|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
97-763 |
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: 1350.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVACAVKKKDEEasDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGK 256
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKES--GKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 257 IAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEAFD 336
Cdd:cd01377 159 IAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 337 ILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNM 416
Cdd:cd01377 239 ILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 417 NQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILE 496
Cdd:cd01377 319 EQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 497 QEEYKKEGIAWEFIDFGMDLQMCIDLIEKP-MGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTKPgkptRPNQGP 575
Cdd:cd01377 399 QEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKP----KPKKSE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 576 AHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKGKSSAFQTISAVHRESLNK 655
Cdd:cd01377 475 AHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGSFRTVSQLHKEQLNK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 656 LMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIPQGFVDG 735
Cdd:cd01377 555 LMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFDDG 634
|
650 660
....*....|....*....|....*...
gi 127773 736 KTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd01377 635 KAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
78-775 |
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: 1047.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 78 NPPKFEKLEDMANMTYLNEASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVAD 157
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 158 NAYQNMVTDRENQSCLITGESGAGKTENTKKVIMYLAKVAcavkkkdeeASDKKEGSLEDQIIQANPVLEAYGNAKTTRN 237
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVS---------GSNTEVGSVEDQILESNPILEAFGNAKTLRN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 238 NNSSRFGKFIRIHFGPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSgLYSFINQG-C 316
Cdd:smart00242 152 NNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPE-DYRYLNQGgC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 317 LTVDNIDDVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQA-ESDGTAEAEKVAFLCGINAGDLL 395
Cdd:smart00242 231 LTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 396 KALLKPKVKVGTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQL 475
Cdd:smart00242 311 KALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 476 CINYTNERLQQFFNHHMFILEQEEYKKEGIAWEFIDFGmDLQMCIDLIE-KPMGILSILEEECMFPKADDKSFQDKLYQN 554
Cdd:smart00242 391 CINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLNQH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 555 HmGKNRMFTKPgkptrPNQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFkaPEEPAgggkk 634
Cdd:smart00242 470 H-KKHPHFSKP-----KKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLF--PSGVS----- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 635 KKGKSSAFQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYS 714
Cdd:smart00242 537 NAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFD 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 127773 715 EFKQRYSILAPNAIPQGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFKAGVLGNLEEMRD 775
Cdd:smart00242 617 EFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
86-763 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1007.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 86 EDMANMTYLNEASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVT 165
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 166 DRENQSCLITGESGAGKTENTKKVIMYLAKVAcavkkkdEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGK 245
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVS-------GSGSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 246 FIRIHFGPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVT-PDSglYSFINQ-GCLTVDNID 323
Cdd:pfam00063 155 YIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTnPKD--YHYLSQsGCYTIDGID 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 324 DVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKV 403
Cdd:pfam00063 233 DSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 404 KVGTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKA-KRNYYIGVLDIAGFEIFDFNSFEQLCINYTNE 482
Cdd:pfam00063 313 KTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVNE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 483 RLQQFFNHHMFILEQEEYKKEGIAWEFIDFGmDLQMCIDLIE-KPMGILSILEEECMFPKADDKSFQDKLYQNHmGKNRM 561
Cdd:pfam00063 393 KLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 562 FTKPgkptrPNQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKGK--- 638
Cdd:pfam00063 471 FQKP-----RLQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKstp 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 639 ----SSAFQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYS 714
Cdd:pfam00063 546 krtkKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 127773 715 EFKQRYSILAPNAIPQGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:pfam00063 626 EFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
97-763 |
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: 987.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVAC---AVKKKDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGP 253
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAAlgdGPGKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 254 TGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDE 333
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 334 AFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKG 413
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 414 QNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMF 493
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 494 ILEQEEYKKEGIAWEFIDFGMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTKPgKPTRPNQ 573
Cdd:cd14927 401 ILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKP-RPDKKRK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 574 GPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFK------APEEPAGGGKKKKGKSSAFQTISA 647
Cdd:cd14927 480 YEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYEnyvgsdSTEDPKSGVKEKRKKAASFQTVSQ 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 648 VHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNA 727
Cdd:cd14927 560 LHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSA 639
|
650 660 670
....*....|....*....|....*....|....*..
gi 127773 728 IPQ-GFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14927 640 IPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
97-763 |
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: 986.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVACAVKKKDEEasdKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGK 256
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAA---KSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 257 IAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEAFD 336
Cdd:cd14909 158 LAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 337 ILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNM 416
Cdd:cd14909 238 ILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 417 NQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILE 496
Cdd:cd14909 318 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 497 QEEYKKEGIAWEFIDFGMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTKPgKPTRPNQGPA 576
Cdd:cd14909 398 QEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKP-KPPKPGQQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 577 HFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFK----APEEPAGGGKKKKGKSSAFQTISAVHRES 652
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAdhagQSGGGEQAKGGRGKKGGGFATVSSAYKEQ 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 653 LNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIpQGF 732
Cdd:cd14909 557 LNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGI-QGE 635
|
650 660 670
....*....|....*....|....*....|.
gi 127773 733 VDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14909 636 EDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
98-763 |
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: 958.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 98 SVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITGE 177
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 178 SGAGKTENTKKVIMYLAKVACAVKKKDEEASdKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGKI 257
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKKKDS-KMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 258 AGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEAFDI 337
Cdd:cd14913 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 338 LGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNMN 417
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 418 QVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILEQ 497
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 498 EEYKKEGIAWEFIDFGMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTKPgKPTRpNQGPAH 577
Cdd:cd14913 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKP-KVVK-GRAEAH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 578 FELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAEL---FKAPEEPAGGGKKKKGKSSAFQTISAVHRESLN 654
Cdd:cd14913 479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLyatFATADADSGKKKVAKKKGSSFQTVSALFRENLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 655 KLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIPQG-FV 733
Cdd:cd14913 559 KLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGqFI 638
|
650 660 670
....*....|....*....|....*....|
gi 127773 734 DGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14913 639 DSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
97-763 |
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: 937.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVACAVKkkdeEASDKKeGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGK 256
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGK----QSSDGK-GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 257 IAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEAFD 336
Cdd:cd14934 156 LAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 337 ILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNM 416
Cdd:cd14934 236 VLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 417 NQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILE 496
Cdd:cd14934 316 EQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 497 QEEYKKEGIAWEFIDFGMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTKPgKPTRPNQGPA 576
Cdd:cd14934 396 QEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKP-KGGKGKGPEA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 577 HFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKapEEPAGGGKKKKGKSSAFQTISAVHRESLNKL 656
Cdd:cd14934 475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFK--EEEAPAGSKKQKRGSSFMTVSNFYREQLNKL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 657 MKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIPQGFVDGK 736
Cdd:cd14934 553 MTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGFVDNK 632
|
650 660
....*....|....*....|....*..
gi 127773 737 TVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14934 633 KASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
98-763 |
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: 904.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 98 SVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITGE 177
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 178 SGAGKTENTKKVIMYLAKVAcAVKKKDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGKI 257
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIA-AIGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 258 AGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEAFDI 337
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 338 LGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNMN 417
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 418 QVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILEQ 497
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 498 EEYKKEGIAWEFIDFGMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTKP----GKPTrpnq 573
Cdd:cd14917 401 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPrnikGKPE---- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 574 gpAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELF---KAPEEPAGGGKKKKGKSSAFQTISAVHR 650
Cdd:cd14917 477 --AHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFanyAGADAPIEKGKGKAKKGSSFQTVSALHR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 651 ESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIPQ 730
Cdd:cd14917 555 ENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPE 634
|
650 660 670
....*....|....*....|....*....|....
gi 127773 731 G-FVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14917 635 GqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
97-763 |
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: 890.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVACAVKKKdeeasdKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGK 256
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESK------KKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 257 IAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAiPELNDVMLVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEAFD 336
Cdd:cd14929 155 LSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGK-KELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 337 ILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNM 416
Cdd:cd14929 234 ILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 417 NQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILE 496
Cdd:cd14929 314 EQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 497 QEEYKKEGIAWEFIDFGMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTKPGKPTRPNQgpA 576
Cdd:cd14929 394 QEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFE--A 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 577 HFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFK---APEEPAGGGKKKKGKSSAFQTISAVHRESL 653
Cdd:cd14929 472 HFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEnyiSTDSAIQFGEKKRKKGASFQTVASLHKENL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 654 NKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIPQG-F 732
Cdd:cd14929 552 NKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSkF 631
|
650 660 670
....*....|....*....|....*....|.
gi 127773 733 VDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14929 632 VSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
33-1597 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 887.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 33 NCWVPDEKEGFASAEIQSSKGDEITVKIVADSSTR---TVKKDDIQS--MNPPKFEKLEDMANMTYLNEASVLYNLRSRY 107
Cdd:COG5022 11 GCWIPDEEKGWIWAEIIKEAFNKGKVTEEGKKEDGesvSVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPAVLHNLEKRY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 108 TSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITGESGAGKTENTK 187
Cdd:COG5022 91 NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 188 KVIMYLAKVacavkkkdEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGKIAGADIETYLL 267
Cdd:COG5022 171 RIMQYLASV--------TSSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 268 EKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVT-PDSglYSFINQG-CLTVDNIDDVEEFKLCDEAFDILGFTKEEK 345
Cdd:COG5022 243 EKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQnPKD--YIYLSQGgCDKIDGIDDAKEFKITLDALKTIGIDEEEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 346 QSMFKCTASILHMGEMKFKQRpREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNMNQVVNSVGA 425
Cdd:COG5022 321 DQIFKILAAILHIGNIEFKED-RNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 426 LAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILEQEEYKKEGI 505
Cdd:COG5022 400 LAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 506 AWEFIDFgMDLQMCIDLIEK--PMGILSILEEECMFPKADDKSFQDKLYQN-HMGKNRMFTKpgkptrPNQGPAHFELHH 582
Cdd:COG5022 480 EWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKK------SRFRDNKFVVKH 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 583 YAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEpagggkkkKGKSSAFQTISAVHRESLNKLMKNLYS 662
Cdd:COG5022 553 YAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEEN--------IESKGRFPTLGSRFKESLNSLMSTLNS 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 663 THPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIPQG----FVDGKTV 738
Cdd:COG5022 625 TQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGeytwKEDTKNA 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 739 SEKILAGLQMDPAEYRLGTTKVFFKAGVLGNLEEMRDERLSKIISMFQAHIRGYLIRKAY-KKLQDQRiglsVIQRNIRK 817
Cdd:COG5022 705 VKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYlQALKRIK----KIQVIQHG 780
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 818 WLVLRN---WQWWKLYSKVKPLLSIARQEEEMKEQLKQMdkmkEDLAKTERIKKELEEQNVTLLEQKNDLFLQlqtledS 894
Cdd:COG5022 781 FRLRRLvdyELKWRLFIKLQPLLSLLGSRKEYRSYLACI----IKLQKTIKREKKLRETEEVEFSLKAEVLIQ------K 850
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 895 MGDQEERVEKLIMqkadfesqikeleerlldeedaaadlegikkkmeadnanLKKDIGDLENtlqKAEQDKAHKdnQIST 974
Cdd:COG5022 851 FGRSLKAKKRFSL---------------------------------------LKKETIYLQS---AQRVELAER--QLQE 886
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 975 LQGEISQQDE-HIGKLNKEKKALeEANKKTSDSLQAEedkCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAK-RKV 1052
Cdd:COG5022 887 LKIDVKSISSlKLVNLELESEII-ELKKSLSSDLIEN---LEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKlHEV 962
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1053 EQDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELqarieeleeeleaernarakveKQ 1132
Cdd:COG5022 963 ESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQL----------------------KE 1020
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1133 RAELNRELEELGERLDEAGGatsaqielNKKREAELLKIRRDLEEASLQHEAQISALRKKHQDAANeMADQVDQLQKVKS 1212
Cdd:COG5022 1021 LPVEVAELQSASKIISSEST--------ELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLL-DDKQLYQLESTEN 1091
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1213 KlekdkkdlkremddlesqmthnmknkgcsEKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQ----L 1288
Cdd:COG5022 1092 L-----------------------------LKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQlvntL 1142
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1289 EDAEHRVSVLSKEKSQLSSQLEDARRS--------LEEETRARSKLQNEVRNMHADMDAIREQLEEE-QESKSDVQRQLS 1359
Cdd:COG5022 1143 EPVFQKLSVLQLELDGLFWEANLEALPspppfaalSEKRLYQSALYDEKSKLSSSEVNDLKNELIALfSKIFSGWPRGDK 1222
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1360 KANNEIQQWRSKFESEGANRTEELED--------QKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDR 1431
Cdd:COG5022 1223 LKKLISEGWVPTEYSTSLKGFNNLNKkfdtpasmSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVGLFNALR 1302
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1432 ANASVNQMEKKQRafdkttaewqakVNSLQSELENSQKESrgysaELYRIKASIEEYQDS--IGALRRENKNLADEIHDL 1509
Cdd:COG5022 1303 TKASSLRWKSATE------------VNYNSEELDDWCREF-----EISDVDEELEELIQAvkVLQLLKDDLNKLDELLDA 1365
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1510 TDQLSEGgrstheldkARRRLemeKEELQAALEEAEgaLEQEEAKVMRAQleiatvrneidkRIQEKEEEFDNTRRNHQR 1589
Cdd:COG5022 1366 CYSLNPA---------EIQNL---KSRYDPADKENN--LPKEILKKIEAL------------LIKQELQLSLEGKDETEV 1419
|
....*...
gi 127773 1590 ALESMQAS 1597
Cdd:COG5022 1420 HLSEIFSE 1427
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
98-763 |
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: 884.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 98 SVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITGE 177
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 178 SGAGKTENTKKVIMYLAKVACAVKKKDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGKI 257
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 258 AGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEAFDI 337
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 338 LGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNMN 417
Cdd:cd14916 242 LGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 418 QVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILEQ 497
Cdd:cd14916 322 QVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 498 EEYKKEGIAWEFIDFGMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTKPGKPTRPNQgpAH 577
Cdd:cd14916 402 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQE--AH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 578 FELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFK----APEEPAGGGKKKKGKSSAFQTISAVHRESL 653
Cdd:cd14916 480 FSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFStyasADTGDSGKGKGGKKKGSSFQTVSALHRENL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 654 NKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIPQG-F 732
Cdd:cd14916 560 NKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqF 639
|
650 660 670
....*....|....*....|....*....|.
gi 127773 733 VDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14916 640 IDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
98-763 |
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: 884.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 98 SVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITGE 177
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 178 SGAGKTENTKKVIMYLAKVACAVKKKDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGKI 257
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 258 AGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEAFDI 337
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAIDI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 338 LGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNMN 417
Cdd:cd14923 242 LGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 418 QVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILEQ 497
Cdd:cd14923 322 QVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 498 EEYKKEGIAWEFIDFGMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTKPgKPTRpNQGPAH 577
Cdd:cd14923 402 EEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKP-KPAK-GKAEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 578 FELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFK-----APEEPAGGGKKKKGKSSAFQTISAVHRES 652
Cdd:cd14923 480 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSnyagaEAGDSGGSKKGGKKKGSSFQTVSAVFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 653 LNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIPQG- 731
Cdd:cd14923 560 LNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGq 639
|
650 660 670
....*....|....*....|....*....|..
gi 127773 732 FVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14923 640 FIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
98-763 |
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: 882.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 98 SVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITGE 177
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 178 SGAGKTENTKKVIMYLAKVACAVKKKDEEA-SDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGK 256
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAaSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 257 IAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEAFD 336
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 337 ILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNM 416
Cdd:cd14915 242 ILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 417 NQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILE 496
Cdd:cd14915 322 QQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 497 QEEYKKEGIAWEFIDFGMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTKPgKPTRpNQGPA 576
Cdd:cd14915 402 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKP-KPAK-GKAEA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 577 HFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFK----APEEPAGGGKKKKGKSSAFQTISAVHRES 652
Cdd:cd14915 480 HFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSggqtAEAEGGGGKKGGKKKGSSFQTVSALFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 653 LNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIPQG- 731
Cdd:cd14915 560 LNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGq 639
|
650 660 670
....*....|....*....|....*....|..
gi 127773 732 FVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14915 640 FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
98-763 |
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: 879.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 98 SVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITGE 177
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 178 SGAGKTENTKKVIMYLAKVAC-AVKKKDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGK 256
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVtGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 257 IAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEAFD 336
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 337 ILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNM 416
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 417 NQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILE 496
Cdd:cd14910 322 QQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 497 QEEYKKEGIAWEFIDFGMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTKPgKPTRpNQGPA 576
Cdd:cd14910 402 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKP-KPAK-GKVEA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 577 HFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFK----APEEPAGGGKKKKGKSSAFQTISAVHRES 652
Cdd:cd14910 480 HFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSgaaaAEAEEGGGKKGGKKKGSSFQTVSALFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 653 LNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIPQG- 731
Cdd:cd14910 560 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGq 639
|
650 660 670
....*....|....*....|....*....|..
gi 127773 732 FVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14910 640 FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
99-763 |
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: 879.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 99 VLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITGES 178
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 179 GAGKTENTKKVIMYLAKVACAVKKKDEEaSDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGKIA 258
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEE-SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 259 GADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEAFDIL 338
Cdd:cd14918 162 SADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 339 GFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNMNQ 418
Cdd:cd14918 242 GFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 419 VVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILEQE 498
Cdd:cd14918 322 VYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 499 EYKKEGIAWEFIDFGMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTKPgkPTRPNQGPAHF 578
Cdd:cd14918 402 EYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKP--KVVKGKAEAHF 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 579 ELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFK---APEEPAGGGKKKKGKSSAFQTISAVHRESLNK 655
Cdd:cd14918 480 SLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFStyaSAEADSGAKKGAKKKGSSFQTVSALFRENLNK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 656 LMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIPQG-FVD 734
Cdd:cd14918 560 LMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGqFID 639
|
650 660
....*....|....*....|....*....
gi 127773 735 GKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14918 640 SKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
98-763 |
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: 869.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 98 SVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITGE 177
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 178 SGAGKTENTKKVIMYLAKVACAVKKKDEE-ASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGK 256
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEiTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 257 IAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEAFD 336
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 337 ILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNM 416
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 417 NQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILE 496
Cdd:cd14912 322 EQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 497 QEEYKKEGIAWEFIDFGMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTKPgkPTRPNQGPA 576
Cdd:cd14912 402 QEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKP--KVVKGKAEA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 577 HFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEP------AGGGKKKKGKSSAFQTISAVHR 650
Cdd:cd14912 480 HFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAegasagGGAKKGGKKKGSSFQTVSALFR 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 651 ESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIPQ 730
Cdd:cd14912 560 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 639
|
650 660 670
....*....|....*....|....*....|....
gi 127773 731 G-FVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14912 640 GqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
97-763 |
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: 864.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGK-RKTEIPPHLFSVADNAYQNMVTDRENQSCLIT 175
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKgRSADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 176 GESGAGKTENTKKVIMYLAKVACAVKKKdeeaSDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTG 255
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSK----SSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 256 KIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGLYSFIN----QGCLTVDNIDDVEEFKLC 331
Cdd:cd00124 157 RLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDylnsSGCDRIDGVDDAEEFQEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 332 DEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREE--QAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEM 409
Cdd:cd00124 237 LDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGET 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 410 VTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRN--YYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQF 487
Cdd:cd00124 317 ITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 488 FNHHMFILEQEEYKKEGIAWEFIDFgMDLQMCIDLIE-KPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTKPG 566
Cdd:cd00124 397 FNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 567 KptrpnqGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGAskeplvaelfkapeepagggkkkkgkssafqtiS 646
Cdd:cd00124 476 K------AKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS---------------------------------G 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 647 AVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPN 726
Cdd:cd00124 517 SQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPG 596
|
650 660 670
....*....|....*....|....*....|....*..
gi 127773 727 AIPQGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd00124 597 ATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
97-763 |
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: 793.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVACAVKK------KDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIH 250
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPKgsgavpHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 251 FGPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTpDSGLYSFINQGCLTVDNIDDVEEFKL 330
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 331 CDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMV 410
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 411 TKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLD-TKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFN 489
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 490 HHMFILEQEEYKKEGIAWEFIDFGMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMgknrmfTKPGKPT 569
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 570 RPNQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFK-------APEEPAGGGKKKKGKSSAF 642
Cdd:cd14911 474 TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKdaeivgmAQQALTDTQFGARTRKGMF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 643 QTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSI 722
Cdd:cd14911 554 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 127773 723 LAPNAIPQGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14911 634 LTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
97-763 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 764.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVACAVKKKDEEASdkkEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGK 256
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNI---PGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 257 IAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPEL-NDVMLVTPDSglYSFINQGCLTVDNIDDVEEFKLCDEAF 335
Cdd:cd14920 158 IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFNN--YRFLSNGYIPIPGQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 336 DILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQN 415
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 416 MNQVVNSVGALAKSLYDRMFNWLVRRVNKTLD-TKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFI 494
Cdd:cd14920 316 KEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 495 LEQEEYKKEGIAWEFIDFGMDLQMCIDLIEKPM---GILSILEEECMFPKADDKSFQDKLYQnHMGKNRMFTKPGKPtrp 571
Cdd:cd14920 396 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQ-EQGSHSKFQKPRQL--- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 572 nQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKGKSSA---------- 641
Cdd:cd14920 472 -KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAfgsayktkkg 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 642 -FQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRY 720
Cdd:cd14920 551 mFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 127773 721 SILAPNAIPQGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14920 631 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
97-763 |
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: 713.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVACAVK-KKDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTG 255
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKtKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 256 KIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDvMLVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEAF 335
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRS-ELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 336 DILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQN 415
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 416 MNQVVNSVGALAKSLYDRMFNWLVRRVNKTLD-TKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFI 494
Cdd:cd14932 320 QEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 495 LEQEEYKKEGIAWEFIDFGMDLQMCIDLIEKPM---GILSILEEECMFPKADDKSFQDKLYQnHMGKNRMFTKPGKPtrp 571
Cdd:cd14932 400 LEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQ-EQGNNPKFQKPKKL--- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 572 nQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKGKSSA---------- 641
Cdd:cd14932 476 -KDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLhgafktrkgm 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 642 FQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYS 721
Cdd:cd14932 555 FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 634
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 127773 722 ILAPNAIPQGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14932 635 ILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
98-763 |
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: 695.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 98 SVLYNLRSRYTSG-LIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVacavkkkdeEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGK 256
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATV---------GGSSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 257 IAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNA-IPELNDVMLVTPDSglYSFINQG-CLTVDNIDDVEEFKLCDEA 334
Cdd:cd01380 153 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKELHLGSAED--FFYTNQGgSPVIDGVDDAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 335 FDILGFTKEEKQSMFKCTASILHMGEMKFKQRpREEQAESDGTAEAEKVAF-LCGINAGDLLKALLKPKVKVGTEMVTKG 413
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKAT-RNDSASISPDDEHLQIACeLLGIDESQLAKWLCKRKIVTRSEVIVKP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 414 QNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDT--KAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHH 491
Cdd:cd01380 310 LTLQQAIVARDALAKHIYAQLFDWIVDRINKALASpvKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 492 MFILEQEEYKKEGIAWEFIDFgMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTKpgKPTRP 571
Cdd:cd01380 390 VFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKHFK--KPRFS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 572 NQGpahFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKeplvaelFKAPeepagggkkkkgkssafqTISAVHRE 651
Cdd:cd01380 467 NTA---FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASK-------NRKK------------------TVGSQFRD 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 652 SLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIPQG 731
Cdd:cd01380 519 SLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLR 598
|
650 660 670
....*....|....*....|....*....|..
gi 127773 732 fVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd01380 599 -DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
97-763 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 691.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVACAVK-KKDEEASdkkeGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTG 255
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKgKKDTSIT----GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 256 KIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTpDSGLYSFINQGCLTVDNIDDVEEFKLCDEAF 335
Cdd:cd14921 157 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLE-GFNNYTFLSNGFVPIPAAQDDEMFQETLEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 336 DILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQN 415
Cdd:cd14921 236 SIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 416 MNQVVNSVGALAKSLYDRMFNWLVRRVNKTLD-TKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFI 494
Cdd:cd14921 316 KEQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 495 LEQEEYKKEGIAWEFIDFGMDLQMCIDLIEKPM---GILSILEEECMFPKADDKSFQDKLYQNHmGKNRMFTKPgkptRP 571
Cdd:cd14921 396 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKP----KQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 572 NQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFK-----------APEEPAGGGKKKKGKSS 640
Cdd:cd14921 471 LKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKdvdrivgldqmAKMTESSLPSASKTKKG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 641 AFQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRY 720
Cdd:cd14921 551 MFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 127773 721 SILAPNAIPQGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14921 631 EILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
97-763 |
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: 671.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVACAVK-KKDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTG 255
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKtKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 256 KIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTpDSGLYSFINQGCLTVDNIDDVEEFKLCDEAF 335
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLE-NYNNYRFLSNGNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 336 DILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQN 415
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 416 MNQVVNSVGALAKSLYDRMFNWLVRRVNKTLD-TKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFI 494
Cdd:cd15896 320 QEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 495 LEQEEYKKEGIAWEFIDFGMDLQMCIDLIEKPM---GILSILEEECMFPKADDKSFQDKLYQNHmGKNRMFTKPGKPtrp 571
Cdd:cd15896 400 LEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKPKKL--- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 572 nQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEE---------PAGGGKKKKGKSSAF 642
Cdd:cd15896 476 -KDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRivgldkvsgMSEMPGAFKTRKGMF 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 643 QTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSI 722
Cdd:cd15896 555 RTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 634
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 127773 723 LAPNAIPQGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd15896 635 LTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
97-763 |
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: 669.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVACAVKKKdeeasdKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGK 256
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSK------KDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 257 IAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGlYSFINQGCLTVDNIDDVEEFKLCDEAFD 336
Cdd:cd14919 155 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNK-YRFLSNGHVTIPGQQDKDMFQETMEAMR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 337 ILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNM 416
Cdd:cd14919 234 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 417 NQVVNSVGALAKSLYDRMFNWLVRRVNKTLD-TKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFIL 495
Cdd:cd14919 314 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 496 EQEEYKKEGIAWEFIDFGMDLQMCIDLIEKPM---GILSILEEECMFPKADDKSFQDKLYQNHmGKNRMFTKPgkptRPN 572
Cdd:cd14919 394 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKP----KQL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 573 QGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKGKSSA----------- 641
Cdd:cd14919 469 KDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETAlpgafktrkgm 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 642 FQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYS 721
Cdd:cd14919 549 FRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYE 628
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 127773 722 ILAPNAIPQGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14919 629 ILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
97-763 |
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: 669.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVACAVKKKDEEASdkkEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGK 256
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGV---PGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 257 IAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGlYSFINQGCLTVDNiDDVEEFKLCDEAFD 336
Cdd:cd14930 158 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 337 ILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNM 416
Cdd:cd14930 236 VLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 417 NQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRN-YYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFIL 495
Cdd:cd14930 316 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 496 EQEEYKKEGIAWEFIDFGMDLQMCIDLIEKPM---GILSILEEECMFPKADDKSFQDKLYQNHmGKNRMFTKPgkptRPN 572
Cdd:cd14930 396 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRP----RHL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 573 QGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKG---------KSSAFQ 643
Cdd:cd14930 471 RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLgdgppggrpRRGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 644 TISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSIL 723
Cdd:cd14930 551 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 127773 724 APNAIPQGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14930 631 TPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
97-763 |
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: 656.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVacavkkkdeeaSDKKEgSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGK 256
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAI-----------SGQHS-WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 257 IAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTpDSGLYSFINQG-CLTVDNIDDVEEFKLCDEAF 335
Cdd:cd01381 149 IEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELG-DASDYYYLTQGnCLTCEGRDDAAEFADIRSAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 336 DILGFTKEEKQSMFKCTASILHMGEMKFKQRPRE--EQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKG 413
Cdd:cd01381 228 KVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 414 QNMNQVVNSVGALAKSLYDRMFNWLVRRVNKT----LDTKAKRNyYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFN 489
Cdd:cd01381 308 LSAEQALDVRDAFVKGIYGRLFIWIVNKINSAiykpRGTDSSRT-SIGVLDIFGFENFEVNSFEQLCINFANENLQQFFV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 490 HHMFILEQEEYKKEGIAWEFIDFgMDLQMCIDLI-EKPMGILSILEEECMFPKADDKSFQDKLYQNHmGKNRMFTKPgkp 568
Cdd:cd01381 387 RHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKP--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 569 trPNQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFkapeepAGGGKKKKGKSSAFQTISAV 648
Cdd:cd01381 462 --KSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF------NEDISMGSETRKKSPTLSSQ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 649 HRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAI 728
Cdd:cd01381 534 FRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIP 613
|
650 660 670
....*....|....*....|....*....|....*
gi 127773 729 PQGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd01381 614 PAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
98-763 |
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: 653.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 98 SVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITGE 177
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 178 SGAGKTENTKKVIMYLakvaCAVKKKDEEAsdkkegslEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGKI 257
Cdd:cd14883 82 SGAGKTETTKLILQYL----CAVTNNHSWV--------EQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 258 AGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAI--PEL-NDVMLVTPDSglYSFINQ-GCLTVDNIDDVEEFKLCDE 333
Cdd:cd14883 150 KGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELkEKLKLGEPED--YHYLNQsGCIRIDNINDKKDFDHLRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 334 AFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAE-SDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTK 412
Cdd:cd14883 228 AMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 413 GQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHM 492
Cdd:cd14883 308 PLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 493 FILEQEEYKKEGIAWEFIDFgMDLQMCIDLIEK-PMGILSILEEECMFPKADDKSFQDKLYQNHmGKNRMFTKPGKPTRP 571
Cdd:cd14883 388 FKLEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPDRRRWK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 572 NQgpahFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKGKSSAFQ-------- 643
Cdd:cd14883 466 TE----FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLGGDTTSrgtskgkp 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 644 TISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSIL 723
Cdd:cd14883 542 TVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCL 621
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 127773 724 APNAIPQGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14883 622 DPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
98-763 |
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: 651.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 98 SVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITGE 177
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 178 SGAGKTENTKKVIMYLAKVacavkkkdeeaSDKKEGSLE---DQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPT 254
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV-----------SGGSESEVErvkDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 255 GKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEA 334
Cdd:cd01378 151 GEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 335 FDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDgTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEM---VT 411
Cdd:cd01378 231 MKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 412 KGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTK-AKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFfnh 490
Cdd:cd01378 310 VPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKsGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQI--- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 491 hmFIL-----EQEEYKKEGIAWEFIDFgMDLQMCIDLIE-KPMGILSILEEECMFP-KADDKSFQDKLYQNHmGKNRMFT 563
Cdd:cd01378 387 --FIEltlkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKLNQLF-SNHPHFE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 564 KPgkPTRPNQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKapeEPAGGGKKKKGKSSAFQ 643
Cdd:cd01378 463 CP--SGHFELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFP---EGVDLDSKKRPPTAGTK 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 644 TisavhRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSIL 723
Cdd:cd01378 538 F-----KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLL 612
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 127773 724 APNAIPQGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd01378 613 SPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
97-763 |
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: 649.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLP-IYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLIT 175
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 176 GESGAGKTENTKKVIMYLAKVAcavKKKDEEASdkkegSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTG 255
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG---GRAVTEGR-----SVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 256 KIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPElnDVM---LVTPDSglYSFINQ-GCLTVDNIDDVEEFKLC 331
Cdd:cd01384 153 RISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPE--DREkykLKDPKQ--FHYLNQsKCFELDGVDDAEEYRAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 332 DEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAES-DGTAE--AEKVAFLCGINAGDLLKALLKPKVKVGTE 408
Cdd:cd01384 229 RRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPkDEKSEfhLKAAAELLMCDEKALEDALCKRVIVTPDG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 409 MVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFF 488
Cdd:cd01384 309 IITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 489 NHHMFILEQEEYKKEGIAWEFIDFgMDLQMCIDLIE-KPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRmFTKPgK 567
Cdd:cd01384 389 NQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKR-FSKP-K 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 568 PTRPNqgpahFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFkaPEEPAgggkKKKGKSSAFQTISA 647
Cdd:cd01384 466 LSRTD-----FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF--PPLPR----EGTSSSSKFSSIGS 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 648 VHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNA 727
Cdd:cd01384 535 RFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEV 614
|
650 660 670
....*....|....*....|....*....|....*.
gi 127773 728 iPQGFVDGKTVSEKILAglQMDPAEYRLGTTKVFFK 763
Cdd:cd01384 615 -LKGSDDEKAACKKILE--KAGLKGYQIGKTKVFLR 647
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
98-763 |
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: 648.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 98 SVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTeiPPHLFSVADNAYQNMVTDRENQSCLITGE 177
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLD--SPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 178 SGAGKTENTKKVIMYLAKVACAVkkkdeeasdkkeGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGKI 257
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGS------------SGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 258 AGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDvMLVTPDSGLYSFINQ-GCLTVDNIDDVEEFKLCDEAFD 336
Cdd:cd01383 148 CGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALRE-KLNLKSASEYKYLNQsNCLTIDGVDDAKKFHELKEALD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 337 ILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNM 416
Cdd:cd01383 227 TVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 417 NQVVNSVGALAKSLYDRMFNWLVRRVNKTLDT-KAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFIL 495
Cdd:cd01383 307 QQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 496 EQEEYKKEGIAWEFIDFgMDLQMCIDLIE-KPMGILSILEEECMFPKADDKSFQDKLYQnHMGKNRMFTKpgkptrpNQG 574
Cdd:cd01383 387 EQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKLKQ-HLKSNSCFKG-------ERG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 575 PAhFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVaELFKAPEEPAGGGKKKKGKSSAF----QTISAVHR 650
Cdd:cd01383 458 GA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLP-QLFASKMLDASRKALPLTKASGSdsqkQSVATKFK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 651 ESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAP-NAIP 729
Cdd:cd01383 536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPeDVSA 615
|
650 660 670
....*....|....*....|....*....|....
