET--EKLLEYITEL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1771 AMMAEELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQIAlkggKKQVQKLEARVKELENELESEQKKSQEyqkgvrK 1850
Cdd:pfam15905 232 SCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQEL----SKQIKDLNEKCKLLESEKEELLREYEE------K 301
|
250 260 270
....*....|....*....|....*....|..
gi 1591544934 1851 FERRIKELsyqgEEDKKNLVRMQELIDKLQAK 1882
Cdd:pfam15905 302 EQTLNAEL----EELKEKLTLEEQEHQKLQQK 329
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1389-1568 |
5.63e-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: 40.90 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1389 QRTEELEESKKKLAVRLQEA--EEAVEASNAKCSSLEKTKHR----------LQTEIEDLVVDL----ERASAAAAALDK 1452
Cdd:pfam09787 14 QKAARILQSKEKLIASLKEGsgVEGLDSSTALTLELEELRQErdllreeiqkLRGQIQQLRTELqeleAQQQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1453 KQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELFKLKNSYEETLEHLETikrenknlqeEITDLSDQI---SQGAK 1529
Cdd:pfam09787 94 QLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREA----------EIEKLRNQLtskSQSSS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1591544934 1530 TIHELEK--------------MKKGLEIEKSEIQAALEEAEGTLEHEESKTLR 1568
Cdd:pfam09787 164 SQSELENrlhqltetliqkqtMLEALSTEKNSLVLQLERMEQQIKELQGEGSN 216
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
851-1052 |
6.45e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 851 AATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEI 930
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 931 MERLEDEEEMSATVLAKKRKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILKLTKEKkaLQEA 1010
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE--AEQA 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1591544934 1011 HQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKL 1052
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDS 226
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1261-1413 |
6.60e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1261 EDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREAtvsQLQRSKNsfsqnveelkkqleeeNKAKNALAHA 1340
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE---QLGNVRN----------------NKEYEALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1591544934 1341 LQSSRHDCDLLREQYDEEQEAKAELQRALSKANGEVAQWRTKYETDAIQRTEELEESKKKLAVRLQEAEEAVE 1413
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1603-1896 |
6.66e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 41.24 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1603 ESMQATLDAEAKSRSEAVRLRKKMEGDLNEM-----------EVQLNHANRLASESQKLLRNLQVQIKDVQLELD--ETI 1669
Cdd:pfam03528 4 EDLQQRVAELEKENAEFYRLKQQLEAEFNQKrakfkelylakEEDLKRQNAVLQEAQVELDALQNQLALARAEMEniKAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1670 HQNEELKEQVAVTERRNNLlASEVEELRALLEQNDRARKLAEHELLEatervnllhsQNTSLINQ-KKKLENDLSTLSNE 1748
Cdd:pfam03528 84 ATVSENTKQEAIDEVKSQW-QEEVASLQAIMKETVREYEVQFHRRLE----------QERAQWNQyRESAEREIADLRRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1749 VDDAVQEcRNAEEkakkaitdaammaeELKKEQDTSAHLERMKKNMEQTIKDLQMRLDEAEQialkggkkQVQKLEA-RV 1827
Cdd:pfam03528 153 LSEGQEE-ENLED--------------EMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAED--------KIKELEAsKM 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1591544934 1828 KELENELESEQKKSQEYQKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQAKVKSYKRQAEEAEDQ 1896
Cdd:pfam03528 210 KELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQ 278
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
854-1311 |
6.80e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 854 EKELASLKEELAKLKEALEKSEVKRKELEerqvsliQEKNDLSLQLQA---EQDNLADAEDRCDLLIKTKIQLEAKVKEI 930
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKSHSITL-------KEIERLSIEYNNamdDYNNLKSALNELSSLEDMKNRYESEIKTA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 931 MERLEDEEE---------------MSATVLAKKRKLED------------------------------ECAELKKDIDDL 965
Cdd:PRK01156 262 ESDLSMELEknnyykeleerhmkiINDPVYKNRNYINDyfkykndienkkqilsnidaeinkyhaiikKLSVLQKDYNDY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 966 EITLAKVEKEKH------ATENKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQV 1039
Cdd:PRK01156 342 IKKKSRYDDLNNqileleGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1040 DDLEGSLEQEKK-LRMDLERVKRKLE---------------GDLKlSMESVMDLENDKQQLEEKLKKKDFEMNEMSTRIE 1103
Cdd:PRK01156 422 SSKVSSLNQRIRaLRENLDELSRNMEmlngqsvcpvcgttlGEEK-SNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIV 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1104 DEQSLVNQLQK-----------KIKELQA-----RTEELEEELEADRACRAKVEKQRGDVARELEELSERLEESGGATSA 1167
Cdd:PRK01156 501 DLKKRKEYLESeeinksineynKIESARAdlediKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLI 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1168 QIEINKKRETDILKLRRDLEEAMLHHEATTAGLRKKHADSVAELSEQIDSLQRVKQKLEkersEAKMEVDDLASTVEQLS 1247
Cdd:PRK01156 581 DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQ----ENKILIEKLRGKIDNYK 656
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1591544934 1248 K---GKASAEKTCRLYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQR 1311
Cdd:PRK01156 657 KqiaEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINE 723
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
848-1086 |
6.82e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 41.38 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 848 LKSAATEKELASLKEELAK-----------LKEALEKSEvkrkelEERQVSLIQEKNDLSLQLQAEQDNLA----DAEDR 912
Cdd:PLN03229 479 VIAMGLQERLENLREEFSKansqdqlmhpvLMEKIEKLK------DEFNKRLSRAPNYLSLKYKLDMLNEFsrakALSEK 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 913 CDLLIKTKIQLEAKVKEIMERLEDEEEMSATvlakkrKLEDECAELKKDIDDLEITLAKVEKEKHATENKVKNLIEEMaA 992
Cdd:PLN03229 553 KSKAEKLKAEINKKFKEVMDRPEIKEKMEAL------KAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSM-G 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 993 LDETILKltkeKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEqEKKLRM-------DLERVK--RKL 1063
Cdd:PLN03229 626 LEVIGVT----KKNKDTAEQTPPPNLQEKIESLNEEINKKIERVIRSSDLKSKIE-LLKLEVakasktpDVTEKEkiEAL 700
|
250 260
....*....|....*....|...
gi 1591544934 1064 EGDLKLSMESVMDLENDKQQLEE 1086
Cdd:PLN03229 701 EQQIKQKIAEALNSSELKEKFEE 723
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1787-1905 |
7.02e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1787 LERMKK-NMEQTIKDLQMRLDEAE------QIALKGGKKQVQKLEARVKELENELESEQKKSQEYQkgvrkfeRRIKELS 1859
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEaersrlQALLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1591544934 1860 YQGEEDKKNLVRMQELIDKLQAKVKSYKRQAEE-------AEDQANTNLSKYR 1905
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADlgrrlnvALAQRVQELNRYR 196
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1569-1928 |
7.64e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1569 IQLELNQIKADVDRKLAEkeeeidnlrrnhqrTLESMQATLDAEAKSRSEAVRLRKkmegdlnemevqlnhANRLASESQ 1648
Cdd:PRK10929 28 ITQELEQAKAAKTPAQAE--------------IVEALQSALNWLEERKGSLERAKQ---------------YQQVIDNFP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1649 KLLRNLQVQIKDvqlELDE--TIHQN---EELKEQVAVTErrNNLLasevEELRALLEQNDRARklaehellEATERVNL 1723
Cdd:PRK10929 79 KLSAELRQQLNN---ERDEprSVPPNmstDALEQEILQVS--SQLL----EKSRQAQQEQDRAR--------EISDSLSQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1724 LHSQNTSLINQKKKLENDLSTLSN---EVDDAVQECRNAEEKAKKAITDaammaeELKkeqdtsahLERMKKNMEQTIKd 1800
Cdd:PRK10929 142 LPQQQTEARRQLNEIERRLQTLGTpntPLAQAQLTALQAESAALKALVD------ELE--------LAQLSANNRQELA- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1801 lQMRLDEAeqialkggKKQVQKLEARVKELENELeseqkKSQEYQKGVRKFErRIKELSYQGEEDKKNLVRM----QELI 1876