gi 127773 730 QGfvDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd01383 616 SQ--DPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
97-763 |
0e+00 |
|
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: 571.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVAcavkkkdeeASDkkeGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGK 256
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVA---------GST---NGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 257 IAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMlvtPDSGLYSFINQ-GCLTVDNIDDVEEFKLCDEAF 335
Cdd:cd14872 149 ICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGW---GSSAAYGYLSLsGCIEVEGVDDVADFEEVVLAM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 336 DILGFTKEEKQSMFKCTASILHMGEMKFKqrprEEQAESDGTA-------EAEKVAFLCGINAGDLLKALlkpkvkVGTE 408
Cdd:cd14872 226 EQLGFDDADINNVMSLIAAILKLGNIEFA----SGGGKSLVSGstvanrdVLKEVATLLGVDAATLEEAL------TSRL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 409 MVTKGQNMN-------QVVNSVGALAKSLYDRMFNWLVRRVNKTLD-TKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYT 480
Cdd:cd14872 296 MEIKGCDPTripltpaQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 481 NERLQQFFNHHMFILEQEEYKKEGIAWEFIDFgMDLQMCIDLIEK-PMGILSILEEECMFPKADDKSFQDKLYQNHmGKN 559
Cdd:cd14872 376 NEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTH-AAK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 560 RMFTKPGKPTRpnqgPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKaPEEPAGGGKKKkgks 639
Cdd:cd14872 454 STFVYAEVRTS----RTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFP-PSEGDQKTSKV---- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 640 safqTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQR 719
Cdd:cd14872 525 ----TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKR 600
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 127773 720 YSILaPNAIPQGF-VDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14872 601 YRFL-VKTIAKRVgPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
97-763 |
1.07e-180 |
|
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: 562.25 E-value: 1.07e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLP-IYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLIT 175
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 176 GESGAGKTENTKKVIMYLAkvacavkkkdeEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTG 255
Cdd:cd01382 81 GESGAGKTESTKYILRYLT-----------ESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 256 KIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPdsglysfinqgcltvdNIDDVEEFKLCDEAF 335
Cdd:cd01382 150 SVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDP----------------LLDDVGDFIRMDKAM 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 336 DILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEK----VAFLCGINAGDLLKALLKpKVKVGTEMVT 411
Cdd:cd01382 214 KKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKSEQsleyAAELLGLDQDELRVSLTT-RVMQTTRGGA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 412 KGQ------NMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKaKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQ 485
Cdd:cd01382 293 KGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFE-TSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 486 QFFNHHMFILEQEEYKKEGIAWEFIDFgMDLQMCIDLIE-KPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRM--- 561
Cdd:cd01382 372 QFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLsip 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 562 ---FTKPGKPTRPNQGpahFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKGK 638
Cdd:cd01382 451 rksKLKIHRNLRDDEG---FLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDSKQKAGK 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 639 SSaFQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQ 718
Cdd:cd01382 528 LS-FISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYN 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 127773 719 RYSILAPNAIPQgfVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd01382 607 MYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
97-763 |
6.14e-175 |
|
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: 547.04 E-value: 6.14e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVAcavkkkdeeasDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFgPTGK 256
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN-----------QRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 257 IAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVM-LVTPDSglYSFINQG--ClTVDNIDDVEEFKLCDE 333
Cdd:cd01387 149 IVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYgLQEAEK--YFYLNQGgnC-EIAGKSDADDFRRLLA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 334 AFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPRE---EQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMV 410
Cdd:cd01387 226 AMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 411 TKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNH 490
Cdd:cd01387 306 FTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 491 HMFILEQEEYKKEGIAWEFIDFgMDLQMCIDLI-EKPMGILSILEEECMFPKADDKSFQDKLYQNHmGKNRMFtkpgkpT 569
Cdd:cd01387 386 HVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELY------S 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 570 RPNQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKaPEEPAGGGKKKKGKSSAF------- 642
Cdd:cd01387 458 KPRMPLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFS-SHRAQTDKAPPRLGKGRFvtmkprt 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 643 QTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSI 722
Cdd:cd01387 537 PTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRC 616
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 127773 723 LAPNAIPQGfVDGKTVSEKILAGLQMDP-AEYRLGTTKVFFK 763
Cdd:cd01387 617 LVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
98-763 |
8.60e-173 |
|
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: 540.33 E-value: 8.60e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 98 SVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITGE 177
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 178 SGAGKTENTKKVIMYLAKVACAVKKkdeeasdkkegSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGKI 257
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKANNR-----------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 258 AGADIETYLLEKSRVTYQQSAERNYHIFYQICS--NAIPELNDVMLvtPDSGLYSFINQGCLTVDNIDD----VEEFKLC 331
Cdd:cd01379 151 TGARISEYLLEKSRVVHQAIGERNFHIFYYIYAglAEDKKLAKYKL--PENKPPRYLQNDGLTVQDIVNnsgnREKFEEI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 332 DEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESD----GTAEAEKVAFLCGINAGDLLKALLKPKVKVGT 407
Cdd:cd01379 229 EQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQTDKSsrisNPEALNNVAKLLGIEADELQEALTSHSVVTRG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 408 EMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTL--DTKAK-RNYYIGVLDIAGFEIFDFNSFEQLCINYTNERL 484
Cdd:cd01379 309 ETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASdEPLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 485 QQFFNHHMFILEQEEYKKEGIAWEFIDFGMD---LQMcidLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRM 561
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYEDNrplLDM---FLQKPMGLLALLDEESRFPKATDQTLVEKFHNNIKSKYYW 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 562 ftkpgkptRPNQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAelfkapeepagggkkkkgkssa 641
Cdd:cd01379 466 --------RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR---------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 642 fQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYS 721
Cdd:cd01379 516 -QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYY 594
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 127773 722 ILAPNAiPQGFVDGKTVSEKILAGLQMDpaEYRLGTTKVFFK 763
Cdd:cd01379 595 FLAFKW-NEEVVANRENCRLILERLKLD--NWALGKTKVFLK 633
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
97-763 |
9.94e-173 |
|
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: 541.21 E-value: 9.94e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLP-IYTDSVIAKYRGKRKTEiPPHLFSVADNAYQNMVTDRENQSCLIT 175
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFIQPSISK-SPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 176 GESGAGKTENTKKVIMYLAkvaCAvkkkdeEASDKKEGSL-EDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHF--- 251
Cdd:cd14888 80 GESGAGKTESTKYVMKFLA---CA------GSEDIKKRSLvEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFskl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 252 ------GPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNA--------IPELNDVML---------VTPDSGL 308
Cdd:cd14888 151 kskrmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAreakntglSYEENDEKLakgadakpiSIDMSSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 309 YSFIN------QGCLTVDNIDDVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFK-QRPREEQA--ESDGTAE 379
Cdd:cd14888 231 EPHLKfryltkSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEnNEACSEGAvvSASCTDD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 380 AEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLD-TKAKRNYYIGV 458
Cdd:cd14888 311 LEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 459 LDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILEQEEYKKEGIAWEFIDFGmDLQMCIDLI-EKPMGILSILEEEC 537
Cdd:cd14888 391 LDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEEC 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 538 MFPKADDKSFQDKLYQNHMGKNRMftKPGKpTRPNQgpahFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPL 617
Cdd:cd14888 470 FVPGGKDQGLCNKLCQKHKGHKRF--DVVK-TDPNS----FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPF 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 618 VAELFKApeePAGGGKKKKGKSSAFQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVL 697
Cdd:cd14888 543 ISNLFSA---YLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVL 619
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 127773 698 EGIRICRKGFPSRLIYSEFKQRYSILAPnaiPQGfvdgkTVSEKILAglqmdpaeyrLGTTKVFFK 763
Cdd:cd14888 620 QAVQVSRAGYPVRLSHAEFYNDYRILLN---GEG-----KKQLSIWA----------VGKTLCFFK 667
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
97-763 |
7.69e-171 |
|
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: 535.88 E-value: 7.69e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEI---PPHLFSVADNAYQNMVTDR----EN 169
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 170 QSCLITGESGAGKTENTKKVIMYLAKVACAVKkkDEEASDKKEG---SLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKF 246
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAK--GASTSKGAANaheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 247 IRIHFGPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSnAIPELNDVMLVTPDSGLYSFINQG-CLTVDNIDDV 325
Cdd:cd14892 159 IQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLA-GLDANENAALELTPAESFLFLNQGnCVEVDGVDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 326 EEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQR--PREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPkv 403
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENadDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVTQ-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 404 kvgTEMVTKGQNM------NQVVNSVGALAKSLYDRMFNWLVRRVNK----------TLDTKAKRNYYIGVLDIAGFEIF 467
Cdd:cd14892 316 ---TTSTARGSVLeikltaREAKNALDALCKYLYGELFDWLISRINAchkqqtsgvtGGAASPTFSPFIGILDIFGFEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 468 DFNSFEQLCINYTNERLQQFFNHHMFILEQEEYKKEGIAWEFIDFgMDLQMCIDLIEK-PMGILSILEEECMFP-KADDK 545
Cdd:cd14892 393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 546 SFQDKLYQNHMGKNRMFTKpgkptrPNQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEplvaelfkap 625
Cdd:cd14892 472 QLLTIYHQTHLDKHPHYAK------PRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK---------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 626 eepagggkkkkgkssafqtisavHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRK 705
Cdd:cd14892 536 -----------------------FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRRE 592
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 127773 706 GFPSRLIYSEFKQRYSILAPN-----AIPQ---GFVDGKTVSEKILAGLqmDPAEYRLGTTKVFFK 763
Cdd:cd14892 593 GFPIRRQFEEFYEKFWPLARNkagvaASPDacdATTARKKCEEIVARAL--ERENFQLGRTKVFLR 656
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
97-763 |
4.12e-168 |
|
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: 528.58 E-value: 4.12e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLP-IYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLIT 175
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 176 GESGAGKTENTKKVIMYLAKVAcavkkkdeeasdkkeGSLED----QIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHF 251
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA---------------GGLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 252 GPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDvMLVTPDSGLYSFINQgCLTVDNIDDVEEFKLC 331
Cdd:cd14903 146 DKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERL-FLDSANECAYTGANK-TIKIEGMSDRKHFART 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 332 DEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAE--SDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEM 409
Cdd:cd14903 224 KEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 410 VTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFN 489
Cdd:cd14903 304 YTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 490 HHMFILEQEEYKKEGIAWEFIDFgMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTKPgKPT 569
Cdd:cd14903 384 QDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFP-RTS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 570 RpnqgpAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKGKSSAFQTISAVH 649
Cdd:cd14903 462 R-----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGALT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 650 --------RESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYS 721
Cdd:cd14903 537 tttvgtqfKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFW 616
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 127773 722 ILAPNAiPQGFVDGKTVSEKILAGLQMD-PAEYRLGTTKVFFK 763
Cdd:cd14903 617 LFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
97-763 |
6.18e-168 |
|
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: 528.19 E-value: 6.18e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLP-IYTDSVIAKYRGKRKTEIPPHLFSVADNAY----QNMVTDRENQS 171
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtqliQSGVLDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 172 CLITGESGAGKTENTKKVIMYLAKV-------ACAVKKKDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFG 244
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARItsgfaqgASGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 245 KFIRIHFGPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPEL-NDVMLVTPDSGLYSFINqgCLTVDNID 323
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALrERLKLQTPVEYFYLRGE--CSSIPSCD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 324 DVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEA-EKVAFLCGINAGDLLKALLKPK 402
Cdd:cd14890 239 DAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTLQSlKLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 403 VKVGTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNE 482
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 483 RLQQFFNHHMFILEQEEYKKEGIAWEFIDFgMDLQMCIDLIE-KPMGILSILE--EECMFPKAD--DKSFQDKLYQNHMG 557
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgKVNGKPGIFItlDDCWRFKGEeaNKKFVSQLHASFGR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 558 KNRMFTKPGKPTR------PNQGPA-HFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAelfkapeepag 630
Cdd:cd14890 478 KSGSGGTRRGSSQhphfvhPKFDADkQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSIRE----------- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 631 ggkkkkgkssafQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSR 710
Cdd:cd14890 547 ------------VSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALR 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 127773 711 LIYSEFKQRYSILAPNAipqgfVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14890 615 EEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
97-763 |
2.22e-167 |
|
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: 527.71 E-value: 2.22e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVacavkkkdeeaSDKKEGS-LEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTG 255
Cdd:cd01385 81 ESGSGKTESTNFLLHHLTAL-----------SQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 256 KIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAiPELNDVM--LVTPDSglYSFINQ-GCLTVDNIDDVEEFKLCD 332
Cdd:cd01385 150 MVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGA-SEEERKElhLKQPED--YHYLNQsDCYTLEGEDEKYEFERLK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 333 EAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRP--REEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMV 410
Cdd:cd01385 227 QAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyhRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 411 TKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTL----DTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQ 486
Cdd:cd01385 307 ILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 487 FFNHHMFILEQEEYKKEGIAWEFIDFgMDLQMCIDLIE-KPMGILSILEEECMFPKADDKSFQDKLYQNHmGKNRMFTKP 565
Cdd:cd01385 387 YFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAKFKQQH-KDNKYYEKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 566 gkptrPNQGPAhFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAEL-----------------FKA---- 624
Cdd:cd01385 465 -----QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrwavlrafFRAmaaf 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 625 ---------PEEPAGGGKKKKGKSSAF--------QTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELV 687
Cdd:cd01385 539 reagrrraqRTAGHSLTLHDRTTKSLLhlhkkkkpPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELV 618
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 688 LHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAP-NAIPQgfvdgKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd01385 619 LRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPkGLISS-----KEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
841-1920 |
8.20e-167 |
|
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: 539.38 E-value: 8.20e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 841 RQEEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQIKELE 920
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 921 ERLLDEEDAAADLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALEEAN 1000
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1001 KKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRK 1080
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1081 EAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGATSAQIEL 1160
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1161 NKKREAELLKIRRDLEEASLQHEAQISALRKKHQDAANEMADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTHNMKNKG 1240
Cdd:pfam01576 322 RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1241 CSEKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEET 1320
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEET 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1321 RARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEGANrTEELEDQKRKLLGKLSEAEQT 1400
Cdd:pfam01576 482 RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT-LEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1401 TEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYR 1480
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1481 IKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQL 1560
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1561 EIATVRNEIDKRIQEKEEEFDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDINELEVALDASNRGKAEMEKTV 1640
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1641 KRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNELTSQVSSV 1720
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1721 QGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEAS 1800
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1801 SLKGGKKMIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVE 1880
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|
gi 127773 1881 EAEEIAAINLAKYRKAQHELEEAEERADTADSTLQKFRAK 1920
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
97-761 |
4.24e-164 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 517.42 E-value: 4.24e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKY------RGKRKTEIPPHLFSVADNAYQNMVTDRE-- 168
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 169 --NQSCLITGESGAGKTENTKKVIMYLAKVACAVKKKDEEASdkkEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKF 246
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATE---RENVRDRVLESNPILEAFGNARTNRNNNSSRFGKF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 247 IRIHFGPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIP-ELNDVMLVtpDSGLYSFINQG-CLT-VDNID 323
Cdd:cd14901 158 IRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSdELHALGLT--HVEEYKYLNSSqCYDrRDGVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 324 DVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREeqAESDGTAEAEKVAFLC---GINAGDLLKALLK 400
Cdd:cd14901 236 DSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGE--GGTFSMSSLANVRAACdllGLDMDVLEKTLCT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 401 PKVKVGTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTL--DTKAKRNYYIGVLDIAGFEIFDFNSFEQLCIN 478
Cdd:cd14901 314 REIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaySESTGASRFIGIVDIFGFEIFATNSLEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 479 YTNERLQQFFNHHMFILEQEEYKKEGIAWEFIDFGMDlQMCIDLIE-KPMGILSILEEECMFPKADDKSFQDKLYQNhMG 557
Cdd:cd14901 394 FANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 558 KNRMFTKpgkpTRPNQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAelfkapeepagggkkkkg 637
Cdd:cd14901 472 KHASFSV----SKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS------------------ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 638 kssafQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFK 717
Cdd:cd14901 530 -----STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFV 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 127773 718 QRYSILAPN-AIPQGFVDGKTVSEKILAGLQM----DPAEYRLGTTKVF 761
Cdd:cd14901 605 HTYSCLAPDgASDTWKVNELAERLMSQLQHSElnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
97-763 |
8.43e-158 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 500.09 E-value: 8.43e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLP-IYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLIT 175
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 176 GESGAGKTENTKKVIMYLAKVAcavKKKDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTG 255
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVIS---QQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 256 KIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTpDSGLYSFINQ-GCLTVDNIDDVEEFKLCDEA 334
Cdd:cd14873 158 NIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLNQsGCVEDKTISDQESFREVITA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 335 FDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAekvAFLCGINAGDLLKALLKPKVKVGTEMVTKGQ 414
Cdd:cd14873 237 MEVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTALGRS---AELLGLDPTQLTDALTQRSMFLRGEEILTPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 415 NMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLdtKAKRNY-YIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMF 493
Cdd:cd14873 314 NVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFkSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 494 ILEQEEYKKEGIAWEFIDFgMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHmGKNRMFTKPGKPTRpnq 573
Cdd:cd14873 392 SLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPRVAVN--- 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 574 gpaHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKGKSSAFQTISAVHRESL 653
Cdd:cd14873 467 ---NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRRPTVSSQFKDSL 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 654 NKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIPQGFV 733
Cdd:cd14873 544 HSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDV 623
|
650 660 670
....*....|....*....|....*....|
gi 127773 734 DGKtvSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14873 624 RGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
97-763 |
1.51e-152 |
|
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: 484.96 E-value: 1.51e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKR-KTEIPPHLFSVADNAYQNMVTDRENQSCLIT 175
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 176 GESGAGKTENTKKVIMYLAKVacavkkkdeeaSDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTG 255
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKL-----------SPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 256 KIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPE-LNDVMLVTPDSglYSFINQGCLTVDNIDDVEEF----KL 330
Cdd:cd14897 150 QLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDrLLYYFLEDPDC--HRILRDDNRNRPVFNDSEELeyyrQM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 331 CDEAFDIL---GFTKEEKQSMFKCTASILHMGEMKFkqrprEEQAESDG-----TAEAEKVAFLCGINAGDLLKALLKPK 402
Cdd:cd14897 228 FHDLTNIMkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGvtvadEYPLHAVAKLLGIDEVELTEALISNV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 403 VKVGTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTK-----AKRNYYIGVLDIAGFEIFDFNSFEQLCI 477
Cdd:cd14897 303 NTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDkdfqiMTRGPSIGILDMSGFENFKINSFDQLCI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 478 NYTNERLQQFFNHHMFILEQEEYKKEGIAWEFIDFgMDLQMCIDLI-EKPMGILSILEEECMFPKADDKSFQDKLyQNHM 556
Cdd:cd14897 383 NLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYC 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 557 GKNRMFTKPgkptrPNQGPAhFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFkapeepagggkkkk 636
Cdd:cd14897 461 GESPRYVAS-----PGNRVA-FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF-------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 637 gkSSAFQtisavhrESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEF 716
Cdd:cd14897 521 --TSYFK-------RSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDF 591
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 127773 717 KQRYSILAPNAiPQGFVDGKTVSEKILAGLQMDpaEYRLGTTKVFFK 763
Cdd:cd14897 592 VKRYKEICDFS-NKVRSDDLGKCQKILKTAGIK--GYQFGKTKVFLK 635
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
97-726 |
1.05e-150 |
|
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: 481.45 E-value: 1.05e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLP-IYTDSVIAKYRGKRK--------TEIPPHLFSVADNAYQNMVTDR 167
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIqngeyfdiKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 168 ENQSCLITGESGAGKTENTKKVIMYLAKVACAVKKKDE--------EASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNN 239
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEvltltssiRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 240 SSRFGKFIRIHFG-PTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPE-LNDVMLVTPDSGL-YSFINQG- 315
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQlLQQLGLKNQLSGDrYDYLKKSn 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 316 CLTVDNIDDVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRP--REEQAESDGTAEAEKVAFLCGINAGD 393
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 394 LLKALLKPKVKVGTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYY--------IGVLDIAGFE 465
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDEKDQQlfqnkylsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 466 IFDFNSFEQLCINYTNERLQQFFNHHMFILEQEEYKKEGIAWEF--IDFgMDLQMCIDLIEK-PMGILSILEEECMFPKA 542
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 543 DDKSFQDKLYQNHmGKNRMFTKPGKPTRPNqgpahFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELF 622
Cdd:cd14907 480 TDEKLLNKIKKQH-KNNSKLIFPNKINKDT-----FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 623 KAPEEPAGGGKKKKGKSSA-FQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIR 701
Cdd:cd14907 554 SGEDGSQQQNQSKQKKSQKkDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIR 633
|
650 660
....*....|....*....|....*
gi 127773 702 ICRKGFPSRLIYSEFKQRYSILAPN 726
Cdd:cd14907 634 VRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
97-763 |
1.42e-150 |
|
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: 479.93 E-value: 1.42e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNL--RSRYTSGLIYTYSGLFCIAVNPYRRLPiytDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRE---NQS 171
Cdd:cd14891 1 AGILHNLeeRSKLDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 172 CLITGESGAGKTENTKKVIMYL---AKVACAVKKKDEEASDKKEG----SLEDQIIQANPVLEAYGNAKTTRNNNSSRFG 244
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLttrAVGGKKASGQDIEQSSKKRKlsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 245 KFIRIHFGPTG-KIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGlYSFINQ-GCLTVDNI 322
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPED-FIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 323 DDVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREE-----QAESDGTAEAeKVAFLCGINAGDLLKA 397
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeiASESDKEALA-TAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 398 LLKPKVKVGTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFD-FNSFEQLC 476
Cdd:cd14891 316 ITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 477 INYTNERLQQFFNHHMFILEQEEYKKEGI-----AWEfidfgmDLQMCIDLI-EKPMGILSILEEECMFPKADDKSFQDK 550
Cdd:cd14891 396 INYANEALQATFNQQVFIAEQELYKSEGIdvgviTWP------DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNET 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 551 LYQNHmGKNRMFTKPgkptRPNQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKeplvaelfkapeepag 630
Cdd:cd14891 470 LHKTH-KRHPCFPRP----HPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSA---------------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 631 ggkkkkgkssAFQtisavhrESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSR 710
Cdd:cd14891 529 ----------KFS-------DQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTR 591
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 127773 711 LIYSEFKQRYSILAPNAIPQGFVD-GKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14891 592 VTYAELVDVYKPVLPPSVTRLFAEnDRTLTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
99-763 |
2.41e-146 |
|
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: 469.00 E-value: 2.41e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 99 VLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMV----TDRENQSCLI 174
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 175 TGESGAGKTENTKKVIMYLAKVAcavkkkdeeasdKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFgPT 254
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC------------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 255 GKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTpDSGLYSFINQGcltVDNIDDVEEFK----- 329
Cdd:cd14889 150 GHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLL-DPGKYRYLNNG---AGCKREVQYWKkkyde 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 330 LCDeAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREE-QAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTE 408
Cdd:cd14889 226 VCN-AMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 409 MVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNY---YIGVLDIAGFEIFDFNSFEQLCINYTNERLQ 485
Cdd:cd14889 305 QIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVelrEIGILDIFGFENFAVNRFEQACINLANEQLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 486 QFFNHHMFILEQEEYKKEGIAWEFIDFgMDLQMCIDL-IEKPMGILSILEEECMFPKADDKSFQDKLyQNHMGKNRMFTK 564
Cdd:cd14889 385 YFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYGK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 565 PGKPTRPnqgpahFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKA---------PEEPAGGGKKK 635
Cdd:cd14889 463 SRSKSPK------FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTAtrsrtgtlmPRAKLPQAGSD 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 636 KGKSSAFQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSE 715
Cdd:cd14889 537 NFNSTRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAE 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 127773 716 FKQRYSILAPNAipqgfvDGKTVSEKILAGLQ-MDPAEYRLGTTKVFFK 763
Cdd:cd14889 617 FAERYKILLCEP------ALPGTKQSCLRILKaTKLVGWKCGKTRLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
98-724 |
1.00e-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: 455.15 E-value: 1.00e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 98 SVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLP-IYTDSVIAKY-----------RGKRKTEIPPHLFSVADNAYQNMV- 164
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMMl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 165 ---TDRENQSCLITGESGAGKTENTKKVIMYLAKVAcAVKKKDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSS 241
Cdd:cd14900 82 glnGVMSDQSILVSGESGSGKTESTKFLMEYLAQAG-DNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 242 RFGKFIRIHFGPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPElndvmlvtpdsglysfinqgCLTVDN 321
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEA--------------------ARKRDM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 322 iddveeFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGT-------AEAEKVAFLCGINAGDL 394
Cdd:cd14900 221 ------YRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSdlapssiWSRDAAATLLSVDATKL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 395 LKALLKPKVKVGTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRN-----YYIGVLDIAGFEIFDF 469
Cdd:cd14900 295 EKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKshgglHFIGILDIFGFEVFPK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 470 NSFEQLCINYTNERLQQFFNHHMFILEQEEYKKEGIAWEFIDFgMDLQMCIDLI-EKPMGILSILEEECMFPKADDKSFQ 548
Cdd:cd14900 375 NSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 549 DKLYQnHMGKNRMFTKpgkpTRPNQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLgaskepLVAELFKapeep 628
Cdd:cd14900 454 SKLYR-ACGSHPRFSA----SRIQRARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLF------VYGLQFK----- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 629 agggkkkkgkssafqtisavhrESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFP 708
Cdd:cd14900 518 ----------------------EQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFP 575
|
650
....*....|....*.
gi 127773 709 SRLIYSEFKQRYSILA 724
Cdd:cd14900 576 IRLLHDEFVARYFSLA 591
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
49-820 |
3.01e-138 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 452.18 E-value: 3.01e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 49 QSSKGDEITVKIV--ADSSTRTVKKDDIQSMNPP-KFEKLEDMANMTYLNEASVLYNLRSRYTSGLIYTYSGLFCIAVNP 125
Cdd:PTZ00014 59 PGSTGEKLTLKQIdpPTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 126 YRRLPIYTDSVIAKYRGKRKTEI-PPHLFSVADNAYQNMVTDRENQSCLITGESGAGKTENTKKVIMYLAkvacavkkkd 204
Cdd:PTZ00014 139 FKDLGNTTNDWIRRYRDAKDSDKlPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA---------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 205 eeASDKKEGSLEDQ--IIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGKIAGADIETYLLEKSRVTYQQSAERNY 282
Cdd:PTZ00014 209 --SSKSGNMDLKIQnaIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSY 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 283 HIFYQICSNAIPELNDVMLVTPDSGlYSFINQGCLTVDNIDDVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMK 362
Cdd:PTZ00014 287 HIFYQLLKGANDEMKEKYKLKSLEE-YKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 363 FKqrPREEQAESDGTA---EAEKV----AFLCGINAGDLLKALLKPKVKVGTEMVTKGQNMNQVVNSVGALAKSLYDRMF 435
Cdd:PTZ00014 366 IE--GKEEGGLTDAAAisdESLEVfneaCELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLF 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 436 NWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILEQEEYKKEGIAWEFIDFGMD 515
Cdd:PTZ00014 444 LWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSN 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 516 LQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHmgKNRMFTKPGKptrpNQGPAHFELHHYAGNVPYSITGWL 595
Cdd:PTZ00014 524 ESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNL--KNNPKYKPAK----VDSNKNFVIKHTIGDIQYCASGFL 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 596 EKNKDPINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKGKSSAFQtisavhrESLNKLMKNLYSTHPHFVRCIIPNE 675
Cdd:PTZ00014 598 FKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLAKGQLIGSQFL-------NQLDSLMSLINSTEPHFIRCIKPNE 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 676 LKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIPQGFVDGKTVSEKILAGLQMDPAEYRL 755
Cdd:PTZ00014 671 NKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAI 750
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127773 756 GTTKVFFKAGVLGNLEEMRDERLSK---IISMFQAHIRGYLIRKAYKK-LQDqrigLSVIQRNIRKWLV 820
Cdd:PTZ00014 751 GKTMVFLKKDAAKELTQIQREKLAAwepLVSVLEALILKIKKKRKVRKnIKS----LVRIQAHLRRHLV 815
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
97-725 |
1.34e-136 |
|
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: 442.81 E-value: 1.34e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYR--GKRKTE-------IPPHLFSVADNAYQNMVTD- 166
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 167 RENQSCLITGESGAGKTENTKKVIMYLAKVACAVKKKDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKF 246
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 247 IRIHFGPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPE------LNDVMLVTPD-SGLYSFINQG-CLT 318
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEehekyeFHDGITGGLQlPNEFHYTGQGgAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 319 VDNIDDVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAE---KVAFLCGINAGDLL 395
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKclaRVAKLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 396 KALLKPKVKVGTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNY--YIGVLDIAGFEIFDFNSFE 473
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrsSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 474 QLCINYTNERLQQFFNHHMFILEQEEYKKEGIAWEFIDFGmDLQMCIDLIE-KPMGILSILEEECMFP-KADDKSFQDKL 551
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 552 YQNHM-GKNRMFTKPGK--PTRPNQGPAHFELHHYAGNVPYSI-TGWLEKNKDPInenvvallgaskePLVAE-LFKAPE 626
Cdd:cd14908 480 YETYLpEKNQTHSENTRfeATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEI-------------PLTADsLFESGQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 627 EpagggkkkkgkssafqtisavHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKG 706
Cdd:cd14908 547 Q---------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSG 605
|
650
....*....|....*....
gi 127773 707 FPSRLIYSEFKQRYSILAP 725
Cdd:cd14908 606 YPVRLPHKDFFKRYRMLLP 624
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
97-763 |
1.64e-136 |
|
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: 441.30 E-value: 1.64e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLP-IYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLIT 175
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 176 GESGAGKTENTKKVIMYLAKVACAVKKKDEeasdkkegsleDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTG 255
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTI-----------AKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 256 KIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNA-IPELNDVMLVTPDSGLYSFINQGCLTVDNIDDVEEFKLCDEA 334
Cdd:cd14904 150 KLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLsSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 335 FDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAeAEKVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQ 414
Cdd:cd14904 230 LSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQ-LSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 415 NMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNY-YIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMF 493
Cdd:cd14904 309 APVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 494 ILEQEEYKKEGIAWEFIDFgMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNH--MGKNRMFTKPgKPTRp 571
Cdd:cd14904 389 KTVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFP-KVKR- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 572 nqgpAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKGKS-SAFQTISAVHR 650
Cdd:cd14904 466 ----TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEGKSGKGtKAPKSLGSQFK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 651 ESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIPQ 730
Cdd:cd14904 542 TSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHS 621
|
650 660 670
....*....|....*....|....*....|...
gi 127773 731 GFVDgKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14904 622 KDVR-RTCSVFMTAIGRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
97-725 |
1.16e-131 |
|
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: 430.08 E-value: 1.16e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLP-IYTDSVIAKYR--------GKRKTEIPPHLFSVADNAYQNMV-TD 166
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 167 RENQSCLITGESGAGKTENTKKVIMYLAKVACAVKKKDEEASDKKEgsLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKF 246
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAVE--IGKRILQTNPILESFGNAQTIRNDNSSRFGKF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 247 IRIHFGPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVmLVTPDSGLYSFINQ-GC----LTVDN 321
Cdd:cd14902 159 IKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDL-LGLQKGGKYELLNSyGPsfarKRAVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 322 IDDVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEA---EKVAFLCGINAGDLLKAL 398
Cdd:cd14902 238 DKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLETLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 399 LKPKVKVGTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYY---------IGVLDIAGFEIFDF 469
Cdd:cd14902 318 SSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGFESLNR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 470 NSFEQLCINYTNERLQQFFNHHMFILEQEEYKKEGIAWEFIDFGMDLQmCIDLIE-KPMGILSILEEECMFPKADDKSFQ 548
Cdd:cd14902 398 NGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAA-CLALFDdKSNGLFSLLDQECLMPKGSNQALS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 549 DKLYQNHMGKNRmftkpgkptrpnqgpahFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEP 628
Cdd:cd14902 477 TKFYRYHGGLGQ-----------------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRD 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 629 AGGGKKKKGKSSAFQT-----ISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRIC 703
Cdd:cd14902 540 SPGADNGAAGRRRYSMlrapsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIA 619
|
650 660
....*....|....*....|..
gi 127773 704 RKGFPSRLIYSEFKQRYSILAP 725
Cdd:cd14902 620 RHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
103-763 |
2.33e-129 |
|
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: 423.21 E-value: 2.33e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 103 LRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDsvIAKYRGKRK--TEIPPHLFSVADNAYQNMVT-------DRENQSCL 173
Cdd:cd14895 7 LAQRYGVDQVYCRSGAVLIAVNPFKHIPGLYD--LHKYREEMPgwTALPPHVFSIAEGAYRSLRRrlhepgaSKKNQTIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 174 ITGESGAGKTENTKKVIMYLAKVAcaVKKKDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGP 253
Cdd:cd14895 85 VSGESGAGKTETTKFIMNYLAESS--KHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVRMFFEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 254 -----TGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPE-LNDVMLVTPDSGLYSFINQGCLTV--DNIDDV 325
Cdd:cd14895 163 heldtSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmKLELQLELLSAQEFQYISGGQCYQrnDGVRDD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 326 EEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEA------------------EKVAFLC 387
Cdd:cd14895 243 KQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAASApcrlasaspssltvqqhlDIVSKLF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 388 GINAGDLLKALLKPKVKVGTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNY-----------YI 456
Cdd:cd14895 323 AVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnkaankdttpCI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 457 GVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILEQEEYKKEGIAWEFIDFGmDLQMCIDLIE-KPMGILSILEE 535
Cdd:cd14895 403 AVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRPSGIFSLLDE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 536 ECMFPKADDKSFQDKLYQNHMGKNRMftkpgKPTRPNQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKE 615
Cdd:cd14895 482 ECVVPKGSDAGFARKLYQRLQEHSNF-----SASRTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTSD 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 616 PLVAEL---FKAPEEPAGGGKK--KKGKSSAFQT--ISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVL 688
Cdd:cd14895 557 AHLRELfefFKASESAELSLGQpkLRRRSSVLSSvgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVS 636
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 689 HQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSIL--APNAipqgfvdGKTVSEKILAGLQMDPAEyrLGTTKVFFK 763
Cdd:cd14895 637 SQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLvaAKNA-------SDATASALIETLKVDHAE--LGKTRVFLR 704
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
97-763 |
5.39e-128 |
|
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: 417.26 E-value: 5.39e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVAcavKKKDEEASDKKEGSLedqiiqanPVLEAYGNAKTTRNNNSSRFGKFIRIHFgPTGK 256
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLY---QDQTEDRLRQPEDVL--------PILESFGHAKTILNANASRFGQVLRLHL-QHGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 257 IAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVM-LVTPDSglYSFINQG--ClTVDNIDDVEEFKLCDE 333
Cdd:cd14896 149 IVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLsLQGPET--YYYLNQGgaC-RLQGKEDAQDFEGLLK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 334 AFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPRE--EQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMVT 411
Cdd:cd14896 226 ALQGLGLCAEELTAIWAVLAAILQLGNICFSSSEREsqEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 412 KGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLD--TKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFN 489
Cdd:cd14896 306 RPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAppGEAESDATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 490 HHMFILEQEEYKKEGIAWEFIDfGMDLQMCIDLI-EKPMGILSILEEECMFPKADDKSFQDKLYQNHmGKNRMFTKPGKP 568
Cdd:cd14896 386 QTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQLP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 569 TrpnqgPAhFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKGKSSAFQtisav 648
Cdd:cd14896 464 L-----PV-FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKPTLASRFQ----- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 649 hrESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAI 728
Cdd:cd14896 533 --QSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQ 610
|
650 660 670
....*....|....*....|....*....|....*....
gi 127773 729 PqgfvdGKTVSEKILAGL-QMDPAE---YRLGTTKVFFK 763
Cdd:cd14896 611 E-----ALSDRERCGAILsQVLGAEsplYHLGATKVLLK 644
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
97-763 |
2.28e-127 |
|
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: 415.54 E-value: 2.28e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRK-TEIPPHLFSVADNAYQNMVTDRENQSCLIT 175
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDlTKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 176 GESGAGKTENTKKVIMYLAKvacavkkkdeEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTG 255
Cdd:cd14876 81 GESGAGKTEATKQIMRYFAS----------AKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 256 KIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELND-VMLVTPDSglYSFINQGCLTVDNIDDVEEFKLCDEA 334
Cdd:cd14876 151 GIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSkYHLLGLKE--YKFLNPKCLDVPGIDDVADFEEVLES 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 335 FDILGFTKEEKQSMFKCTASILHMGEMKF--KQRPREEQA---ESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEM 409
Cdd:cd14876 229 LKSMGLTEEQIDTVFSIVSGVLLLGNVKItgKTEQGVDDAaaiSNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 410 VTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFN 489
Cdd:cd14876 309 IEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 490 HHMFILEQEEYKKEGIAWEFIDFGMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNhMGKNRMFTKPGKPT 569
Cdd:cd14876 389 DIVFERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSK-LKSNGKFKPAKVDS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 570 RPNqgpahFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKGKSSAFQTisavh 649
Cdd:cd14876 468 NIN-----FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKGSLIGSQFLK----- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 650 reSLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIP 729
Cdd:cd14876 538 --QLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIAN 615
|
650 660 670
....*....|....*....|....*....|....
gi 127773 730 QGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14876 616 DKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
97-761 |
1.01e-121 |
|
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: 400.00 E-value: 1.01e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLP-IYTDSVIAKYRGK-RKTEIPPHLFSVADNAYQNMVTDRE--NQSC 172
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAApQPQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 173 LITGESGAGKTENTKKVIMYLAKVACAVKK-KDEEASDKkegsLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHF 251
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSwESHKIAER----IEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 252 GPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPElNDVMLVTPDSGLYSFINQGcltvDNIDDVEEFKLC 331
Cdd:cd14880 157 NRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASAD-ERLQWHLPEGAAFSWLPNP----ERNLEEDCFEVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 332 DEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAES--DGTAEAEKV-AFLCGINAGDLLKALLKPKVKVGTE 408
Cdd:cd14880 232 REAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQpmDDTKESVRTsALLLKLPEDHLLETLQIRTIRAGKQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 409 MVT--KGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKR-NYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQ 485
Cdd:cd14880 312 QQVfkKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 486 QFFNHHMFILEQEEYKKEGIAWEFIDFgMDLQMCIDLIE-KPMGILSILEEECMFPKADDKS-FQDKL-----YQNHMGK 558
Cdd:cd14880 392 QHFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSSAAqLQTRIesalaGNPCLGH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 559 NRMFTKPgkptrpnqgpaHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEPAGGGKKKKGK 638
Cdd:cd14880 471 NKLSREP-----------SFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQS 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 639 SSAFQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQ 718
Cdd:cd14880 540 RAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVE 619
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 127773 719 RYSILAPN--AIPQGFVDGKTvsekilAGLQMDPAeyRLGTTKVF 761
Cdd:cd14880 620 RYKLLRRLrpHTSSGPHSPYP------AKGLSEPV--HCGRTKVF 656
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
97-763 |
1.28e-118 |
|
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: 390.79 E-value: 1.28e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLP-IYTDSVIAKYRGKR-----KTEIPPHLFSVADNAYQNMVTDRENQ 170
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADtsrgfPSDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 171 SCLITGESGAGKTENTKKVIMYLAKvacavkkkdeeASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIH 250
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAY-----------GHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 251 FGPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVM-LVTPDSglYSFINQG-CLTVDNIDDVEEF 328
Cdd:cd14886 150 VGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLgFKSLES--YNFLNASkCYDAPGIDDQKEF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 329 KLCDEAFDILgFTKEEKQSMFKCTASILHMGEMKFKQRPR---EEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKV 405
Cdd:cd14886 228 APVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 406 GTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQ 485
Cdd:cd14886 307 NNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 486 QFFNHHMFILEQEEYKKEGIAWEFIDFgMDLQMCIDLIEKP-MGILSILEEECMFPKADDKSFQDKLyqNHMGKNRMFTk 564
Cdd:cd14886 387 QYFINQVFKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC--KSKIKNNSFI- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 565 PGKPTRPNqgpahFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELF-KAPEEPAGGGKkkkgkssafQ 643
Cdd:cd14886 463 PGKGSQCN-----FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFsDIPNEDGNMKG---------K 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 644 TISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSIL 723
Cdd:cd14886 529 FLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKIL 608
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 127773 724 A--PNAIPQGFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14886 609 IshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
97-763 |
1.22e-116 |
|
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: 385.70 E-value: 1.22e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTS-GLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTE-IPPHLFSVADNAY-QNMVTDRENQSCL 173
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRlLPPHIWQVAHKAFnAIFVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 174 ITGESGAGKTENTKKVIMYLAKVACAVKKKDEEAS--DKKEGSLEdqiiQANPVLEAYGNAKTTRNNNSSRFGKFIRIHF 251
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQRSiaDKIDENLK----WSNPVMESFGNARTVRNDNSSRFGKYIKLYF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 252 GPT-GKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVM--LVTPD-----SGLYSFINQGcltVDN-- 321
Cdd:cd14875 157 DPTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELggLKTAQdykclNGGNTFVRRG---VDGkt 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 322 IDDVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCgINAGDLLKALLkp 401
Cdd:cd14875 234 LDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFLTACRLLQ-LDPAKLRECFL-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 402 kVKVGTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRN--YYIGVLDIAGFEIFDFNSFEQLCINY 479
Cdd:cd14875 311 -VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSgcKYIGLLDIFGFENFTRNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 480 TNERLQQFFNHHMFILEQEEYKKEGIAWEFIDFGmDLQMCIDLIE-KPMGILSILEEECMFPKADDKSFQDKLYQNHMGK 558
Cdd:cd14875 390 ANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 559 NRMFTKPgKPTRPNQgpahFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFkaPEEPAGGGKKkkgk 638
Cdd:cd14875 469 SPYFVLP-KSTIPNQ----FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLL--STEKGLARRK---- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 639 ssafQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQ 718
Cdd:cd14875 538 ----QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCR 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 127773 719 RYSILAPNAIPQGFVDGK--TVSEKILAGLQM----DPAEYRLGTTKVFFK 763
Cdd:cd14875 614 YFYLIMPRSTASLFKQEKysEAAKDFLAYYQRlygwAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
97-726 |
2.08e-113 |
|
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: 378.17 E-value: 2.08e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLP-IYTDSVIAKYRGKRK-TEIPPHLFSVADNAYQNMVTDRENQSCLI 174
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 175 TGESGAGKTENTKKVIMYLAKVACAvKKKDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPT 254
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSS-NQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 255 -GKIAGADIETYLLEKSRVTYQ-QSAERNYHIFYQICSNAIPELNDVMLVTPDSGLYSFINQGCLTVD------------ 320
Cdd:cd14906 160 dGKIDGASIETYLLEKSRISHRpDNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISsfksqssnknsn 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 321 ---NIDDVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQ-----RPREEQAESdgTAEAEKVAFLCGINAG 392
Cdd:cd14906 240 hnnKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEdsdfsKYAYQKDKV--TASLESVSKLLGYIES 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 393 DLLKALLKPKVKVGTE--MVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLD-----------TKAKRNYYIGVL 459
Cdd:cd14906 318 VFKQALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNqntqsndlaggSNKKNNLFIGVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 460 DIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILEQEEYKKEGIAWEFIDFgMDLQMCIDLIE-KPMGILSILEEECM 538
Cdd:cd14906 398 DIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 539 FPKADDKSFQDKLYQNHMGKNRMFTKP-GKPTrpnqgpahFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPL 617
Cdd:cd14906 477 MPKGSEQSLLEKYNKQYHNTNQYYQRTlAKGT--------LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFL 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 618 VAELFKAPEepaGGGKKKKGKSSAFQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVL 697
Cdd:cd14906 549 KKSLFQQQI---TSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVL 625
|
650 660
....*....|....*....|....*....
gi 127773 698 EGIRICRKGFPSRLIYSEFKQRYSILAPN 726
Cdd:cd14906 626 NTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
97-720 |
6.03e-106 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 356.71 E-value: 6.03e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLP-IYTDSVIAKYR-------GKRKTEI---PPHLFSVADNAYQNMVT 165
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 166 DRENQSCLITGESGAGKTENTKKVIMYLAkVACAVKKKDEEASDKKEG-------SLEDQIIQANPVLEAYGNAKTTRNN 238
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFA-VHCGTGNNNLTNSESISPpaspsrtTIEEQVLQSNPILEAFGNARTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 239 NSSRFGKFIRIHF-GPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSN----AIPELNDVMLVTPDSGLYSFIN 313
Cdd:cd14899 160 NSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSGGPQSFRLLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 314 QGCLTV--DNIDDVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRP--REEQAESDGTAEAE-------- 381
Cdd:cd14899 240 QSLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPhkGDDTVFADEARVMSsttgafdh 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 382 --KVAFLCGINAGDLLKALLKPKVKVGTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTL------------- 446
Cdd:cd14899 320 ftKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgades 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 447 --DTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILEQEEYKKEGIAWEFIDFGMDlQMCIDLIE 524
Cdd:cd14899 400 dvDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 525 -KPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNrmfTKPGKPTRPN-QGPAHFELHHYAGNVPYSITGWLEKNKDPI 602
Cdd:cd14899 479 hRPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKN---SHPHFRSAPLiQRTTQFVVAHYAGCVTYTIDGFLAKNKDSF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 603 NENVVALLGASKEPLVAEL------FKAPEEPAGGGKKKKGKSSAFQTISAVH-----RESLNKLMKNLYSTHPHFVRCI 671
Cdd:cd14899 556 CESAAQLLAGSSNPLIQALaagsndEDANGDSELDGFGGRTRRRAKSAIAAVSvgtqfKIQLNELLSTVRATTPRYVRCI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 127773 672 IPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRY 720
Cdd:cd14899 636 KPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
97-763 |
3.26e-104 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 350.84 E-value: 3.26e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLAKVACAVKKKdeeasdkkegSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGK 256
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV----------LSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 257 IAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELN-----DVMLVTPDSGLYSFINQGcltvDNIDDVEEF-KL 330
Cdd:cd01386 151 LASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRtelhlNQLAESNSFGIVPLQKPE----DKQKAAAAFsKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 331 CdEAFDILGFTKEEKQSMFKCTASILHM---GEMKFKQRPREEQAEsdgTAEAEKVAFLCGINAGDLLKALLKPKVKVGT 407
Cdd:cd01386 227 Q-AAMKTLGISEEEQRAIWSILAAIYHLgaaGATKAASAGRKQFAR---PEWAQRAAYLLGCTLEELSSAIFKHHLSGGP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 408 EMVT-------------KGQNMNQvVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFN---- 470
Cdd:cd01386 303 QQSTtssgqesparsssGGPKLTG-VEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqr 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 471 --SFEQLCINYTNERLQQFFNHHMFILEQEEYKKEGIAwefIDFGMDL----QMCiDLIEK---------------PMGI 529
Cdd:cd01386 382 gaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPElspgALV-ALIDQapqqalvrsdlrdedRRGL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 530 LSILEEECMFPKADDKSFQDKLYqNHMGKNRMFTKPGkPTRPNQGPAHFELHHYAGN--VPYSITGWLEKNK-DPINENV 606
Cdd:cd01386 458 LWLLDEEALYPGSSDDTFLERLF-SHYGDKEGGKGHS-LLRRSEGPLQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNA 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 607 VALLGASKEPLVAELFKAPeepagggkkkkgkssAFQTISAVhreslNKLMKNLYSTHPHFVRCIIP--NELKQPG---- 680
Cdd:cd01386 536 TQLLQESQKETAAVKRKSP---------------CLQIKFQV-----DALIDTLRRTGLHFVHCLLPqhNAGKDERstss 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 681 ------LVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAP-----NAIPQGFVDGKTVSEKILAGLQMD 749
Cdd:cd01386 596 paagdeLLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPpltkkLGLNSEVADERKAVEELLEELDLE 675
|
730
....*....|....
gi 127773 750 PAEYRLGTTKVFFK 763
Cdd:cd01386 676 KSSYRIGLSQVFFR 689
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
97-763 |
1.34e-102 |
|
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: 344.88 E-value: 1.34e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYR---GKRKTEIPPHLFSVADNAYQNMVTDRENQSCL 173
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 174 ITGESGAGKTENTKKVIMYLAKvacavkkkdeeASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGP 253
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTC-----------RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 254 TGK-IAGADIETYLLEKSRVTYQQSAERNYHIFYQicsnaipeLNDVMLVTPDSGLY-------SFINQGCL----TVDN 321
Cdd:cd14878 150 RKKhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYL--------LMDGLSAEEKYGLHlnnlcahRYLNQTMRedvsTAER 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 322 IDDVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKP 401
Cdd:cd14878 222 SLNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 402 KVKVGTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTL----DTKAKRNYYIGVLDIAGFEIFDFNSFEQLCI 477
Cdd:cd14878 302 IQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 478 NYTNERLQQFFNHHMFILEQEEYKKEGIAWEFIDFGMDLQMCID-LIEKPMGILSILEEECMFPKADDKSFQDKL--YQN 554
Cdd:cd14878 382 NMTNEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPSGFLSLLDEESQMIWSVEPNLPKKLqsLLE 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 555 HMGKNRMFTKP----GKPTRPNQGPAhFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKapeepag 630
Cdd:cd14878 462 SSNTNAVYSPMkdgnGNVALKDQGTA-FTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 631 ggkkkkgksSAFQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSR 710
Cdd:cd14878 534 ---------SKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVR 604
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 127773 711 LIYSEFKQRYSILAPNAIpqGFVDGKTVSEKILAGLQMDPAE-YRLGTTKVFFK 763
Cdd:cd14878 605 LSFSDFLSRYKPLADTLL--GEKKKQSAEERCRLVLQQCKLQgWQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
98-727 |
4.49e-97 |
|
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: 326.08 E-value: 4.49e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 98 SVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDsviAKYRGKRKTEIPPHLFSVADNAYQNMVTdRENQSCLITGE 177
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGA---MKAYLKNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 178 SGAGKTENTKKVIMYLAKvacavkkkdeeaSDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFgpTGKI 257
Cdd:cd14898 78 SGSGKTENAKLVIKYLVE------------RTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 258 AGADIETYLLEKSRVTYQQSAERNYHIFYQIC-SNAIPELNDvmlvtpdsglysFINQGCLTVDNIDDV---EEFKLCDE 333
Cdd:cd14898 144 TGAKFETYLLEKSRVTHHEKGERNFHIFYQFCaSKRLNIKND------------FIDTSSTAGNKESIVqlsEKYKMTCS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 334 AFDILGFTKeeKQSMFKCTASILHMGEMKFKqrpreeqaeSDGTAEAEK------VAFLCGINAGDLLKALLKPKVKVGT 407
Cdd:cd14898 212 AMKSLGIAN--FKSIEDCLLGILYLGSIQFV---------NDGILKLQRnesfteFCKLHNIQEEDFEESLVKFSIQVKG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 408 EMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNyyIGVLDIAGFEIFDFNSFEQLCINYTNERLQQF 487
Cdd:cd14898 281 ETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQND 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 488 FNHHMFILEQEEYKKEGIAWEFIDFgMDLQMCIDLIEKPMGILSILEEECMFPKADDKSFQDKL--YQNHmgknRMFTKP 565
Cdd:cd14898 359 FIKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNG----FINTKA 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 566 GKPTRPNqgpahfelhHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKapeepagggkkkkgkssafqti 645
Cdd:cd14898 434 RDKIKVS---------HYAGDVEYDLRDFLDKNREKGQLLIFKNLLINDEGSKEDLVK---------------------- 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 646 saVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSILAP 725
Cdd:cd14898 483 --YFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGI 560
|
..