Cdd:PRK10929 207 -RLRSELA--------KKRSQQLDAYLQALRNQL-----NSQRQREAERALE-STELLAEQSGDLPKSIVAQfkinRELS 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1591544934 1877 DKL--QAK----VKSYKRQAEEAEDQANTNLSKYRKLQHELDDAEERADMAETQVTKL 1928
Cdd:PRK10929 272 QALnqQAQrmdlIASQQRQAASQTLQVRQALNTLREQSQWLGVSNALGEALRAQVARL 329
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
849-1091 |
7.74e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 849 KSAATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIK-------TKI 921
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEkvkelkeERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 922 QLEAKVKEIMERLEDEEEMSATVLAKKRKLEdecaELKKDIDDLEITL-----------------AKVEKEKHATE---- 980
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSID----KLRKEIERLEWRQqtevlspeeekelvekiKELEKELEKAKkale 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 981 --NKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEGSLEQE--------K 1050
Cdd:COG1340 158 knEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELheeiielqK 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1591544934 1051 KLRMDLERVKRKLEGDLKLSM-ESVMDLENDKQQLEEKLKKK 1091
Cdd:COG1340 238 ELRELRKELKKLRKKQRALKReKEKEELEEKAEEIFEKLKKG 279
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
980-1144 |
7.89e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 980 ENKVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDDLQAEED----KVNTLTKAQAKLEQQVDDLEGSLeqeKKLRMD 1055
Cdd:PHA02562 187 DMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKtikaEIEELTDELLNLVMDIEDPSAAL---NKLNTA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1056 LERVKRKLEgdlKLSMESVMDLEND-----KQQLEE------KLKKKDFEM----NEMSTRIEDEQSLVNQ---LQKKIK 1117
Cdd:PHA02562 264 AAKIKSKIE---QFQKVIKMYEKGGvcptcTQQISEgpdritKIKDKLKELqhslEKLDTAIDELEEIMDEfneQSKKLL 340
|
170 180
....*....|....*....|....*....
gi 1591544934 1118 ELQA--RTEELEEELEADRACRAKVEKQR 1144
Cdd:PHA02562 341 ELKNkiSTNKQSLITLVDKAKKVKAAIEE 369
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1167-1408 |
7.97e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1167 AQIEINKKRETDILKLRrdleeamlhHEATTAGLRKKHADSVAE------LSEQIDSLQRVKQKLEKERSEAKMEVDDLA 1240
Cdd:COG3206 125 KNLTVEPVKGSNVIEIS---------YTSPDPELAAAVANALAEayleqnLELRREEARKALEFLEEQLPELRKELEEAE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1241 STVEQLSKGKASAEktcrlYEDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSknsfsqnv 1320
Cdd:COG3206 196 AALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS-------- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1321 eelkkqlEEENKAKNALAhALQSSRhdcDLLREQYDEE----QEAKAELQRALSKANGEVAQWRTKYETD---AIQRTEE 1393
Cdd:COG3206 263 -------PVIQQLRAQLA-ELEAEL---AELSARYTPNhpdvIALRAQIAALRAQLQQEAQRILASLEAEleaLQAREAS 331
|
250
....*....|....*
gi 1591544934 1394 LEESKKKLAVRLQEA 1408
Cdd:COG3206 332 LQAQLAQLEARLAEL 346
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1213-1417 |
8.37e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1213 EQIDSLQRVKQK---LEKERSEAKMEVDDLASTVEQLSKGKASAEKTcRLyedqmneAKAKVEELQRQLNETNSHRARAQ 1289
Cdd:PRK11281 70 ALLDKIDRQKEEteqLKQQLAQAPAKLRQAQAELEALKDDNDEETRE-TL-------STLSLRQLESRLAQTLDQLQNAQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1290 AESSELSRKLEEREatvSQLQRSKNSFSQNVeelkKQLEEENKAKNALAHALQSSRHDcdlLREQYDEEQ---EAKAELQ 1366
Cdd:PRK11281 142 NDLAEYNSQLVSLQ---TQPERAQAALYANS----QRLQQIRNLLKGGKVGGKALRPS---QRVLLQAEQallNAQNDLQ 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1367 RALSKANG---EVAQWRTKYETDAIQRTEE----LEE--SKKKLAVRLQEAEEAVEASNA 1417
Cdd:PRK11281 212 RKSLEGNTqlqDLLQKQRDYLTARIQRLEHqlqlLQEaiNSKRLTLSEKTVQEAQSQDEA 271
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
854-1103 |
8.62e-03 |
|
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: 40.99 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 854 EKELASLKEELAKLKEALEKSEVK--RKELEERQVSLIQEKNDLSL------QLQAE-QDNLADAEDRCDLLIKTKIQLE 924
Cdd:pfam06160 152 EKQLAEIEEEFSQFEELTESGDYLeaREVLEKLEEETDALEELMEDipplyeELKTElPDQLEELKEGYREMEEEGYALE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 925 AKvkEIMERLEDEEEMSATVLAKKRKLEDECAE-----LKKDIDDLEITLAKVEKEKHATENKVKNLIEEMAALDETILK 999
Cdd:pfam06160 232 HL--NVDKEIQQLEEQLEENLALLENLELDEAEealeeIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1000 LTKEKKALQEAHQQTLDDLQaeedKVNTLTKAQAKLEQQVDDLEGSLEQEKK----LRMDLERVKRKLEG---DLKLSME 1072
Cdd:pfam06160 310 LKEELERVQQSYTLNENELE----RVRGLEKQLEELEKRYDEIVERLEEKEVayseLQEELEEILEQLEEieeEQEEFKE 385
|
250 260 270
....*....|....*....|....*....|.
gi 1591544934 1073 SVMDLENDKQQLEEKLKKKDFEMNEMSTRIE 1103
Cdd:pfam06160 386 SLQSLRKDELEAREKLDEFKLELREIKRLVE 416
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
839-1047 |
8.65e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 839 KLFFKIKPLLKSAATEKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKN------DLSLQLQAEQDNladaedr 912
Cdd:PRK05771 70 NPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIErlepwgNFDLDLSLLLGF------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 913 cdlliKTKIQLEAKV-KEIMERLEDEEEMSATVLAKKRKLEDECA--ELKKDIDDLEITLAKVEKEkhatenkvKNLIEE 989
Cdd:PRK05771 143 -----KYVSVFVGTVpEDKLEELKLESDVENVEYISTDKGYVYVVvvVLKELSDEVEEELKKLGFE--------RLELEE 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1591544934 990 MAALDETILKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAQ-AKLEQQVDDLEGSLE 1047
Cdd:PRK05771 210 EGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALyEYLEIELERAEALSK 268
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1261-1505 |
8.74e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.01 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1261 EDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREatvSQLQRSKNSFSQNVEelkkqleeenKAKNALAHA 1340
Cdd:pfam00261 7 KEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLE---EELERTEERLAEALE----------KLEEAEKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1341 LQSSRhDCDLLREQYDEEQEAKAELQRALSKAngevaqwrTKYETDAIQRTEELEESKKKLAVRLQEAEEAVEASNAKCS 1420
Cdd:pfam00261 74 DESER-GRKVLENRALKDEEKMEILEAQLKEA--------KEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1421 SLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQKCEECQAELETSQKESRSLSTELFKLKNSYEETL 1500
Cdd:pfam00261 145 ELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAIS 224
|
....*
gi 1591544934 1501 EHLET 1505
Cdd:pfam00261 225 EELDQ 229
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
868-1055 |
8.80e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 39.74 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 868 KEALEKSEVKRKELEERQvSLIQEKNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEIMERLEDE-EEMSATVLA 946
Cdd:cd00176 19 KEELLSSTDYGDDLESVE-ALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRwEELRELAEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 947 KKRKLED---------ECAELKKDIDDLEITLAKVEKEKHATEnkVKNLIEEMAALDETILKLTKEKKALQEAHQQTLDD 1017
Cdd:cd00176 98 RRQRLEEaldlqqffrDADDLEQWLEEKEAALASEDLGKDLES--VEELLKKHKELEEELEAHEPRLKSLNELAEELLEE 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 1591544934 1018 lqAEEDKVNTLTKAQAKLEQQVDDLEGSLEQEKKLRMD 1055
Cdd:cd00176 176 --GHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
854-1038 |
9.05e-03 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 39.94 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 854 EKELASLKEELAKLKEALEKSEVKRKELEERQVSLIQEKNDLSLQLQAEQDNLADAEDRCDLLiktkiqleAKVKEIMER 933
Cdd:pfam15934 50 LKEFTVQNQRLACQIDNLHETLKDRDHQIKQLQSMITGYSDISENNRLKEEIHDLKQKNCVQA--------RVVRKMGLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 934 LEDEEEMSATVLAKKRKL----EDECAELK---KDIDDLEITLAKVEKEKHATENKVKNLIEEMAALdetilkltKEKKA 1006
Cdd:pfam15934 122 LKGQEEQRVELCDKYESLlgsfEEQCQELKranRRVQSLQTRLSQVEKLQEELRTERKILREEVIAL--------KEKDA 193
|
170 180 190
....*....|....*....|....*....|....*..