gi 127773 726 NA 727
Cdd:cd14898 561 TL 562
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
94-762 |
3.70e-94 |
|
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: 319.88 E-value: 3.70e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 94 LNEASVLYNLRSRYTSGLIYTY---SGLfcIAVNPYRRLPIYTDSVIAKYR-------GKRKTEIPPHLFSVADNAYQNM 163
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 164 VTDRENQSCLITGESGAGKTENTKKVIMYLAKVAcavkkkdeeASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRF 243
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLS---------SHSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNASRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 244 GKFIRIHFGPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPE------LNDVmlvtpdSGLYSFINQGC- 316
Cdd:cd14879 150 GRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEerqhlgLDDP------SDYALLASYGCh 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 317 ---LTVDnIDDVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFkQRPREEQAES---DGTAEAEKVAFLCGIN 390
Cdd:cd14879 224 plpLGPG-SDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEF-TYDHEGGEESavvKNTDVLDIVAAFLGVS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 391 AGDlLKALLKPKVK-VGTEMVTkgqnmnqvV--NSVGA------LAKSLYDRMFNWLVRRVNKTL-DTKAKRNYYIGVLD 460
Cdd:cd14879 302 PED-LETSLTYKTKlVRKELCT--------VflDPEGAaaqrdeLARTLYSLLFAWVVETINQKLcAPEDDFATFISLLD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 461 IAGFEIFD---FNSFEQLCINYTNERLQQFFNHHMFILEQEEYKKEGIAWEFIDFgMDLQMCIDLI-EKPMGILSILEEE 536
Cdd:cd14879 373 FPGFQNRSstgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQ 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 537 C-MFPKADDKSFQDKLYQNHMGKNRMFTKPGKPTRpnQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKE 615
Cdd:cd14879 452 TrRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATR--SGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRGATQ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 616 plvaelfkapeepagggkkkkgkssafqtisavHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNG 695
Cdd:cd14879 530 ---------------------------------LNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLG 576
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 696 VLEGIRICRKGFPSRLIYSEFKQRYSILAPNAIPQgfvdgkTVSEKILAGLQMDPAEYRLGTTKVFF 762
Cdd:cd14879 577 LPELAARLRVEYVVSLEHAEFCERYKSTLRGSAAE------RIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
97-763 |
4.50e-92 |
|
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: 316.59 E-value: 4.50e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTS--------GLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRE 168
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 169 NQSCLITGESGAGKTENTKKVIMYLAKVacavkkkdeeaSDKKEG----SLEDQIIQANPVLEAYGNAKTTRNNNSSRFG 244
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAV-----------SDRRHGadsqGLEARLLQSGPVLEAFGNAHTVLNANSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 245 KFIRIHFGPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAipelndVMLVTPDSglysfinqgcLTVDNIDD 324
Cdd:cd14887 150 KMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAA------VAAATQKS----------SAGEGDPE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 325 VEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKF--KQRPRE-------------EQAESDGTAEAEKVAFLCGI 389
Cdd:cd14887 214 STDLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFttDQEPETskkrkltsvsvgcEETAADRSHSSEVKCLSSGL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 390 NAGDLLKALLKPKVK-VGTEMVTKGQNM-------------------NQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTK 449
Cdd:cd14887 294 KVTEASRKHLKTVARlLGLPPGVEGEEMlrlalvsrsvretrsffdlDGAAAARDAACKNLYSRAFDAVVARINAGLQRS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 450 AKRNY--------------YIGVLDIAGFEIF---DFNSFEQLCINYTNERLQQFFNHHMFILEQEEYKKEGIAWEFI-- 510
Cdd:cd14887 374 AKPSEsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcs 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 511 DFGMDLQMCIDLIEKP------------------------MGILSILEEE-CMFPKADDKSFQDKLYQNHMGKNRMFTKP 565
Cdd:cd14887 454 AFPFSFPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKNIINSAK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 566 GKPTRPNQGPAH--FELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKeplvaelFKAPEEPAGGGKKKKGKSSAFQ 643
Cdd:cd14887 534 YKNITPALSRENleFTVSHFACDVTYDARDFCRANREATSDELERLFLACS-------TYTRLVGSKKNSGVRAISSRRS 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 644 TISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSIL 723
Cdd:cd14887 607 TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETK 686
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 127773 724 APNAIPQgFVDGKTVSEKILAGLQMDPAEYRLGTTKVFFK 763
Cdd:cd14887 687 LPMALRE-ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
97-763 |
6.60e-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: 310.41 E-value: 6.60e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLpiytDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVI-MYLAKVacavkKKDEEASDkkegSLEDqiiqANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTG 255
Cdd:cd14937 77 ESGSGKTEASKLVIkYYLSGV-----KEDNEISN----TLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 256 KIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPELNDVMLVTPDSGlYSFINQGCLTVDNIDDVEEFKLCDEAF 335
Cdd:cd14937 144 NIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENE-YKYIVNKNVVIPEIDDAKDFGNLMISF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 336 DILGFTkEEKQSMFKCTASILHMGEMKFKQ-----RPREEQAESDGTAEAEKVAFLCGINAGDLLKALLKPKVKVGTEMV 410
Cdd:cd14937 223 DKMNMH-DMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 411 TKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNH 490
Cdd:cd14937 302 EIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 491 HMFILEQEEYKKEGIAWEFIDFGMDlQMCIDLIEKPMGILSILEEECMFPKADDKSFQdKLYQNHMGKNRMFTKPGKPTR 570
Cdd:cd14937 382 IVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESIV-SVYTNKFSKHEKYASTKKDIN 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 571 PNqgpahFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEEPAGGGKKkkgkssafQTISAVHR 650
Cdd:cd14937 460 KN-----FVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRK--------NLITFKYL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 651 ESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRIcRKGFPSRLIYSEFKQRYSILAPNAIPQ 730
Cdd:cd14937 527 KNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKD 605
|
650 660 670
....*....|....*....|....*....|...
gi 127773 731 GFVDGKTVSEKILAGlQMDPAEYRLGTTKVFFK 763
Cdd:cd14937 606 SSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
97-763 |
1.36e-84 |
|
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: 291.77 E-value: 1.36e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYrgkrkteippHLFSVADNAYQNMVTDREN-QSCLIT 175
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 176 GESGAGKTENTKKVIMYLakvacaVKKKDEEASDKKEGSLEDqiiqanpVLEAYGNAKTTRNNNSSRFGKFIRIHFgPTG 255
Cdd:cd14874 71 GESGSGKSYNAFQVFKYL------TSQPKSKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSIDLLY-KRN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 256 KIAGADIE-TYLLEKSRVTYQQSAERNYHIFYQICSNaipeLNDVM---LVTPDSGLYSFINQGCLTVDNIDDVEEFKLC 331
Cdd:cd14874 137 VLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHG----LNDEMkakFGIKGLQKFFYINQGNSTENIQSDVNHFKHL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 332 DEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQR--PREEQ--AESDGTAEAEKVAFLCGINAGDLLKALLkPKVKVGT 407
Cdd:cd14874 213 EDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKrnPNVEQdvVEIGNMSEVKWVAFLLEVDFDQLVNFLL-PKSEDGT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 408 EMvtkgqNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTkAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQF 487
Cdd:cd14874 292 TI-----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKC-PLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 488 FNHHMFILEQEEYKKEGIAWEF-----IDFGMDLQMcidLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMf 562
Cdd:cd14874 366 FVKHSFHDQLVDYAKDGISVDYkvpnsIENGKTVEL---LFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSY- 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 563 tkpGKPTrpNQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKApeepaGGGKKKKGKSSAF 642
Cdd:cd14874 442 ---GKAR--NKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFES-----YSSNTSDMIVSQA 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 643 QTISAVHRESLNKLMKnlysTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSI 722
Cdd:cd14874 512 QFILRGAQEIADKING----SHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRC 587
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 127773 723 LAPNAIPQgFVDGKTVSEKILAGLQMDPAE-YRLGTTKVFFK 763
Cdd:cd14874 588 LLPGDIAM-CQNEKEIIQDILQGQGVKYENdFKIGTEYVFLR 628
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
97-715 |
1.13e-76 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 269.85 E-value: 1.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 97 ASVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLP-IYTDSVIAKYRGKRKTE-------IPPHLFSVADNAYQNMVTDRE 168
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 169 NQSCLITGESGAGKTENTKKVIMYLAKVAcavkkkdeeaSDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIR 248
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQ----------TDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 249 IHF---------GPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPE-LNDVMLVTpDSGLYSFIN----- 313
Cdd:cd14884 151 LIFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEdLARRNLVR-NCGVYGLLNpdesh 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 314 -----QGCLTVDNID----------DVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKqrpreeqaesdgtA 378
Cdd:cd14884 230 qkrsvKGTLRLGSDSldpseeekakDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-------------A 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 379 EAEkvafLCGINAGDLLKALLKPKVKVGTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKT-LDTKAKR----- 452
Cdd:cd14884 297 AAE----CLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNvLKCKEKDesdne 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 453 ------NYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILEQEEYKKEGIAWEFIdfgmDLQMCIDLIEKP 526
Cdd:cd14884 373 diysinEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSD----VAPSYSDTLIFI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 527 MGILSILEE-----ECMFPKADDKSFQDKLYQNHMGKNRMFTKPGK-PTRPNQGPA--------HFELHHYAGNVPYSIT 592
Cdd:cd14884 449 AKIFRRLDDitklkNQGQKKTDDHFFRYLLNNERQQQLEGKVSYGFvLNHDADGTAkkqnikknIFFIRHYAGLVTYRIN 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 593 GWLEKNKDPINENVVALLGASKEPLVAElfkapeepagggKKKKGKSSAFQTISAVHRESLNKLMKNLYSTHPHFVRCII 672
Cdd:cd14884 529 NWIDKNSDKIETSIETLISCSSNRFLRE------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFL 596
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 127773 673 PNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSE 715
Cdd:cd14884 597 PNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
103-763 |
2.88e-71 |
|
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: 253.86 E-value: 2.88e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 103 LRSRYTSGLIYTYSGLFCIAVNPYRRLP-IYTDSVIAKYRGKRKteIPPHLFSVADNAYQNMVTDRENQSCLITGESGAG 181
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYNQRRG--LPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 182 KTENTKKVIMYLAKVACAVKKkdeeasdkkegSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGKIAGAD 261
Cdd:cd14905 85 KSENTKIIIQYLLTTDLSRSK-----------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 262 IETYLLEKSRVTYQQSAERNYHIFYQICsNAIPELNDVMLVTPDSGLYSFINQ-GCLTVDNIDDVEEFKLCDEAFDILGF 340
Cdd:cd14905 154 LYSYFLDENRVTYQNKGERNFHIFYQFL-KGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 341 TKEEKQSMFKCTASILHMGEMKFKQrpREEQAESDGTAEAEKVAFLCGINAGDLLKALLKpkvkvgtemvTKGQNMNQVV 420
Cdd:cd14905 233 PSEKIDLIFKTLSFIIILGNVTFFQ--KNGKTEVKDRTLIESLSHNITFDSTKLENILIS----------DRSMPVNEAV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 421 NSVGALAKSLYDRMFNWLVRRVNKTLdTKAKRNYYIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILEQEEY 500
Cdd:cd14905 301 ENRDSLARSLYSALFHWIIDFLNSKL-KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 501 KKEGIAWEFIDFGMDLQMCIDLIEKpmgILSILEEECMFPKADDKSFQDKLyQNHMGKNRMFTKpgkptRPNQgpahFEL 580
Cdd:cd14905 380 QTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL-QNFLSRHHLFGK-----KPNK----FGI 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 581 HHYAGNVPYSITGWLEKNKDPI-------NENVVALLGASKEPL------VAELFKAPEEPAGGGKKKKGKSSAFQTISA 647
Cdd:cd14905 447 EHYFGQFYYDVRGFIIKNRDEIlqrtnvlHKNSITKYLFSRDGVfninatVAELNQMFDAKNTAKKSPLSIVKVLLSCGS 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 648 VHRESLNKLMKN-------------------LYSTHP-------------HFVRCIIPNELKQPGLVDAELVLHQLQCNG 695
Cdd:cd14905 527 NNPNNVNNPNNNsgggggggnsgggsgsggsTYTTYSstnkainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLC 606
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 127773 696 VLEGIRICRKGFPSRLIYSEFKQRYSILAPNAipQGFvdgKTVSEKILAG-LQMD---PAEYRLGTTKVFFK 763
Cdd:cd14905 607 LLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNF---QNLFEKLKENdINIDsilPPPIQVGNTKIFLR 673
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
100-720 |
5.73e-70 |
|
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: 251.81 E-value: 5.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 100 LYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRK----------TEIPPHLFSVADNAYQNMVTDREN 169
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 170 QSCLITGESGAGKTENTKKVIMYLAKVACAVK-KKDEEASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIR 248
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEpRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 249 IHFGPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAI--PELNDVMLVTPDSGLYSFINQGCLTVDNID-DV 325
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQADPLATNFAlDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 326 EEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPREEQAESDGTAEAEKVAFLCGIN--AGDLLKALL---K 400
Cdd:cd14893 244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTVSDAQSCALKdpAQILLAAKLlevE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 401 PKV------------KVGTEMVT--KGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTL----DTKAKRNYYIG----- 457
Cdd:cd14893 324 PVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNIVINsqgvh 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 458 VLDIAGFEIFD--FNSFEQLCINYTNERLQQFFNHHMFILEQEEYKKEGIAWE-------FIDFGMDLQMCIDLIE-KPM 527
Cdd:cd14893 404 VLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVEnrltvnsNVDITSEQEKCLQLFEdKPF 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 528 GILSILEEECMFPKADDKSFQDKLYQNHmgknrmfTKPGKPTRPNQGPAH--------------FELHHYAGNVPYSITG 593
Cdd:cd14893 484 GIFDLLTENCKVRLPNDEDFVNKLFSGN-------EAVGGLSRPNMGADTtneylapskdwrllFIVQHHCGKVTYNGKG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 594 WLEKNKDPINENVVALLGASKEPLVAELFKA------PEEPAGGGKKKKGKSSAFQTISAVHRESLN------------- 654
Cdd:cd14893 557 LSSKNMLSISSTCAAIMQSSKNAVLHAVGAAqmaaasSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynqa 636
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 655 -KLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRY 720
Cdd:cd14893 637 dALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
98-763 |
6.33e-69 |
|
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: 245.81 E-value: 6.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 98 SVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITGE 177
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 178 SGAGKTENTKKVIMYLAKVAcavkkkdeeasDKKEGSLEdQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFGPTGKI 257
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG-----------DGNRGATG-RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 258 AGADIETYLLEKSRVTYQQSAERNYHIFYQICS--NAIPELNDVMLV-------------TPDSGLYSFINqgcltvDNI 322
Cdd:cd14882 150 SGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKagrnyrylrippeVPPSKLKYRRD------DPE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 323 DDVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRprEEQAESDGTAEAEKVAFLCGINAGDLLKALLKPK 402
Cdd:cd14882 224 GNVERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQN--GGYAELENTEIASRVAELLRLDEKKFMWALTNYC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 403 VKVGTEMVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLD-TKA--KRNYYIGVLDIAGFEIFDFNSFEQLCINY 479
Cdd:cd14882 302 LIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfPRAvfGDKYSISIHDMFGFECFHRNRLEQLMVNT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 480 TNERLQQFFNHHMFILEQEEYKKEGIAWEFIDFgMDLQMCID-LIEKPMGILSILEEEcmfpkadDKSFQDKLY--QNHM 556
Cdd:cd14882 382 LNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDqLMTKPDGLFYIIDDA-------SRSCQDQNYimDRIK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 557 GKNRMFTKPGKPTrpnqgpaHFELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFKAPEepagggkkkk 636
Cdd:cd14882 454 EKHSQFVKKHSAH-------EFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQ---------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 637 gkSSAFQTISAVHRESLNKLMKNLY----STHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGFPSRLI 712
Cdd:cd14882 517 --VRNMRTLAATFRATSLELLKMLSiganSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIP 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 713 YSEFKQRYSILApnaipqgFVDGKTVSEK------ILAGLQMDpaEYRLGTTKVFFK 763
Cdd:cd14882 595 FQEFLRRYQFLA-------FDFDETVEMTkdncrlLLIRLKME--GWAIGKTKVFLK 642
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
98-744 |
3.76e-65 |
|
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: 234.62 E-value: 3.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 98 SVLYNLRSRYTSGLIYTYSGLFCIAVNPYR-----RLPIYTDSVIAKyrgkrkteipPHLFSVADNAYQNMVTDRENQSC 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRdvgnpLTLTSTRSSPLA----------PQLLKVVQEAVRQQSETGYPQAI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 173 LITGESGAGKTENTkkviMYLAKVACAVkkkdeeASDKKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRIHFg 252
Cdd:cd14881 72 ILSGTSGSGKTYAS----MLLLRQLFDV------AGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 253 PTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICSNAIPElNDVML----VTPDSglYSFINQGCLTVDNIDDVEEF 328
Cdd:cd14881 141 TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQE-ERVKLhldgYSPAN--LRYLSHGDTRQNEAEDAARF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 329 KLCDEAFDILG--FTkeekqSMFKCTASILHMGEMKFKQrPREEQAESDGTAEAEKVAFLCGINAGDLLKALlkpkvkvg 406
Cdd:cd14881 218 QAWKACLGILGipFL-----DVVRVLAAVLLLGNVQFID-GGGLEVDVKGETELKSVAALLGVSGAALFRGL-------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 407 temVTKGQNM-NQVVNSV----------GALAKSLYDRMFNWLVRRVNK------TLDTKAKRNYyIGVLDIAGFEIFDF 469
Cdd:cd14881 284 ---TTRTHNArGQLVKSVcdanmsnmtrDALAKALYCRTVATIVRRANSlkrlgsTLGTHATDGF-IGILDMFGFEDPKP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 470 NSFEQLCINYTNERLQQFFNHHMFILEQEEYKKEGIAWEF-IDFgMDLQMCIDLIEK-PMGILSILEEECMfPKADDKSF 547
Cdd:cd14881 360 SQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESY 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 548 QDKLYQNHMGKNRMFTkpgkpTRPnQGPAHFELHHYAGNVPYSITGWLEKNKDPINENVVALLgaskeplvaelfkapee 627
Cdd:cd14881 438 VAKIKVQHRQNPRLFE-----AKP-QDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVF----------------- 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 628 pagggkKKKGKSSAFQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGF 707
Cdd:cd14881 495 ------YKQNCNFGFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGY 568
|
650 660 670
....*....|....*....|....*....|....*..
gi 127773 708 PSRLIYSEFKQRYSILAPNAIPQGFVDGKTVSEKILA 744
Cdd:cd14881 569 PHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALIL 605
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
119-249 |
4.08e-59 |
|
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: 201.03 E-value: 4.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 119 FCIAVNPYRRLPIYTDS-VIAKYRGKRKTEIPPHLFSVADNAYQNMVTDRENQSCLITGESGAGKTENTKKVIMYLAKVA 197
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 127773 198 CAVKKKDEEASD----KKEGSLEDQIIQANPVLEAYGNAKTTRNNNSSRFGKFIRI 249
Cdd:cd01363 81 FNGINKGETEGWvyltEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
98-761 |
1.07e-46 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 180.80 E-value: 1.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 98 SVLYNLRSRYTSGLIYTYSGLFCIAVNPYRRLPIYTDSVIAKYRGKRKTE-IPPHLFSVADNAYQNMVTDRENQSCLITG 176
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 177 ESGAGKTENTKKVIMYLA-------------KVACAVKKKDEEASDKKeGSLEDQIIQANPVLEAYGNAKTTRNNNSSRF 243
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAyqvkgsrrlptnlNDQEEDNIHNEENTDYQ-FNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 244 GKFIRIHFgPTGKIAGADIETYLLEKSRVTYQQSAERNYHIFYQICsNAIPELNDVMLVTPDSGLYSFINQGCLTVDNID 323
Cdd:cd14938 161 SKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYII-NGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 324 DVEEFKLCDEAFDILGFTKEEKQSMFKCTASILHMGEMKFKQRPRE-----------------------EQAESDGTAEA 380
Cdd:cd14938 239 YSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAFRKksllmgknqcgqninyetilselENSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 381 EKVAFLcginAGDLLKALLKPKVKVGTE-------MVTKGQNMNQVVNSVGALAKSLYDRMFNWLVRRVNKTLDTKAKRN 453
Cdd:cd14938 319 VKNLLL----ACKLLSFDIETFVKYFTTnyifndsILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNIN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 454 Y---YIGVLDIAGFEIFDFNSFEQLCINYTNERLQQFFNHHMFILEQEEYKKEGIAWEFIDFGMD-LQMCIDLIEKPMGI 529
Cdd:cd14938 395 IntnYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDnEPLYNLLVGPTEGS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 530 LSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTKPGKPTRPNQGpahFELHHYAGNVPYSITGWLEKNKDPINENVVAL 609
Cdd:cd14938 475 LFSLLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT---FVITHSCGDIIYNAENFVEKNIDILTNRFIDM 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 610 LGASKEPLVAEL--FKAPEEPAGGGKKKKGKS--SAF-----------QTISAVHRESLNKLMKNLYSTHPHFVRCIIPN 674
Cdd:cd14938 552 VKQSENEYMRQFcmFYNYDNSGNIVEEKRRYSiqSALklfkrrydtknQMAVSLLRNNLTELEKLQETTFCHFIVCMKPN 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 675 ELKQP-GLVDAELVLHQLQCNGVLEGIRICRKGFPSRLIYSEFKQRYSIlaPNAipqgfvDGKTVSEKILAGLQMDPAEY 753
Cdd:cd14938 632 ESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDI--KNE------DLKEKVEALIKSYQISNYEW 703
|
....*...
gi 127773 754 RLGTTKVF 761
Cdd:cd14938 704 MIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1019-1874 |
2.20e-37 |
|
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: 154.44 E-value: 2.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1019 KLKAKLEQA---LDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQEnvedlervKRELEENVRRKEAEIS-----SLNSK 1090
Cdd:TIGR02168 169 KYKERRKETerkLERTRENLDRLEDILNELERQLKSLERQAEKAER--------YKELKAELRELELALLvlrleELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1091 LEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAggatSAQIELNKKREAELLK 1170
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL----EQQKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1171 IRRDLEEASLQHEAQisalRKKHQDAANEMADQVDQLQKvksklekdkkdlkrEMDDLESQMTHnmknkgcSEKVMKQFE 1250
Cdd:TIGR02168 317 QLEELEAQLEELESK----LDELAEELAELEEKLEELKE--------------ELESLEAELEE-------LEAELEELE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1251 SQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDAR-----RSLEEETRARSK 1325
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELEE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1326 LQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFES-EGANRTE-ELEDQKRKLLGKLSEAEQTTEA 1403
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlEGFSEGVkALLKNQSGLSGILGVLSELISV 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1404 ANAKCSALEKA-KSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIK 1482
Cdd:TIGR02168 532 DEGYEAAIEAAlGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFD 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1483 ASIEEYQDSIGALRRENKNLADEIHDLT-------------DQLSEGGRSTHELDKAR-----RRLEMEK-EELQAALEE 1543
Cdd:TIGR02168 612 PKLRKALSYLLGGVLVVDDLDNALELAKklrpgyrivtldgDLVRPGGVITGGSAKTNssileRRREIEElEEKIEELEE 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1544 AEGALEQEEAKVMRAQLEIATVRNEIDKRIQEKEEEFDNTR------RNHQRALESMQASLEAEakgKADAMRIKKKLEQ 1617
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRkdlarlEAEVEQLEERIAQLSKE---LTELEAEIEELEE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1618 DINELEVALDASNRGKAEMEKTVKRYQQQ-------IREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALE 1690
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEElkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1691 QAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADAARLADELRAEQ 1770
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1771 DHSNQVEKVRKNLESQVKE-FQIRLDEAEASSLKgGKKMIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAF 1849
Cdd:TIGR02168 929 LRLEGLEVRIDNLQERLSEeYSLTLEEAEALENK-IEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTA 1007
|
890 900
....*....|....*....|....*
gi 127773 1850 QADEDRKNQERLQELIDKLNAKIKT 1874
Cdd:TIGR02168 1008 QKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
947-1734 |
8.36e-33 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 139.42 E-value: 8.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 947 LKKDIGDLENTLQKAEQDKAHKDN----QISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCNHLNKLKA 1022
Cdd:TIGR02168 198 LERQLKSLERQAEKAERYKELKAElrelELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1023 KLEQALDELEDNLEREKKVRGDVEKAKRK-------VEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQ 1095
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQIlrerlanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1096 NLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGATSAQIELNKKREAELLKIRRDL 1175
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1176 EEASL-QHEAQISALRKKHQDAANEMADQVDQLQKVKSKLEKDKKDLKR---EMDDLESQMThNMKNKGCSEKVMKQFES 1251
Cdd:TIGR02168 438 LQAELeELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQlqaRLDSLERLQE-NLEGFSEGVKALLKNQS 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1252 QMSDLNARLEDSQRSINELQSQKSRLQAENSD--LTRQLEDAEHRVSVLSKEKSQLSSQLE---DARRSLEEETRARSKL 1326
Cdd:TIGR02168 517 GLSGILGVLSELISVDEGYEAAIEAALGGRLQavVVENLNAAKKAIAFLKQNELGRVTFLPldsIKGTEIQGNDREILKN 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1327 QNEVRNMHADMDAIREQLE-------------EEQESKSDVQRQLSKANNEI----QQWRSKFESEGA------------ 1377
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRkalsyllggvlvvDDLDNALELAKKLRPGYRIVtldgDLVRPGGVITGGsaktnssilerr 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1378 NRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKV 1457
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1458 NSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEEL 1537
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1538 QAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKrIQEKEEEFDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQ 1617
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1618 DINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRctlmsgEVEELRAALEQAERARK 1697
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR------RLKRLENKIKELGPVNL 989
|
810 820 830
....*....|....*....|....*....|....*..
gi 127773 1698 ASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAM 1734
Cdd:TIGR02168 990 AAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1163-1906 |
2.96e-32 |
|
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: 137.88 E-value: 2.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1163 KREAELLKIRRDLEEASLQHEAQISALRKKhqdaanEMADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTHNMKNKGCS 1242
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLVLRLE------ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1243 EKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRA 1322
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1323 RSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEGANRtEELEDQKRKLLGKLSEAEQttE 1402
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR-ERLQQEIEELLKKLEEAEL--K 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1403 AANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSA------ 1476
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllknqs 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1477 ----------ELYRI----KASIEEY-QDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKAR-RRLEMEKEELQAA 1540
Cdd:TIGR02168 517 glsgilgvlsELISVdegyEAAIEAAlGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKgTEIQGNDREILKN 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1541 LEEAEGALEQEEAKVMRAQLEIA----------TVRNEIDKRIQEKEEEFDNTRRNHQRALESMQASLEAEAKGKADAMR 1610
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRKALSyllggvlvvdDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERR 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1611 IK-KKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRC-------TLMSGEV 1682
Cdd:TIGR02168 677 REiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqleeriAQLSKEL 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1683 EELRAALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADAARL 1762
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1763 ADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEaSSLKGGKKMIQKLESRVHELEAELDNEQRRhaetqknMRKADR 1842
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE-SELEALLNERASLEEALALLRSELEELSEE-------LRELES 908
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127773 1843 RLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEAEEIAA-INLAKYRKAQHELEEAEER 1906
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLeEAEALENKIEDDEEEARRR 973
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
839-1655 |
1.59e-31 |
|
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: 135.18 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 839 IARQEEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTL----------LEQKNDLF-LQLQTLEDSMGDQEERVEKLIM 907
Cdd:TIGR02168 167 ISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLerqaekaeryKELKAELReLELALLVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 908 QKADFESQIKELEERLLDEEDAAADLEGIKKKMEADNA-------NLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEIS 980
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 981 QQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLERekkVRGDVEKAKRKVEQDLKSTQ 1060
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET---LRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1061 ENVEDLERVKRELEENVRRKEAEISSL-NSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRE 1139
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1140 LEELGERLD---------EAGGATSAQIELNKKREAELLKIRRDLEEASLQHEAQISALRKKHQDA-----ANEMADQVD 1205
Cdd:TIGR02168 484 LAQLQARLDslerlqenlEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvvenLNAAKKAIA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1206 QLQKVKSKLEKDKKDLKREMDDLESQMTHNMKNKGCSEKVMKQFESQMSDLNARLED--SQ----RSINELQSQKSRLQA 1279
Cdd:TIGR02168 564 FLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllGGvlvvDDLDNALELAKKLRP 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1280 ENSDLTRQLE-----------DAEHRVSVLSKEKS--QLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEE 1346
Cdd:TIGR02168 644 GYRIVTLDGDlvrpggvitggSAKTNSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1347 EQESKSDVQRQLSKANNEIQQWRSKFESEGANRTEeLEDQKRKLLGKLSEAEQTTEAANAKcsalekaKSRLQQELEDMS 1426
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTE-LEAEIEELEERLEEAEEELAEAEAE-------IEELEAQIEQLK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1427 IEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEI 1506
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1507 HDLTDQLSeggrsthELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDK---RIQEKEEEFdnt 1583
Cdd:TIGR02168 876 EALLNERA-------SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGlevRIDNLQERL--- 945
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 1584 rRNHQRALESMQASLEAEAKGKADAMRIK-KKLEQDINEL-EVALDASNrgkaEMEKTVKRYQ---QQIREMQTSIE 1655
Cdd:TIGR02168 946 -SEEYSLTLEEAEALENKIEDDEEEARRRlKRLENKIKELgPVNLAAIE----EYEELKERYDfltAQKEDLTEAKE 1017
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
103-709 |
4.34e-31 |
|
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: 133.33 E-value: 4.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 103 LRSRYTSGLIYTYSGLFCIAV-NPYRRL------PIYTDSVIAKY--RGKRKTEIPPHLFSVADNAYQNMVTDREN---- 169
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMAVmNPYRLLqtarftSIYDEQVVLTYadTANAETVLAPHPFAIAKQSLVRLFFDNEHtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 170 ---------------QSCLITGESGAGKTENTKKVIMYLAKVACAVKKKDEEASDKKEGS-------------------- 214
Cdd:cd14894 87 pstissnrsmtegrgQSLFLCGESGSGKTELAKDLLKYLVLVAQPALSKGSEETCKVSGStrqpkiklftsstkstiqmr 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 215 ------------------------------------------------------------LEDQ---------------- 218
Cdd:cd14894 167 teeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehLEDEeqlrmyfknphaakkl 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 219 --IIQANPVLEAYGNAKTTRNNNSSRFGKF--IRIHFGPTG---KIAGADIETYLLEKSRVTYQQSAER------NYHIF 285
Cdd:cd14894 247 siVLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERGRESgdqnelNFHIL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 286 YQICS--NAIPEL----NDVMLVTPDSGLYSFINQ------GCLTVDNI--DDVEEFKLCDEAFDILGFTKEEKQSMFKC 351
Cdd:cd14894 327 YAMVAgvNAFPFMrllaKELHLDGIDCSALTYLGRsdhklaGFVSKEDTwkKDVERWQQVIDGLDELNVSPDEQKTIFKV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 352 TASILHMG--EMKFKQRPREEQAESDGTAEA-EKVAFLCGINAGDLLKALLKPK---VKVGTEMVTKGQNMNQVVNSVGA 425
Cdd:cd14894 407 LSAVLWLGniELDYREVSGKLVMSSTGALNApQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRDT 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 426 LAKSLYDRMFNWLVRRVNKT--------------LDTKAKRNYYIGVL---DIAGFEIFDFNSFEQLCINYTNERLqqFF 488
Cdd:cd14894 487 LARLLYQLAFNYVVFVMNEAtkmsalstdgnkhqMDSNASAPEAVSLLkivDVFGFEDLTHNSLDQLCINYLSEKL--YA 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 489 NHHMFILEQEEYKKEGIAWefiDFGMDLqmcIDLIEKPMGILSILEEECMFPKADDKSFQDKLYQNHMGKNRMFTK---- 564
Cdd:cd14894 565 REEQVIAVAYSSRPHLTAR---DSEKDV---LFIYEHPLGVFASLEELTILHQSENMNAQQEEKRNKLFVRNIYDRnssr 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 565 -PGKPTRPNQGPAH---------FELHHYAGNVPYSITGWLEKNKDPINENVVALLGASKEPLVAELFK-------APEE 627
Cdd:cd14894 639 lPEPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNessqlgwSPNT 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 628 PAGGGKKKKGKSSAFQTISAVHRESLNKLMKNLYSTHPHFVRCIIPNELKQPGLVDAELVLHQLQCNGVLEGIRICRKGF 707
Cdd:cd14894 719 NRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRNSS 798
|
..
gi 127773 708 PS 709
Cdd:cd14894 799 SS 800
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1129-1906 |
8.81e-31 |
|
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: 132.88 E-value: 8.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1129 VEKQRAElnRELEELGERLDEAggatsaQIELNKKREaELLKIRRDLEEASlqheaQISALRKKHQDA-ANEMADQVDQL 1207
Cdd:TIGR02169 170 RKKEKAL--EELEEVEENIERL------DLIIDEKRQ-QLERLRREREKAE-----RYQALLKEKREYeGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1208 QKVKSKLEKDKKDLKREMDDLESQMTHNMKNKGCSEKVMKQFESQMSDLNA-RLEDSQRSINELQSQKSRLQAENSDLTR 1286
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1287 QLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQEsksdvqrqlskannEIQ 1366
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK--------------EFA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1367 QWRSKFESeganRTEELEDQKRKLlgklseaeqtteaanakcSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAF 1446
Cdd:TIGR02169 382 ETRDELKD----YREKLEKLKREI------------------NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1447 DKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIhDLTDQLSEGGRSTHELDKA 1526
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA-RASEERVRGGRAVEEVLKA 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1527 RRR--------LEMEKEELQAALEEAEGALEQ----EEAKVMRAQLEIATVRN---------------EIDKRIQEKEE- 1578
Cdd:TIGR02169 519 SIQgvhgtvaqLGSVGERYATAIEVAAGNRLNnvvvEDDAVAKEAIELLKRRKagratflplnkmrdeRRDLSILSEDGv 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1579 --------EFDNTRRNHQR-------ALESMQA-----------SLEAEAKGKADAM-----------RIKKKLEQDINE 1621
Cdd:TIGR02169 599 igfavdlvEFDPKYEPAFKyvfgdtlVVEDIEAarrlmgkyrmvTLEGELFEKSGAMtggsraprggiLFSRSEPAELQR 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1622 LEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAERARKASDN 1701
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1702 ELADANDRVNELTSQVSSVQGQKRKLEGDINamQTDLDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVEKVRK 1781
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1782 NLESQVKEFQIRLDE--AEASSLKGGKK----MIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDR 1855
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSieKEIENLNGKKEeleeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 127773 1856 KNQERLQELIDKLNAKIKTFKRQVEEAEEIAAiNLAKYRKAQHELEEAEER 1906
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLEDVQAELQRVEEE 966
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1258-1920 |
2.29e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 131.72 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1258 ARLEDSqrsINELQSQKSRLQAENS------DLTRQLEDAEHRVSVLSKEksQLSSQLEDARRSLEEETRARSKLQNEVR 1331
Cdd:TIGR02168 189 DRLEDI---LNELERQLKSLERQAEkaerykELKAELRELELALLVLRLE--ELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1332 NMHADMDAIREQLEEEQESKSDVQRQLSKANNEIqqwrSKFESE---GANRTEELEDQKRKLLGKLSEAEQTTEAANAKC 1408
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEI----SRLEQQkqiLRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1409 SALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEY 1488
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1489 QDSIGALRRENKNLadEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIA---TV 1565
Cdd:TIGR02168 420 QQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDsleRL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1566 RNEIDKRIQEKEEEFDN----------------TRRNHQRALE-----SMQA--------------SLEAEAKGKADAMR 1610
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNqsglsgilgvlselisVDEGYEAAIEaalggRLQAvvvenlnaakkaiaFLKQNELGRVTFLP 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1611 IKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIRE----------MQTSIEEEQRQRDEARESYNM---------- 1670
Cdd:TIGR02168 578 LDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllggvlVVDDLDNALELAKKLRPGYRIvtldgdlvrp 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1671 ------------------------AERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRK 1726
Cdd:TIGR02168 658 ggvitggsaktnssilerrreieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1727 LEGDINAMQTDLDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEASslkggk 1806
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE------ 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1807 kmIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEAEE-I 1885
Cdd:TIGR02168 812 --LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEaL 889
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 127773 1886 AAINLAKY-------------RKAQHELEEAEERADTADSTLQKFRAK 1920
Cdd:TIGR02168 890 ALLRSELEelseelreleskrSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
843-1586 |
4.10e-30 |
|
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: 130.57 E-value: 4.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 843 EEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVT-LLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQIKELEE 921
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQALLKEKREYEGYeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 922 RLLDEEdaaadlEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALE---E 998
Cdd:TIGR02169 273 LLEELN------KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEreiE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 999 ANKKTSDSLQAE-EDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVE---QDLKSTQENVEDLERVKRELE 1074
Cdd:TIGR02169 347 EERKRRDKLTEEyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINelkRELDRLQEELQRLSEELADLN 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1075 ENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERL----DEA 1150
Cdd:TIGR02169 427 AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseERV 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1151 GGATSAQIELNKKRE------AELLKIRRD----LEEAS------------LQHEAQISALRKKHQDAA-----NEMADQ 1203
Cdd:TIGR02169 507 RGGRAVEEVLKASIQgvhgtvAQLGSVGERyataIEVAAgnrlnnvvveddAVAKEAIELLKRRKAGRAtflplNKMRDE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1204 VDQLQKVKSKLEKDKKDLKRE------------------MDDLES----------------------QMTHNMKNKGCSE 1243
Cdd:TIGR02169 587 RRDLSILSEDGVIGFAVDLVEfdpkyepafkyvfgdtlvVEDIEAarrlmgkyrmvtlegelfeksgAMTGGSRAPRGGI 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1244 KVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRAR 1323
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1324 SKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKfesEGANRTEELEDQKRKLLGKLSEAEQTTEA 1403
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP---EIQAELSKLEEEVSRIEARLREIEQKLNR 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1404 ANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKA 1483
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1484 SIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHEL------DKARRRLEMEKEELQA---ALEEAEGALEQEEAK 1554
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipeeELSLEDVQAELQRVEEeirALEPVNMLAIQEYEE 983
|
810 820 830
....*....|....*....|....*....|....*
gi 127773 1555 VMRAQLEIATVRNEID---KRIQEKEEEFDNTRRN 1586
Cdd:TIGR02169 984 VLKRLDELKEKRAKLEeerKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1022-1734 |
1.45e-29 |
|
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: 129.03 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1022 AKLEQALDELEDNLEREKKVRGDVEKAKRKVE--QDLKSTQENVEDLERVKRELE-----ENVRRKEAEISSLNSKLEDE 1094
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLErlRREREKAERYQALLKEKREYEgyellKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1095 QNLVSQLQRKIKELQARIeeleeeleaernarAKVEKQRAELNRELEELGE----RLDEAGGATSAQIELNKKREAELLK 1170
Cdd:TIGR02169 250 EEELEKLTEEISELEKRL--------------EEIEQLLEELNKKIKDLGEeeqlRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1171 IRRDLEEASLQHEAQISALRKKHQDAANEMADQVDQLQKVKSKLEKDKKdlkrEMDDLESQMthnmknkGCSEKVMKQFE 1250
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE----ELEDLRAEL-------EEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1251 SQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEV 1330
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1331 RNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKfESEGANRTEELEDQKRKL------LGKLSEAEQT---- 1400
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER-VRGGRAVEEVLKASIQGVhgtvaqLGSVGERYATaiev 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1401 ------------TEAANAKCSALEKAK----------SRLQQELEDMS--------------IEVDRANAS--------- 1435
Cdd:TIGR02169 544 aagnrlnnvvveDDAVAKEAIELLKRRkagratflplNKMRDERRDLSilsedgvigfavdlVEFDPKYEPafkyvfgdt 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1436 --VNQMEKKQR-------------AFDKT----------------TAEWQAKVNSLQSELENSQKESRGYSAELYRIKAS 1484
Cdd:TIGR02169 624 lvVEDIEAARRlmgkyrmvtlegeLFEKSgamtggsraprggilfSRSEPAELQRLRERLEGLKRELSSLQSELRRIENR 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1485 IEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIAT 1564
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1565 VRNEID-KRIQEKEEEFDNTRRNHQR----------ALESMQASLEAEAKGKADAMRIKKKLEQDINELEVALDASNRGK 1633
Cdd:TIGR02169 784 LEARLShSRIPEIQAELSKLEEEVSRiearlreieqKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1634 AEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNEL 1713
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
810 820
....*....|....*....|....*..
gi 127773 1714 TSQVSS------VQGQKRKLEGDINAM 1734
Cdd:TIGR02169 944 EEIPEEelsledVQAELQRVEEEIRAL 970
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1286-1920 |
3.18e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 121.32 E-value: 3.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1286 RQLEDAEH---RVSVLSKEksqLSSQLEDARRSLEEETRARsKLQNEVRNMH-----ADMDAIREQLEEEQESKSDVQRQ 1357
Cdd:TIGR02168 179 RKLERTREnldRLEDILNE---LERQLKSLERQAEKAERYK-ELKAELRELElallvLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1358 LSKANNEIQQWRSKFEseganrteELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVN 1437
Cdd:TIGR02168 255 LEELTAELQELEEKLE--------ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1438 QMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGG 1517
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1518 RSTHELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNE--------IDKRIQEKEEEFDNTRRNHQR 1589
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELErleealeeLREELEEAEQALDAAERELAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1590 ------ALESMQASLEAEAKGKADAMRIKKKLEQDI----------NELEVALDA------------------------- 1628
Cdd:TIGR02168 487 lqarldSLERLQENLEGFSEGVKALLKNQSGLSGILgvlselisvdEGYEAAIEAalggrlqavvvenlnaakkaiaflk 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1629 -SNRGKAEM--EKTVKRYQQQIREMQ------------------------------------TSIEEEQRQRDEARESYN 1669
Cdd:TIGR02168 567 qNELGRVTFlpLDSIKGTEIQGNDREilkniegflgvakdlvkfdpklrkalsyllggvlvvDDLDNALELAKKLRPGYR 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1670 M----------------------------------AERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNELTS 1715
Cdd:TIGR02168 647 IvtldgdlvrpggvitggsaktnssilerrreieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1716 QVSSVQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLD 1795
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1796 EAEASslkggkkmIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTF 1875
Cdd:TIGR02168 807 ELRAE--------LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 127773 1876 KRQVEEAEEIAAINLAKYRKAQHELEEAEERADTADSTLQKFRAK 1920
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1258-1908 |
8.51e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.11 E-value: 8.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1258 ARLEDSqrsINELQSQKSRL--QAENS----DLTRQLEDAEHRVSVLSKEksQLSSQLEDARRSLEEETRARSKLQNEVR 1331
Cdd:COG1196 189 ERLEDI---LGELERQLEPLerQAEKAeryrELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1332 NMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRskfesegaNRTEELEDQKRKLLGKLSEAEQTTEAANAKCSAL 1411
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLE--------QDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1412 EKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKEsrgysaelyrikasIEEYQDS 1491
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA--------------AAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1492 IGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDK 1571
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1572 RIQEKEEefdntRRNHQRALESMQASLEAEAKGKAdAMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQ 1651
Cdd:COG1196 482 LLEELAE-----AAARLLLLLEAEADYEGFLEGVK-AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1652 TSIEEEQRQRDEAREsynmAERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDI 1731
Cdd:COG1196 556 DEVAAAAIEYLKAAK----AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1732 NAMQTDLDEMHGELKGADERckkAMADAARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEASSLKGGKKMIQK 1811
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTL---EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1812 LESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEAEeiaAINLA 1891
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG---PVNLL 785
|
650
....*....|....*..
gi 127773 1892 kyrkAQHELEEAEERAD 1908
Cdd:COG1196 786 ----AIEEYEELEERYD 798
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1019-1656 |
2.30e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.57 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1019 KLKAKLEQALDELED---NLEREKKVRGDVEKakrkveQdLKSTQENVEDLERVkRELEENVRRKEAEISSLnsKLEDEQ 1095
Cdd:COG1196 169 KYKERKEEAERKLEAteeNLERLEDILGELER------Q-LEPLERQAEKAERY-RELKEELKELEAELLLL--KLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1096 NLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGgATSAQIELNKKREAELlkiRRDL 1175
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-AELARLEQDIARLEER---RREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1176 EEASLQHEAQISALRKKHQDAANEMADQVDQLQKVKSKLEKDKKDLKREmddlesqmthnmknkgcsEKVMKQFESQMSD 1255
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA------------------EEALLEAEAELAE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1256 LNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHA 1335
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1336 DMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFES-EGANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKA 1414
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLlLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1415 KSRLQQELEDMSIEVDRANASVnqmEKKQRAFDKTTAEWQAK---VNSLQSELENSQKESRGYSAELYRIKASIEEYQDs 1491
Cdd:COG1196 537 EAALEAALAAALQNIVVEDDEV---AAAAIEYLKAAKAGRATflpLDKIRARAALAAALARGAIGAAVDLVASDLREAD- 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1492 iGALRRENKNLADEIHDLTDQLSEGGRS-THELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVR-NEI 1569
Cdd:COG1196 613 -ARYYVLGDTLLGRTLVAARLEAALRRAvTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERlAEE 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1570 DKRIQEKEEEFDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIRE 1649
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
....*..