gi 1591544934 1007 LQEAHQQTLDD----LQAEEDKVNTLT-KAQAKLEQQ 1038
Cdd:pfam15934 194 KSNGRERALQDqlkcCQTEIEKSRTLIrNMQSHLQLE 230
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1707-1913 |
9.35e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1707 RKLAEhELLEaterVNLLHSQNTSLINQKKKLENDLSTLSNEVDDAVQECR-------NAEEKAKKAITD-AAMMAEELK 1778
Cdd:PHA02562 153 RKLVE-DLLD----ISVLSEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKtynknieEQRKKNGENIARkQNKYDELVE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1779 KEQDTSAHLERMK---KNMEQTIKDLQMRLDE--AEQIALKGGKKQVQKLE-------------ARVKELENELESEQKK 1840
Cdd:PHA02562 228 EAKTIKAEIEELTdelLNLVMDIEDPSAALNKlnTAAAKIKSKIEQFQKVIkmyekggvcptctQQISEGPDRITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1841 SQEYQKGVRKFERRIKELSYQGEEDKKNLVRMQELIDKLQ----------AKVKSYKRQAEEAEDQANTNLSKYRKLQHE 1910
Cdd:PHA02562 308 LKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKIStnkqslitlvDKAKKVKAAIEELQAEFVDNAEELAKLQDE 387
|
...
gi 1591544934 1911 LDD 1913
Cdd:PHA02562 388 LDK 390
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
867-1099 |
9.53e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 41.07 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 867 LKEALEKSEVKRKELEERQVSLIQE---KNDLSLQLQAEQDNLADAEDRCDLLIKTKIQLEAKVKEIM-ERLEDEEEMSA 942
Cdd:PLN03188 1045 PEKKLEQERLRWTEAESKWISLAEElrtELDASRALAEKQKHELDTEKRCAEELKEAMQMAMEGHARMlEQYADLEEKHI 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 943 TVLAKKRKLEDECAELKKD-------------IDDL--EITLAKVEKEKHAT----ENK-----VKNLIEEMAALDETIL 998
Cdd:PLN03188 1125 QLLARHRRIQEGIDDVKKAaaragvrgaeskfINALaaEISALKVEREKERRylrdENKslqaqLRDTAEAVQAAGELLV 1204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 999 KLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAQAKLEQQVDDLEgslEQEKKLRMDLERVKRKLEGDLKLSMESVMDLE 1078
Cdd:PLN03188 1205 RLKEAEEALTVAQKRAMDAEQEAAEAYKQIDKLKRKHENEISTLN---QLVAESRLPKEAIRPACNDDCMAKYDAGEPLS 1281
|
250 260
....*....|....*....|....*
gi 1591544934 1079 NDKQQLEEKL----KKKDFEMNEMS 1099
Cdd:PLN03188 1282 EGDQQWREEFepfyKKEDGELSKLA 1306
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1261-1466 |
9.57e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1261 EDQMNEAKAKVEELQRQLNETNSHRARAQAESSELSRKLEEREATVSQLQRSKNSFSQNVEELKKQLEEENKAKNALAHA 1340
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1591544934 1341 LQSSRHDCDLL---------------REQYDEEQEAKAELQRALSKANGEVAQwrtkYETDAIQRTEELEESKKKLAVRL 1405
Cdd:COG3883 95 LYRSGGSVSYLdvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEA----KKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1591544934 1406 QEAEEAVEASNAKCSSLEKTKHRLQTEIEDLVVDLERASAAAAALDKKQRNFDKVLAEWRQ 1466
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| |