gi 127773 1650 MQTSIEE 1656
Cdd:COG1196 772 LEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1380-1914 |
5.25e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.41 E-value: 5.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1380 TEELEDQkrklLGKLS-EAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVN 1458
Cdd:COG1196 195 LGELERQ----LEPLErQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1459 SLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQ 1538
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1539 AALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQEKEEEfDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQD 1618
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1619 INELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESynMAERRCTLMSGEVEELRAALEQAERARKA 1698
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA--LAELLEELAEAAARLLLLLEAEADYEGFL 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1699 SDNELADANDRVNELTSQVSSVQGQKRKLEGDI-----NAMQTDLDEMHGELKGADERCKKAMADAARL-------ADEL 1766
Cdd:COG1196 508 EGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaalaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpldkirARAA 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1767 RAEQDHSNQVEKVRKNLESQVKEFQIRL---------DEAEASSLKGGKKMIQKLESRVHELEAELDNEQRRHAET---- 1833
Cdd:COG1196 588 LAAALARGAIGAAVDLVASDLREADARYyvlgdtllgRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTggsr 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1834 QKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEAEEIAAINLAKYRKAQHELEEAEERADTADST 1913
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
.
gi 127773 1914 L 1914
Cdd:COG1196 748 L 748
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1255-1874 |
7.65e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.94 E-value: 7.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1255 DLNARLEdsQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMH 1334
Cdd:COG1196 217 ELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1335 ADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEGAnRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKA 1414
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1415 KSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGA 1494
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1495 LRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQ 1574
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1575 EKEEEFDNTRRnhqrALESMQASLEAEAKGKADAMRIKKKLEQDINELevALDASNRGKAEMEKTVKRYQQQIREMQTSI 1654
Cdd:COG1196 534 AAYEAALEAAL----AAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL--PLDKIRARAALAAALARGAIGAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1655 EEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAM 1734
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1735 QTDLDEMHGELKGADERCKKAMADA-ARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEASSLKGGKKmIQKLE 1813
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAeEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD-LEELE 766
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1814 SRVHELEAELDN---------EQrrHAETQKnmrkadrRLKELAFQADEDRKNQERLQELIDKLNAKIKT 1874
Cdd:COG1196 767 RELERLEREIEAlgpvnllaiEE--YEELEE-------RYDFLSEQREDLEEARETLEEAIEEIDRETRE 827
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1276-1910 |
1.17e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.17 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1276 RLQAENSDLTRqLEDaehRVSVLSKEKSQLSSQLEDARR----SLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESK 1351
Cdd:COG1196 180 KLEATEENLER-LED---ILGELERQLEPLERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1352 SDVQRQLSKANNEIQQWRSKFEseganrteELEDQKRKLLGKLSEAEQTTEAanakcsaLEKAKSRLQQELEDMSIEVDR 1431
Cdd:COG1196 256 EELEAELAELEAELEELRLELE--------ELELELEEAQAEEYELLAELAR-------LEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1432 ANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTD 1511
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1512 QLSEGGRSTHELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIAtvrneidkriqEKEEEFDNTRRNHQRAL 1591
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA-----------ELEEEEEALLELLAELL 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1592 ESMQASLEAEAKGKADAMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMA 1671
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1672 ERRCTlmsgEVEELRAALEQAERARKASDNELADANDRVNELTSQVSsvqgQKRKLEGDINAMQTDLDEmhgelkgaDER 1751
Cdd:COG1196 550 NIVVE----DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAAL----ARGAIGAAVDLVASDLRE--------ADA 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1752 CKKAMADAARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEASSLKGGKKMIQKLESRVHELEAELDNEQRRHA 1831
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127773 1832 ETQKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEAEEIAAINLAKYRKAQHELEEAEERADTA 1910
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1092-1791 |
8.12e-22 |
|
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: 103.66 E-value: 8.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1092 EDEQNLVSQLQRKIKELQARIEELEEELeaernarakvEKQRAELNRELEELGERLDEAGGATSAQIELNKKREAELLKI 1171
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRLNESNELH----------EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1172 RRDLEEASlqHEaqISALRKKHQDAANEMADQVDQLQK-----------VKSKLEKDKKDLKREMDDLESQMTHNMKNKG 1240
Cdd:pfam15921 144 RNQLQNTV--HE--LEAAKCLKEDMLEDSNTQIEQLRKmmlshegvlqeIRSILVDFEEASGKKIYEHDSMSTMHFRSLG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1241 CS-EKVMKQFESQMSDLNARL---EDSQRSI-NELQSQKSRLQAENSDLTRQLeDAEHRVSV--LSKEKSQLSSQLEDAR 1313
Cdd:pfam15921 220 SAiSKILRELDTEISYLKGRIfpvEDQLEALkSESQNKIELLLQQHQDRIEQL-ISEHEVEItgLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1314 RSLE---EETRARSKL-QNEVRNMHADMDAIREQLEEEQESKSD----VQRQLSKANNEIQQWRS---KFESEGANrtee 1382
Cdd:pfam15921 299 SQLEiiqEQARNQNSMyMRQLSDLESTVSQLRSELREAKRMYEDkieeLEKQLVLANSELTEARTerdQFSQESGN---- 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1383 LEDQKRKLLGKLSEAEQTTeaanakcsALEKAKSR---------------LQQELEDMSIEVDRANASVNQME------- 1440
Cdd:pfam15921 375 LDDQLQKLLADLHKREKEL--------SLEKEQNKrlwdrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKsecqgqm 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1441 KKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGalrrenknladeihDLTDQLSEGGRST 1520
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS--------------DLTASLQEKERAI 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1521 H----ELDKARRRLEMEKEELQAALEEAEGALE-QEEAKVMRAQLE-----IATVRNEIDKRIQ---------------- 1574
Cdd:pfam15921 513 EatnaEITKLRSRVDLKLQELQHLKNEGDHLRNvQTECEALKLQMAekdkvIEILRQQIENMTQlvgqhgrtagamqvek 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1575 -EKEEEFDNTRRNHQ-------------RALESMQASLEAE----AKGKADAMR----IKKKLEQDINELEVALDASN-- 1630
Cdd:pfam15921 593 aQLEKEINDRRLELQefkilkdkkdakiRELEARVSDLELEkvklVNAGSERLRavkdIKQERDQLLNEVKTSRNELNsl 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1631 -----------RGKAE-MEKTVKRYQQQIREMQTSIEEEQR--QRDEARESYNMA-----ERRCTLMSGEVEELRAALEQ 1691
Cdd:pfam15921 673 sedyevlkrnfRNKSEeMETTTNKLKMQLKSAQSELEQTRNtlKSMEGSDGHAMKvamgmQKQITAKRGQIDALQSKIQF 752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1692 AERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADAARLADELRAEQD 1771
Cdd:pfam15921 753 LEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQ 832
|
810 820
....*....|....*....|
gi 127773 1772 HSNQVeKVRKNLEsqVKEFQ 1791
Cdd:pfam15921 833 ESVRL-KLQHTLD--VKELQ 849
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1287-1918 |
1.51e-21 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 102.84 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1287 QLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQ--------NEVRNMHADMDAIREQLEEEQESKSDVQRQL 1358
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKReyegyellKEKEALERQKEAIERQLASLEEELEKLTEEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1359 SKANNEIQQWRSKFESEGANRTEELEDQKRKLLGKLSEAEqtteaanAKCSALEKAKSRLQQELEDMSIEVDRANASVNQ 1438
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELE-------AEIASLERSIAEKERELEDAEERLAKLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1439 MEKKQRAFDKTTAEWQAKVNSLQSELENSQ--------------KESRGYSAELYRIKASIEEYQDSIGALRRENKNLAD 1504
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRDKLTEEYAELKeeledlraeleevdKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1505 EIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEID---KRIQEKEEEFD 1581
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDrveKELSKLQRELA 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1582 ntrrnhqRALESMQASLEAEAKGKADAMRIKKKL--------------EQDINELEVAldASNRGKA---EMEKTVKRYQ 1644
Cdd:TIGR02169 494 -------EAEAQARASEERVRGGRAVEEVLKASIqgvhgtvaqlgsvgERYATAIEVA--AGNRLNNvvvEDDAVAKEAI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1645 QQIREMQ-------------------------------------------------------TSIEEEQRQRDEAR---- 1665
Cdd:TIGR02169 565 ELLKRRKagratflplnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvvEDIEAARRLMGKYRmvtl 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1666 ---------------ESYNMAERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGD 1730
Cdd:TIGR02169 645 egelfeksgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKE 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1731 INAMQTDLDEMHGELKGADER---CKKAMADAARLADELRAE----QDHSNQVEKVRKNLESQVKEFQIRLDEAEASSLk 1803
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDlssLEQEIENVKSELKELEARieelEEDLHKLEEALNDLEARLSHSRIPEIQAELSKL- 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1804 ggKKMIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEAE 1883
Cdd:TIGR02169 804 --EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881
|
730 740 750
....*....|....*....|....*....|....*.
gi 127773 1884 EiAAINLAKYR-KAQHELEEAEERADTADSTLQKFR 1918
Cdd:TIGR02169 882 S-RLGDLKKERdELEAQLRELERKIEELEAQIEKKR 916
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
972-1571 |
1.59e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.32 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 972 ISTLQGEISQQdehIGKLNKEKKALEEANKktsdsLQAEEDKC---------NHLNKLKAKLEQALDELEDNLEREKKVR 1042
Cdd:COG1196 191 LEDILGELERQ---LEPLERQAEKAERYRE-----LKEELKELeaellllklRELEAELEELEAELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1043 GDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAE 1122
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1123 RNARAKVEKQRAELNRELEELGERLDEAGGATSAQIELNKKREAELLKIRRDLEEAslqhEAQISALRKKHQDAANEMAD 1202
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL----AAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1203 QVDQLQKVKSKLEKDKKDLKREMDDLESQmthnmknkgcsekvmkqfESQMSDLNARLEDSQRSINELQSQKSRLQAENS 1282
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEA------------------AEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1283 DLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARskLQNEVRNMHADMDAIREQLEE-EQESKSDVQRQLSKA 1361
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG--LAGAVAVLIGVEAAYEAALEAaLAAALQNIVVEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1362 NNEIQQWRSKFESEGANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAK---SRLQQELEDMSIEVDRANASVNQ 1438
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADaryYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1439 MEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGR 1518
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 127773 1519 STHELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDK 1571
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1025-1889 |
3.38e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 101.76 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1025 EQALDELEDNLERE--KKVRGDVEKAKRKVEQDLKSTQENVEDLERVK--RELEENVRRKEAEISSLNSKLEDEQNLvsQ 1100
Cdd:PTZ00121 1078 DFDFDAKEDNRADEatEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEdaRKAEEARKAEDARKAEEARKAEDAKRV--E 1155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1101 LQRKIKEL-QARIEELEEELEAERNARAKVEKQRAELNRELEELgERLDEAggatsaqielnkkREAEllKIRRDLEEAS 1179
Cdd:PTZ00121 1156 IARKAEDArKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDA-RKAEAA-------------RKAE--EERKAEEARK 1219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1180 LQHEAQISALRKKHQdaANEMADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTHNMKNKGCSEKVMKQFESQMSDlNAR 1259
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEE--AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAK 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1260 LEDSQRSINELQsQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRsleEETRARSKLQNEVRNMHADmda 1339
Cdd:PTZ00121 1297 KAEEKKKADEAK-KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA---EAEAAADEAEAAEEKAEAA--- 1369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1340 irEQLEEEQESKSDVQRQLSKANNEIQQWRSKFEsEGANRTEEL---EDQKRKLLGKLSEAEQTTEAANAKCSALEKAKS 1416
Cdd:PTZ00121 1370 --EKKKEEAKKKADAAKKKAEEKKKADEAKKKAE-EDKKKADELkkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1417 rlqQELEDMSIEVDRANASVNQMEKKQRAFD-KTTAEWQAKVNSLQSELENSQKESRgysaelyRIKASIEEYQDSIGAL 1495
Cdd:PTZ00121 1447 ---DEAKKKAEEAKKAEEAKKKAEEAKKADEaKKKAEEAKKADEAKKKAEEAKKKAD-------EAKKAAEAKKKADEAK 1516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1496 RRENKNLADEIHDltdqlSEGGRSTHELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQE 1575
Cdd:PTZ00121 1517 KAEEAKKADEAKK-----AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE 1591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1576 KEEEFDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIE 1655
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1656 EEQRQRDEARESYNMAERRCTLMSGEVEELRaaleQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDI-NAM 1734
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAK----KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKkKAE 1747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1735 QTDLDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVEKVRKNLESQVKEFQirldEAEASSLKGGKKMiqklES 1814
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF----DNFANIIEGGKEG----NL 1819
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127773 1815 RVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEAEEIAAIN 1889
Cdd:PTZ00121 1820 VINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKID 1894
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
946-1589 |
3.10e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.09 E-value: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 946 NLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCNHLNKLKAKLE 1025
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1026 QALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKI 1105
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1106 KELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAggatsaqielnKKREAELLKIRRDLEEASLQHEAQ 1185
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE-----------EEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1186 ISALRKKHQDAANEMADQVDQLQKVKSklEKDKKDLKREMDDLESQMTHNMKNKGCSEKVMKQFESQMSDLNARledsqr 1265
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAA--RLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY------ 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1266 sinELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKsqlssqLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLE 1345
Cdd:COG1196 537 ---EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAK------AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1346 EEQESKSDVQRQLSKANNEIQQWRSKFESEGANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDM 1425
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1426 SIEVDRANASVNQMEKKQRAfdkttAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADE 1505
Cdd:COG1196 688 LAEEELELEEALLAEEEEER-----ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1506 ihdltdqlseggrstHELDKARRRLEMEKEEL----QAALEEAEGALEQEEAkvMRAQLE-----IATVRN---EIDKRI 1573
Cdd:COG1196 763 ---------------EELERELERLEREIEALgpvnLLAIEEYEELEERYDF--LSEQREdleeaRETLEEaieEIDRET 825
|
650
....*....|....*..
gi 127773 1574 QEK-EEEFDNTRRNHQR 1589
Cdd:COG1196 826 RERfLETFDAVNENFQE 842
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
844-1431 |
2.13e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.39 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 844 EEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTLLeqkndlFLQLQTLEDSMGDQEERVEKLIMQKADFESQIKELEERL 923
Cdd:COG1196 196 GELERQLEPLERQAEKAERYRELKEELKELEAELL------LLKLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 924 LDEEDAAADLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALEEAnkkt 1003
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE---- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1004 sdsLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAE 1083
Cdd:COG1196 346 ---LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1084 ISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGATSAQIELNKK 1163
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1164 REAELLKIRRDLEEASLQHEAQISALR---KKHQDAANEMADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTHNMKNKG 1240
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLigvEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKI 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1241 CSEKVMKQFESQMSDLNAR--LEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLS---KEKSQLSSQLEDARRS 1315
Cdd:COG1196 583 RARAALAAALARGAIGAAVdlVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAgrlREVTLEGEGGSAGGSL 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1316 LEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEGANRTEELEDQKRKLLGKLS 1395
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL 742
|
570 580 590
....*....|....*....|....*....|....*.
gi 127773 1396 EAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDR 1431
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1570-1909 |
1.72e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.69 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1570 DKRIQEKEEEFDNTRRNHQRA------LESMQASLEAEAKgKAdamRIKKKLEQDINELEVALDASNRgkAEMEKTVKRY 1643
Cdd:COG1196 171 KERKEEAERKLEATEENLERLedilgeLERQLEPLERQAE-KA---ERYRELKEELKELEAELLLLKL--RELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1644 QQQIREMQTSIEEEQRQRDEAREsynmaerrctlmsgEVEELRAALEQAERARKASDNELADANDRVNELTSQVSSVQGQ 1723
Cdd:COG1196 245 EAELEELEAELEELEAELAELEA--------------ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1724 KRKLEGDINAMQTDLDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEASSLK 1803
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1804 GGKKmIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEAE 1883
Cdd:COG1196 391 ALRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
330 340
....*....|....*....|....*.
gi 127773 1884 EIAAINLAKYRKAQHELEEAEERADT 1909
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLL 495
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
837-1367 |
5.49e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.77 E-value: 5.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 837 LSIARQEEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQI 916
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 917 KELEERLLDEEDAAADLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKAL 996
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 997 EEANKKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEEN 1076
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1077 VRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNREL---------------- 1140
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavligveaaye 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1141 EELGERLDEAGGATSAQIELNKKREAELLKIRRD-------LEEASLQHEAQISALRKKHQDAANEMADQVDQLQKVKSK 1213
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1214 LEKDKKDLKREMDDLESQMTHNMKNKGcSEKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEH 1293
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAG-RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1294 RVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQ--------ESKSDVQRQLSKANNEI 1365
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpepPDLEELERELERLEREI 776
|
..
gi 127773 1366 QQ 1367
Cdd:COG1196 777 EA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
838-1594 |
5.53e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 90.89 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 838 SIARQEEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQIK 917
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 918 eleerlldeeDAAADLEGIKKKMEADNANLKKDIGDLENTLQKA-EQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKAL 996
Cdd:TIGR02168 397 ----------SLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 997 EEANKKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKvrgdVEKAKRKVEQDLKSTQENVEDLERVKRELEEN 1076
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA----LLKNQSGLSGILGVLSELISVDEGYEAAIEAA 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1077 ---------VRRKEAEISSLNSKLEDEQNLVSQL---QRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELG 1144
Cdd:TIGR02168 543 lggrlqavvVENLNAAKKAIAFLKQNELGRVTFLpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLL 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1145 ERL---DEAGGATSAQIELNKK-----REAELLKIRRDLEEASLQHEAQISALRKKHQDAANEMADQVDQLQKVKsklek 1216
Cdd:TIGR02168 623 GGVlvvDDLDNALELAKKLRPGyrivtLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELE----- 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1217 dkkdlkREMDDLESQMThnmknkgcsekvmkQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVS 1296
Cdd:TIGR02168 698 ------KALAELRKELE--------------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1297 VLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRskfeseg 1376
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE------- 830
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1377 aNRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAK 1456
Cdd:TIGR02168 831 -RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1457 VNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEggrsthELDKARRRLEMEKEE 1536
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE------EARRRLKRLENKIKE 983
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127773 1537 L----QAALEEAEGA------LEQEEAKVMRAQLEIATVRNEIDKRIQEK-EEEFDNTRRNHQRALESM 1594
Cdd:TIGR02168 984 LgpvnLAAIEEYEELkerydfLTAQKEDLTEAKETLEEAIEEIDREARERfKDTFDQVNENFQRVFPKL 1052
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
839-1542 |
4.00e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 88.66 E-value: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 839 IARQEEEMK--EQLKQMDKMK--EDLAKTERIKKeLEEQNVTLLEQKNDlflQLQTLEDSMGDQEERVEKLIMQKADFES 914
Cdd:PTZ00121 1168 EARKAEDAKkaEAARKAEEVRkaEELRKAEDARK-AEAARKAEEERKAE---EARKAEDAKKAEAVKKAEEAKKDAEEAK 1243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 915 QIKELEERLLDEEDAAADLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQgEISQQDEHIGKLNKEKK 994
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD-EAKKKAEEAKKADEAKK 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 995 ALEEANKKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQdLKSTQENVEDLERVKRELE 1074
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA-AKKKAEEKKKADEAKKKAE 1401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1075 ENvRRKEAEIsslnSKLEDEQNLVSQLQRKIKELQariEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGAT 1154
Cdd:PTZ00121 1402 ED-KKKADEL----KKAAAAKKKADEAKKKAEEKK---KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1155 SAQIELNKKREAELLK------------IRRDLEEASLQHEAQISALRKKHQDAAN-EMADQVDQLQKVKSKLEKDKKDL 1221
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKkkaeeakkkadeAKKAAEAKKKADEAKKAEEAKKADEAKKaEEAKKADEAKKAEEKKKADELKK 1553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1222 KREMDDLESQMTHNMKNKGCSEKVM--------KQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEH 1293
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMalrkaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1294 RVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKAnNEIQQWRSKFE 1373
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-KKAEELKKKEA 1712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1374 SEGAN----RTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAK-SRLQQELEDMSIEVDRANASVNQMEKKQRAfDK 1448
Cdd:PTZ00121 1713 EEKKKaeelKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKiAHLKKEEEKKAEEIRKEKEAVIEEELDEED-EK 1791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1449 TTAEWQAKVNSLQSELENSQKESRGYSAELYRIK----ASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELD 1524
Cdd:PTZ00121 1792 RRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKemedSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFN 1871
|
730
....*....|....*...
gi 127773 1525 KARRRLEMEKEELQAALE 1542
Cdd:PTZ00121 1872 KEKDLKEDDEEEIEEADE 1889
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1308-1891 |
5.06e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 84.58 E-value: 5.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1308 QLEDARRSLEEETRARSKLQnevrnmhaDMDAIREQLEEEQESKSDVQRQLSKAnneiQQWRSKFESE-GANRTEELEDQ 1386
Cdd:COG4913 236 DLERAHEALEDAREQIELLE--------PIRELAERYAAARERLAELEYLRAAL----RLWFAQRRLElLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1387 KRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQ-QELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELE 1465
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1466 NSQKESRgysAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLS--EGGRST--HELDKARRRLEME-------- 1533
Cdd:COG4913 384 ALRAEAA---ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslERRKSNipARLLALRDALAEAlgldeael 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1534 ---KEELQAALEE------AEGAL----------EQEEAKVMRA----------------------------------QL 1560
Cdd:COG4913 461 pfvGELIEVRPEEerwrgaIERVLggfaltllvpPEHYAAALRWvnrlhlrgrlvyervrtglpdperprldpdslagKL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1561 EIAT------VRNEIDKRIQ----EKEEEFdntrRNHQRAL-ESMQASLEAEAKGKADAMRIKKK-------------LE 1616
Cdd:COG4913 541 DFKPhpfrawLEAELGRRFDyvcvDSPEEL----RRHPRAItRAGQVKGNGTRHEKDDRRRIRSRyvlgfdnraklaaLE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1617 QDINELEVALDASNRGKAEMEKTVKRYQQQ----------------IREMQTSIEEEQRQRDEARESynmaerrctlmSG 1680
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAELEAELERLDAS-----------SD 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1681 EVEELRAALEQAERARKASDNELADAndrvneltsqvssvQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADaa 1760
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDEL--------------KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA-- 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1761 rLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEasslkggkkmiQKLESRVHELEAELDNEQRRHAETQKNMRKA 1840
Cdd:COG4913 750 -LLEERFAAALGDAVERELRENLEERIDALRARLNRAE-----------EELERAMRAFNREWPAETADLDADLESLPEY 817
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 1841 DRRLKELafQADEDRKNQERLQELIDKLN-AKIKTFKRQVEEA-----EEIAAINLA 1891
Cdd:COG4913 818 LALLDRL--EEDGLPEYEERFKELLNENSiEFVADLLSKLRRAireikERIDPLNDS 872
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
868-1501 |
8.23e-16 |
|
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: 83.53 E-value: 8.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 868 KELEEQNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQIKELEERLLDEEDAAADLEGIKKKMEADNANL 947
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 948 KKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLN-------KEKKALEEANKKTSDSLQAEEDKCNHLNKL 1020
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNnkyndlkKQKEELENELNLLEKEKLNIQKNIDKIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1021 KAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENvrrkEAEISSLNSKLEDEQNlvsQ 1100
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNT----QTQLNQLKDEQNKIKK---Q 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1101 LQRKIKELQarieeleeeleAERNARAKVEKQRAELNRELEELGERLDEaggatsaqiELNKKREAELLKIRRDLEEAsl 1180
Cdd:TIGR04523 269 LSEKQKELE-----------QNNKKIKELEKQLNQLKSEISDLNNQKEQ---------DWNKELKSELKNQEKKLEEI-- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1181 qhEAQISalrkKHQDAANEMADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTHNMKNKGCSEKVMKQFESQMSDLNARL 1260
Cdd:TIGR04523 327 --QNQIS----QNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1261 EDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAI 1340
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1341 REQLEEEQESKSDVQRQLSKANNEIQQWRSKFE------SEGANRTEELEDQKRKLLGKLS--EAEQTTEAANAKCSALE 1412
Cdd:TIGR04523 481 KQNLEQKQKELKSKEKELKKLNEEKKELEEKVKdltkkiSSLKEKIEKLESEKKEKESKISdlEDELNKDDFELKKENLE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1413 KAKSRLQQELEDMSIEVDRANAS-------VNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASI 1485
Cdd:TIGR04523 561 KEIDEKNKEIEELKQTQKSLKKKqeekqelIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
650
....*....|....*.
gi 127773 1486 EEYQDSIGALRRENKN 1501
Cdd:TIGR04523 641 NKLKQEVKQIKETIKE 656
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1062-1674 |
9.06e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 83.57 E-value: 9.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1062 NVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELnRELE 1141
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV-KELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1142 ELGERLDEAggatsaqielnKKREAELLKIRRDLEEASLQHEAQISALRKKHQdaanEMADQVDQLQKVKsKLEKDKKDL 1221
Cdd:PRK03918 235 ELKEEIEEL-----------EKELESLEGSKRKLEEKIRELEERIEELKKEIE----ELEEKVKELKELK-EKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1222 KREMDDLesqmthnmknkgcsEKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQaensDLTRQLEDAEHRVSVLsKE 1301
Cdd:PRK03918 299 SEFYEEY--------------LDELREIEKRLSRLEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEEL-EE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1302 KSQLssqLEDARRSLEEETRARSKLQNEvrnmhaDMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFES------- 1374
Cdd:PRK03918 360 RHEL---YEEAKAKKEELERLKKRLTGL------TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElkkaiee 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1375 -EGANRT----------EELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSiEVDRANASVNQM---E 1440
Cdd:PRK03918 431 lKKAKGKcpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES-ELIKLKELAEQLkelE 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1441 KKQRAFDKTTAEWQAKvnslqsELENSQKESRGYSAELYRIKASIE---EYQDSIGALRRENKNLADEIHDLTDQLSEGG 1517
Cdd:PRK03918 510 EKLKKYNLEELEKKAE------EYEKLKEKLIKLKGEIKSLKKELEkleELKKKLAELEKKLDELEEELAELLKELEELG 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1518 -RSTHELDKARRRLE-------------MEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQE-KEEEFDN 1582
Cdd:PRK03918 584 fESVEELEERLKELEpfyneylelkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKySEEEYEE 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1583 TRRNHQRaLESMQASLEAEAKGkadamrikkkLEQDINELEVALDASNRGKAEMEKtvkrYQQQIREMQTSIEEEQRQRD 1662
Cdd:PRK03918 664 LREEYLE-LSRELAGLRAELEE----------LEKRREEIKKTLEKLKEELEEREK----AKKELEKLEKALERVEELRE 728
|
650
....*....|..
gi 127773 1663 EARESYNMAERR 1674
Cdd:PRK03918 729 KVKKYKALLKER 740
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
845-1658 |
9.62e-16 |
|
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: 83.63 E-value: 9.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 845 EMKEQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNDLFLQLQTL-EDSMGDQEERVEKLIMQKADFESQIKELEERL 923
Cdd:pfam15921 114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLkEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 924 LDEEDAAAdlegiKKKMEADNANlKKDIGDLENTLQKAEQDkahKDNQISTLQGEISQQDEHIGKLNKEKKaleeankkt 1003
Cdd:pfam15921 194 VDFEEASG-----KKIYEHDSMS-TMHFRSLGSAISKILRE---LDTEISYLKGRIFPVEDQLEALKSESQ--------- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1004 sdslqaeedkcnhlNKLKAKLEQALDELEDNL-EREKKVRGDVEKAKRKVEQdLKSTQENVEDLERVKRELEENVRRKEA 1082
Cdd:pfam15921 256 --------------NKIELLLQQHQDRIEQLIsEHEVEITGLTEKASSARSQ-ANSIQSQLEIIQEQARNQNSMYMRQLS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1083 EISSLNSKLEDEQNLVSQL-QRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGATSAQIELN 1161
Cdd:pfam15921 321 DLESTVSQLRSELREAKRMyEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQN 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1162 KKreaellkirrdLEEASLQHEAQISALRKKHQDAANEMADQVDQLQKVKSklekdkkdlkremdDLESQMTHNMKNKGC 1241
Cdd:pfam15921 401 KR-----------LWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKS--------------ECQGQMERQMAAIQG 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1242 SEKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAEN---SDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEE 1318
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSErtvSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQH 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1319 ETRARSKLQN------EVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEGANRTEELEDQK----- 1387
Cdd:pfam15921 536 LKNEGDHLRNvqteceALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdk 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1388 -----RKLLGKLSEAE-QTTEAANAKCSALEKAKSrLQQELEDMSIEVDRANASVNQMEK-----------KQRAFDKTT 1450
Cdd:pfam15921 616 kdakiRELEARVSDLElEKVKLVNAGSERLRAVKD-IKQERDQLLNEVKTSRNELNSLSEdyevlkrnfrnKSEEMETTT 694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1451 AEWQAKVNSLQSELE---NSQKESRGYSAELYRIKASIeeyQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKAR 1527
Cdd:pfam15921 695 NKLKMQLKSAQSELEqtrNTLKSMEGSDGHAMKVAMGM---QKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEK 771
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1528 RRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKR----------IQEKEEEFDNTRRNHQRALESMQ-- 1595
Cdd:pfam15921 772 NKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAslqfaecqdiIQRQEQESVRLKLQHTLDVKELQgp 851
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 127773 1596 -----ASLEAEAKGKADAMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQ 1658
Cdd:pfam15921 852 gytsnSSMKPRLLQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEP 919
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
970-1669 |
1.06e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 83.15 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 970 NQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAK 1049
Cdd:TIGR04523 26 NIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1050 RKVEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKV 1129
Cdd:TIGR04523 106 SKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1130 EKQRAELNRELEELGERLdeaggatsAQIELNKKREAELlkirrdleeaslqhEAQISALRKKHqdaaNEMADQVDQLQK 1209
Cdd:TIGR04523 186 QKNIDKIKNKLLKLELLL--------SNLKKKIQKNKSL--------------ESQISELKKQN----NQLKDNIEKKQQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1210 VKSKLEKDKKDLKREMDDLESQMTHNMKNKGCSEKVMKQFESQMSDLNARLEDSQRSINELQSQKSrlQAENSDLTRQLE 1289
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QDWNKELKSELK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1290 DAEhrvsvlsKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQwr 1369
Cdd:TIGR04523 318 NQE-------KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN-- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1370 skfeseganrteeLEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKT 1449
Cdd:TIGR04523 389 -------------LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1450 TAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSeggrsthELDKARRR 1529
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS-------SLKEKIEK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1530 LEMEKEELQAALEEAEGALEQEEAKVMRAQLEiaTVRNEIDKRIQEKEEEfdntrrnhQRALESMQASLEAEAKGKADAM 1609
Cdd:TIGR04523 529 LESEKKEKESKISDLEDELNKDDFELKKENLE--KEIDEKNKEIEELKQT--------QKSLKKKQEEKQELIDQKEKEK 598
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 127773 1610 R-IKKKLE---QDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYN 1669
Cdd:TIGR04523 599 KdLIKEIEekeKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWP 662
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1260-1823 |
1.07e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.08 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1260 LEDSQRSINELQSQKSrlQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEetrARSKLQnEVRNMHADMDA 1339
Cdd:PRK02224 182 LSDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDE---ADEVLE-EHEERREELET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1340 IREQLEEEQESKSDVQRQLSKANNEIQQWRSkfeseganRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQ 1419
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRE--------RLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1420 QELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRREN 1499
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1500 KNLADEIHDLTDQLSE-GGRSTH---ELDKARRRLEmEKEELQAA------------------LEEAEGALEQEEAKVMR 1557
Cdd:PRK02224 408 GNAEDFLEELREERDElREREAEleaTLRTARERVE-EAEALLEAgkcpecgqpvegsphvetIEEDRERVEELEAELED 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1558 AQLEIATVRNEID--KRIQEKEEEFDnTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDinelevaLDASNRGKAE 1635
Cdd:PRK02224 487 LEEEVEEVEERLEraEDLVEAEDRIE-RLEERREDLEELIAERRETIEEKRERAEELRERAAE-------LEAEAEEKRE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1636 MEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNmaerrctlmsgEVEELRAALEQAERARKASDNELADANDRVNELTS 1715
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLAELKERIESLE-----------RIRTLLAAIADAEDEIERLREKREALAELNDERRE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1716 QVSSVQGQKRKLEGDINAMQTDldemhgELKGADERCKKAMADAARLADELRAEQDH-SNQVEKVRKNLEsQVKEFQIRL 1794
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEARIE------EAREDKERAEEYLEQVEEKLDELREERDDlQAEIGAVENELE-ELEELRERR 700
|
570 580 590
....*....|....*....|....*....|.
gi 127773 1795 DEAEA--SSLKGGKKMIQKLESRVHELEAEL 1823
Cdd:PRK02224 701 EALENrvEALEALYDEAEELESMYGDLRAEL 731
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
29-74 |
1.40e-14 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 69.38 E-value: 1.40e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 127773 29 DGKKNCWVPDEKEGFASAEIQSSKGDEITVKiVADSSTRTVKKDDI 74
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVE-TEDGKTVTVKKDDV 45
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
979-1798 |
1.55e-14 |
|
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: 80.00 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 979 ISQQDEHIgKLNKEKKALEEANKKTSDSLQAEEDkcnHLNKLKAKLEQAldelednlEREKKVRGDVEKAKRKVEQdlks 1058
Cdd:COG3096 302 AEEQYRLV-EMARELEELSARESDLEQDYQAASD---HLNLVQTALRQQ--------EKIERYQEDLEELTERLEE---- 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1059 TQENVEDLERVKRELEENVRRKEAEISSLNSKLED-EQNLVSQLQRKIKELQARieeleeeleaERNARAKVEKQRAELN 1137
Cdd:COG3096 366 QEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADyQQALDVQQTRAIQYQQAV----------QALEKARALCGLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1138 RE-----LEELGERLDEAggaTSAQIELNKKReaellkirRDLEEASLQHEAQISALRKkhqdaaneMADQVDqlqkvKS 1212
Cdd:COG3096 436 PEnaedyLAAFRAKEQQA---TEEVLELEQKL--------SVADAARRQFEKAYELVCK--------IAGEVE-----RS 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1213 KLEKDKKDLKREMDDLESQmthnmknkgcSEKVmKQFESQMSDLNARLE---DSQRSINELQSQKSRLQAENSDLTRQLE 1289
Cdd:COG3096 492 QAWQTARELLRRYRSQQAL----------AQRL-QQLRAQLAELEQRLRqqqNAERLLEEFCQRIGQQLDAAEELEELLA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1290 DAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDA---IREQLEEEQESKSDVQRQLSK-ANNEI 1365
Cdd:COG3096 561 ELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDAlerLREQSGEALADSQEVTAAMQQlLERER 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1366 QQWRSKfeSEGANRTEELEDQKRKLLgklseaeQTTEAANAKCSALekaKSRLQQEL-----EDMSIE------------ 1428
Cdd:COG3096 641 EATVER--DELAARKQALESQIERLS-------QPGGAEDPRLLAL---AERLGGVLlseiyDDVTLEdapyfsalygpa 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1429 -----VDRANASVNQMEKKQ-------------RAFDKTTAEWQakvnslqsELEN------SQKESRgYSaelyRI--- 1481
Cdd:COG3096 709 rhaivVPDLSAVKEQLAGLEdcpedlyliegdpDSFDDSVFDAE--------ELEDavvvklSDRQWR-YS----RFpev 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1482 ----KASIEEyqdSIGALRREnknlADEIHDLTDQLSEGGRSTHELDKARRRL-------------EMEKEELQAALEEA 1544
Cdd:COG3096 776 plfgRAAREK---RLEELRAE----RDELAEQYAKASFDVQKLQRLHQAFSQFvgghlavafapdpEAELAALRQRRSEL 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1545 EGALEQEEAKVMRAQLEIATVRNEID---KRIQEKEEEFDNTrrnHQRALESMQASLEAEAKGKADAMRIKKKLEQdINE 1621
Cdd:COG3096 849 ERELAQHRAQEQQLRQQLDQLKEQLQllnKLLPQANLLADET---LADRLEELREELDAAQEAQAFIQQHGKALAQ-LEP 924
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1622 LEVALDASNRGKAEMEKTVKRYQQQIREMQTSIE--EEQRQRDEAReSYNMAERRCTLMSGEVEELRAALEQAERARKAS 1699
Cdd:COG3096 925 LVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFalSEVVQRRPHF-SYEDAVGLLGENSDLNEKLRARLEQAEEARREA 1003
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1700 DNELADANDRVNE----LTSQVSSVQGQKRKLegdiNAMQTDLDEMhgELKGADERCKKAMADAARLADELRAEQDHSNQ 1775
Cdd:COG3096 1004 REQLRQAQAQYSQynqvLASLKSSRDAKQQTL----QELEQELEEL--GVQADAEAEERARIRRDELHEELSQNRSRRSQ 1077
|
890 900
....*....|....*....|...
gi 127773 1776 VEKVRKNLESQVKEFQIRLDEAE 1798
Cdd:COG3096 1078 LEKQLTRCEAEMDSLQKRLRKAE 1100
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1023-1713 |
2.18e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.19 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1023 KLEQALDELEDNLEREKKVRGDVEKAKRKVEQdLKSTQENVEDLERVKRELEENVRRKEAeisslnskLEDEQNlvsqlQ 1102
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERYAAARERLAELEYLRAA--------LRLWFA-----Q 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1103 RKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGATSAQIelnkkreaellkirrdleeaslqh 1182
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQL------------------------ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1183 EAQISALRKKHQDAANEMADQVDQLQKVKSKLEKDKkdlkremddlesqmthnmknkgcsekvmKQFESQMSDLNARLED 1262
Cdd:COG4913 344 EREIERLERELEERERRRARLEALLAALGLPLPASA----------------------------EEFAALRAEAAALLEA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1263 SQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETR-ARSKLQN-----EVRNMHAD 1336
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGlDEAELPFvgeliEVRPEEER 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1337 -MDAIrEQL----------EEEQEsksdvqRQLSKANNEIqQWRSKFESEGANRTEELEDQK--------RKLLGKLSEA 1397
Cdd:COG4913 476 wRGAI-ERVlggfaltllvPPEHY------AAALRWVNRL-HLRGRLVYERVRTGLPDPERPrldpdslaGKLDFKPHPF 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1398 EQTTEAANAKCSALEKAKSrlQQELEDmsieVDRANASVNQMEKKQRAFDK-----TTAEW------QAKVNSLQSELEN 1466
Cdd:COG4913 548 RAWLEAELGRRFDYVCVDS--PEELRR----HPRAITRAGQVKGNGTRHEKddrrrIRSRYvlgfdnRAKLAALEAELAE 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1467 SQKESRGYSAELYRIKASIEEYQDSIGALRR---------ENKNLADEIHDLTDQLSEGGRSTHELDKARRRLemekEEL 1537
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDASSDDLAALEEQL----EEL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1538 QAALEEAEGALEQEEAKVMRAQLEIATVRNEIDkRIQEKEEEFDNTRRNHQRA-LESMQASLEAEAKGKadamRIKKKLE 1616
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEELD-ELQDRLEAAEDLARLELRAlLEERFAAALGDAVER----ELRENLE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1617 QDINELEVALDASNRgkaEMEKTVKRYQQQ----IREMQTSIE---------EEQRQRD--EAREsyNMAERRCTLMSGE 1681
Cdd:COG4913 773 ERIDALRARLNRAEE---ELERAMRAFNREwpaeTADLDADLEslpeylallDRLEEDGlpEYEE--RFKELLNENSIEF 847
|
730 740 750
....*....|....*....|....*....|..
gi 127773 1682 VEELRAALEQAERarkasdnelaDANDRVNEL 1713
Cdd:COG4913 848 VADLLSKLRRAIR----------EIKERIDPL 869
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1166-1884 |
2.61e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.80 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1166 AELLKIRRDLEEASLQHEA--QISALRKKHQDAANEMADQVDQLQKVKSKLEKdkkdlkREMDDLESQMThnmknkgcse 1243
Cdd:COG4913 235 DDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQ------RRLELLEAELE---------- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1244 kvmkqfesqmsDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRvsvlskEKSQLSSQLEDARRSLEEETRAR 1323
Cdd:COG4913 299 -----------ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1324 SKLQNEVRNMHADMDAIREQLEEEQEsksdvqrqlskannEIQQWRSKFESEganrTEELEDQKRKLLGKLSEAEQTTEA 1403
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRA--------------EAAALLEALEEE----LEALEEALAEAEAALRDLRRELRE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1404 ANAKCSALEKAKSRLQQELEDMS--------------------IEV-----------------------------DRANA 1434
Cdd:COG4913 424 LEAEIASLERRKSNIPARLLALRdalaealgldeaelpfvgelIEVrpeeerwrgaiervlggfaltllvppehyAAALR 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1435 SVNQMEKKQR-------AFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYrikASIEEYQ--DSIGALRRENKNLade 1505
Cdd:COG4913 504 WVNRLHLRGRlvyervrTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAEL---GRRFDYVcvDSPEELRRHPRAI--- 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1506 ihdlTDQ-LSEGGRSTHELDK-------------ARRRLEMEKEELQAALEEAEGAleQEEAKVMRAQLEIATVRNEIDK 1571
Cdd:COG4913 578 ----TRAgQVKGNGTRHEKDDrrrirsryvlgfdNRAKLAALEAELAELEEELAEA--EERLEALEAELDALQERREALQ 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1572 RIQEKEEEFDNTRRnHQRALESMQASLEAEAKGKADAMRIKKKLEqdinELEVALDASNRGKAEMEKTVKRYQQQIREMQ 1651
Cdd:COG4913 652 RLAEYSWDEIDVAS-AEREIAELEAELERLDASSDDLAALEEQLE----ELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1652 TSIEEEQRQRDEAresynmAERRCTLMSGEVEELRAALEQAERARKASDN---ELADANDRVNELTSQVSSVQGQ-KRKL 1727
Cdd:COG4913 727 EELDELQDRLEAA------EDLARLELRALLEERFAAALGDAVERELRENleeRIDALRARLNRAEEELERAMRAfNREW 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1728 EGDINAMQTDLDemhgelkgaderckkAMADAARLADELRAEqdhsnqvekvrkNLESQVKEFQIRLDEAeasslkggkk 1807
Cdd:COG4913 801 PAETADLDADLE---------------SLPEYLALLDRLEED------------GLPEYEERFKELLNEN---------- 843
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 127773 1808 MIQKLESRVHELEAELDNEQRRhaetqknMRKADRRLKELAFQADedrknqERLQ-ELIDKLNAKIKTFKRQVEEAEE 1884
Cdd:COG4913 844 SIEFVADLLSKLRRAIREIKER-------IDPLNDSLKRIPFGPG------RYLRlEARPRPDPEVREFRQELRAVTS 908
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1316-1906 |
3.19e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.80 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1316 LEE---ETRARSKLQN--EVRNMHADMDAIREQLEeeqesksdvqrQLSKANNEIQQWRSKFEseganRTEELEDQKRKL 1390
Cdd:COG4913 218 LEEpdtFEAADALVEHfdDLERAHEALEDAREQIE-----------LLEPIRELAERYAAARE-----RLAELEYLRAAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1391 lgKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFD-KTTAEWQAKVNSLQSELENSQK 1469
Cdd:COG4913 282 --RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1470 ESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEggrsthELDKARRRLEMEKEELQAALEEAEgALE 1549
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE------ALAEAEAALRDLRRELRELEAEIA-SLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1550 Q------EEAKVMRAQLEIATVRNEIDKR-------IQEKEEEFDN--------------------------TRRNHQRA 1590
Cdd:COG4913 433 RrksnipARLLALRDALAEALGLDEAELPfvgelieVRPEEERWRGaiervlggfaltllvppehyaaalrwVNRLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1591 ---LESMQASLEAEAKGKADAMRIKKKLEQDINELEVALDAS-----NRGKAEMEKTVKRYQQQI-REMQTSIEEEQRQ- 1660
Cdd:COG4913 513 rlvYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAElgrrfDYVCVDSPEELRRHPRAItRAGQVKGNGTRHEk 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1661 --RDEARESYNM---AERRctlmsgeVEELRAALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQ 1735
Cdd:COG4913 593 ddRRRIRSRYVLgfdNRAK-------LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1736 tdLDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEASslkggkkmIQKLESR 1815
Cdd:COG4913 666 --AEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE--------LDELQDR 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1816 VHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDR-KNQERLQELIDKLNAKIKTFKRQ-----------VEEAE 1883
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIdALRARLNRAEEELERAMRAFNREwpaetadldadLESLP 815
|
650 660
....*....|....*....|....
gi 127773 1884 EIAAInlakYRK-AQHELEEAEER 1906
Cdd:COG4913 816 EYLAL----LDRlEEDGLPEYEER 835
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
947-1515 |
4.67e-14 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 77.84 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 947 LKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLN-------KEKKALEEANKKTSDSLQAEEDKCNHLNK 1019
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTflleesrDKANQLEEKTKLQDENLKELIEKKDHLTK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1020 lkaKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVS 1099
Cdd:pfam05483 297 ---ELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1100 QLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGATSAQIELnKKREAELLKIRRDLEEAS 1179
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEEL-KGKEQELIFLLQAREKEI 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1180 LQHEAQISALRKKHQDAANEMADQVDQLQKVK------SKLEKDKKDLKREMDDLESQMTHNMKNKGCSEKVMKQFESQM 1253
Cdd:pfam05483 453 HDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlknielTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1254 SDLNARLEDSQRSI-NELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRN 1332
Cdd:pfam05483 533 LKQIENLEEKEMNLrDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1333 MHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEGANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALE 1412
Cdd:pfam05483 613 LHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1413 KAKSRLQQELEDMsievdranasVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSI 1492
Cdd:pfam05483 693 EIDKRCQHKIAEM----------VALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQL 762
|
570 580
....*....|....*....|...
gi 127773 1493 GALRRENKNLADEIHDLTDQLSE 1515
Cdd:pfam05483 763 EIEKEEKEKLKMEAKENTAILKD 785
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
848-1847 |
5.68e-14 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 78.16 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 848 EQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQIKELEERLLDEE 927
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 928 DAAADLEGIKKKMEADNANLK-KDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKAL-----EEANK 1001
Cdd:TIGR00606 269 NEIKALKSRKKQMEKDNSELElKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLnqektELLVE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1002 KTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLER----EKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENV 1077
Cdd:TIGR00606 349 QGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERgpfsERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQA 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1078 RRKEAEISSLNSKLEDEQNL----VSQLQRKIKELQarieeleeeleAERNARAKVEKQRAELNRELEELgERLDEagga 1153
Cdd:TIGR00606 429 DEIRDEKKGLGRTIELKKEIlekkQEELKFVIKELQ-----------QLEGSSDRILELDQELRKAEREL-SKAEK---- 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1154 tSAQIELNKKREAELLKIRRDLEEaSLQHEAQISALRKKHQDAANEM-------ADQVDQLQKVKSklekdkkdlkREMD 1226
Cdd:TIGR00606 493 -NSLTETLKKEVKSLQNEKADLDR-KLRKLDQEMEQLNHHTTTRTQMemltkdkMDKDEQIRKIKS----------RHSD 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1227 DLESQMTHnMKNKGCSEKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSqLS 1306
Cdd:TIGR00606 561 ELTSLLGY-FPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQD-EE 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1307 SQLEDARRSLEEETRARSKLQNEVrnmhADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEganrteeledq 1386
Cdd:TIGR00606 639 SDLERLKEEIEKSSKQRAMLAGAT----AVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSK----------- 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1387 krkllgklseaeqtTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKkqrafdkttaewqakvnslqsELEN 1466
Cdd:TIGR00606 704 --------------LRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEK---------------------EIPE 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1467 SQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLT--DQLSEggrsthELDKARRRLEMEKEELQAAleEA 1544
Cdd:TIGR00606 749 LRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTimERFQM------ELKDVERKIAQQAAKLQGS--DL 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1545 EGALEQEEAKVMRAQLEIATVRNEID---KRIQEKEEEFDNtrrnhqraLESMQASLEAEAKGKADAMRIKKKLEQDINE 1621
Cdd:TIGR00606 821 DRTVQQVNQEKQEKQHELDTVVSKIElnrKLIQDQQEQIQH--------LKSKTNELKSEKLQIGTNLQRRQQFEEQLVE 892
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1622 LEVALDASNRgkaemekTVKRYQQQIREMQTSIEEEQRQRDEA----RESYNMAERRCTLMSGEVEELRAALEQAER-AR 1696
Cdd:TIGR00606 893 LSTEVQSLIR-------EIKDAKEQDSPLETFLEKDQQEKEELisskETSNKKAQDKVNDIKEKVKNIHGYMKDIENkIQ 965
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1697 KASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMHGElkgadERCKKAMADAARLADELRaeqdhsnQV 1776
Cdd:TIGR00606 966 DGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQ-----ERWLQDNLTLRKRENELK-------EV 1033
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 127773 1777 EKVRKNLESQVKEFQIRLDEAEASSLKGGKKMIQKLESRVHELEAELDnEQRRHAETQ---KNMRKADRRLKEL 1847
Cdd:TIGR00606 1034 EEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYE-KEIKHFKKElrePQFRDAEEKYREM 1106
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1258-1721 |
1.69e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.96 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1258 ARLEDSQRSINELQSQKSRLQAensdLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLE--EETRARSKLQNEVRNMHA 1335
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1336 DMDAIREQLEEEQEsksdVQRQLSKANNEIQQWRSKFESEGANRTEELEDQkrkllgkLSEAEQTTEAANAKCSALEKAK 1415
Cdd:COG4717 147 RLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLSLATEEE-------LQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1416 SRLQQELEDMSIEVDRANASVNQMEKKQRafdKTTAEWQAKVNSLQSELEnsqkesrGYSAELYRIKASIEEYQDSIGAL 1495
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEER---LKEARLLLLIAAALLALL-------GLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1496 rrenknLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRnEIDKRIQE 1575
Cdd:COG4717 286 ------LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ-ELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1576 KEEEFDNTRRNHQRA--LESMQASLEAEAKGKADAMRIKKKLEQDINELEVALDASNRGKAEMEKTV--KRYQQQIREMQ 1651
Cdd:COG4717 359 LEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELE 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 127773 1652 TSIEEEQRQRDEAREsynmaerrctlmsgEVEELRAALEQAERARKASDN--ELADANDRVNELTSQVSSVQ 1721
Cdd:COG4717 439 EELEELEEELEELRE--------------ELAELEAELEQLEEDGELAELlqELEELKAELRELAEEWAALK 496
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1035-1906 |
4.31e-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: 75.08 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1035 LEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKlEDEQNLVSQLQRKIKELQARIEE 1114
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSY-ENELDPLKNRLKEIEHNLSKIMK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1115 LEEELEaernARAKVEKQRAELNRELEELGERLDEAGGATSAQIELNKKREA-----ELLKIRRDLEEasLQHEAQISAL 1189
Cdd:TIGR00606 267 LDNEIK----ALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVrekerELVDCQRELEK--LNKERRLLNQ 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1190 RKKH---QDAANEMADQVDQLQKVKSKLEKDKKDLKREMDDLES--------QMTHNMKNKGCSEKVmKQFESQMSDLNA 1258
Cdd:TIGR00606 341 EKTEllvEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERgpfserqiKNFHTLVIERQEDEA-KTAAQLCADLQS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1259 RLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNmhADMD 1338
Cdd:TIGR00606 420 KERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKN--SLTE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1339 AIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFES---------EGANRTEELEDQKRK----LLGKLSEAEQTTEAAN 1405
Cdd:TIGR00606 498 TLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTrtqmemltkDKMDKDEQIRKIKSRhsdeLTSLLGYFPNKKQLED 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1406 AKCSaLEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKV------NSLQSELENSQKESRGYSAELY 1479
Cdd:TIGR00606 578 WLHS-KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRA 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1480 RIKASIEEYQDSIGALRREN--------------KNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQaaleeae 1545
Cdd:TIGR00606 657 MLAGATAVYSQFITQLTDENqsccpvcqrvfqteAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEML------- 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1546 GALEQEEAKVMRAQLEIATVRNEIDKRIQEKEEEFDNTRRNhQRALESMQASLEAEAKGKADAMRIK------KKLEQDI 1619
Cdd:TIGR00606 730 GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ-ETLLGTIMPEEESAKVCLTDVTIMErfqmelKDVERKI 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1620 NELEVALDASN--RGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAERARK 1697
Cdd:TIGR00606 809 AQQAAKLQGSDldRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEE 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1698 ASDneladanDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVE 1777
Cdd:TIGR00606 889 QLV-------ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIE 961
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1778 K-VRKNLESQVKEFQIRLDEAEAsSLKGGKKMIQKLESRVHELEAELDNEQRRHAETQKNM--RKADRRLKELA------ 1848
Cdd:TIGR00606 962 NkIQDGKDDYLKQKETELNTVNA-QLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlRKRENELKEVEeelkqh 1040
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127773 1849 ------FQADEDRKNQERLQELIDKL-NAKIKTFKRQVEEAEEIAainLAKYRKAQHELEEAEER 1906
Cdd:TIGR00606 1041 lkemgqMQVLQMKQEHQKLEENIDLIkRNHVLALGRQKGYEKEIK---HFKKELREPQFRDAEEK 1102
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1237-1915 |
4.89e-13 |
|
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: 74.76 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1237 KNKGCSEKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQ-------AENSDLTRQLEDAEHRVSVLSKEKSQLSSQL 1309
Cdd:pfam05483 92 KWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSlkleeeiQENKDLIKENNATRHLCNLLKETCARSAEKT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1310 EDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEeqeSKSDVQRQLSKANNEIQQWRSKFESEGANRteelEDQKRK 1389
Cdd:pfam05483 172 KKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAEN---ARLEMHFKLKEDHEKIQHLEEEYKKEINDK----EKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1390 LLGKLSEAEQtteaanakcsalekaksrlqqELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENsqk 1469
Cdd:pfam05483 245 LLIQITEKEN---------------------KMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED--- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1470 esrgysaelyrIKASIEEYQDSIGALRRENKNLADEIHDLTDqlsEGGRSTHELDKARRRLEMEKEELQAALEEAEGALE 1549
Cdd:pfam05483 301 -----------IKMSLQRSMSTQKALEEDLQIATKTICQLTE---EKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1550 QEEAKVMRAQLEIATVRNEIDKRIQEKEE--EFDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDINELEVALD 1627
Cdd:pfam05483 367 TEQQRLEKNEDQLKIITMELQKKSSELEEmtKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQ 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1628 ASNRGKAEMEKTV-------KRYQQQIREMQTSIEEEQRQRDEARESynmaerrCTLMSGEVEELRAALEQAERARKASD 1700
Cdd:pfam05483 447 AREKEIHDLEIQLtaiktseEHYLKEVEDLKTELEKEKLKNIELTAH-------CDKLLLENKELTQEASDMTLELKKHQ 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1701 NELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDL----DEMHGELKGADERCKKAMADAARLADELRAEQDHSNQV 1776
Cdd:pfam05483 520 EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1777 EKVRKNLESQVKEFQirlDEAEASSLKGG--KKMIQKLESRVHELEAELDNEQRRHAETQKNMRK--ADRRLKELAF--- 1849
Cdd:pfam05483 600 KKQIENKNKNIEELH---QENKALKKKGSaeNKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKeiEDKKISEEKLlee 676
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 127773 1850 ------QADEDRKNQE----RLQELIDKLNAKIKTFKRQVEEAEEIAAINLAKYRKAQHELEEAEERADTADSTLQ 1915
Cdd:pfam05483 677 vekakaIADEAVKLQKeidkRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIK 752
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1058-1836 |
5.94e-13 |
|
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: 74.37 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1058 STQENVEDLERVKRELEENVRR-------KEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVE 1130
Cdd:pfam05483 68 SDFENSEGLSRLYSKLYKEAEKikkwkvsIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1131 KQraelNRELEELGERLDEAGGATSaqiELNKKREAELLKIRRDLEEASLQHEAQISALRKKHQDAANEMADQVDQLQKV 1210
Cdd:pfam05483 148 KE----NNATRHLCNLLKETCARSA---EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKED 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1211 KSKLEKDKKDLKREMDDLESQMTHNMKNkgCSEKvmkqfESQMSDLNARLEDSQRSINELQsQKSRLQAENsdltrqled 1290
Cdd:pfam05483 221 HEKIQHLEEEYKKEINDKEKQVSLLLIQ--ITEK-----ENKMKDLTFLLEESRDKANQLE-EKTKLQDEN--------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1291 aehrVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRS 1370
Cdd:pfam05483 284 ----LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTC 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1371 KFES---EGANRTEELEDQKR----KLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSievdranasvnqmEKKQ 1443
Cdd:pfam05483 360 SLEEllrTEQQRLEKNEDQLKiitmELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLD-------------EKKQ 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1444 raFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYqdsigalrrenknlADEIHDLTDQLSEGGRSTHEL 1523
Cdd:pfam05483 427 --FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY--------------LKEVEDLKTELEKEKLKNIEL 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1524 DKARRRLEMEKEELqaaleeaegaleQEEAKVMRAQLeiatvrneidkriQEKEEEFDNTRRNHQRALESMQASLEAEAK 1603
Cdd:pfam05483 491 TAHCDKLLLENKEL------------TQEASDMTLEL-------------KKHQEDIINCKKQEERMLKQIENLEEKEMN 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1604 GKADAMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVE 1683
Cdd:pfam05483 546 LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1684 ELRAALEQAERARKASDNELADANDRVNELTS----QVSSVQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADA 1759
Cdd:pfam05483 626 AENKQLNAYEIKVNKLELELASAKQKFEEIIDnyqkEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEM 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1760 ARLADElraeqdHSNQVEKVRKNLESQVKEFQIRldEAEASSLKGG-----KKMIQKLESRVHELEAELDNEQRRHAETQ 1834
Cdd:pfam05483 706 VALMEK------HKHQYDKIIEERDSELGLYKNK--EQEQSSAKAAleielSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
..
gi 127773 1835 KN 1836
Cdd:pfam05483 778 EN 779
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
991-1905 |
8.34e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 74.24 E-value: 8.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 991 KEKKALEEANKKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVK 1070
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1071 RELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEEleaERNARAKVEKQRAELNRELEELGERLDEA 1150
Cdd:pfam02463 250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEE---LKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1151 ggatSAQIELNKKREAELLKIRRDLEEASLQHEAQISALRKKHQDAANEMADQVDQLQKVKsklekdkkdlkremddles 1230
Cdd:pfam02463 327 ----EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES------------------- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1231 qmthnmknkgcsekvmKQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLskEKSQLSSQLE 1310
Cdd:pfam02463 384 ----------------ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE--EESIELKQGK 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1311 DARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDvQRQLSKANNEIQQWRSKFESEGANRTEeledQKRKL 1390
Cdd:pfam02463 446 LTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL-LLSRQKLEERSQKESKARSGLKVLLAL----IKDGV 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1391 LGKLSEAEQTTEAANAKCSALEKAKSRLQQEledmsiEVDRANASVNQMEKKQRAFdkttaeWQAKVNSLQSELENSQKE 1470
Cdd:pfam02463 521 GGRIISAHGRLGDLGVAVENYKVAISTAVIV------EVSATADEVEERQKLVRAL------TELPLGARKLRLLIPKLK 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1471 SRGYSAELYRIKASIEEYQ-DSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMeKEELQAALEEAEGALE 1549
Cdd:pfam02463 589 LPLKSIAVLEIDPILNLAQlDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKG-VSLEEGLAEKSEVKAS 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1550 QEEAKVMRAQLEIATVRNEIDKRIQEKEEEFDNTRRNHQRALESMQASLEAEAKGKADamriKKKLEQDINELEVALDAS 1629
Cdd:pfam02463 668 LSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLAD----RVQEAQDKINEELKLLKQ 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1630 NRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAErrctLMSGEVEELRAALEQAERARKASDNELADANDR 1709
Cdd:pfam02463 744 KIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKL----KVEEEKEEKLKAQEEELRALEEELKEEAELLEE 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1710 VNELTSQVSsvqgqkrklegdiNAMQTDLDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVEKVRKNLESQVKE 1789
Cdd:pfam02463 820 EQLLIEQEE-------------KIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKD 886
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1790 FQIRLDEAEASSLKGGKKMIQKLEsrvhELEAELDNEQRRHAETQKNMRKADRRLKELAFQAD----EDRKNQERLQELI 1865
Cdd:pfam02463 887 ELESKEEKEKEEKKELEEESQKLN----LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEAdekeKEENNKEEEEERN 962
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 127773 1866 DKLNAKIKTFKRQVEEAEEIAAINLAKYRKAQHELEEAEE 1905
Cdd:pfam02463 963 KRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEE 1002
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
842-1399 |
8.34e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.92 E-value: 8.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 842 QEEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNDLFL----------QLQTLEDSMGDQEERVEKLIMQKAD 911
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEvleeheerreELETLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 912 FESQIKELEERLLDEEDAAADLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNK 991
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 992 EKKALEEANKKTSDSLQAEEDKCnhlnklkAKLEQALDELEDNLErekkvrgDVEKAKRKVEQDLKSTQENVEDLERVKR 1071
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAV-------EDRREEIEELEEEIE-------ELRERFGDAPVDLGNAEDFLEELREERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1072 ELEENVRRKEAEISSLNSKLEDEQNLVSqlQRKIKELQARIEEL--EEELEAERNARAKVEKQRAELNRELEELGERLDE 1149
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEALLE--AGKCPECGQPVEGSphVETIEEDRERVEELEAELEDLEEEVEEVEERLER 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1150 AGGATSAQIELNKKRE-AELLKIRRDLEEASLQHEA-QISALRKKHQDAANEMADQVDQLQKVKSklekDKKDLKREMDD 1227
Cdd:PRK02224 501 AEDLVEAEDRIERLEErREDLEELIAERRETIEEKReRAEELRERAAELEAEAEEKREAAAEAEE----EAEEAREEVAE 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1228 LESQMTHNmknkgcsekvmkqfESQMSDLNaRLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSS 1307
Cdd:PRK02224 577 LNSKLAEL--------------KERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEA 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1308 QLEDARrsLEEetrARSKLQNEVrnmhADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFEseganRTEELEDQK 1387
Cdd:PRK02224 642 EFDEAR--IEE---AREDKERAE----EYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRE-----RREALENRV 707
|
570
....*....|..
gi 127773 1388 RKLLGKLSEAEQ 1399
Cdd:PRK02224 708 EALEALYDEAEE 719
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
838-1387 |
1.13e-12 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 73.72 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 838 SIARQEEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNDlflQLQTLEDSMGDQEERVEKLIMQKADFESqiK 917
Cdd:pfam12128 302 KRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQE---QLPSWQSELENLEERLKALTGKHQDVTA--K 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 918 ELEERLLDEEDAAADLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTlqgEISQQDEHIGKLNKEKKALE 997
Cdd:pfam12128 377 YNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKL---EFNEEEYRLKSRLGELKLRL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 998 EANKKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKREL---- 1073
Cdd:pfam12128 454 NQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLfpqa 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1074 -----------------------EENVRRKEAEISSLNSKLEDEQNLVS---QLQR--------KIKELQARIEELEEEL 1119
Cdd:pfam12128 534 gtllhflrkeapdweqsigkvisPELLHRTDLDPEVWDGSVGGELNLYGvklDLKRidvpewaaSEEELRERLDKAEEAL 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1120 EAERNARAKVEKQRAELNRELEELGERLDEAG----GATSAQIELNKKREAELLKIRRDLEEASLQH-------EAQISA 1188
Cdd:pfam12128 614 QSAREKQAAAEEQLVQANGELEKASREETFARtalkNARLDLRRLFDEKQSEKDKKNKALAERKDSAnerlnslEAQLKQ 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1189 LRKKHQDAANEMADQV-------------------DQLQKVKSKLEKDKKDLKREMDDLESQMTHNMKNKGCSEKVMKQF 1249
Cdd:pfam12128 694 LDKKHQAWLEEQKEQKreartekqaywqvvegaldAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKL 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1250 ESQMSDLNARLEDSQRSINELQS----QKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSK 1325
Cdd:pfam12128 774 KREIRTLERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEK 853
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 127773 1326 LQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKA--NNEIQQWRSKFESEGANRTEELEDQK 1387
Cdd:pfam12128 854 QQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGerLAQLEDLKLKRDYLSESVKKYVEHFK 917
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1175-1884 |
1.71e-12 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 72.95 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1175 LEEASLQHEAQISALRKKHQDAA--NEMADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTH----NMKNKGCSEKVMKQ 1248
Cdd:pfam12128 272 TLIASRQEERQETSAELNQLLRTldDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAfldaDIETAAADQEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1249 FESQMSDLNARLEDSQRSINELQSQKSRLQAENSdltrqledaEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQN 1328
Cdd:pfam12128 352 WQSELENLEERLKALTGKHQDVTAKYNRRRSKIK---------EQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALES 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1329 EvrnmhadmdaIREQLEEEQESKSDVQRQLSKANNEIqqwrsKFESEGANRTEELEDQKRKLLGKLSEAEQTTEAANAKC 1408
Cdd:pfam12128 423 E----------LREQLEAGKLEFNEEEYRLKSRLGEL-----KLRLNQATATPELLLQLENFDERIERAREEQEAANAEV 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1409 SALEKAKSRLQQELEDMSIEVDRANASVNQmekKQRAFDKTTAEWQAKVNSLqseLENSQKESRGYSaelyrikasieey 1488
Cdd:pfam12128 488 ERLQSELRQARKRRDQASEALRQASRRLEE---RQSALDELELQLFPQAGTL---LHFLRKEAPDWE------------- 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1489 qDSIGALRRENKNLADEIHDLTDQLSEGGRSTheLDKARRRLE--------MEKEELQAALEEAEGALEQEEAKVMRAQL 1560
Cdd:pfam12128 549 -QSIGKVISPELLHRTDLDPEVWDGSVGGELN--LYGVKLDLKridvpewaASEEELRERLDKAEEALQSAREKQAAAEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1561 EIATVRNEIDKriQEKEEEF-----DNTRRNHQRALESMQAslEAEAKGKADAMRIKKKLEQdINELEVALDASNRGKAE 1635
Cdd:pfam12128 626 QLVQANGELEK--ASREETFartalKNARLDLRRLFDEKQS--EKDKKNKALAERKDSANER-LNSLEAQLKQLDKKHQA 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1636 MEKTVKRyqqQIREMQTSIEEEQRQRDEAResynmaerrctlmSGEVEELRAALEQAERARKASDNELADANDRvnELTS 1715
Cdd:pfam12128 701 WLEEQKE---QKREARTEKQAYWQVVEGAL-------------DAQLALLKAAIAARRSGAKAELKALETWYKR--DLAS 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1716 QvsSVQGQK-RKLEGDINAMQTDLdemhgelkgadERCKKAMADAARLADELRAEQDHSNQVEKVRK-NLESQVKEFQIR 1793
Cdd:pfam12128 763 L--GVDPDViAKLKREIRTLERKI-----------ERIAVRRQEVLRYFDWYQETWLQRRPRLATQLsNIERAISELQQQ 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1794 LDEAEASSlkggKKMIQKLESRVHELEAELDneqrrhaETQKNMRKADRRLKELAFQADEdrKNQERLQELIDKLNAKIK 1873
Cdd:pfam12128 830 LARLIADT----KLRRAKLEMERKASEKQQV-------RLSENLRGLRCEMSKLATLKED--ANSEQAQGSIGERLAQLE 896
|
730
....*....|.
gi 127773 1874 TFKRQVEEAEE 1884
Cdd:pfam12128 897 DLKLKRDYLSE 907
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
832-1488 |
2.11e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.87 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 832 KVKPLLSIARQEEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNDlflqlqtlEDSMGDQEERVEKLIMQKAD 911
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE--------AEAAADEAEAAEEKAEAAEK 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 912 FESQIKELEERLLDEEDAAADLEGIKKKMEADNANLKKdigdlentLQKAEQDKAHKDnqistlqgEISQQDEHIGKLNK 991
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE--------LKKAAAAKKKAD--------EAKKKAEEKKKADE 1435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 992 EKKALEEANKKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKvrgdVEKAKRKVEQDLKSTQEnVEDLERVKR 1071
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK----ADEAKKKAEEAKKKADE-AKKAAEAKK 1510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1072 ELEENVRRKEAEISSLNSKLEDEQNlvSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELgERLDEAG 1151
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKK--ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL-RKAEEAK 1587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1152 GATSAQIELNKKREAELLKIRRdlEEASLQHEAQISA--------LRKKHQDAANEMADQVDQLQKVKSKLEKDKKDLKR 1223
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKA--EEAKKAEEAKIKAeelkkaeeEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1224 EMDDLESQmthnmKNKGCSEKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKS 1303
Cdd:PTZ00121 1666 EAKKAEED-----KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1304 QLSSQLEDARRSlEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLsKANNEIQQWRSKFES--EGANRTE 1381
Cdd:PTZ00121 1741 EDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM-EVDKKIKDIFDNFANiiEGGKEGN 1818
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1382 ELEDQKRKLlgklsEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKV---- 1457
Cdd:PTZ00121 1819 LVINDSKEM-----EDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEieki 1893
|
650 660 670
....*....|....*....|....*....|...
gi 127773 1458 --NSLQSELENSQKESRGYsaELYRIKASIEEY 1488
Cdd:PTZ00121 1894 dkDDIEREIPNNNMAGKNN--DIIDDKLDKDEY 1924
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
833-1189 |
5.45e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 833 VKPLLSIARQEEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADF 912
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 913 ESQIkeleerlldeedaaADLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEhigklnke 992
Cdd:TIGR02168 746 EERI--------------AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-------- 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 993 kkALEEANKKTSDslqaeedkcnhLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRE 1072
Cdd:TIGR02168 804 --ALDELRAELTL-----------LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1073 LEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGG 1152
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS 950
|
330 340 350
....*....|....*....|....*....|....*...
gi 127773 1153 AT-SAQIELNKKREAELLKIRRDLEeaslQHEAQISAL 1189
Cdd:TIGR02168 951 LTlEEAEALENKIEDDEEEARRRLK----RLENKIKEL 984
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
847-1465 |
6.44e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.86 E-value: 6.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 847 KEQLKQMDKMKEDLAKTERIK---KELEEQNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQIKELEERL 923
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEeliKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 924 LDEEDAAADLEGIKKKMEadnaNLKKDIGDLENTLQKAEQDKAHKDNQIsTLQGEISQQDEHIGKLNKEKKALEEANKKT 1003
Cdd:PRK03918 252 GSKRKLEEKIRELEERIE----ELKKEIEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1004 SDSLQAEEDKCNHLNKLKAKLEqaldELEDNLEREKKVRGDVEKAKRKVEQDLK-STQENVEDLERVKRELEENVRRKEa 1082
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAKE- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1083 eisslnsKLEDEqnlVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRE-LEELGERLDEAGGATSAQIELN 1161
Cdd:PRK03918 402 -------EIEEE---ISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhRKELLEEYTAELKRIEKELKEI 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1162 KKREAELLKIRRDLEEAsLQHEAQISALRkkhqdaanEMADQVDQLQ-KVKSKLEKDKKDLKREMDDLEsqmthnmknkg 1240
Cdd:PRK03918 472 EEKERKLRKELRELEKV-LKKESELIKLK--------ELAEQLKELEeKLKKYNLEELEKKAEEYEKLK----------- 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1241 csEKVMKqFESQMSDLNARLEdsqrSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQlssQLEDARRSLEEET 1320
Cdd:PRK03918 532 --EKLIK-LKGEIKSLKKELE----KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVE---ELEERLKELEPFY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1321 RARSKLQNEVRnmhaDMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEGANRTEELEDQKRKLLGKLSEAeqt 1400
Cdd:PRK03918 602 NEYLELKDAEK----ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRE--- 674
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127773 1401 TEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTaEWQAKVNSLQSELE 1465
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE-ELREKVKKYKALLK 738
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
937-1545 |
9.30e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 70.71 E-value: 9.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 937 KKKMEADNANLKKDIGDLENTLQKAEQDKAHKD--NQISTLQGEISQQDEHIGKLNKEKKALE-EANKKTSDSLQAEEDK 1013
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1014 cnhLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVE-QDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLE 1092
Cdd:COG4913 300 ---LRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1093 DEQnlvSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLdeaggatsAQIELNKKR-EAELLKI 1171
Cdd:COG4913 377 ASA---EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI--------ASLERRKSNiPARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1172 RRDLEEASLQHEAQI---------------------SALR---------KKHQDAANEMADQVDQLQKVKSKLEKDKKDL 1221
Cdd:COG4913 446 RDALAEALGLDEAELpfvgelievrpeeerwrgaieRVLGgfaltllvpPEHYAAALRWVNRLHLRGRLVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1222 KREMDDLESQMTHNM--KNKGCSEKVMKQFESQMS----DLNARLEDSQRSI--NELQSQKSRLQA--ENSDLTRQL--- 1288
Cdd:COG4913 526 PERPRLDPDSLAGKLdfKPHPFRAWLEAELGRRFDyvcvDSPEELRRHPRAItrAGQVKGNGTRHEkdDRRRIRSRYvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1289 EDAEHRVSVLSKEKSQLSSQLEDARRSLEEetrarskLQNEVRNMHADMDAIReQLEEEQESKSDV---QRQLSKANNEI 1365
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEA-------LEAELDALQERREALQ-RLAEYSWDEIDVasaEREIAELEAEL 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1366 QQWRskfesEGANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASV--------- 1436
Cdd:COG4913 678 ERLD-----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArlelralle 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1437 ---------NQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKE-SRGYSAELYRIKASIEEYQDSIGALRR-ENKNLA-- 1503
Cdd:COG4913 753 erfaaalgdAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALLDRlEEDGLPey 832
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 127773 1504 -DEIHDLTDQLSEGGRST--HELDKARRRLEMEKEELQAALEEAE 1545
Cdd:COG4913 833 eERFKELLNENSIEFVADllSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1342-1906 |
9.76e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 9.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1342 EQLEEEQESKSDVQRQLSKANNEIQQWRSKfESEGANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQ- 1420
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKR-TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEl 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1421 --ELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSqKESRGYSAELYRIKASIEEYQDSIGALRRE 1498
Cdd:PRK03918 237 keEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1499 NKNLADEIHDLTDQLSEGGRSTHELDKarrrLEMEKEELQAALEEAEG-ALEQEEAKVMRAQLEiatvrnEIDKRIQEKE 1577
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLEELEErHELYEEAKAKKEELE------RLKKRLTGLT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1578 -EEFDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDINELEVA----------LDASNRG--KAEMEKTVKRYQ 1644
Cdd:PRK03918 386 pEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgreLTEEHRKelLEEYTAELKRIE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1645 QQIREMqTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRaalEQAERARKASDNELADANDRVNELTSQVSSVQGQK 1724
Cdd:PRK03918 466 KELKEI-EEKERKLRKELRELEKVLKKESELIKLKELAEQLK---ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1725 RKLEGDINamqtDLDEMHGELKGADERCKKAMADAARLADELRAEQDHS-NQVEKVRKNLESQVKEFqirldeaeaSSLK 1803
Cdd:PRK03918 542 KSLKKELE----KLEELKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPFYNEY---------LELK 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1804 GGKKMIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADED-----RKNQERLQELIDKLNAKIKTFKRQ 1878
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEeyeelREEYLELSRELAGLRAELEELEKR 688
|
570 580
....*....|....*....|....*...
gi 127773 1879 VEEAEEiaaiNLAKYRKAQHELEEAEER 1906
Cdd:PRK03918 689 REEIKK----TLEKLKEELEEREKAKKE 712
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1651-1894 |
1.53e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 68.25 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1651 QTSIEEEQRQRDEAREsynmaerrctlmsgEVEELRAALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGD 1730
Cdd:COG4942 19 ADAAAEAEAELEQLQQ--------------EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1731 INAMQTDLDEMHGELKGADERCKKAMADAARLAD----ELRAEQDHSNQVEKVRKNLESQVKEFQIRLDE--AEASSLKG 1804
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1805 GKKMIQKLESRVHELEAELDNEQRR----HAETQKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKtfkrqvE 1880
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAAlealKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA------A 238
|
250
....*....|....
gi 127773 1881 EAEEIAAINLAKYR 1894
Cdd:COG4942 239 AAERTPAAGFAALK 252
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
953-1466 |
1.99e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.30 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 953 DLENTLQKAEQDKAHKdnQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCNHLnklkAKLEQALDELE 1032
Cdd:PRK02224 191 QLKAQIEEKEEKDLHE--RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL----ETLEAEIEDLR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1033 DNL---EREKK-VRGDVEKAKRKVEQ-----------------DLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKL 1091
Cdd:PRK02224 265 ETIaetEREREeLAEEVRDLRERLEEleeerddllaeaglddaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1092 EDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGgatsAQIELNKKREAELLKI 1171
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP----VDLGNAEDFLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1172 RRDLEEaslqHEAQISALRKKHQDAANEMADQVDQ------LQKVKSKLEKDKKDLKRE-MDDLESQmthnmknkgcsek 1244
Cdd:PRK02224 421 RDELRE----REAELEATLRTARERVEEAEALLEAgkcpecGQPVEGSPHVETIEEDRErVEELEAE------------- 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1245 vMKQFESQMSDLNARLE------DSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARrslEE 1318
Cdd:PRK02224 484 -LEDLEEEVEEVEERLEraedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKR---EA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1319 ETRARSKLQnEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANN---EIQQWRSKFESEGanrteELEDQKRKLLGKLS 1395
Cdd:PRK02224 560 AAEAEEEAE-EAREEVAELNSKLAELKERIESLERIRTLLAAIADaedEIERLREKREALA-----ELNDERRERLAEKR 633
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 127773 1396 EAEQTTEAANAKcSALEKAKSRLQqeledmsievdRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELEN 1466
Cdd:PRK02224 634 ERKRELEAEFDE-ARIEEAREDKE-----------RAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1298-1884 |
2.56e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 68.89 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1298 LSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFES--- 1374
Cdd:TIGR04523 80 LEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKlnn 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1375 ---EGANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMsievDRANASVNQMEKKQRAFDKTTA 1451
Cdd:TIGR04523 160 kynDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN----KSLESQISELKKQNNQLKDNIE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1452 EWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEggrstheldkarrrle 1531
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD---------------- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1532 MEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDK---RIQEKEEEFDNTRRNH---QRALESMQASLEAEAKGK 1605
Cdd:TIGR04523 300 LNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQlneQISQLKKELTNSESENsekQRELEEKQNEIEKLKKEN 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1606 ADAMRIKKKLEQDINELEVALDasnrgkaEMEKTVKRYQQQIREMQTSIEEEQRqrdearesynmaerrctlmsgEVEEL 1685
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQ-------NQEKLNQQKDEQIKKLQQEKELLEK---------------------EIERL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1686 RAALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMHGELKgaderckkamadaaRLADE 1765
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK--------------SKEKE 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1766 LRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEASSLKGGKKmIQKLESRVHELEAELDNEQrrhaeTQKNMRKADRRLK 1845
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK-ISDLEDELNKDDFELKKEN-----LEKEIDEKNKEIE 571
|
570 580 590
....*....|....*....|....*....|....*....
gi 127773 1846 ELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEAEE 1884
Cdd:TIGR04523 572 ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEK 610
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1412-1906 |
2.70e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1412 EKAKSRLQQELEDMSIevDRANASVNQMEKKQrafDKTTAEWQAKVNSLQSELensqKESRGYSAELYRIKASIEEYQDS 1491
Cdd:COG4717 33 EAGKSTLLAFIRAMLL--ERLEKEADELFKPQ---GRKPELNLKELKELEEEL----KEAEEKEEEYAELQEELEELEEE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1492 IGALRRENKNLADEIHDLTDQLSeggrsTHELDKARRRLEMEKEELQAALEEaegaLEQEEAKVMRAQLEIATVRNEIDK 1571
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQ-----LLPLYQELEALEAELAELPERLEE----LEERLEELRELEEELEELEAELAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1572 RIQEKEEEFDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDINELEVALDasnrgKAEMEKTVKRYQQQIREMQ 1651
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE-----QLENELEAAALEERLKEAR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1652 TSI--------------------------------------EEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAE 1693
Cdd:COG4717 250 LLLliaaallallglggsllsliltiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1694 RARKASDNELADANDRVNELTSQVSSVQGQKRKLEgdINAMQTDLDEMHGELKGADErckkamADAARLADELRAEQDHS 1773
Cdd:COG4717 330 LPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVEDE------EELRAALEQAEEYQELK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1774 NQVEKVRKNLESQVKEFQIRLDEAEASSLkggkkmiqklESRVHELEAELDNEQRRHAETQKNMRKADRRLKELafqadE 1853
Cdd:COG4717 402 EELEELEEQLEELLGELEELLEALDEEEL----------EEELEELEEELEELEEELEELREELAELEAELEQL-----E 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 127773 1854 DRKNQERLQELIDKLNAKIKtfkrqvEEAEEIAAINLAKYrKAQHELEEAEER 1906
Cdd:COG4717 467 EDGELAELLQELEELKAELR------ELAEEWAALKLALE-LLEEAREEYREE 512
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1063-1617 |
2.88e-11 |
|
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: 68.70 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1063 VEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRK------IKELQARIEELEEELEAERNARAKVEKQRAEL 1136
Cdd:pfam10174 129 AKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLQSKglpkksGEEDWERTRRIAEAEMQLGHLEVLLDQKEKEN 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1137 NRELEELGERLDEAGGATSAQ-----IELNKKREAELLKIRRDLEE-----------ASLQHEAQISALR--KKHQDAAN 1198
Cdd:pfam10174 209 IHLREELHRRNQLQPDPAKTKalqtvIEMKDTKISSLERNIRDLEDevqmlktngllHTEDREEEIKQMEvyKSHSKFMK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1199 EMADQVDQ-LQKVKSklekdkkdlkrEMDDLESQM-THNMKNKGCSE--KVMKQ-----------FESQMSDLNARLEDS 1263
Cdd:pfam10174 289 NKIDQLKQeLSKKES-----------ELLALQTKLeTLTNQNSDCKQhiEVLKEsltakeqraaiLQTEVDALRLRLEEK 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1264 QRSINE-------LQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHAD 1336
Cdd:pfam10174 358 ESFLNKktkqlqdLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTA 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1337 MDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEGANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKS 1416
Cdd:pfam10174 438 LTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDS 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1417 RLQQELEDMSIEVDRANASVNQMEKKQRAFD--KTTAEWQAKVNSLQSELENSQKESRGYSAELYRIkasieeyqdsIGA 1494
Cdd:pfam10174 518 KLKSLEIAVEQKKEECSKLENQLKKAHNAEEavRTNPEINDRIRLLEQEVARYKEESGKAQAEVERL----------LGI 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1495 LRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQ--AALEEAEGALEQEEAKVMRAQLEIATVRNEIDKR 1572
Cdd:pfam10174 588 LREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKkkGAQLLEEARRREDNLADNSQQLQLEELMGALEKT 667
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 127773 1573 IQEKEEEfdntrrnhQRALESMQASLeAEAKGKADAMRI--KKKLEQ 1617
Cdd:pfam10174 668 RQELDAT--------KARLSSTQQSL-AEKDGHLTNLRAerRKQLEE 705
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1381-1914 |
4.67e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1381 EELED--QKRKLLGKLSEAEQTTEAANAKCSALEKAKSRL-----QQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEW 1453
Cdd:COG4913 242 EALEDarEQIELLEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1454 QAKVNSLQSELENSQkesrgySAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEggrSTHELDKARRRLEME 1533
Cdd:COG4913 322 REELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA---SAEEFAALRAEAAAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1534 KEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIdkriqekeEEFDNTRRNHQRALESMQASLEAEAKGKADAMRIkk 1613
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELRELEAEI--------ASLERRKSNIPARLLALRDALAEALGLDEAELPF-- 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1614 kleqdINEL-EVALDASN-RGKAEmektvkRYqqqIREMQTSIEEEQRQRDEARESYNmaERRctlmsgevEELRAALEQ 1691
Cdd:COG4913 463 -----VGELiEVRPEEERwRGAIE------RV---LGGFALTLLVPPEHYAAALRWVN--RLH--------LRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1692 AERARKASDNELADANDRVNELTSQVSSVQGQ-KRKLEGDINAMQ-TDLDEMH---------GELKGADERCKKAMADA- 1759
Cdd:COG4913 519 VRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWlEAELGRRFDYVCvDSPEELRrhpraitraGQVKGNGTRHEKDDRRRi 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1760 --------------ARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEA-SSLKGGKKMIQKLESRVHELEAELD 1824
Cdd:COG4913 599 rsryvlgfdnraklAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlAEYSWDEIDVASAEREIAELEAELE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1825 NeqrrhaetqknMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEAEEIAainlakyRKAQHELEEAE 1904
Cdd:COG4913 679 R-----------LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL-------DELQDRLEAAE 740
|
570
....*....|
gi 127773 1905 ERADTADSTL 1914
Cdd:COG4913 741 DLARLELRAL 750
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1053-1843 |
6.45e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 67.69 E-value: 6.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1053 EQDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEdEQNLVSQLQRKIKELQARIeeleeelEAERNARAKVEKQ 1132
Cdd:TIGR00618 211 PCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE-AQEEQLKKQQLLKQLRARI-------EELRAQEAVLEET 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1133 RAELNRELEelgerldeaggatSAQIELNKKREAEllkIRRDLEEASLQHEAQISALRKKHQDAANEMADQVDQLQKvks 1212
Cdd:TIGR00618 283 QERINRARK-------------AAPLAAHIKAVTQ---IEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ--- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1213 klekdkkdlKREMDDLESQMTHNMKNKGCSEKVMKQFESQMSDLNaRLEDSQRSINELQSQKSRLQAENSDLTRQledaE 1292
Cdd:TIGR00618 344 ---------RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQSLCKELDILQRE----Q 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1293 HRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKF 1372
Cdd:TIGR00618 410 ATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKK 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1373 ESEGAnRTEELEDQKRKLLGKLSEAEQ------TTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAF 1446
Cdd:TIGR00618 490 AVVLA-RLLELQEEPCPLCGSCIHPNParqdidNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEI 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1447 DKTTAEWQAKVNSLQSELENSQKEsrgysaelyrikasIEEYQDSIGALRRENKNLADEIHDLTDQLSeggrstHELDKA 1526
Cdd:TIGR00618 569 QQSFSILTQCDNRSKEDIPNLQNI--------------TVRLQDLTEKLSEAEDMLACEQHALLRKLQ------PEQDLQ 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1527 RRRLEMEKEELQAALEEAegALEQEEAKVMRAQLEIATVrneidkRIQEKEEEFDNTRRNHQRALESMQASLEAEAKGKA 1606
Cdd:TIGR00618 629 DVRLHLQQCSQELALKLT--ALHALQLTLTQERVREHAL------SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLA 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1607 DAMRIKKKLEQDINEL----EVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEV 1682
Cdd:TIGR00618 701 QCQTLLRELETHIEEYdrefNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAEL 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1683 EELRAALEQAERARKASDNELAdandrvnELTSQVssvqGQKRKLEGDINAMQTDLdemhgeLKGADERCKKAMADAARL 1762
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEDTHLLK-------TLEAEI----GQEIPSDEDILNLQCET------LVQEEEQFLSRLEEKSAT 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1763 ADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEASSLKGGKKMIQKLESRVHELEAELDNEQRRHAETQKNMRKADR 1842
Cdd:TIGR00618 844 LGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRFHGRYADS 923
|
.
gi 127773 1843 R 1843
Cdd:TIGR00618 924 H 924
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
839-1454 |
7.72e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 67.76 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 839 IARQEEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNDlflQLQTLEDSMGDQEERVEKLI-----MQKADFE 913
Cdd:TIGR00606 417 LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIK---ELQQLEGSSDRILELDQELRkaereLSKAEKN 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 914 SQIKELEERLLDEEDAAADLEGIKKKMEADNANLKKDIGDLENTLQKAeQDKAHKDNQISTLQGEIS------------- 980
Cdd:TIGR00606 494 SLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT-KDKMDKDEQIRKIKSRHSdeltsllgyfpnk 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 981 -QQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNL----------EREKKVRGDVEKAK 1049
Cdd:TIGR00606 573 kQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsqdeeSDLERLKEEIEKSS 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1050 R-------------------------------KVEQDLKSTQENVEDLERVKR-------ELEENVRRKEAEISSLNSKL 1091
Cdd:TIGR00606 653 KqramlagatavysqfitqltdenqsccpvcqRVFQTEAELQEFISDLQSKLRlapdklkSTESELKKKEKRRDEMLGLA 732
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1092 EDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGATSAQIEL--NKKREAELL 1169
Cdd:TIGR00606 733 PGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELkdVERKIAQQA 812
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1170 KirrdlEEASLQHEAQISALRKKHQDAANEM---ADQVDQLQKVKSKLEKDKKDLKREMDDLES---QMTHNMKNKGCSE 1243
Cdd:TIGR00606 813 A-----KLQGSDLDRTVQQVNQEKQEKQHELdtvVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFE 887
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1244 KVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLED----AEHRVSVLSKEKSQLSSQLEDARRSLeEE 1319
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETsnkkAQDKVNDIKEKVKNIHGYMKDIENKI-QD 966
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1320 TRARSKLQNEvrnmhADMDAIREQLEEEQESKsdvqrqlSKANNEIQQWRSKFESEgANRTEELEDQ--KRKLLGKLSEA 1397
Cdd:TIGR00606 967 GKDDYLKQKE-----TELNTVNAQLEECEKHQ-------EKINEDMRLMRQDIDTQ-KIQERWLQDNltLRKRENELKEV 1033
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 127773 1398 EQT-----TEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQ 1454
Cdd:TIGR00606 1034 EEElkqhlKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1054-1280 |
8.04e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.94 E-value: 8.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1054 QDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQR 1133
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1134 AELNRELEELGERLDEAGGATSAQIELNKKREAELLKIRRDLEEASLQHEAQISALRKKhqdaANEMADQVDQLQKVKSK 1213
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 1214 LEKDKKDLKREMDDLESQMTHNmknkgcsEKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAE 1280
Cdd:COG4942 176 LEALLAELEEERAALEALKAER-------QKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
945-1624 |
1.15e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 66.92 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 945 ANLKKDIGDLENTLQKAEQDKAH------KDNQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDS-----LQAEEDK 1013
Cdd:TIGR00618 222 QVLEKELKHLREALQQTQQSHAYltqkreAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRArkaapLAAHIKA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1014 CNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEaeisSLNSKLED 1093
Cdd:TIGR00618 302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE----ISCQQHTL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1094 EQNLVSQLQRKIKELQarieeleeeleAERNARAKVEKQRAELNRELEELGERLDEAGGATSAqielnkKREAELLKIRR 1173
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQ-----------KLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHA------KKQQELQQRYA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1174 DLEEASLQHEAQISALRKKHQDAANEMADQVDQLQKVKskleKDKKDLKREMDDLESQMTHNMKNKGCsekvmkQFESQM 1253
Cdd:TIGR00618 441 ELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK----EQIHLQETRKKAVVLARLLELQEEPC------PLCGSC 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1254 SDLNARLEDSQRSiNELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNM 1333
Cdd:TIGR00618 511 IHPNPARQDIDNP-GPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1334 HADMDAIR----EQLEEEQESKSDVQRQLSKANNEIQQWR-SKFESEGANRTEELEDQKRKLLGKLSEAEQTTEAANAKC 1408
Cdd:TIGR00618 590 QNITVRLQdlteKLSEAEDMLACEQHALLRKLQPEQDLQDvRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRV 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1409 SALEKAKSRLQQELEDMSI---------EVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELEnsqkesrgysaely 1479
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEkeqltywkeMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLA-------------- 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1480 rikASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQ 1559
Cdd:TIGR00618 736 ---AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEI 812
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 127773 1560 LEIATVRNEIDKRIQEKEEEFDNT-RRNHQR--ALESMQASLEAEAKGKADAMRIKKKLEQDINELEV 1624
Cdd:TIGR00618 813 PSDEDILNLQCETLVQEEEQFLSRlEEKSATlgEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG 880
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1263-1892 |
1.20e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 67.17 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1263 SQRSINELQSQKSRLQAEN----SDLTRQLEDAEHRVSVLSKEKSQLSSqledarrsleeetrARSKLQNEVRNMHADMD 1338
Cdd:pfam12128 207 EDDGVVPPKSRLNRQQVEHwirdIQAIAGIMKIRPEFTKLQQEFNTLES--------------AELRLSHLHFGYKSDET 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1339 AIREQLEEEQESKSDVQRQLSKANNEIQQWRskfeseganrtEELEDQKRKLLGKLSEAEQTTEAANAKCSA-----LEK 1413
Cdd:pfam12128 273 LIASRQEERQETSAELNQLLRTLDDQWKEKR-----------DELNGELSAADAAVAKDRSELEALEDQHGAfldadIET 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1414 AKSRLQQ------ELEDMSIEVDRANASVNQMEKK-QRAFDKTTAEWQAKVNSLQSELENsQKESRGysaelyRIKASIE 1486
Cdd:pfam12128 342 AAADQEQlpswqsELENLEERLKALTGKHQDVTAKyNRRRSKIKEQNNRDIAGIKDKLAK-IREARD------RQLAVAE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1487 -EYQDSIGALRRENKNLADEIHDLTDQLSEG-GRSTHELDKAR--RRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEI 1562
Cdd:pfam12128 415 dDLQALESELREQLEAGKLEFNEEEYRLKSRlGELKLRLNQATatPELLLQLENFDERIERAREEQEAANAEVERLQSEL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1563 ATVRNEIDkriqekeEEFDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDINELE------------------- 1623
Cdd:pfam12128 495 RQARKRRD-------QASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEqsigkvispellhrtdldp 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1624 VALDASNRGKAEMEKTVKRYQQ-QIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAERARKASDNE 1702
Cdd:pfam12128 568 EVWDGSVGGELNLYGVKLDLKRiDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1703 LADANDRVNELTSQVSSVQGQKRK-LEGDINAMQTDLDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVekvrk 1781
Cdd:pfam12128 648 LKNARLDLRRLFDEKQSEKDKKNKaLAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQV----- 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1782 nLESQVKEFQIRLDEAEASSLKGGKKMIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDRKNQERL 1861
Cdd:pfam12128 723 -VEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWY 801
|
650 660 670
....*....|....*....|....*....|.
gi 127773 1862 QELIDKLNAKIKTFKRQVEEAEEIAAINLAK 1892
Cdd:pfam12128 802 QETWLQRRPRLATQLSNIERAISELQQQLAR 832
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
978-1798 |
1.26e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.90 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 978 EISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDkcnHLNKLKAKLEQAldelednlEREKKVRGDVEKAKRKVEQDLK 1057
Cdd:PRK04863 301 QLAAEQYRLVEMARELAELNEAESDLEQDYQAASD---HLNLVQTALRQQ--------EKIERYQADLEELEERLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1058 STQENVEDLErvkrELEENVRRKEAEISSLNSKLEDeqnlvsqLQRKIKELQARIEELEEELEAERNARA---------- 1127
Cdd:PRK04863 370 VVEEADEQQE----ENEARAEAAEEEVDELKSQLAD-------YQQALDVQQTRAIQYQQAVQALERAKQlcglpdltad 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1128 KVEKQRAELNRELEELGERLDEAGgatsaqielNKKREAEllkirrdleEASLQHEAQISALRKkhqdaaneMADQVDql 1207
Cdd:PRK04863 439 NAEDWLEEFQAKEQEATEELLSLE---------QKLSVAQ---------AAHSQFEQAYQLVRK--------IAGEVS-- 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1208 qkvKSKLEKDKKDLKRemdDLESQMTHNMKnkgcsekvMKQFESQMSDLNARLE---DSQRSINELQSQKSRLQAENSDL 1284
Cdd:PRK04863 491 ---RSEAWDVARELLR---RLREQRHLAEQ--------LQQLRMRLSELEQRLRqqqRAERLLAEFCKRLGKNLDDEDEL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1285 TRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQN---EVRNMHADMDAIREQLEEEQESKSDVQRQlska 1361
Cdd:PRK04863 557 EQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAArapAWLAAQDALARLREQSGEEFEDSQDVTEY---- 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1362 nneIQQWRSKFESEGANRtEELEDQKRKLLGKLSEAEQTTEAANAKCSALekaKSRLQQEL-----EDMSIEvDRANAS- 1435
Cdd:PRK04863 633 ---MQQLLERERELTVER-DELAARKQALDEEIERLSQPGGSEDPRLNAL---AERFGGVLlseiyDDVSLE-DAPYFSa 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1436 ----------VNQMEKKQRAFDK----------TTAEWQAKVNSLQS--ELEN------SQKESRgYSaelyRI------ 1481
Cdd:PRK04863 705 lygparhaivVPDLSDAAEQLAGledcpedlylIEGDPDSFDDSVFSveELEKavvvkiADRQWR-YS----RFpevplf 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1482 -KASIEEYqdsIGALRREnknlADEIHDLTDQLSEGGRSTHELDKARRRL-------------EMEKEELQAALEEAEGA 1547
Cdd:PRK04863 780 gRAAREKR---IEQLRAE----REELAERYATLSFDVQKLQRLHQAFSRFigshlavafeadpEAELRQLNRRRVELERA 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1548 LEQEEAKVMRAQLEIATVRNEID------------------KRIQEKEEEFDNTR------RNHQRA---LESMQASLEA 1600
Cdd:PRK04863 853 LADHESQEQQQRSQLEQAKEGLSalnrllprlnlladetlaDRVEEIREQLDEAEeakrfvQQHGNAlaqLEPIVSVLQS 932
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1601 EakgkadamrikkklEQDINELEVALDasnrgkaEMEKTVKRYQQQIREMQtsieeEQRQRdEARESYNMAERRCTLMSG 1680
Cdd:PRK04863 933 D--------------PEQFEQLKQDYQ-------QAQQTQRDAKQQAFALT-----EVVQR-RAHFSYEDAAEMLAKNSD 985
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1681 EVEELRAALEQAERAR-------KASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEmhgelkGADERck 1753
Cdd:PRK04863 986 LNEKLRQRLEQAEQERtrareqlRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADS------GAEER-- 1057
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 127773 1754 kAMADAARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAE 1798
Cdd:PRK04863 1058 -ARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLE 1101
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
837-1309 |
1.68e-10 |
|
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: 66.35 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 837 LSIARQEEEMKEQLKQMDK--------MKEDLAKTERIKK---ELEEQNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKL 905
Cdd:pfam01576 639 LSLARALEEALEAKEELERtnkqlraeMEDLVSSKDDVGKnvhELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRL 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 906 --IMQ--KADFESqikeleerlldeedaaaDLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQ 981
Cdd:pfam01576 719 evNMQalKAQFER-----------------DLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKE 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 982 QDEHIGKLNKEKkalEEANKKTSdSLQAE-EDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDV----------EKAKR 1050
Cdd:pfam01576 782 LEAQIDAANKGR---EEAVKQLK-KLQAQmKDLQRELEEARASRDEILAQSKESEKKLKNLEAELlqlqedlaasERARR 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1051 KVEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVE 1130
Cdd:pfam01576 858 QAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSE 937
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1131 KQRAELNRELEELGERLDEAGGATSAQielnkkreaellkirrdleeaslqHEAQISALRKKhqdaANEMADQVDQLQKV 1210
Cdd:pfam01576 938 SARQQLERQNKELKAKLQEMEGTVKSK------------------------FKSSIAALEAK----IAQLEEQLEQESRE 989
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1211 KSKLEKDKKDLKREMDDLESQMTHNMKNKgcsekvmKQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLED 1290
Cdd:pfam01576 990 RQAANKLVRRTEKKLKEVLLQVEDERRHA-------DQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDD 1062
|
490
....*....|....*....
gi 127773 1291 AEHRVSVLSKEKSQLSSQL 1309
Cdd:pfam01576 1063 ATESNESMNREVSTLKSKL 1081
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1302-1883 |
2.77e-10 |
|
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: 65.53 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1302 KSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQqwrskfesEGANRTE 1381
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALR--------EQAELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1382 ELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANasvNQMEKKQRAFDKTTAEWQaKVNSLQ 1461
Cdd:pfam05557 80 LKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTN---SELEELQERLDLLKAKAS-EAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1462 SELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLAD--EIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQA 1539
Cdd:pfam05557 156 QNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLREHNKHLNENIENKLLLKEEVEDLKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1540 ALEEAEGAleQEEAKVMRAQLEiatvrneidkRIQEKEEEFDNTRRNHQRALESMQASleaeakgkadAMRIKKKLEQDI 1619
Cdd:pfam05557 236 KLEREEKY--REEAATLELEKE----------KLEQELQSWVKLAQDTGLNLRSPEDL----------SRRIEQLQQREI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1620 NELEVALDASNRGKaEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEqaerarkAS 1699
Cdd:pfam05557 294 VLKEENSSLTSSAR-QLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILE-------SY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1700 DNELADAN------DRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEmHGELKGADERCKKAMADAARLADELRAEQDHS 1773
Cdd:pfam05557 366 DKELTMSNyspqllERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGG-YKQQAQTLERELQALRQQESLADPSYSKEEVD 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1774 NQVEKVrKNLESQVKEFQIRLDEAEAS----SLKGgkkMIQKLESRV--HELEAELDNEQRRHAETQKnMRKADRRLKEL 1847
Cdd:pfam05557 445 SLRRKL-ETLELERQRLREQKNELEMElerrCLQG---DYDPKKTKVlhLSMNPAAEAYQQRKNQLEK-LQAEIERLKRL 519
|
570 580 590
....*....|....*....|....*....|....*..
gi 127773 1848 AFQADEDRKNQERLQELIDKLNAK-IKTFKRQVEEAE 1883
Cdd:pfam05557 520 LKKLEDDLEQVLRLPETTSTMNFKeVLDLRKELESAE 556
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
855-1443 |
2.86e-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: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 855 KMKEDLAKTERIKKELEEQNVTLLEQKNDLFLQLQTLEDSMGDQ----EERVEKLIMQKADFESQIKELEERLLDEEDAA 930
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLtfllEESRDKANQLEEKTKLQDENLKELIEKKDHLT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 931 ADLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAE 1010
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1011 EDKCN----HLNKLKAKLEQaLDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEISS 1086
Cdd:pfam05483 376 EDQLKiitmELQKKSSELEE-MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHD 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1087 LNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEaggaTSAQIELNKKREA 1166
Cdd:pfam05483 455 LEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKK----HQEDIINCKKQEE 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1167 ELLKIRRDLEEASLQHEAQISALRKKHQDAANEMADQVDQLQKVKSKLEKDKKDLkremddlesqmthnmknkgcsEKVM 1246
Cdd:pfam05483 531 RMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKK---------------------EKQM 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1247 KQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKE----KSQLSSQLEDARRSLEEETRA 1322
Cdd:pfam05483 590 KILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELElasaKQKFEEIIDNYQKEIEDKKIS 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1323 RSKLQNEVRNMHADMDairEQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEGANRTEELEDQKRKllgklsEAEQTTE 1402
Cdd:pfam05483 670 EEKLLEEVEKAKAIAD---EAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNK------EQEQSSA 740
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 127773 1403 AAnakcsALEKAKSRLQQELEDM--SIEVDRANASVNQMEKKQ 1443
Cdd:pfam05483 741 KA-----ALEIELSNIKAELLSLkkQLEIEKEEKEKLKMEAKE 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1500-1906 |
3.14e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1500 KNLADEIHDLTDQLSEGGRSThelDKARRRLEMEKEElqaALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQEKEEE 1579
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKT---ETGKAEEARKAEE---AKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1580 FDNTRrnhqRALESMQASLEAEAKGKADAMRIKKKLE----QDINELEVALDASNRGKAEmekTVKRYQQQIR-EMQTSI 1654
Cdd:PTZ00121 1160 AEDAR----KAEEARKAEDAKKAEAARKAEEVRKAEElrkaEDARKAEAARKAEEERKAE---EARKAEDAKKaEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1655 EEEQRQRDEAR----ESYNMAERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNEL--TSQVSSVQGQKRKLE 1728
Cdd:PTZ00121 1233 EEAKKDAEEAKkaeeERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkAEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1729 gdinamqtdldemhgELKGADERCKKAmADAARLADELRaeqdhsNQVEKVRKNLESQVKEFQIRLDEAEASSLKGGKKM 1808
Cdd:PTZ00121 1313 ---------------EAKKADEAKKKA-EEAKKKADAAK------KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1809 IQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNaKIKTFKRQVEEAE--EIA 1886
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEEAKkaDEA 1449
|
410 420
....*....|....*....|
gi 127773 1887 AINLAKYRKAQHELEEAEER 1906
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEA 1469
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
956-1180 |
3.53e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 956 NTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNL 1035
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1036 EREKKVRGDV----EKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQAR 1111
Cdd:COG4942 100 EAQKEELAELlralYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127773 1112 IEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGATSAQIELNKKREAELLKIRRDLEEASL 1180
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
929-1127 |
4.44e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 929 AAADLEGIKKKMEADNANL---KKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSD 1005
Cdd:COG4942 25 AEAELEQLQQEIAELEKELaalKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1006 SLQA------------------EEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLE 1067
Cdd:COG4942 105 ELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1068 RVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARA 1127
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1476-1707 |
5.44e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 5.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1476 AELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEGALEQEEAKV 1555
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1556 mrAQLEIATVRNEIDKRI-----QEKEEEFDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDINELEVALDASN 1630
Cdd:COG4942 107 --AELLRALYRLGRQPPLalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 1631 RGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEAREsynmaerrctlmsgEVEELRAALEQAERARKASDNELADAN 1707
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQ--------------EAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
949-1421 |
6.87e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 949 KDIGDLENTLQKAEQDKAhkdnQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDkCNHLNKLKAKLEQAL 1028
Cdd:COG4717 71 KELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-YQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1029 DELEDnLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKR-ELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKE 1107
Cdd:COG4717 146 ERLEE-LEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1108 LQARIEeleeeleaernaRAKVEKQRAELNRELEELGERLdeAGGATSAQIELNKKREAELLKIRRDLEEASLQHEAQIS 1187
Cdd:COG4717 225 LEEELE------------QLENELEAAALEERLKEARLLL--LIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1188 ALRKKHQDAANEMADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTHNMKNKGCSEKVMKQFESQMSDLNARLEdsqrsI 1267
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-----L 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1268 NELQSQKSRLQAENS-----DLTRQLEDAEHRVSvLSKEKSQLSSQLEDARRSLEEETRARSKlqnevRNMHADMDAIRE 1342
Cdd:COG4717 366 EELEQEIAALLAEAGvedeeELRAALEQAEEYQE-LKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEE 439
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127773 1343 QLEEEQESKSDVQRQLSKANNEIQQWrskfesEGANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQE 1421
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQL------EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1095-1376 |
7.96e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 7.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1095 QNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAggatsaqielnkkrEAELLKIRRD 1174
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL--------------EQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1175 LEEAslqhEAQISALRKKHQDAANEMADQVDQLQKVKSKLEKDKKDLKREMDDLESQMThnmknkgcsekVMKQFESQMs 1254
Cdd:COG4942 85 LAEL----EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ-----------YLKYLAPAR- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1255 dlnarledsQRSINELQSQKSRLQAENSDLTRQLedaehrvsvlsKEKSQLSSQLEDARRSLEEETRARSKLQNEVRnmh 1334
Cdd:COG4942 149 ---------REQAEELRADLAELAALRAELEAER-----------AELEALLAELEEERAALEALKAERQKLLARLE--- 205
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 127773 1335 ADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEG 1376
Cdd:COG4942 206 KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1385-1609 |
9.09e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 9.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1385 DQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSEL 1464
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1465 ENSQKESRGYSAELYRIKASIEEY----QDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAA 1540
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127773 1541 LEEaegaLEQEEAKVMRAQLEIATVRNEIDKRIQEKEEEFDNTRRNhQRALESMQASLEAEAKGKADAM 1609
Cdd:COG4942 180 LAE----LEEERAALEALKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAERT 243
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1224-1885 |
9.10e-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: 63.89 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1224 EMDDLESQMTHNMKNKGCSEKVMKQFESQMSDLNARLEDSQRSINELQS--------------QKSRLQAENSDLTRQLE 1289
Cdd:TIGR04523 55 ELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSdlskinseikndkeQKNKLEVELNKLEKQKK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1290 DAEH-------RVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKaN 1362
Cdd:TIGR04523 135 ENKKnidkfltEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQK-N 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1363 NEIQQWRSKFESEGANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRL---QQELEDMSIEVDRANASVNQM 1439
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLsekQKELEQNNKKIKELEKQLNQL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1440 EKKQRAFDKTTAewQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEggrs 1519
Cdd:TIGR04523 294 KSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE---- 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1520 theldkARRRLEMEKEELQAALEEAEgALEQEEAKVMRAQLEIATVRNEIDKRIQEKEEEFDNTRRNHQRaLESMQASLE 1599
Cdd:TIGR04523 368 ------KQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER-LKETIIKNN 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1600 AEAKgkadamrikkKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQrdearesynmaerrctlms 1679
Cdd:TIGR04523 440 SEIK----------DLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE------------------- 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1680 geveelraaLEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAmada 1759
Cdd:TIGR04523 491 ---------LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKE---- 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1760 aRLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEASSLKGGKKmIQKLESRVHELEAELDNEQRRHaetqknmrk 1839
Cdd:TIGR04523 558 -NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE-IEEKEKKISSLEKELEKAKKEN--------- 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 127773 1840 adrrlkelafqadedrknqERLQELIDKLNAKIKTFKRQVEEAEEI 1885
Cdd:TIGR04523 627 -------------------EKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1309-1892 |
9.63e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 63.77 E-value: 9.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1309 LEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQwrskfeseganrteeLEDQKR 1388
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNN---------------AMDDYN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1389 KLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELED---MSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELE 1465
Cdd:PRK01156 236 NLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKnnyYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILS 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1466 NSQKESRGYSAELYRIKASIEEYQDSIGALRR--ENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEE 1543
Cdd:PRK01156 316 NIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRydDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1544 AEGALEQEEAkvmraqlEIATVRNEIDKRIQEkeeefdntrrnhqraLESMQASLEAeakgKADAMRIKK-KLEQDINEL 1622
Cdd:PRK01156 396 ILKIQEIDPD-------AIKKELNEINVKLQD---------------ISSKVSSLNQ----RIRALRENLdELSRNMEML 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1623 E----VALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQ-RDEARESYNMAERRCTLMSGEVEELRAALEQAERAR- 1696
Cdd:PRK01156 450 NgqsvCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEvKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARa 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1697 -----KASDNELADANDRVNELTSQVSSVQGQ--KRKLEGDINAM-QTDLDEMHGELKGADERcKKAMADAARLADELRA 1768
Cdd:PRK01156 530 dlediKIKINELKDKHDKYEEIKNRYKSLKLEdlDSKRTSWLNALaVISLIDIETNRSRSNEI-KKQLNDLESRLQEIEI 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1769 E-QDHSNQVEKVRKNLESQVKEFQIRLDEAEASslkggKKMIQKLESRVHELE---AELDNEQRRHAETQKNMRKADRRL 1844
Cdd:PRK01156 609 GfPDDKSYIDKSIREIENEANNLNNKYNEIQEN-----KILIEKLRGKIDNYKkqiAEIDSIIPDLKEITSRINDIEDNL 683
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 127773 1845 KELAFQADEDRKNQERLQELID-------KLNAKIKTFKRQVEEAEEI-AAINLAK 1892
Cdd:PRK01156 684 KKSRKALDDAKANRARLESTIEilrtrinELSDRINDINETLESMKKIkKAIGDLK 739
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
812-1678 |
9.68e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 64.20 E-value: 9.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 812 QRNIRKWLVLRNwqwwKLYSKVKPLLSIARQEEEMKEQLKQMDKMKEDLA---------------------KTERIKKEL 870
Cdd:COG3096 281 RELSERALELRR----ELFGARRQLAEEQYRLVEMARELEELSARESDLEqdyqaasdhlnlvqtalrqqeKIERYQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 871 EEQNVTLLEQK---NDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQIKELEERLLDEEDAAADLEGIKKKMEADNANL 947
Cdd:COG3096 357 EELTERLEEQEevvEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCGLPDLTP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 948 KkDIGDLENTLQKAEQDKahkDNQISTLQGEISQQDEHIGKLNKEKKAL---------EEANKKTSDSLQAEEDKCNHLN 1018
Cdd:COG3096 437 E-NAEDYLAAFRAKEQQA---TEEVLELEQKLSVADAARRQFEKAYELVckiageverSQAWQTARELLRRYRSQQALAQ 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1019 KLKAkLEQALDELEDNLEREkkvrgdvEKAKRKVEQDLKSTQENVEDLERVKRELEEnvrrKEAEISSLNSKLEDEQNLV 1098
Cdd:COG3096 513 RLQQ-LRAQLAELEQRLRQQ-------QNAERLLEEFCQRIGQQLDAAEELEELLAE----LEAQLEELEEQAAEAVEQR 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1099 SQLQRKIKELQARIEELEEELEAERNARAKVEKQRaelnrelEELGERLDEAGGATSA-QIELNKKREAELLkiRRDLEE 1177
Cdd:COG3096 581 SELRQQLEQLRARIKELAARAPAWLAAQDALERLR-------EQSGEALADSQEVTAAmQQLLEREREATVE--RDELAA 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1178 ASLQHEAQISALRKKHQDAANEMADQVDQLQKV------------KSKLEKDKKDLKRE---MDDLESQMTHNMKNKGCS 1242
Cdd:COG3096 652 RKQALESQIERLSQPGGAEDPRLLALAERLGGVllseiyddvtleDAPYFSALYGPARHaivVPDLSAVKEQLAGLEDCP 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1243 EKV-MKQFESQMSDlnarleDSQRSINELqsqksrlqaENSDLTrQLEDAEHRVSVLSKE----KSQLSSQLEDARRSLE 1317
Cdd:COG3096 732 EDLyLIEGDPDSFD------DSVFDAEEL---------EDAVVV-KLSDRQWRYSRFPEVplfgRAAREKRLEELRAERD 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1318 EETRARSKLQNEVRNM---HADMDAI-------------REQLEEEQESKSDVQRQLSKANNEIQQWRSKFESeganrTE 1381
Cdd:COG3096 796 ELAEQYAKASFDVQKLqrlHQAFSQFvgghlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQ-----LK 870
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1382 ELEDQKRKLLGKLSEAEQTTeaanakcsalekaksrLQQELEDMSIEVDRANASVNQMekkqRAFDKTTAEWQAKVNSLQ 1461
Cdd:COG3096 871 EQLQLLNKLLPQANLLADET----------------LADRLEELREELDAAQEAQAFI----QQHGKALAQLEPLVAVLQ 930
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1462 S---ELENSQKESRGYSAELYRIKASIEEYQDSIGalRRENKNLADEIhdltDQLSEggrsTHEL-DKARRRLemekEEL 1537
Cdd:COG3096 931 SdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVQ--RRPHFSYEDAV----GLLGE----NSDLnEKLRARL----EQA 996
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1538 QAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKR---IQEKEEEFDntrrnhqrALEsMQASLEAEAKGkadamRIKKK 1614
Cdd:COG3096 997 EEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKqqtLQELEQELE--------ELG-VQADAEAEERA-----RIRRD 1062
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127773 1615 leqdinELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMA-ERRCTLM 1678
Cdd:COG3096 1063 ------ELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAkAGWCAVL 1121
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1251-1470 |
1.18e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1251 SQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQnev 1330
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1331 rnmhadmdairEQLEEEQESKSDVQRQLSKaNNEIQQWRSKFESEGANR-----------TEELEDQKRKLLGKLSEAEQ 1399
Cdd:COG4942 97 -----------AELEAQKEELAELLRALYR-LGRQPPLALLLSPEDFLDavrrlqylkylAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 127773 1400 TTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKE 1470
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
845-1229 |
1.32e-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: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 845 EMKEQLKQMDKMKEDLAKT-ERIKKELEEQNV---TLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQIKELE 920
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESEnSEKQRELEEKQNeieKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 921 ERLLDEEDAAADLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTL--------------QGEISQQDEHI 986
Cdd:TIGR04523 419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLsrsinkikqnleqkQKELKSKEKEL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 987 GKLNKEKKALEEANKKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREK--KVRGDVEKAKRKVEQDLKSTQENVE 1064
Cdd:TIGR04523 499 KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDfeLKKENLEKEIDEKNKEIEELKQTQK 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1065 DLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELG 1144
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIR 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1145 ERLDEaggaTSAQIELNKKREAELLKIRRDLEEASLQHEAQISALRKKHQDAAnEMADQVDQLQKVKSKLEKDKKDLKRE 1224
Cdd:TIGR04523 659 NKWPE----IIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRIKDLP-KLEEKYKEIEKELKKLDEFSKELENI 733
|
....*
gi 127773 1225 MDDLE 1229
Cdd:TIGR04523 734 IKNFN 738
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1561-1919 |
1.44e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1561 EIATVrNEIDKRIQEKEEEFDNTRRNHQRA---LESMQASLEAEAKGKADAMRIKKkLEQDINELEVALDASNrgKAEME 1637
Cdd:TIGR02169 161 EIAGV-AEFDRKKEKALEELEEVEENIERLdliIDEKRQQLERLRREREKAERYQA-LLKEKREYEGYELLKE--KEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1638 KTVKRYQQQIREMQTSIEEEQRQRDEAREsynmaerrctlmsgEVEELRAALEQ-AERARKASDNEladandrVNELTSQ 1716
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEK--------------RLEEIEQLLEElNKKIKDLGEEE-------QLRVKEK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1717 VSSVQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDE 1796
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1797 AEASSlkggkkmiQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAfQADEDRKNQ-----ERLQELIDKLNAK 1871
Cdd:TIGR02169 376 VDKEF--------AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS-EELADLNAAiagieAKINELEEEKEDK 446
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 127773 1872 IKTFKRQVEEAEEIAAINLA---KYRKAQHELEEAEERADTADSTLQKFRA 1919
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKyeqELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
945-1157 |
1.50e-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: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 945 ANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCNHLNKLKAKL 1024
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1025 EQALDELEDNLEREKKVR-----------GDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLED 1093
Cdd:COG4942 103 KEELAELLRALYRLGRQPplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 127773 1094 EQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGATSAQ 1157
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1023-1491 |
1.61e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1023 KLEQALDELEDnLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEIsslnsKLEDEQNLVSQLQ 1102
Cdd:COG4717 65 KPELNLKELKE-LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1103 RKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGATSAQIELNKKREAELLKIRRDLEEASLQH 1182
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1183 EAQISALRKKHQDAANEMADQvDQLQKVKSKLEKDKKDLKREMddLESQMTHNMKNKGCSEKVMKQFESQMSDLNARL-- 1260
Cdd:COG4717 219 QEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAAALLA--LLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLar 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1261 --EDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRnmhadMD 1338
Cdd:COG4717 296 ekASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL-----EQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1339 AIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFeseganrtEELEDQKRKLLGKLSE--AEQTTEAANAKCSALEKAKS 1416
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEYQELKEEL--------EELEEQLEELLGELEEllEALDEEELEEELEELEEELE 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127773 1417 RLQQELEDMSIEVDRANASVNQMEKkqrafDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDS 1491
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
926-1703 |
1.79e-09 |
|
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: 63.07 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 926 EEDAAADLEGIKKKmeadNANLKKDigdlENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSD 1005
Cdd:pfam02463 159 EEEAAGSRLKRKKK----EALKKLI----EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1006 SLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEIS 1085
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1086 SLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGATSAQIELNKKRE 1165
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1166 AELLKIRRDLEEASLQHEAQISALRKKHQDAANEMADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTHNMKNKGCSEKV 1245
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1246 MKQFES------QMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEE 1319
Cdd:pfam02463 471 EDLLKEtqlvklQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVI 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1320 TR---------ARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQ---RQLSKANNEIQQWRSKFESEGANRTEELEDQK 1387
Cdd:pfam02463 551 VEvsatadeveERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleIDPILNLAQLDKATLEADEDDKRAKVVEGILK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1388 RKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENS 1467
Cdd:pfam02463 631 DTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1468 QKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDL--------TDQLSEGGRSTHELDKARRRLEMEKEELQA 1539
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEeksrlkkeEKEEEKSELSLKEKELAEEREKTEKLKVEE 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1540 ALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQEKEEEFDNTR-RNHQRALESMQASLEAEAKGKADAMRIKKKLEQD 1618
Cdd:pfam02463 791 EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELeELALELKEEQKLEKLAEEELERLEEEITKEELLQ 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1619 INELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARE-SYNMAERRCTLMSGEVEELRAALEQAERARK 1697
Cdd:pfam02463 871 ELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEiEERIKEEAEILLKYEEEPEELLLEEADEKEK 950
|
....*.
gi 127773 1698 ASDNEL 1703
Cdd:pfam02463 951 EENNKE 956
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1529-1920 |
2.47e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 62.34 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1529 RLEMEKEELQAALEEAEGALEQEEAkvMRAQLEIATVRNEIDKRIQE--KEEEFDNTRRNHQRALESMQASLEAEAKGKA 1606
Cdd:COG3206 58 TLLVEPQSSDVLLSGLSSLSASDSP--LETQIEILKSRPVLERVVDKlnLDEDPLGEEASREAAIERLRKNLTVEPVKGS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1607 DAmrikkkleqdineLEVALDASNRGKAEmeKTVKRYQQQIREMQTsieeeQRQRDEARESYNMAERRctlmsgeVEELR 1686
Cdd:COG3206 136 NV-------------IEISYTSPDPELAA--AVANALAEAYLEQNL-----ELRREEARKALEFLEEQ-------LPELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1687 AALEQAERARKA--SDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQtdldemhgelkgaderckkamadaARLAd 1764
Cdd:COG3206 189 KELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE------------------------ARLA- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1765 elraeqdhsnqvekvrkNLESQVKEFQIRLDEAEASSLkggkkmIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRL 1844
Cdd:COG3206 244 -----------------ALRAQLGSGPDALPELLQSPV------IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 1845 KEL-AFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEAEEiaaiNLAKYRKAQHELEEAEERADTADSTLQKFRAK 1920
Cdd:COG3206 301 AALrAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA----RLAELPELEAELRRLEREVEVARELYESLLQR 373
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1498-1916 |
2.66e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1498 ENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEM------EKEELQAALEEAEGA-LEQEEAKVMRAQLEIATVRNEID 1570
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIELlepireLAERYAAARERLAELeYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1571 K------RIQEKEEEFDNTRRNHQRALESMQASLeAEAKGKAdamriKKKLEQDINELEVALDasnrgkaEMEKTVKRYQ 1644
Cdd:COG4913 299 ElraelaRLEAELERLEARLDALREELDELEAQI-RGNGGDR-----LEQLEREIERLERELE-------ERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1645 QQIREMQTSIEEEQRQRDEARESynmAERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNELTSQVSSVQGQK 1724
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1725 RKLEGDIN-AMQTDLDEMH--GEL---KGADERCKKAM------------------ADAARLADELRAEQDHsnQVEKVR 1780
Cdd:COG4913 443 LALRDALAeALGLDEAELPfvGELievRPEEERWRGAIervlggfaltllvppehyAAALRWVNRLHLRGRL--VYERVR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1781 KNLESQVKEfqirldEAEASSLkggkkmIQKLESRVHELEAELDNE---------------------------QRRHAET 1833
Cdd:COG4913 521 TGLPDPERP------RLDPDSL------AGKLDFKPHPFRAWLEAElgrrfdyvcvdspeelrrhpraitragQVKGNGT 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1834 --QKNMRK-----------ADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEAEEIAA-----INLAKYRK 1895
Cdd:COG4913 589 rhEKDDRRrirsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeIDVASAER 668
|
490 500
....*....|....*....|.
gi 127773 1896 AQHELEEAEERADTADSTLQK 1916
Cdd:COG4913 669 EIAELEAELERLDASSDDLAA 689
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
950-1465 |
4.10e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 61.84 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 950 DIGDLENTLQKaeqdkahKDNQISTLQGEISQQDEHIGKLNKEKKALEEAnkktsdsLQAEEDKCNHLNklkakleQALD 1029
Cdd:PRK01156 184 NIDYLEEKLKS-------SNLELENIKKQIADDEKSHSITLKEIERLSIE-------YNNAMDDYNNLK-------SALN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1030 ELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEIS---SLNSKLEDEQNLVSQLQRKIK 1106
Cdd:PRK01156 243 ELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINdyfKYKNDIENKKQILSNIDAEIN 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1107 ELQArIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGATSAQIELNKKREAELLKIRRDLEEASLQHEAQ- 1185
Cdd:PRK01156 323 KYHA-IIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQe 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1186 -----ISALRKKHQDAANEMADQVDQLQKVKSKLEKDKKDLKREMDDLESQM------THNMKNKgcSEKVMKQFESQMS 1254
Cdd:PRK01156 402 idpdaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgTTLGEEK--SNHIINHYNEKKS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1255 DLNARLEDSQRSINELQSQKSRLQAENSDL-TRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRArSKLQNEVRNM 1333
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVDLKKRKEYLeSEEINKSINEYNKIESARADLEDIKIKINELKDKHDKY-EEIKNRYKSL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1334 H-ADMDAIREQ------------LEEEQESKSDVQRQLSKANNEIQQWRSKF---ESEGANRTEELEDQKRKLLGKLSEA 1397
Cdd:PRK01156 559 KlEDLDSKRTSwlnalavislidIETNRSRSNEIKKQLNDLESRLQEIEIGFpddKSYIDKSIREIENEANNLNNKYNEI 638
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 127773 1398 EQTTEAANAKCSALEKAKSRL------QQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELE 1465
Cdd:PRK01156 639 QENKILIEKLRGKIDNYKKQIaeidsiIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRIN 712
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1247-1482 |
4.45e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1247 KQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKL 1326
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1327 QNEVRNMHADMDAIREQLEEE----QESKSDVQRQLsKANNEIQQWRskfesegANRTEELEDQKRKLLGKLSEAEQTTE 1402
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRL-QYLKYLAPAR-------REQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1403 AANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIK 1482
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
931-1916 |
6.19e-09 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 61.61 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 931 ADLEGIKKKMEADNANLKKDI-GDLENTLQKAEQDKAHKDNQISTLQGEISQQDEhigKLNKEKKALEEANKKTSDSLQ- 1008
Cdd:TIGR01612 725 SNIENKKNELLDIIVEIKKHIhGEINKDLNKILEDFKNKEKELSNKINDYAKEKD---ELNKYKSKISEIKNHYNDQINi 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1009 ---AEEDKCNHLNKLKAKLEQ---ALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRK-- 1080
Cdd:TIGR01612 802 dniKDEDAKQNYDKSKEYIKTisiKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEis 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1081 EAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAER---NARAKVEKQRAELNRELEELGERLDEAGGATSAQ 1157
Cdd:TIGR01612 882 DDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKiceNTKESIEKFHNKQNILKEILNKNIDTIKESNLIE 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1158 IELNKKREAELLKIRRDLE----EASLQ-HEAQISALRKKHQD--------AANEMADQVDQLQKVKSKLEKDKKDLKRE 1224
Cdd:TIGR01612 962 KSYKDKFDNTLIDKINELDkafkDASLNdYEAKNNELIKYFNDlkanlgknKENMLYHQFDEKEKATNDIEQKIEDANKN 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1225 MDDLESQMTHNMKNkgCSEKVMKQFESQMSDLNAR-LEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVlSKEKS 1303
Cdd:TIGR01612 1042 IPNIEIAIHTSIYN--IIDEIEKEIGKNIELLNKEiLEEAEINITNFNEIKEKLKHYNFDDFGKEENIKYADEI-NKIKD 1118
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1304 QLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIrEQLEEEQESKSDVQRQLSKANNEIQQwrskfesegANRTEEL 1383
Cdd:TIGR01612 1119 DIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDL-EDVADKAISNDDPEEIEKKIENIVTK---------IDKKKNI 1188
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1384 EDQKRKLLGKLSEAEQ-TTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQakvnslqs 1462
Cdd:TIGR01612 1189 YDEIKKLLNEIAEIEKdKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSP-------- 1260
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1463 ELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADeIHDLTDQLSEGGRSTHELDKARRrlEMEKEELQAALE 1542
Cdd:TIGR01612 1261 EIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISD-IREKSLKIIEDFSEESDINDIKK--ELQKNLLDAQKH 1337
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1543 EAEGALEQEEAKVMRAQLEIATVRNEIDKrIQEKEEEFDNTRRNHQRALESMQasleaeakgkadamRIKKKLEQDINEL 1622
Cdd:TIGR01612 1338 NSDINLYLNEIANIYNILKLNKIKKIIDE-VKEYTKEIEENNKNIKDELDKSE--------------KLIKKIKDDINLE 1402
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1623 EValdasnrgKAEMEKTVKRYQ-----QQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAERARK 1697
Cdd:TIGR01612 1403 EC--------KSKIESTLDDKDideciKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKK 1474
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1698 asDNELADANDRVNELTSQVSsvQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVE 1777
Cdd:TIGR01612 1475 --DNATNDHDFNINELKEHID--KSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIII 1550
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1778 KVRKNLESQ--------------VKEFQIRLDEAEASSLKGGKKMIQkLESRVHELEAEL---DNEQRRHAETQKNMRKA 1840
Cdd:TIGR01612 1551 KEIKDAHKKfileaekseqkikeIKKEKFRIEDDAAKNDKSNKAAID-IQLSLENFENKFlkiSDIKKKINDCLKETESI 1629
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1841 DRRLKELAFQADE----------------------DRKNQERLQELIDKLNAKIKTFKRQVEEAEEIAAINLAKYRK--A 1896
Cdd:TIGR01612 1630 EKKISSFSIDSQDtelkengdnlnslqefleslkdQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKeiA 1709
|
1050 1060
....*....|....*....|
gi 127773 1897 QHELEEAEERADTADSTLQK 1916
Cdd:TIGR01612 1710 IANKEEIESIKELIEPTIEN 1729
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
898-1128 |
6.38e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 898 QEERVEKLIMQKADFESQIKELEERLLDEEDAAADLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQG 977
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 978 EISQQDEHIGKLNKEKKALEEANKKT----SDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVE 1053
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127773 1054 QDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAK 1128
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1006-1209 |
7.35e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1006 SLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEIS 1085
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1086 SLNSKLEDEQNLVSQLQRKIKELQAR-----IEELEEELEAERNAR--AKVEKQRAELNRELEELGERLDEAGGATSAQI 1158
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQpplalLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 127773 1159 ELNKKREAELLKIRRDLEEASLQHEAQISALRKK---HQDAANEMADQVDQLQK 1209
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKElaeLAAELAELQQEAEELEA 227
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
845-1885 |
7.76e-09 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 61.22 E-value: 7.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 845 EMKEQLKQMDKMKEDLAKTERIKKELEEQNVTL--------------LEQKNDLFLQL-----QTLEDSMGDQEERVEKL 905
Cdd:TIGR01612 604 ELKEKIKNISDKNEYIKKAIDLKKIIENNNAYIdelakispyqvpehLKNKDKIYSTIkselsKIYEDDIDALYNELSSI 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 906 IMQKA-----------DFESQIKELEERLLDEEDAAADL-----EGIKKKMEADNANLKKDI-GDLENTLQKAEQDKAHK 968
Cdd:TIGR01612 684 VKENAidntedkakldDLKSKIDKEYDKIQNMETATVELhlsniENKKNELLDIIVEIKKHIhGEINKDLNKILEDFKNK 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 969 DNQISTLQGEISQQDEhigKLNKEKKALEEANKKTSDSLQ----AEEDKCNHLNKLKAKLEQ---ALDELEDNLEREKKV 1041
Cdd:TIGR01612 764 EKELSNKINDYAKEKD---ELNKYKSKISEIKNHYNDQINidniKDEDAKQNYDKSKEYIKTisiKEDEIFKIINEMKFM 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1042 RGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRK--EAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEEL 1119
Cdd:TIGR01612 841 KDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEisDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVD 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1120 EAER---NARAKVEKQRAELNRELEELGERLDEAGGATSAQIELNKKREAELLKIRRDLE----EASLQ-HEAQISALRK 1191
Cdd:TIGR01612 921 EYIKiceNTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDkafkDASLNdYEAKNNELIK 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1192 KHQD--------AANEMADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTHNMKNkgCSEKVMKQFESQMSDLNAR-LED 1262
Cdd:TIGR01612 1001 YFNDlkanlgknKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYN--IIDEIEKEIGKNIELLNKEiLEE 1078
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1263 SQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVlSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIrE 1342
Cdd:TIGR01612 1079 AEINITNFNEIKEKLKHYNFDDFGKEENIKYADEI-NKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDL-E 1156
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1343 QLEEEQESKSDVQRQLSKANNEIQQwrskfesegANRTEELEDQKRKLLGKLSEAEQ-TTEAANAKCSALEKAKSRLQQE 1421
Cdd:TIGR01612 1157 DVADKAISNDDPEEIEKKIENIVTK---------IDKKKNIYDEIKKLLNEIAEIEKdKTSLEEVKGINLSYGKNLGKLF 1227
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1422 LEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQakvnslqsELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKN 1501
Cdd:TIGR01612 1228 LEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSP--------EIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDEN 1299
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1502 LADeIHDLTDQLSEGGRSTHELDKARRrlEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKrIQEKEEEFD 1581
Cdd:TIGR01612 1300 ISD-IREKSLKIIEDFSEESDINDIKK--ELQKNLLDAQKHNSDINLYLNEIANIYNILKLNKIKKIIDE-VKEYTKEIE 1375
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1582 NTRRNHQRALESMQasleaeakgkadamRIKKKLEQDINELEValdasnrgKAEMEKTVKRYQ-----QQIREMQTSIEE 1656
Cdd:TIGR01612 1376 ENNKNIKDELDKSE--------------KLIKKIKDDINLEEC--------KSKIESTLDDKDideciKKIKELKNHILS 1433
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1657 EQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAERARKasDNELADANDRVNELTSQVSsvQGQKRKLEGDINAMQT 1736
Cdd:TIGR01612 1434 EESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKK--DNATNDHDFNINELKEHID--KSKGCKDEADKNAKAI 1509
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1737 DLDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVEKVRKNLESQ--------------VKEFQIRLDEAEASSL 1802
Cdd:TIGR01612 1510 EKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKfileaekseqkikeIKKEKFRIEDDAAKND 1589
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1803 KGGKKMIQkLESRVHELEAEL---DNEQRRHAETQKNMRKADRRLKELAFQADEDR-----KNQERLQELIDKLNAKIKT 1874
Cdd:TIGR01612 1590 KSNKAAID-IQLSLENFENKFlkiSDIKKKINDCLKETESIEKKISSFSIDSQDTElkengDNLNSLQEFLESLKDQKKN 1668
|
1130
....*....|.
gi 127773 1875 FKRQVEEAEEI 1885
Cdd:TIGR01612 1669 IEDKKKELDEL 1679
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
841-1448 |
8.79e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 60.69 E-value: 8.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 841 RQEEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNDLFLQLQtledSMGDQEERVEKLIMQKADFESqikele 920
Cdd:PRK01156 194 SSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN----ELSSLEDMKNRYESEIKTAES------ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 921 erlldeedaaadlegiKKKMEADNANlkkDIGDLENTLQKAEQDKAHKD----NQISTLQGEISQQDEHIGKLNKEKKAL 996
Cdd:PRK01156 264 ----------------DLSMELEKNN---YYKELEERHMKIINDPVYKNrnyiNDYFKYKNDIENKKQILSNIDAEINKY 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 997 EEANKKTSDsLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKstqenveDLERVKRELEEN 1076
Cdd:PRK01156 325 HAIIKKLSV-LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSK-------NIERMSAFISEI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1077 VRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEEleeeleaernarakvekqraeLNRELEELGERLDEAGGATSA 1156
Cdd:PRK01156 397 LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRA---------------------LRENLDELSRNMEMLNGQSVC 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1157 QIELNKKREAELLKIRRDLEEASLQHEAQISALRKKHQDAANEMADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTHNM 1236
Cdd:PRK01156 456 PVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIK 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1237 KNKGC-------SEKVMKQFES-QMSDLNARLED-----SQRSINELQSQKSRLQAENSdltrQLEDAEHRVSVLSKEKS 1303
Cdd:PRK01156 536 IKINElkdkhdkYEEIKNRYKSlKLEDLDSKRTSwlnalAVISLIDIETNRSRSNEIKK----QLNDLESRLQEIEIGFP 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1304 QLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQrQLSKANNEIQQWRSKFEsegaNRTEEL 1383
Cdd:PRK01156 612 DDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIE----DNLKKS 686
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127773 1384 EDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMsievDRANASVNQMEKKQRAFDK 1448
Cdd:PRK01156 687 RKALDDAKANRARLESTIEILRTRINELSDRINDINETLESM----KKIKKAIGDLKRLREAFDK 747
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
839-1177 |
1.11e-08 |
|
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: 60.47 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 839 IARQEEEMKEQLkqmDKMKEDLAKTERIKKELEEqnvtLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQIKE 918
Cdd:TIGR02169 697 LRRIENRLDELS---QELSDASRKIGEIEKEIEQ----LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 919 leerlldeedaaadlegikkkMEADNANLKKDIGDLENTLQKAEQDKahKDNQISTLQGEISQQDEHIGKLNKEKKALEE 998
Cdd:TIGR02169 770 ---------------------LEEDLHKLEEALNDLEARLSHSRIPE--IQAELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 999 ANKKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVR 1078
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1079 RKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARaKVEKQRAELNRELEELGE----RLDEAGGAT 1154
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE-DVQAELQRVEEEIRALEPvnmlAIQEYEEVL 985
|
330 340
....*....|....*....|...
gi 127773 1155 SAQIELNKKReAELLKIRRDLEE 1177
Cdd:TIGR02169 986 KRLDELKEKR-AKLEEERKAILE 1007
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
840-1165 |
1.23e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.44 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 840 ARQEEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQIKEL 919
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 920 EERLLDEED---------------------AAADLEGIKKKMEADNANLKKDIGDLENTLQKAEqdkahkdnqistlqgE 978
Cdd:PRK02224 439 RERVEEAEAlleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAE---------------D 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 979 ISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCNHLNKLKAKLEqalDELEDNLEREKKVRGDVEKAKRKV---EQD 1055
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE---AEAEEKREAAAEAEEEAEEAREEVaelNSK 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1056 LKSTQENVEDLERVkRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAE 1135
Cdd:PRK02224 581 LAELKERIESLERI-RTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAE 659
|
330 340 350
....*....|....*....|....*....|....*....
gi 127773 1136 -----LNRELEELGERLDE----AGGATSAQIELNKKRE 1165
Cdd:PRK02224 660 eyleqVEEKLDELREERDDlqaeIGAVENELEELEELRE 698
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1405-1760 |
1.38e-08 |
|
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: 59.31 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1405 NAKCSALEKAKSR---LQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRI 1481
Cdd:pfam19220 37 EAILRELPQAKSRlleLEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1482 KASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGG----RSTHELDKARRR---LEMEKEELQAALEEAEGALEQEEAK 1554
Cdd:pfam19220 117 TAQAEALERQLAAETEQNRALEEENKALREEAQAAEkalqRAEGELATARERlalLEQENRRLQALSEEQAAELAELTRR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1555 VMraqlEIATVRNEIDKRIQEKEEEFDNTRRNHQRALESMQASLEAeakgkadamrikkkLEQDINELEVALDASNRGKA 1634
Cdd:pfam19220 197 LA----ELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEA--------------HRAERASLRMKLEALTARAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1635 EMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAERAR--------------KASD 1700
Cdd:pfam19220 259 ATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARaeleeraemltkalAAKD 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1701 NELADANDRVNELTSQVSSVQgqkRKLEGDINAMQTDLDEMHGELKGadERCKKAMADAA 1760
Cdd:pfam19220 339 AALERAEERIASLSDRIAELT---KRFEVERAALEQANRRLKEELQR--ERAERALAQGA 393
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1393-1608 |
1.82e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1393 KLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELEN----SQ 1468
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraLY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1469 KESRGYSAELYRIKA-SIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEGA 1547
Cdd:COG3883 97 RSGGSVSYLDVLLGSeSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 127773 1548 LEQEEAKVMRAQLEIATVRNEIDKRIQEKEEEFDNTRRNHQRALESMQASLEAEAKGKADA 1608
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1573-1911 |
2.60e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1573 IQEKEEEFDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQT 1652
Cdd:PTZ00121 1048 IDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDA 1127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1653 SIEEEQRQRDEAR---ESYNMAERRCTLMSGEVEELRaaleQAERARKASDNELADANDRVNELTSQVSSVQGQK-RKLE 1728
Cdd:PTZ00121 1128 RKAEEARKAEDARkaeEARKAEDAKRVEIARKAEDAR----KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDaRKAE 1203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1729 GdinAMQTDLDEMHGELKGADERCKkamADAARLADELRAEQDHSNQVEKVRKNLESQvkefqiRLDEAEASSLKGGKKM 1808
Cdd:PTZ00121 1204 A---ARKAEEERKAEEARKAEDAKK---AEAVKKAEEAKKDAEEAKKAEEERNNEEIR------KFEEARMAHFARRQAA 1271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1809 IQKLESRVHElEAELDNEQRRHAETQKNMRKadRRLKELAFQADEDRKNQErLQELIDKLNAKIKTFKRQVEEAEEIAAI 1888
Cdd:PTZ00121 1272 IKAEEARKAD-ELKKAEEKKKADEAKKAEEK--KKADEAKKKAEEAKKADE-AKKKAEEAKKKADAAKKKAEEAKKAAEA 1347
|
330 340
....*....|....*....|...
gi 127773 1889 NLAKYRKAQHELEEAEERADTAD 1911
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAE 1370
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1242-1494 |
2.73e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1242 SEKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETR 1321
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1322 ARSKLQ------------NEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKfeseganrTEELEDQKRK 1389
Cdd:COG3883 101 SVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL--------KAELEAAKAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1390 LLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQK 1469
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
250 260
....*....|....*....|....*
gi 127773 1470 ESRGYSAELYRIKASIEEYQDSIGA 1494
Cdd:COG3883 253 GAAGAAAGSAGAAGAAAGAAGAGAA 277
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1316-1819 |
2.88e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1316 LEEETRARSKLQNevrnMHADMDAIREQLEEEQESKSDVQ---RQLSKANNEIQQWRSKFESEGANRTEELEDQKRKLLG 1392
Cdd:PRK04863 222 LPENSGVRKAFQD----MEAALRENRMTLEAIRVTQSDRDlfkHLITESTNYVAADYMRHANERRVHLEEALELRRELYT 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1393 ---KLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAfdkttaewQAKVNSLQSELENSQK 1469
Cdd:PRK04863 298 srrQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERY--------QADLEELEERLEEQNE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1470 ESRGYSAELYRIKASIEEYQDSIGALRrenKNLADEIHDLTDQLSEGGRSTHeldkARRRLEMEKEELQAAleeaegALE 1549
Cdd:PRK04863 370 VVEEADEQQEENEARAEAAEEEVDELK---SQLADYQQALDVQQTRAIQYQQ----AVQALERAKQLCGLP------DLT 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1550 QEEAKVMRAQLeiatvrneidkriQEKEEEFDNTRRNHQRALESMQASLEAEAKgkadAMRIKKKLEQDINelevALDAS 1629
Cdd:PRK04863 437 ADNAEDWLEEF-------------QAKEQEATEELLSLEQKLSVAQAAHSQFEQ----AYQLVRKIAGEVS----RSEAW 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1630 NRGK-----AEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAERarkasdnELA 1704
Cdd:PRK04863 496 DVARellrrLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEA-------RLE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1705 DANDRVNELTSQVSSVQGQKRKLEGDINamqtdldemhgELKGADERCKKAMADAARLADELRAEQDHSNQVEKVRKNLE 1784
Cdd:PRK04863 569 SLSESVSEARERRMALRQQLEQLQARIQ-----------RLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLL 637
|
490 500 510
....*....|....*....|....*....|....*
gi 127773 1785 SQVKEFQIRLDEAEASslkggkkmIQKLESRVHEL 1819
Cdd:PRK04863 638 ERERELTVERDELAAR--------KQALDEEIERL 664
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1592-1870 |
2.90e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 59.15 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1592 ESMQASLEAEAKGKaDAMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQ---QIREMQTSIEEEQRQR-DEARES 1667
Cdd:PRK11281 39 ADVQAQLDALNKQK-LLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQapaKLRQAQAELEALKDDNdEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1668 YNmaerrctlmSGEVEELRAALEQAErarkasdNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMHGELKG 1747
Cdd:PRK11281 118 LS---------TLSLRQLESRLAQTL-------DQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1748 ADERcKKAMADAARlaDELRAEQDHSN-QVEKVRKNLE--SQVKE-FQIRLDEAEASslkggkkmIQKLESRVHELEaEL 1823
Cdd:PRK11281 182 GKVG-GKALRPSQR--VLLQAEQALLNaQNDLQRKSLEgnTQLQDlLQKQRDYLTAR--------IQRLEHQLQLLQ-EA 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 127773 1824 DNEQRRhAETQKNMRKADRRLKELAFQ-----ADEDRKNQERLQELI---DKLNA 1870
Cdd:PRK11281 250 INSKRL-TLSEKTVQEAQSQDEAARIQanplvAQELEINLQLSQRLLkatEKLNT 303
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
839-1203 |
3.26e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 839 IARQEEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTL--LEQKNDLFLQLQTLEDSMGDQEERVEKLimqkadfesqi 916
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIAELEAELERL----------- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 917 keleerlldeEDAAADLEGIKKKMEAdnanLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKAL 996
Cdd:COG4913 681 ----------DASSDDLAALEEQLEE----LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 997 EEANkktSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLER-EKKVRGDVEKAKRK---VEQDLKSTQENVEDLERVKRE 1072
Cdd:COG4913 747 LRAL---LEERFAAALGDAVERELRENLEERIDALRARLNRaEEELERAMRAFNREwpaETADLDADLESLPEYLALLDR 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1073 LEEN-VRRKEAEISSLnsKLEDEQNLVSQLQRKIKElqarieeleeeleaernARAKVEKQRAELNRELEEL----GERL 1147
Cdd:COG4913 824 LEEDgLPEYEERFKEL--LNENSIEFVADLLSKLRR-----------------AIREIKERIDPLNDSLKRIpfgpGRYL 884
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 127773 1148 deaggatsaQIELNKKREAELLKIRRDLEEASLQHEAQISALRKKHQDAANEMADQ 1203
Cdd:COG4913 885 ---------RLEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIER 931
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
935-1637 |
3.55e-08 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 58.91 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 935 GIKKKMEADNaNLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEdKC 1014
Cdd:TIGR01612 545 GLKESYELAK-NWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDKNEYIK-KA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1015 NHLNKLKAKLEQALDELEDNLEREKKvrgDVEKAKRKVEQDLKSTQENV--EDLERVKRELEENVRRKEAEISSLNSKLE 1092
Cdd:TIGR01612 623 IDLKKIIENNNAYIDELAKISPYQVP---EHLKNKDKIYSTIKSELSKIyeDDIDALYNELSSIVKENAIDNTEDKAKLD 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1093 DEQNLVSQLQRKIKELQ-ARIEELEEELEAERNARAK--VEKQR---AELNRELEELGERLDEAGGATSAQIELNKKREA 1166
Cdd:TIGR01612 700 DLKSKIDKEYDKIQNMEtATVELHLSNIENKKNELLDiiVEIKKhihGEINKDLNKILEDFKNKEKELSNKINDYAKEKD 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1167 ELLKIRRDLEEASLQHEAQISALRKKHQDAANEMaDQVDQLQKVKSKLEKDKKDLKREMDDLESQMTH------NMKNKg 1240
Cdd:TIGR01612 780 ELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNY-DKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNkvdkfiNFENN- 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1241 CSEKV---MKQFESQMSDLNARLEDSQRSINELQSQKSRlqAENSDLTRQLEDAEHRVSVLSKEKSQLSSqLEDARRSLE 1317
Cdd:TIGR01612 858 CKEKIdseHEQFAELTNKIKAEISDDKLNDYEKKFNDSK--SLINEINKSIEEEYQNINTLKKVDEYIKI-CENTKESIE 934
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1318 EETRARSKLqNEVRNMHADMDAIREQLEEEQESK-----SDVQRQLSKA------------NNEIQQWRSKF-ESEGANR 1379
Cdd:TIGR01612 935 KFHNKQNIL-KEILNKNIDTIKESNLIEKSYKDKfdntlIDKINELDKAfkdaslndyeakNNELIKYFNDLkANLGKNK 1013
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1380 TEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKA------------KSRLQQELEDMSIEV-DRANASVNQMEK----- 1441
Cdd:TIGR01612 1014 ENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAihtsiyniideiEKEIGKNIELLNKEIlEEAEINITNFNEikekl 1093
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1442 KQRAFDKTTAEWQAK----VNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIgalrrenKNLADEIHDLTDQlSEGG 1517
Cdd:TIGR01612 1094 KHYNFDDFGKEENIKyadeINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEI-------KAQINDLEDVADK-AISN 1165
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1518 RSTHELDKARRRLEMEKEELQAALEEAEGALeQEEAKVMRAQLEIATVRN-------EIDKRIQEKeeeFDNTRRNHQRA 1590
Cdd:TIGR01612 1166 DDPEEIEKKIENIVTKIDKKKNIYDEIKKLL-NEIAEIEKDKTSLEEVKGinlsygkNLGKLFLEK---IDEEKKKSEHM 1241
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 127773 1591 LESMQASLEaeakgkaDAMRIKKKLEQDINELEVALDAsnrgKAEME 1637
Cdd:TIGR01612 1242 IKAMEAYIE-------DLDEIKEKSPEIENEMGIEMDI----KAEME 1277
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1408-1631 |
3.70e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1408 CSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFdkttaewQAKVNSLQSELENSQKESRGYSAELYRIKASIEE 1487
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKAL-------LKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1488 YQDSIGALRRENKNLADEIHDLTDQLSEGGR--------STHELDKARRRLEMEKEELQAALEEAEgALEQEEAKVMRAQ 1559
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRqpplalllSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127773 1560 LEIATVRNEIDKRIQEKEEE---FDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDINELEVALDASNR 1631
Cdd:COG4942 167 AELEAERAELEALLAELEEEraaLEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1275-1667 |
4.02e-08 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 58.76 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1275 SRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDV 1354
Cdd:PLN02939 11 SHGCGPIRSRAPFYLPSRRRLAVSCRARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1355 QRQLSKANNEIQQWRSKFESEGANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANA 1434
Cdd:PLN02939 91 TSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1435 SVNQMEKKQRAFD---KTTAEWQAKVNSLQSELENSQKE--SRGYSAELYRIKASIEeyqdsIGALRRENKNLADEIHDL 1509
Cdd:PLN02939 171 KINILEMRLSETDariKLAAQEKIHVEILEEQLEKLRNEllIRGATEGLCVHSLSKE-----LDVLKEENMLLKDDIQFL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1510 TDQLS---EGGRSTHELDKARRRLEMEKEELQAALEEAE------GALEQEE--AKVMRAQLEIATVRNEIDKRIQEKEE 1578
Cdd:PLN02939 246 KAELIevaETEERVFKLEKERSLLDASLRELESKFIVAQedvsklSPLQYDCwwEKVENLQDLLDRATNQVEKAALVLDQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1579 EfdntrRNHQRALESMQASLEaEAKGKADAMRIKKKLEQDINELEVALDASNrgkAEMEKTVKRYQQQIREMQTSI---- 1654
Cdd:PLN02939 326 N-----QDLRDKVDKLEASLK-EANVSKFSSYKVELLQQKLKLLEERLQASD---HEIHSYIQLYQESIKEFQDTLsklk 396
|
410
....*....|....
gi 127773 1655 -EEEQRQRDEARES 1667
Cdd:PLN02939 397 eESKKRSLEHPADD 410
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1533-1904 |
4.26e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 57.98 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1533 EKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQEKEEEFDNTRRNHQRALES---MQASLEAEAKGKADAM 1609
Cdd:pfam07888 42 ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKykeLSASSEELSEEKDALL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1610 RIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAAL 1689
Cdd:pfam07888 122 AQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1690 EQaerarkaSDNELADANDRVNELTSQVSSVQGQKRKLEgdinamqtdldEMHGELKGADERCKKAMADAARLADELR-- 1767
Cdd:pfam07888 202 AQ-------RDTQVLQLQDTITTLTQKLTTAHRKEAENE-----------ALLEELRSLQERLNASERKVEGLGEELSsm 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1768 -AEQDHSnQVEKVRKNLesQVKEFQIRLDEAEASSLKGGKKMIQKLESRVHELEAELDNEQRRHAETQKnmrkadrrlKE 1846
Cdd:pfam07888 264 aAQRDRT-QAELHQARL--QAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQR---------LE 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1847 LAFQadEDRKNQERLQ-EL-IDKLNAKIKTFKRQVEEAEEIAAINLAKYRKAQHELEEAE 1904
Cdd:pfam07888 332 ERLQ--EERMEREKLEvELgREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQE 389
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1020-1580 |
4.73e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 58.21 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1020 LKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELE------ENVRRKEAEISSLNSKLED 1093
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEkreaeaEEALREQAELNRLKKKYLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1094 EQNLVSQlQRKIKELQARiEELEEELEAERNARAKVEKQRAEL---NRELEELGERLDEAggatsaqielnKKREAELLK 1170
Cdd:pfam05557 87 ALNKKLN-EKESQLADAR-EVISCLKNELSELRRQIQRAELELqstNSELEELQERLDLL-----------KAKASEAEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1171 IRRDLE---EASLQHEAQIsalrkkhQDAANEMADQVDQLQKVKSKLEKDKK--DLKREMDDLESQMTHNMKNKGCSEKV 1245
Cdd:pfam05557 154 LRQNLEkqqSSLAEAEQRI-------KELEFEIQSQEQDSEIVKNSKSELARipELEKELERLREHNKHLNENIENKLLL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1246 MKQFESQMSDLNaRLEDSQRSINELQSQKSRLQAE---------NSDLT-RQLEDAEHRVSVLSKEKSQLSSQLEDARRS 1315
Cdd:pfam05557 227 KEEVEDLKRKLE-REEKYREEAATLELEKEKLEQElqswvklaqDTGLNlRSPEDLSRRIEQLQQREIVLKEENSSLTSS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1316 LEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEGANRTEELEDQKrkllgkls 1395
Cdd:pfam05557 306 ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQ-------- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1396 eaeqtteaanakcsalekaKSRLQQELEDMSIEVDRANASVN-QMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGY 1474
Cdd:pfam05557 378 -------------------LLERIEEAEDMTQKMQAHNEEMEaQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSY 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1475 SAELY-RIKASIEEYQDSIGALRRENKNLADEIHDLTDQ------------LSEGGRSTHELDKAR--RRLEMEKEELQA 1539
Cdd:pfam05557 439 SKEEVdSLRRKLETLELERQRLREQKNELEMELERRCLQgdydpkktkvlhLSMNPAAEAYQQRKNqlEKLQAEIERLKR 518
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 127773 1540 ALEEAEGALEQ-------------EEAKVMRAQLEIATVRNEIDKRI-QEKEEEF 1580
Cdd:pfam05557 519 LLKKLEDDLEQvlrlpettstmnfKEVLDLRKELESAELKNQRLKEVfQAKIQEF 573
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1566-1906 |
5.81e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.43 E-value: 5.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1566 RNEIDKRIQEKEEEFD--NTRRNHQRALESMQASLEAEAKGKADamrikkkLEQDINELEVALDASNRGKAEMEKtVKRY 1643
Cdd:PRK04863 282 RVHLEEALELRRELYTsrRQLAAEQYRLVEMARELAELNEAESD-------LEQDYQAASDHLNLVQTALRQQEK-IERY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1644 QQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRA------------------------ALEQAERARKAS 1699
Cdd:PRK04863 354 QADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSqladyqqaldvqqtraiqyqqavqALERAKQLCGLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1700 DNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTdldemhgelkgADERCKKAMADAARLADELRAEQDHSNQVEKV 1779
Cdd:PRK04863 434 DLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQA-----------AHSQFEQAYQLVRKIAGEVSRSEAWDVARELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1780 RKnLESQVkefqirldeAEASSLkggkkmiQKLESRVHELEAELDNEQRrhaetqknmrkADRRLKELAFQADEDRKNQE 1859
Cdd:PRK04863 503 RR-LREQR---------HLAEQL-------QQLRMRLSELEQRLRQQQR-----------AERLLAEFCKRLGKNLDDED 554
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 127773 1860 RLQELIDKLNAKIKTFKRQVEEAEEiaainlaKYRKAQHELEEAEER 1906
Cdd:PRK04863 555 ELEQLQEELEARLESLSESVSEARE-------RRMALRQQLEQLQAR 594
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1571-1768 |
5.84e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1571 KRIQEKEEEFDNTrrnhQRALESMQASLEAEAKGKADAMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREM 1650
Cdd:COG4942 20 DAAAEAEAELEQL----QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1651 QTSIEEEQRQ-RDEARESYNM-----------------AERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNE 1712
Cdd:COG4942 96 RAELEAQKEElAELLRALYRLgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 127773 1713 LTSQVSSVQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADAARLADELRA 1768
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1056-1659 |
6.01e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.99 E-value: 6.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1056 LKSTQENVEDLERVKRELeenvRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEEleeeleaernarakVEKQRAE 1135
Cdd:PRK01156 175 IDMLRAEISNIDYLEEKL----KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNN--------------AMDDYNN 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1136 LNRELEELGERLDEAggatsaqielnKKREAELLKIRRDLEEASLQHeaqisalrkkhqdaaNEMADQVDQLQKVKSKLE 1215
Cdd:PRK01156 237 LKSALNELSSLEDMK-----------NRYESEIKTAESDLSMELEKN---------------NYYKELEERHMKIINDPV 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1216 KDKKDLKREMDDLESQMthnmknkGCSEKVMKQFESQMSdlnaRLEDSQRSINELQSQKSrlqaensdltrQLEDAEHRV 1295
Cdd:PRK01156 291 YKNRNYINDYFKYKNDI-------ENKKQILSNIDAEIN----KYHAIIKKLSVLQKDYN-----------DYIKKKSRY 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1296 SVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESe 1375
Cdd:PRK01156 349 DDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSS- 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1376 ganrteeLEDQKRKLLGKLSEAEQTTEAANA--KC----SALEKAKSRlqQELEDMSIEVDRANASVNQMEKKQRAFDKT 1449
Cdd:PRK01156 428 -------LNQRIRALRENLDELSRNMEMLNGqsVCpvcgTTLGEEKSN--HIINHYNEKKSRLEEKIREIEIEVKDIDEK 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1450 TAEWQAKVNSLQSELENsqkESRGYSAELYRIKASIEEYQDSIGALRrenknladEIHDLTDQLSEGGRSTHELDKARRR 1529
Cdd:PRK01156 499 IVDLKKRKEYLESEEIN---KSINEYNKIESARADLEDIKIKINELK--------DKHDKYEEIKNRYKSLKLEDLDSKR 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1530 LEMEK----------EELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQEKEEEFDNTR------RNHQRALES 1593
Cdd:PRK01156 568 TSWLNalavislidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNnkyneiQENKILIEK 647
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 127773 1594 MQASLEAEAKGKADAMRIKKKL----------EQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQR 1659
Cdd:PRK01156 648 LRGKIDNYKKQIAEIDSIIPDLkeitsrindiEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINE 723
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
842-1096 |
7.94e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 842 QEEEMKEQLKQMDKMKEDLAKTERIKKELEEQnvtlleqKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQIKElee 921
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKE-------EKALLKQLAALERRIAALARRIRALEQELAALEAELAE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 922 rlldeedaaadLEGIKKKMEADNANLKKDIGDLENTLQKAeqdkahkdNQISTLQGEISQQDehIGKLNKEKKALEEANK 1001
Cdd:COG4942 88 -----------LEKEIAELRAELEAQKEELAELLRALYRL--------GRQPPLALLLSPED--FLDAVRRLQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1002 KTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKE 1081
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*
gi 127773 1082 AEISSLNSKLEDEQN 1096
Cdd:COG4942 227 ALIARLEAEAAAAAE 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1022-1175 |
8.20e-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: 8.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1022 AKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNL---- 1097
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1098 -----VSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGATSAQIE-LNKKREAELLKI 1171
Cdd:COG1579 93 alqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEeLEAEREELAAKI 172
|
....
gi 127773 1172 RRDL 1175
Cdd:COG1579 173 PPEL 176
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1247-1476 |
9.00e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 9.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1247 KQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEetRARSKL 1326
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--RARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1327 QNEVRNMHADM--------DAIR--EQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEganrTEELEDQKRKLLGKLSE 1396
Cdd:COG3883 97 RSGGSVSYLDVllgsesfsDFLDrlSALSKIADADADLLEELKADKAELEAKKAELEAK----LAELEALKAELEAAKAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1397 AEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSA 1476
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
854-1428 |
9.87e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 854 DKMKEDLAKTERIKKELE--EQNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQikeleerllDEEDAAA 931
Cdd:COG4913 228 DALVEHFDDLERAHEALEdaREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE---------LLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 932 DLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKA-HKDNQISTLQGEISQQDEHIGKLNKE----KKALEEANKKTSDS 1006
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRgNGGDRLEQLEREIERLERELEERERRrarlEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1007 LQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENV----EDLERVKRELEENVRRKEA 1082
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEALGLDEA 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1083 EISS----LNSKLEDE--QN-------------LV-----SQLQRKIKE--LQARIEELEEELEAERNARAKVEKQ---- 1132
Cdd:COG4913 459 ELPFvgelIEVRPEEErwRGaiervlggfaltlLVppehyAAALRWVNRlhLRGRLVYERVRTGLPDPERPRLDPDslag 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1133 ---------RAELNRELEELG-----ERLDEAGGATSA-----QIELNKKREAelLKIRRDLEEASL---QHEAQISALR 1190
Cdd:COG4913 539 kldfkphpfRAWLEAELGRRFdyvcvDSPEELRRHPRAitragQVKGNGTRHE--KDDRRRIRSRYVlgfDNRAKLAALE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1191 KKHQDAANEMADQVDQLQKVKSKLEKDKKDLK-------------------REMDDLESQMTHNMKNKGcsekVMKQFES 1251
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREalqrlaeyswdeidvasaeREIAELEAELERLDASSD----DLAALEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1252 QMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQnevr 1331
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR---- 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1332 nmhadmDAIREQLEEEQESKSDVQRQLSKAnneIQQWRSKFESEGANRTEELED--QKRKLLGKLSEaeqtteaanakcS 1409
Cdd:COG4913 769 ------ENLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESlpEYLALLDRLEE------------D 827
|
650
....*....|....*....
gi 127773 1410 ALEKAKSRLQQELEDMSIE 1428
Cdd:COG4913 828 GLPEYEERFKELLNENSIE 846
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
646-673 |
1.22e-07 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 53.50 E-value: 1.22e-07
10 20
....*....|....*....|....*...
gi 127773 646 SAVHRESLNKLMKNLYSTHPHFVRCIIP 673
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1277-1567 |
1.34e-07 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 55.70 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1277 LQAENSDLTRQLEDAEHRVSVL-SKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQ 1355
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1356 RQLSKANNEIQQ---WRSKFESEGANRTEELEDQK-------RKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDM 1425
Cdd:pfam00038 103 NDLVGLRKDLDEatlARVDLEAKIESLKEELAFLKknheeevRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1426 sievdranASVNQMEKKQrafdkttaEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADE 1505
Cdd:pfam00038 183 --------AAKNREEAEE--------WYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQ 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127773 1506 IHDLTDQLSeggrstHELDKARRRLEMEKEELQAALEEAEGALE--QEEAKV-MRAQLEIATVRN 1567
Cdd:pfam00038 247 LAETEERYE------LQLADYQELISELEAELQETRQEMARQLReyQELLNVkLALDIEIATYRK 305
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1522-1920 |
1.48e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1522 ELDKARRRLEmEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDK-RIQEKEEEFDNTRRNHQRALESMQASLEa 1600
Cdd:COG4717 72 ELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLE- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1601 eakgkadamrikkKLEQDINELEvaldasnrgkaEMEKTVKRYQQQIREMQTSIEEEQRQRDEAresynmAERRCTLMSG 1680
Cdd:COG4717 150 -------------ELEERLEELR-----------ELEEELEELEAELAELQEELEELLEQLSLA------TEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1681 EVEELRAALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGD----INAMQTDLDEMHGELKGADERCKKAM 1756
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARllllIAAALLALLGLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1757 ADAARLA-----DELRAEQDHSNQVEKV----------RKNLESQVKEFQIRLDEAEASSLKGGKKM--IQKLESRVHEL 1819
Cdd:COG4717 280 FLVLGLLallflLLAREKASLGKEAEELqalpaleeleEEELEELLAALGLPPDLSPEELLELLDRIeeLQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1820 EAELD---NEQRRHAETQKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEAEEIAAinLAKYRKA 1896
Cdd:COG4717 360 EEELQleeLEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEEL 437
|
410 420
....*....|....*....|....
gi 127773 1897 QHELEEAEERADTADSTLQKFRAK 1920
Cdd:COG4717 438 EEELEELEEELEELREELAELEAE 461
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1057-1576 |
1.56e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1057 KSTQENVEDLERVKRELEEnVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELeaernARAKVEKQRAEL 1136
Cdd:COG4717 64 RKPELNLKELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1137 NRELEELGERLDEAggatSAQIELNKKREAELLKIRRDLEEASLQHEAQISALRKKHQDAANEMADQVDQLQKVKSKLEK 1216
Cdd:COG4717 138 EAELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1217 DKKDLKREMDDLESQMTH--NMKNKGCSEKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAensdLTRQLEDAEHR 1294
Cdd:COG4717 214 ELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV----LFLVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1295 VSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRskfes 1374
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ----- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1375 eganrTEELEDQKRKLLGklsEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVnqmekKQRAFDKTTAEWQ 1454
Cdd:COG4717 365 -----LEELEQEIAALLA---EAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL-----EELLEALDEEELE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1455 AKVNSLQSELENSQKEsrgysaelyrikasIEEYQDSIGALRRENKNLADEihdltdqlseggrstHELdkarrrlemek 1534
Cdd:COG4717 432 EELEELEEELEELEEE--------------LEELREELAELEAELEQLEED---------------GEL----------- 471
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 127773 1535 EELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQEK 1576
Cdd:COG4717 472 AELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
844-1195 |
1.58e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.57 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 844 EEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQIKeleerl 923
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK------ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 924 ldeedaaadlegikkkmeadnaNLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALEEANKKT 1003
Cdd:TIGR04523 388 ----------------------NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1004 SDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKvrgdvekakrkveqdlkstqenveDLERVKRELEEnvrrKEAE 1083
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ------------------------NLEQKQKELKS----KEKE 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1084 ISSLNSKLEDEQNLVSQLQRKIKELQARIEE----------------LEEELEAERNARAKVEKQRAELNRELEELGERL 1147
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKlesekkekeskisdleDELNKDDFELKKENLEKEIDEKNKEIEELKQTQ 577
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 127773 1148 DEAGGATSAQIELNKKREAELLKIRRDLEE---ASLQHEAQISALRKKHQD 1195
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEKKDLIKEIEEkekKISSLEKELEKAKKENEK 628
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1220-1432 |
1.86e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1220 DLKREMDDLESQMTHNMKNKGCSEKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEH----RV 1295
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEelaeLL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1296 SVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKfese 1375
Cdd:COG4942 111 RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE---- 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 1376 gANRTEELEDQKRKLLGKLSEAEQTTEAANAkcsALEKAKSRLQQELEDMSIEVDRA 1432
Cdd:COG4942 187 -RAALEALKAERQKLLARLEKELAELAAELA---ELQQEAEELEALIARLEAEAAAA 239
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
940-1212 |
2.21e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 55.79 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 940 MEADNANLKKDIGDLENTLQKAEQDKAHKDnQISTLQGEIS----QQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCN 1015
Cdd:PHA02562 145 MQLSAPARRKLVEDLLDISVLSEMDKLNKD-KIRELNQQIQtldmKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYD 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1016 HLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENvrrkeAEISSLNSKLEDEQ 1095
Cdd:PHA02562 224 ELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKG-----GVCPTCTQQISEGP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1096 NLVSQLQRKIKELQARIEeleeeleaernarakvekqraELNRELEELGERLDEAGGATSAQIELNKKREAELLKIRRDL 1175
Cdd:PHA02562 299 DRITKIKDKLKELQHSLE---------------------KLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLV 357
|
250 260 270
....*....|....*....|....*....|....*..
gi 127773 1176 EEAsLQHEAQISALRKKHQDAANEMADQVDQLQKVKS 1212
Cdd:PHA02562 358 DKA-KKVKAAIEELQAEFVDNAEELAKLQDELDKIVK 393
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1123-1910 |
2.60e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1123 RNARAKVEKQRAELNRELEELGERLDE---AGGATSAQIE-----LNKKREAELL--KIRR---DLEEASLQHEAQisal 1189
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAElneAESDLEQDYQaasdhLNLVQTALRQqeKIERyqaDLEELEERLEEQ---- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1190 rkkhQDAANEMADQVDQLQKVKSKLEKdkkdlkrEMDDLESQMTHNMKNKGCSEKVMKQFESQMSDL---NARLEDSQRS 1266
Cdd:PRK04863 368 ----NEVVEEADEQQEENEARAEAAEE-------EVDELKSQLADYQQALDVQQTRAIQYQQAVQALeraKQLCGLPDLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1267 INELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETR------ARSKLQN--EVRNMHADMD 1338
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRseawdvARELLRRlrEQRHLAEQLQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1339 AIREQ---LEEEQESKSDVQRQLSKANneiQQWRSKFESEganrtEELEDQkrkllgkLSEAEQTTEAANAKCSALEKAK 1415
Cdd:PRK04863 517 QLRMRlseLEQRLRQQQRAERLLAEFC---KRLGKNLDDE-----DELEQL-------QEELEARLESLSESVSEARERR 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1416 SRLQQELEDMSIEVDR----------ANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASI 1485
Cdd:PRK04863 582 MALRQQLEQLQARIQRlaarapawlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEI 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1486 EEYQDSIGALRRENKNLAD--------------EIHDLTDQLSEGGRSTH-----ELDKARRRLEmEKEELQAALEEAEG 1546
Cdd:PRK04863 662 ERLSQPGGSEDPRLNALAErfggvllseiyddvSLEDAPYFSALYGPARHaivvpDLSDAAEQLA-GLEDCPEDLYLIEG 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1547 ALEQEEAKVMRAQL---EIATVRNEIDKRIQEKEEEFDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLE---QDIN 1620
Cdd:PRK04863 741 DPDSFDDSVFSVEElekAVVVKIADRQWRYSRFPEVPLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQrlhQAFS 820
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1621 E-----LEVALDASNrgKAEMEKTVKRYQQQIREMQTSIEEEQRQR---DEARESYNMAERRCTLMS--------GEVEE 1684
Cdd:PRK04863 821 RfigshLAVAFEADP--EAELRQLNRRRVELERALADHESQEQQQRsqlEQAKEGLSALNRLLPRLNlladetlaDRVEE 898
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1685 LRAALEQAERARKAsdneladandrvneltsqVSSVQGQKRKLEGDINAMQTDlDEMHGELKGADERCKKAMADA---AR 1761
Cdd:PRK04863 899 IREQLDEAEEAKRF------------------VQQHGNALAQLEPIVSVLQSD-PEQFEQLKQDYQQAQQTQRDAkqqAF 959
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1762 LADELRAEQDH---SNQVEKVRKN--LESQVKEfqiRLDEAEA--SSLKGGKKMIQKLESRVHELEAELDNEQRRHAETQ 1834
Cdd:PRK04863 960 ALTEVVQRRAHfsyEDAAEMLAKNsdLNEKLRQ---RLEQAEQerTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQML 1036
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1835 KnmrKADRRLKELAFQADEDRKNQERLQEliDKLNAKIKTFKRQVEEAE------EIAAINLAK-YRKAQHELEEAEERA 1907
Cdd:PRK04863 1037 Q---ELKQELQDLGVPADSGAEERARARR--DELHARLSANRSRRNQLEkqltfcEAEMDNLTKkLRKLERDYHEMREQV 1111
|
...
gi 127773 1908 DTA 1910
Cdd:PRK04863 1112 VNA 1114
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1454-1846 |
2.82e-07 |
|
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: 55.07 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1454 QAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEME 1533
Cdd:pfam19220 26 KADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1534 KEELQAAL-------EEAEGALEQEEAKVMRAQLEIATVRNEI---DKRIQEKEEEFDNTRRNHQRalesmqasLEAEAK 1603
Cdd:pfam19220 106 KEELRIELrdktaqaEALERQLAAETEQNRALEEENKALREEAqaaEKALQRAEGELATARERLAL--------LEQENR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1604 gkadamRIKKKLEQDINELeVALDASNrgkAEMEKTVKRYQQQIREMQTSIEEEQ--RQRDEAresynmaerrctlmsge 1681
Cdd:pfam19220 178 ------RLQALSEEQAAEL-AELTRRL---AELETQLDATRARLRALEGQLAAEQaeRERAEA----------------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1682 veELRAALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADAAR 1761
Cdd:pfam19220 231 --QLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLER 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1762 LADELraeqdhsNQVEKVRKNLESQVkefqirldEAEASSLKGGKKMIQKLESRVHELEAELDNEQRRHAETQKNMRKAD 1841
Cdd:pfam19220 309 RTQQF-------QEMQRARAELEERA--------EMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQAN 373
|
....*
gi 127773 1842 RRLKE 1846
Cdd:pfam19220 374 RRLKE 378
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1088-1727 |
3.27e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 55.52 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1088 NSKLEDEQNLVSQLQRKIKElqarieeleeELEAERNARAKVEKQRAELNRELEELGERLDEaggaTSAQIELNKKREAE 1167
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQ----------MELEHKRARIELEKKASALKRQLDRESDRNQE----LQKRIRLLEKREAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1168 llkirrdlEEASLQHEAQISALRKKHQDAAN----EMADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTHNMKNKGCSE 1243
Cdd:pfam05557 67 --------AEEALREQAELNRLKKKYLEALNkklnEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1244 KVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQaensDLTRQLEDAEHRVSVLSKEKSQLSS--QLEDARRSLEEETR 1321
Cdd:pfam05557 139 ERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIK----ELEFEIQSQEQDSEIVKNSKSELARipELEKELERLREHNK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1322 ARSKLQNE---VRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEGAN-RTEELedqkrkLLGKLSEA 1397
Cdd:pfam05557 215 HLNENIENkllLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNlRSPED------LSRRIEQL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1398 EQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRafdkttaEWQAKVNSLQSELENSQKESRGYsae 1477
Cdd:pfam05557 289 QQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLK-------RHKALVRRLQRRVLLLTKERDGY--- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1478 lyriKASIEEYQDsigalrrenknladeihDLTDqlseggrSTHELDKARRRLEMEK--EELQAALEEAEGALEQEEAKV 1555
Cdd:pfam05557 359 ----RAILESYDK-----------------ELTM-------SNYSPQLLERIEEAEDmtQKMQAHNEEMEAQLSVAEEEL 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1556 MRAQLEIATVRNEIDKRIQEKEEEFDNTRRNHQRALESMQASLEAEakgkadamriKKKLEQDINELEVALDASN-RGKA 1634
Cdd:pfam05557 411 GGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLELE----------RQRLREQKNELEMELERRClQGDY 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1635 EMEKTvkrYQQQIREMQTSIEEEQRQrdearESYNMAERRCTLMSGEVEELRAALEQAERARKASDNEladANDRVNELT 1714
Cdd:pfam05557 481 DPKKT---KVLHLSMNPAAEAYQQRK-----NQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTM---NFKEVLDLR 549
|
650
....*....|...
gi 127773 1715 SQVSSVQGQKRKL 1727
Cdd:pfam05557 550 KELESAELKNQRL 562
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1346-1631 |
3.31e-07 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 56.00 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1346 EEQESKSDVQRQLSKANNEiQQWRSKFESEGANRtEELEDQKRKLLGKLSEAEQTTEAANAkcSALEK----AKSRLQQE 1421
Cdd:NF012221 1539 ESSQQADAVSKHAKQDDAA-QNALADKERAEADR-QRLEQEKQQQLAAISGSQSQLESTDQ--NALETngqaQRDAILEE 1614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1422 LEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAK-----VNSLQSELENSQKESRGYSAEL-YRIKASIEEYQDSIG-- 1493
Cdd:NF012221 1615 SRAVTKELTTLAQGLDALDSQATYAGESGDQWRNPfagglLDRVQEQLDDAKKISGKQLADAkQRHVDNQQKVKDAVAks 1694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1494 --ALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEGALEQEeakVMRAQLEIATVRNEIdK 1571
Cdd:NF012221 1695 eaGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQD---ASAAENKANQAQADA-K 1770
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1572 RIQEKEEEFDNTRRNHQRALESMQASLEA----------EAKGKADAMRIKKKLEQDINELEVALDASNR 1631
Cdd:NF012221 1771 GAKQDESDKPNRQGAAGSGLSGKAYSVEGvaepgshinpDSPAAADGRFSEGLTEQEQEALEGATNAVNR 1840
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1584-1906 |
3.59e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.73 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1584 RRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDineLEVALDASNRGKAEM---EKtVKRYQQQIREMQTSIEEEQRQ 1660
Cdd:COG3096 294 LFGARRQLAEEQYRLVEMARELEELSARESDLEQD---YQAASDHLNLVQTALrqqEK-IERYQEDLEELTERLEEQEEV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1661 RDEARESYNMAERRCTLMSGEVEEL----------------RA--------ALEQAERARKASDNELADANDRVNELTSQ 1716
Cdd:COG3096 370 VEEAAEQLAEAEARLEAAEEEVDSLksqladyqqaldvqqtRAiqyqqavqALEKARALCGLPDLTPENAEDYLAAFRAK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1717 VSSVQGQKRKLE---GDINAMQTDLDEMHGELKG---------ADERCKKAMADAARL------ADELRAEQDHSNQVEK 1778
Cdd:COG3096 450 EQQATEEVLELEqklSVADAARRQFEKAYELVCKiageversqAWQTARELLRRYRSQqalaqrLQQLRAQLAELEQRLR 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1779 VRKNLESQVKEFQIRLDEaEASSLKGGKKMIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDRKNQ 1858
Cdd:COG3096 530 QQQNAERLLEEFCQRIGQ-QLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQ 608
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 127773 1859 ERLQELIDKLNAKIKTfKRQVEEAEEIAainLAKYRKAQHELEEAEER 1906
Cdd:COG3096 609 DALERLREQSGEALAD-SQEVTAAMQQL---LEREREATVERDELAAR 652
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
828-1290 |
3.83e-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: 55.50 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 828 KLYSKVKPLLSIARQEEEMKEqlKQMDKMKEDLAKTERIKKELEEqnvtLLEQKNDLFLQLQTLEDSMGDQEerveKLIM 907
Cdd:pfam05483 353 EFEATTCSLEELLRTEQQRLE--KNEDQLKIITMELQKKSSELEE----MTKFKNNKEVELEELKKILAEDE----KLLD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 908 QKADFEsqikeleerlldeeDAAADLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIG 987
Cdd:pfam05483 423 EKKQFE--------------KIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNI 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 988 KLNKEKKALEEANKK----TSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENV 1063
Cdd:pfam05483 489 ELTAHCDKLLLENKEltqeASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1064 EDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEEL 1143
Cdd:pfam05483 569 DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASA 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1144 GERLDEAGGATSAQIELNKKREAELLKirrDLEEASLQHEAQISALRKKHQDAANEMADQVDQLQKVKSKLEKDKkdlkr 1223
Cdd:pfam05483 649 KQKFEEIIDNYQKEIEDKKISEEKLLE---EVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKII----- 720
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 1224 EMDDLESQMTHNMKNKGCSEKVmkQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLED 1290
Cdd:pfam05483 721 EERDSELGLYKNKEQEQSSAKA--ALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1003-1318 |
4.26e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 55.30 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1003 TSDSLQAEEDKcnhLNK----------LKAKLEQALDELeDNLEREKKvrgDVEKAKRKVEQDLKSTQENVEDLERVKRE 1072
Cdd:PRK11281 37 TEADVQAQLDA---LNKqklleaedklVQQDLEQTLALL-DKIDRQKE---ETEQLKQQLAQAPAKLRQAQAELEALKDD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1073 LEENVRRKEAEIS--SLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEelGERLDEA 1150
Cdd:PRK11281 110 NDEETRETLSTLSlrQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLK--GGKVGGK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1151 GGATSAQIELNKkrEAELLKIRRDLEEASLQHEAQISALRKKHQDaanEMADQVDQLQKvksklekdkkdlkrEMDDLes 1230
Cdd:PRK11281 188 ALRPSQRVLLQA--EQALLNAQNDLQRKSLEGNTQLQDLLQKQRD---YLTARIQRLEH--------------QLQLL-- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1231 QMTHNMKNKGCSEKVMKQFESQmsdlnarlEDSQRSI-NELQSQKSrlqAENSDLTRQLEDAEHRVSVLSKEKSQLSSQL 1309
Cdd:PRK11281 247 QEAINSKRLTLSEKTVQEAQSQ--------DEAARIQaNPLVAQEL---EINLQLSQRLLKATEKLNTLTQQNLRVKNWL 315
|
330
....*....|..
gi 127773 1310 EDA---RRSLEE 1318
Cdd:PRK11281 316 DRLtqsERNIKE 327
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
938-1157 |
4.50e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 938 KKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCNHL 1017
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1018 NKLK------------AKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEIS 1085
Cdd:COG3883 106 DVLLgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 127773 1086 SLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGATSAQ 1157
Cdd:COG3883 186 QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1237-1554 |
4.70e-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: 54.52 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1237 KNKGCSEKVMKQFESQMSDLNARLEdsqrsinELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSL 1316
Cdd:pfam07888 59 KEKERYKRDREQWERQRRELESRVA-------ELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1317 EEETRARSKLQNEVRNMHADMDAIRE-------QLEEEQESKSDVQRQLSKANNEIQQWRSKFES------EGANRTEEL 1383
Cdd:pfam07888 132 RELEEDIKTLTQRVLERETELERMKErakkagaQRKEEEAERKQLQAKLQQTEEELRSLSKEFQElrnslaQRDTQVLQL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1384 EDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSR----------LQQELEDMSIEVDRANASV-----------NQMEKK 1442
Cdd:pfam07888 212 QDTITTLTQKLTTAHRKEAENEALLEELRSLQERlnaserkvegLGEELSSMAAQRDRTQAELhqarlqaaqltLQLADA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1443 QRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRREnknLADEIHDLTDQLSEGGRSTHE 1522
Cdd:pfam07888 292 SLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE---LGREKDCNRVQLSESRRELQE 368
|
330 340 350
....*....|....*....|....*....|..
gi 127773 1523 LDKARRRLEMEKEELQAALEEAEGALEQEEAK 1554
Cdd:pfam07888 369 LKASLRVAQKEKEQLQAEKQELLEYIRQLEQR 400
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1020-1919 |
6.14e-07 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 54.83 E-value: 6.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1020 LKAKLEQALDELEDNLER-----EKKVR--------GDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRK-EAEIS 1085
Cdd:NF041483 328 LKAEAEQALADARAEAEKlvaeaAEKARtvaaedtaAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREaEAEAD 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1086 SLNSKLEDE-QNLVSQLQRKIKELQARieeLEEELEAERNARAKVEKQRAELNREleelGERL-DEAGGATSAQIELNKK 1163
Cdd:NF041483 408 RLRGEAADQaEQLKGAAKDDTKEYRAK---TVELQEEARRLRGEAEQLRAEAVAE----GERIrGEARREAVQQIEEAAR 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1164 REAELL-KIRRDLEEASLQHEAQISALRKKHQDAANEMADQVDQ-LQKVKSKLEkdkkdlkREMDDLESQmthnmknkgc 1241
Cdd:NF041483 481 TAEELLtKAKADADELRSTATAESERVRTEAIERATTLRRQAEEtLERTRAEAE-------RLRAEAEEQ---------- 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1242 SEKVMKQFESQMSDLNarlEDSQRSINELQSQKSRlqaensDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEET- 1320
Cdd:NF041483 544 AEEVRAAAERAARELR---EETERAIAARQAEAAE------ELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETe 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1321 RARSKLQNEVRNMHADMDAIREQLEEEqeSKSDVQRQLSKANNEIQQWRSKFESEGAN-RTEELEDQKRKLLGKLSEAEQ 1399
Cdd:NF041483 615 RLRTEAAERIRTLQAQAEQEAERLRTE--AAADASAARAEGENVAVRLRSEAAAEAERlKSEAQESADRVRAEAAAAAER 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1400 T-TEAANAKCSALEKAkSRLQQELEDMsieVDRANASVNQMEKKQRA-FDKTTAEWQAKVNSLQSELENSQKESRGYSAE 1477
Cdd:NF041483 693 VgTEAAEALAAAQEEA-ARRRREAEET---LGSARAEADQERERAREqSEELLASARKRVEEAQAEAQRLVEEADRRATE 768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1478 LyrikasieeyqdsIGALRRENKNLADEIHDLTDQLSE---GGRST--HELDKARRRLEMEKEELQA-ALEEAEGALE-- 1549
Cdd:NF041483 769 L-------------VSAAEQTAQQVRDSVAGLQEQAEEeiaGLRSAaeHAAERTRTEAQEEADRVRSdAYAERERASEda 835
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1550 -------QEEAKVMRAQLEiATVRNEIDKRIQEKEEEFDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDINEL 1622
Cdd:NF041483 836 nrlrreaQEETEAAKALAE-RTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDAAAQ 914
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1623 EVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEAREsynmAERRCTLMSGEVEELRA--------ALEQAER 1694
Cdd:NF041483 915 ADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQ----AEQLIAEATGEAERLRAeaaetvgsAQQHAER 990
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1695 ARKASDNELADANDRVNELTSQVSS----------VQGQKRKLEGdinAMQTDlDEMHGELKGADERCKKAMADAARLAD 1764
Cdd:NF041483 991 IRTEAERVKAEAAAEAERLRTEAREeadrtldearKDANKRRSEA---AEQAD-TLITEAAAEADQLTAKAQEEALRTTT 1066
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1765 ElrAEQDHSNQVEKVRKNLESQVKEFQI----RLDEAEASS---LKGGKKMIQKLESRVHELEAELDNE-----QRRHAE 1832
Cdd:NF041483 1067 E--AEAQADTMVGAARKEAERIVAEATVegnsLVEKARTDAdelLVGARRDATAIRERAEELRDRITGEieelhERARRE 1144
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1833 TQKNMRKADRRLKELAFQADEDR-KNQERLQELIDKLNAkiktfkrqveeaeEIAAINLAKYRKAQHELEEAEERADTAD 1911
Cdd:NF041483 1145 SAEQMKSAGERCDALVKAAEEQLaEAEAKAKELVSDANS-------------EASKVRIAAVKKAEGLLKEAEQKKAELV 1211
|
....*...
gi 127773 1912 STLQKFRA 1919
Cdd:NF041483 1212 REAEKIKA 1219
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1271-1494 |
6.49e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1271 QSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEetrarskLQNEVRNMHADMDAIREQLEEEQES 1350
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA-------LQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1351 KSDVQRQLSKANNEIQQWRSKFESEGANRteeledqkrkLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVD 1430
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLGSESFSD----------FLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 127773 1431 RANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGA 1494
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1126-1327 |
7.14e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 7.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1126 RAKVEKQRAELNRELEELGERLDEAggatsaqielnkkrEAELLKIRR-----DLEEASLQHEAQISALRKKHQDAANEM 1200
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEA--------------EAALEEFRQknglvDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1201 ADQVDQLQKVKSKLEKDKKDL------------KREMDDLESQMTHNMKNKGCSEKVMKQFESQMSDLNARLED-SQRSI 1267
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALpellqspviqqlRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRIL 315
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127773 1268 NELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSS---QLEDARRSLE------EETRARSKLQ 1327
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRlerEVEVARELYEsllqrlEEARLAEALT 384
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1663-1919 |
7.89e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1663 EARESYNMAERrctlMSGEVEELRAALEQAERARKASD--NELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLde 1740
Cdd:COG4913 219 EEPDTFEAADA----LVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL-- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1741 mhgelkgADERCkkamadaARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAeasslkGGKkmiqklesRVHELE 1820
Cdd:COG4913 293 -------LEAEL-------EELRAELARLEAELERLEARLDALREELDELEAQIRGN------GGD--------RLEQLE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1821 AELDNEQRRHAETQKNMRKADRRLKELAFQADEDRK----NQERLQELIDKLNAKIKTFKRQVEEAEEIAAINLAKYRKA 1896
Cdd:COG4913 345 REIERLERELEERERRRARLEALLAALGLPLPASAEefaaLRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424
|
250 260
....*....|....*....|...
gi 127773 1897 QHELEEAEERADTADSTLQKFRA 1919
Cdd:COG4913 425 EAEIASLERRKSNIPARLLALRD 447
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1683-1920 |
9.15e-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: 54.29 E-value: 9.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1683 EELRAALEQA-------ERaRKASDNELADAN-------DRVNELTSQVSSVQGQKRK------LEGDINAMQ-----TD 1737
Cdd:TIGR02168 155 EERRAIFEEAagiskykER-RKETERKLERTRenldrleDILNELERQLKSLERQAEKaerykeLKAELRELElallvLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1738 LDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAeasslkggKKMIQKLESRVH 1817
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL--------ANEISRLEQQKQ 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1818 ELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEAEEIAAINLAKYRKAQ 1897
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
250 260
....*....|....*....|...
gi 127773 1898 HELEEAEERADTADSTLQKFRAK 1920
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEAR 408
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1383-1920 |
9.25e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.14 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1383 LEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRafdkttaewqaKVNSLQS 1462
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLED-----------MKNRYES 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1463 ELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKarrrlEMEK-EELQAAL 1541
Cdd:PRK01156 257 EIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDA-----EINKyHAIIKKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1542 EEAEGALEQEEAKVMRaqleiatvRNEIDKRIQEKEEEFDNTRrNHQRALESMQASLEAEAKgkaDAMRIKKKLEQDINE 1621
Cdd:PRK01156 332 SVLQKDYNDYIKKKSR--------YDDLNNQILELEGYEMDYN-SYLKSIESLKKKIEEYSK---NIERMSAFISEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1622 LEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERR--CTLMSGEVEElraalEQAERARKAS 1699
Cdd:PRK01156 400 QEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvCPVCGTTLGE-----EKSNHIINHY 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1700 DNELADANDRVNELTSQVSSVQGQKRKLE--------GDINAMQTDLDEMhgelKGADERCKKAMADAARLAD-ELRAEQ 1770
Cdd:PRK01156 475 NEKKSRLEEKIREIEIEVKDIDEKIVDLKkrkeylesEEINKSINEYNKI----ESARADLEDIKIKINELKDkHDKYEE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1771 D----HSNQVEKVRKNLESQVKEFQIRLD---EAEASSLKGGKKMIQKLESRVHELEAELDNEQrrhAETQKNMRKADRR 1843
Cdd:PRK01156 551 IknryKSLKLEDLDSKRTSWLNALAVISLidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1844 LKELAFQADEdrknQERLQELIDKLNAKIKTFKRQVEEAEEI----AAINlAKYRKAQHELEEAEERADTADSTLQKFRA 1919
Cdd:PRK01156 628 ANNLNNKYNE----IQENKILIEKLRGKIDNYKKQIAEIDSIipdlKEIT-SRINDIEDNLKKSRKALDDAKANRARLES 702
|
.
gi 127773 1920 K 1920
Cdd:PRK01156 703 T 703
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1074-1329 |
1.01e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1074 EENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAggA 1153
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER--A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1154 TSAQIELNKKREAELLkirrdLEEASLQheaqisalrkkhqdaanEMADQVDQLQKVKSKLEKDKKDLKREMDDLESQMT 1233
Cdd:COG3883 93 RALYRSGGSVSYLDVL-----LGSESFS-----------------DFLDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1234 HNMKNKGCSEKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDAR 1313
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250
....*....|....*.
gi 127773 1314 RSLEEETRARSKLQNE 1329
Cdd:COG3883 231 AAAAAAAAAAAAAASA 246
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
834-1367 |
1.20e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.90 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 834 KPLLSIARQEEEMKEQLKQMDKMKEDLAKTERIKKELEE-QNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADF 912
Cdd:TIGR01612 1173 KKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEvKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDL 1252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 913 EsQIKELEERLLDEEDAAADlegIKKKMEADNANLKKDiGDLENTLQKAEQDKAH-KDNQISTLQGEISQQDehIGKLNK 991
Cdd:TIGR01612 1253 D-EIKEKSPEIENEMGIEMD---IKAEMETFNISHDDD-KDHHIISKKHDENISDiREKSLKIIEDFSEESD--INDIKK 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 992 E-KKALEEANKKTSDSLQAEEDKCNHLNKLKakleqaldelednLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVK 1070
Cdd:TIGR01612 1326 ElQKNLLDAQKHNSDINLYLNEIANIYNILK-------------LNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLI 1392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1071 RELEENVRRKEAEiSSLNSKLEDEQnlVSQLQRKIKELQARIEELEEELEAE-RNARAKVEKQRAELNreleelgerlde 1149
Cdd:TIGR01612 1393 KKIKDDINLEECK-SKIESTLDDKD--IDECIKKIKELKNHILSEESNIDTYfKNADENNENVLLLFK------------ 1457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1150 aggatsaQIELNKKREAELLKIRRDleEASLQHEAQISALrKKHQDAANEMADQVDQLQKVKSKLEKDKKDLKREMDDL- 1228
Cdd:TIGR01612 1458 -------NIEMADNKSQHILKIKKD--NATNDHDFNINEL-KEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELl 1527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1229 ----ESQMTHNM-KNKGCSEKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAENS----------DLTRQLEDAEH 1293
Cdd:TIGR01612 1528 nkysALAIKNKFaKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAkndksnkaaiDIQLSLENFEN 1607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1294 RVSVLSKEKSQLSSQLEDArRSLEEETRARS------KLQNEVRNMHAdMDAIREQLEEEQESKSDVQRQLSKANNEIQQ 1367
Cdd:TIGR01612 1608 KFLKISDIKKKINDCLKET-ESIEKKISSFSidsqdtELKENGDNLNS-LQEFLESLKDQKKNIEDKKKELDELDSEIEK 1685
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1172-1882 |
1.37e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.80 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1172 RRDLEEASLQHEAQISALRKK---HQDAANEMADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTHNmknkgcsEKVmKQ 1248
Cdd:COG3096 280 RRELSERALELRRELFGARRQlaeEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQ-------EKI-ER 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1249 FESQMSDLNARLEDSQRSINELQSQKSRLQAensdltrQLEDAEHRVSvlskeksQLSSQLEDARRSLEE-ETRA----- 1322
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEA-------RLEAAEEEVD-------SLKSQLADYQQALDVqQTRAiqyqq 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1323 ------RSKLQNEVRNMHAD-----MDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFES----EGANRTEELEDQK 1387
Cdd:COG3096 418 avqaleKARALCGLPDLTPEnaedyLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELvckiAGEVERSQAWQTA 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1388 RKLLGKLSEAE---QTTEAANAKCSALEKAKSRlQQELEDMSIEVD-RANASVNQMEkkqrAFDKTTAEWQAKVNSLQSE 1463
Cdd:COG3096 498 RELLRRYRSQQalaQRLQQLRAQLAELEQRLRQ-QQNAERLLEEFCqRIGQQLDAAE----ELEELLAELEAQLEELEEQ 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1464 LENSQKESRGYSAELYRIKASIEEYQDSIGALRRenknLADEIHDLTDQLSEGGRSTHELDKAR-------RRLEMEKEE 1536
Cdd:COG3096 573 AAEAVEQRSELRQQLEQLRARIKELAARAPAWLA----AQDALERLREQSGEALADSQEVTAAMqqllereREATVERDE 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1537 LQAALEEAEGALEQ---------------------------------EEAKVMRAQL----------EIATVRNEIDKR- 1572
Cdd:COG3096 649 LAARKQALESQIERlsqpggaedprllalaerlggvllseiyddvtlEDAPYFSALYgparhaivvpDLSAVKEQLAGLe 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1573 --------IQEKEEEFDNTRRNHQ----------------------------RALESMQASLEAE--------AKGKADA 1608
Cdd:COG3096 729 dcpedlylIEGDPDSFDDSVFDAEeledavvvklsdrqwrysrfpevplfgrAAREKRLEELRAErdelaeqyAKASFDV 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1609 MRIkKKLEQDINE-----LEVALDASNrgkaemEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSG--- 1680
Cdd:COG3096 809 QKL-QRLHQAFSQfvgghLAVAFAPDP------EAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKllp 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1681 ------------EVEELRAALEQAERARkasdNELADANDRVNELTSQVSSVQGQKRKLEgdinAMQTDLDEMHGELKGA 1748
Cdd:COG3096 882 qanlladetladRLEELREELDAAQEAQ----AFIQQHGKALAQLEPLVAVLQSDPEQFE----QLQADYLQAKEQQRRL 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1749 DERCKK-----------AMADAARLADE-------LRAEQDHsnqVEKVRKNLESQVKEFQIRLDEAEA--SSLKGG--- 1805
Cdd:COG3096 954 KQQIFAlsevvqrrphfSYEDAVGLLGEnsdlnekLRARLEQ---AEEARREAREQLRQAQAQYSQYNQvlASLKSSrda 1030
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1806 -KKMIQKLESRVHELEAELDNE---------QRRHAETQKNMRKADRRLKELAFQADEdrknQERLQELIDKLNAKIKTF 1875
Cdd:COG3096 1031 kQQTLQELEQELEELGVQADAEaeerarirrDELHEELSQNRSRRSQLEKQLTRCEAE----MDSLQKRLRKAERDYKQE 1106
|
....*..
gi 127773 1876 KRQVEEA 1882
Cdd:COG3096 1107 REQVVQA 1113
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1150-1417 |
1.40e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1150 AGGATSAQIELNKKREAELLKIRRDLEEAslqhEAQISALRKKHQDAANEMADQVDQLQKVksklekdkkdlkremddle 1229
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAEL----EKELAALKKEEKALLKQLAALERRIAAL------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1230 sqmthnmknkgcsEKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQL 1309
Cdd:COG4942 68 -------------ARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1310 EDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEE----------EQESKSDVQRQLSKANNEIQQWRSKFESEGANR 1379
Cdd:COG4942 135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAeraeleallaELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
250 260 270
....*....|....*....|....*....|....*...
gi 127773 1380 TEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSR 1417
Cdd:COG4942 215 LAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1131-1916 |
1.47e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.43 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1131 KQRAELNRELEELgerlDEAGGATSAQIELNKKREAELLKIRRDLEEASLQHEAQISALRKKHQDAANEMADQVDQLQKV 1210
Cdd:TIGR00618 163 KEKKELLMNLFPL----DQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1211 KSKLEKDKKDlkremddLESQMTHNMKNKGCSEKVMKqfESQMSDLNARLEDSQRSINeLQSQKSRLQAENSDLTRQLED 1290
Cdd:TIGR00618 239 QQSHAYLTQK-------REAQEEQLKKQQLLKQLRAR--IEELRAQEAVLEETQERIN-RARKAAPLAAHIKAVTQIEQQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1291 AEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEvRNMHADMDAIREQLEEEQESKSDVQRQLSKANNeIQQWRS 1370
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL-QTLHSQEIHIRDAHEVATSIREISCQQHTLTQH-IHTLQQ 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1371 KFESEganrtEELEDQKRKLLGKLSEAEQTTEAANAKCSALE--KAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDK 1448
Cdd:TIGR00618 387 QKTTL-----TQKLQSLCKELDILQREQATIDTRTSAFRDLQgqLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1449 TTAEWQAKvnslqsELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDkarr 1528
Cdd:TIGR00618 462 QESAQSLK------EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ---- 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1529 RLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDK---RIQEKEEEFDNTRRNHQRALESMQASLEAEAKGK 1605
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIltqCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1606 ADAMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQ-RDEARESYNMAERRCTLMSGEVEE 1684
Cdd:TIGR00618 612 CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSiRVLPKELLASRQLALQKMQSEKEQ 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1685 LRAALEQAERARKA--SDNELADANDRVNELTSQVSSVQGQKrkLEGDINAMQTDLDEMHGElkgADERCKKAMADAARL 1762
Cdd:TIGR00618 692 LTYWKEMLAQCQTLlrELETHIEEYDREFNEIENASSSLGSD--LAAREDALNQSLKELMHQ---ARTVLKARTEAHFNN 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1763 ADELRAEQDHSNQVEKVRKNLESQVKEFqirldeaeasslkggkkmiqklESRVHELeAELDNEQRRHaetqknmRKADR 1842
Cdd:TIGR00618 767 NEEVTAALQTGAELSHLAAEIQFFNRLR----------------------EEDTHLL-KTLEAEIGQE-------IPSDE 816
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 127773 1843 RLKELafqadEDRKNQERLQELIDKLnakiktfkrqveeaeeiaAINLAKYRKAQHELEEAEERADTADSTLQK 1916
Cdd:TIGR00618 817 DILNL-----QCETLVQEEEQFLSRL------------------EEKSATLGEITHQLLKYEECSKQLAQLTQE 867
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1307-1565 |
1.55e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1307 SQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQwrskfeseganrTEELEDQ 1386
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE------------AEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1387 KRKLLGKLSEAEQTTEAANAKCSALEKAKSrlqqeLEDMsieVDRANAsVNQMEKKQRAFDKTTAEWQAKVNSLQSELEN 1466
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVLLGSES-----FSDF---LDRLSA-LSKIADADADLLEELKADKAELEAKKAELEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1467 SQKESRGYSAELYRIKASIEEYQDSIGALrreNKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEG 1546
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEAL---LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
250
....*....|....*....
gi 127773 1547 ALEQEEAKVMRAQLEIATV 1565
Cdd:COG3883 232 AAAAAAAAAAAAASAAGAG 250
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1260-1473 |
1.66e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1260 LEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADM-- 1337
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1338 -DAIREQLEEEQESKS--------DVQRQLSKANNEIQQwrskfesEGANRTEELEDQKRKLLGKLSEAEQTTEAANAKC 1408
Cdd:COG3883 98 sGGSVSYLDVLLGSESfsdfldrlSALSKIADADADLLE-------ELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127773 1409 SALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRG 1473
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
842-1110 |
1.70e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 842 QEEEMKEQLKQMDKMKEDL-AKTERIK--KELEEQNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQIKE 918
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVeERLERAEdlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEE 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 919 LEERLLDEEDAAADLEGIKKKMEADNANLKKDIGDLENtlqkaeqdkahkdnqISTLQGEISQQDEHIGKLNKEKKALEE 998
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER---------------IRTLLAAIADAEDEIERLREKREALAE 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 999 ANKKTSDSLQAEEDKcnhlnklKAKLEQALDelEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLER----VKRELE 1074
Cdd:PRK02224 621 LNDERRERLAEKRER-------KRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAeigaVENELE 691
|
250 260 270
....*....|....*....|....*....|....*...
gi 127773 1075 --ENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQA 1110
Cdd:PRK02224 692 elEELRERREALENRVEALEALYDEAEELESMYGDLRA 729
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1757-1915 |
1.87e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1757 ADAARLADELRAEQDHSNQVEKV--RKNLESQVKEFQIRLDEAEASsLKGGKKMIQKLESRVHELEAELDNEQRRHAETQ 1834
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLLlkLRELEAELEELEAELEELEAE-LEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1835 KNMRKADRRL----KELAFQADEDRKNQERLQEL---IDKLNAKIKTFKRQVEEAEEIAAINLAKYRKAQHELEEAEERA 1907
Cdd:COG1196 288 AEEYELLAELarleQDIARLEERRRELEERLEELeeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
....*...
gi 127773 1908 DTADSTLQ 1915
Cdd:COG1196 368 LEAEAELA 375
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
838-1139 |
2.25e-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: 53.15 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 838 SIARQEEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQIK 917
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 918 ELEERLLDEEdaAADLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALE 997
Cdd:TIGR02169 790 HSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 998 EANKKTSDSLQAEEDKCNHLNK----LKAKL---EQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVK 1070
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKerdeLEAQLrelERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP 947
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 127773 1071 RE------LEENVRRKEAEISSL---NSKLEDEQNLVsqlQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRE 1139
Cdd:TIGR02169 948 EEelsledVQAELQRVEEEIRALepvNMLAIQEYEEV---LKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFME 1022
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1024-1190 |
2.45e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1024 LEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLER--VKRELEENVRRKEAEISSLNSKLEDEQNLVSQL 1101
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIAL 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1102 QRKIKELQARIEELEEELEAE-RNARAKVEKQRAELNRELEELGERLDEAGGATSAQIELNkkREAELLK-----IRRDL 1175
Cdd:COG3206 297 RAQIAALRAQLQQEAQRILASlEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLE--REVEVARelyesLLQRL 374
|
170
....*....|....*
gi 127773 1176 EEASLQHEAQISALR 1190
Cdd:COG3206 375 EEARLAEALTVGNVR 389
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1485-1723 |
2.49e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1485 IEEYQDSIGALRRENKNLADEIHDLTDQLSEggrstheldkarrrLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIAT 1564
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEE--------------LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1565 VRNEIDKRIQEKEE------------------EFDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDINELEVAL 1626
Cdd:COG3883 84 RREELGERARALYRsggsvsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1627 DASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAERARKASDNELADA 1706
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
250
....*....|....*..
gi 127773 1707 NDRVNELTSQVSSVQGQ 1723
Cdd:COG3883 244 ASAAGAGAAGAAGAAAG 260
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1409-1653 |
3.41e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1409 SALEKAKSRLQQELEDMSIEVDRAnasvnqmEKKQRAFDKttaewQAKVNSLQSELENSQKESRGYSAELYRIKASIEEY 1488
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEA-------EAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1489 QDSIGALRRENKNLADEIHDLTDqlseggrsthelDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNE 1568
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQ------------SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1569 IDKRIQEKEEEFDNTRRNHQRALESMQASLEaEAKGKADAMrikKKLEQDINELEVALDASnrgKAEMEKTVKRYQQ-QI 1647
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASLQAQLA-QLEARLAEL---PELEAELRRLEREVEVA---RELYESLLQRLEEaRL 379
|
....*.
gi 127773 1648 REMQTS 1653
Cdd:COG3206 380 AEALTV 385
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1405-1884 |
4.94e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 51.67 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1405 NAKCSALEKAKSRLQQELEDMSIEVDRAnasVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKesrgysaelyRIKAS 1484
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRA---RIELEKKASALKRQLDRESDRNQELQKRIRLLEK----------REAEA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1485 IEEYQDSIGALRRENKNLAdeihdltdqlseggrstheldkARRRLEMEKEELQAALEEAEGALEQEEA----KVMRAQL 1560
Cdd:pfam05557 68 EEALREQAELNRLKKKYLE----------------------ALNKKLNEKESQLADAREVISCLKNELSelrrQIQRAEL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1561 EIATVRNEIdKRIQEKEEEFDNTRRNHqralESMQASLEAEAKGKADAmrikkklEQDINELEVALDASNRGKAEMeKTV 1640
Cdd:pfam05557 126 ELQSTNSEL-EELQERLDLLKAKASEA----EQLRQNLEKQQSSLAEA-------EQRIKELEFEIQSQEQDSEIV-KNS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1641 KRYQQQIREMqtsiEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNELTSQVSSV 1720
Cdd:pfam05557 193 KSELARIPEL----EKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1721 QGQKRK------LEGDINAMQTDlDEMHGELKGADERCKKAMADAAR-LADELRAEQDHSNQVEKVRKNLESQVKEFQIR 1793
Cdd:pfam05557 269 QDTGLNlrspedLSRRIEQLQQR-EIVLKEENSSLTSSARQLEKARReLEQELAQYLKKIEDLNKKLKRHKALVRRLQRR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1794 ---------------------LDEAEASS-----LKGGKKMIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKEL 1847
Cdd:pfam05557 348 vllltkerdgyrailesydkeLTMSNYSPqllerIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQAL 427
|
490 500 510
....*....|....*....|....*....|....*..
gi 127773 1848 AFQadEDRKNQERLQELIDKLNAKIKTFKRQVEEAEE 1884
Cdd:pfam05557 428 RQQ--ESLADPSYSKEEVDSLRRKLETLELERQRLRE 462
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1281-1469 |
5.09e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1281 NSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEEtrarsKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSK 1360
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEF-----RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1361 ANNEIQQWRSKFESEGANRTE---------------ELEDQKRKLLGKLSEAEQTTEAANAKCSALEKA-KSRLQQELED 1424
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPEllqspviqqlraqlaELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILAS 317
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 127773 1425 MSIEVDRANASVNQMEKKQRAFD---KTTAEWQAKVNSLQSELENSQK 1469
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEarlAELPELEAELRRLEREVEVARE 365
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
759-1167 |
7.94e-06 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 51.33 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 759 KVFFKAGVLGNLEEMRDERLSKIISMFQ----AHIRGYL-----------------IRKAYKKLQDQRIGLSVIQ--RNI 815
Cdd:PTZ00341 676 KFFFEKKLSMNDLDNKSEHLLKFMEQYQkereAHISENLinilqpciagdrkwdvpIIDKIEELKGSPFDIAIIDsiGWI 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 816 RKWLVLRNWQWWKLYSKVKPLLSIARQEEEMKEQLKQMDKMKEDLAKTERIKK-ELEEQNVTLLEQKNDLFLQLQTLedS 894
Cdd:PTZ00341 756 FKHVAKSHLKKPKKAAKKLEQRSKANKEELANENNKLMNILKEYFGNNEQINSiTYNFENINLNEDNENGSKKILDL--N 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 895 MGDQEERVEKLI-----MQKADFESQIKELEERLLDEEdaAADLEGIKKKMEAdnanLKKDIGDLENTLQKAEQDKAHKD 969
Cdd:PTZ00341 834 HKDQKEIFEEIIsyivdISLSDIENTAKNAAEQILSDE--GLDEKKLKKRAES----LKKLANAIEKYAGGGKKDKKAKK 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 970 NQISTLQGEISQQdehIGKLNKEkkaLEEANKKTSDSLQaEEDKCNHLNKLKAKLEQALDE-LEDNLER--EKKVRGDVE 1046
Cdd:PTZ00341 908 KDAKDLSGNIAHE---INLINKE---LKNQNENVPEHLK-EHAEANIEEDAEENVEEDAEEnVEENVEEnvEENVEENVE 980
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1047 KakrKVEQDLK-STQENVEdlERVKRELEENVRRKEAEISSLNSKLEDEQNL--VSQLQRKIKELQARIEELEEELEAER 1123
Cdd:PTZ00341 981 E---NVEENVEeNVEENVE--ENVEENIEENVEENVEENIEENVEEYDEENVeeVEENVEEYDEENVEEIEENAEENVEE 1055
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 127773 1124 NARAKVEKQRAELNRELEE-----LGERLDEAGGATSAQIELNKKREAE 1167
Cdd:PTZ00341 1056 NIEENIEEYDEENVEEIEEnieenIEENVEENVEENVEEIEENVEENVE 1104
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
983-1150 |
8.31e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 50.91 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 983 DEHIGKLNKEKKALEEANKktsdslQAEEDKcNHLNKLKAKLEQALDELEDNLER-----EKKVRGDVEKAKRKVEQ--- 1054
Cdd:COG1193 517 EKLIEELERERRELEEERE------EAERLR-EELEKLREELEEKLEELEEEKEEilekaREEAEEILREARKEAEElir 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1055 DLKSTQENVEDLERVKRELEENVRRKEAE------------------------ISSLNSK-----LEDEQNLVSQ----- 1100
Cdd:COG1193 590 ELREAQAEEEELKEARKKLEELKQELEEKlekpkkkakpakppeelkvgdrvrVLSLGQKgevleIPKGGEAEVQvgilk 669
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 127773 1101 LQRKIKELQaRIEELEEELEAERNARAKVEKQRA-ELNRELEELGERLDEA 1150
Cdd:COG1193 670 MTVKLSDLE-KVEKKKPKKPKKRPAGVSVSVSKAsTVSPELDLRGMRVEEA 719
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
840-1202 |
9.21e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 840 ARQEEEMKEQLKQMDKMKEDLAKTERIKKELEE--QNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQIK 917
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 918 ELEERLLDEEDAAADLEgikKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALE 997
Cdd:COG4717 164 ELEELEAELAELQEELE---ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 998 EANKK------------------TSDSLQAEEDKC---------------NHLNKLKAKLEQALDELEDNLEREKKVRGD 1044
Cdd:COG4717 241 LEERLkearlllliaaallallgLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1045 VEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLnskledeqnlvsQLQRKIKELQARIEELEEELEAERN 1124
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL------------QLEELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1125 ARAKVEKQRAELNRELEELGERLDEAGGATSAQIELNKKR--EAELLKIRRDLEEAslqhEAQISALRKKHQDAANEMAD 1202
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEEL----EEELEELREELAELEAELEQ 464
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1485-1801 |
1.10e-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: 50.51 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1485 IEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRsthELDKaRRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIAT 1564
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAR---EVER-RRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1565 VRNEIDKRIQE------------KEEEFDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDINELEVAldASNRG 1632
Cdd:pfam17380 353 IRQEERKRELErirqeeiameisRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI--RAEQE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1633 KAEMEKTVKRYQQQIREMQTSIEEEQ-RQRDEARESYNMAERRCTLMSGEVEELRAALEQAERaRKASDNELADANDRVN 1711
Cdd:pfam17380 431 EARQREVRRLEEERAREMERVRLEEQeRQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR-RKILEKELEERKQAMI 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1712 EltsqvssvQGQKRK-LEGDINAMQTDLDEMHGELKGADERCK-KAMADAARLADELRAEQDHSNQVEKVRKNLE--SQV 1787
Cdd:pfam17380 510 E--------EERKRKlLEKEMEERQKAIYEEERRREAEEERRKqQEMEERRRIQEQMRKATEERSRLEAMEREREmmRQI 581
|
330
....*....|....
gi 127773 1788 KEFQIRLDEAEASS 1801
Cdd:pfam17380 582 VESEKARAEYEATT 595
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1223-1864 |
1.37e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.21 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1223 REMDDLESQMTHNMKN-------KGCSEKVMKQFE-SQMSDLNARLEDSQRSINELQSQKSRLQAE---NSDLTRQLEDA 1291
Cdd:pfam10174 17 RELDIKESKLGSSMNSiktfwspELKKERALRKEEaARISVLKEQYRVTQEENQHLQLTIQALQDElraQRDLNQLLQQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1292 EHRVSVLSKEKSQLSSQLEDARRSLEEETRARSK----LQNEVRNMHADMDAIREQLEEEQESKSD----VQRQ-LSKAN 1362
Cdd:pfam10174 97 FTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKelflLRKTLEEMELRIETQKQTLGARDESIKKllemLQSKgLPKKS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1363 NEIQQWRSKFESEGANRTEELE---DQKRKLLGKLSE----------------AEQTT-EAANAKCSALEkaksRLQQEL 1422
Cdd:pfam10174 177 GEEDWERTRRIAEAEMQLGHLEvllDQKEKENIHLREelhrrnqlqpdpaktkALQTViEMKDTKISSLE----RNIRDL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1423 EDmSIEVDRANASVN----QMEKKQRAFDKTTAEW-QAKVNSLQSELENSQKESRGYSAELYRI-------KASIEEYQD 1490
Cdd:pfam10174 253 ED-EVQMLKTNGLLHtedrEEEIKQMEVYKSHSKFmKNKIDQLKQELSKKESELLALQTKLETLtnqnsdcKQHIEVLKE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1491 SIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRneid 1570
Cdd:pfam10174 332 SLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQ---- 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1571 KRIQEKEEEFDNTRR----------NHQRALESMQaslEAEAKGKADAMRIKKKLEQDINELEVALDASNRGKAEMEKTV 1640
Cdd:pfam10174 408 EQLRDKDKQLAGLKErvkslqtdssNTDTALTTLE---EALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKV 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1641 KRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEV----EELRAALEQAERARKASDNELA--DANDRVNELT 1714
Cdd:pfam10174 485 SALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVeqkkEECSKLENQLKKAHNAEEAVRTnpEINDRIRLLE 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1715 SQVSSVQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADAARLADE--LRAEQDHSNQVEKVRKNLEsQVKEFQI 1792
Cdd:pfam10174 565 QEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEqnKKVANIKHGQQEMKKKGAQ-LLEEARR 643
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127773 1793 RLDEAEASSLKggkkmiQKLESRVHELE---AELDNEQRRHAETQKNMRKADRRLKELAFqadEDRKNQERLQEL 1864
Cdd:pfam10174 644 REDNLADNSQQ------LQLEELMGALEktrQELDATKARLSSTQQSLAEKDGHLTNLRA---ERRKQLEEILEM 709
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1421-1579 |
1.57e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1421 ELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALR--RE 1498
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1499 NKNLADEIHDLTDQLSEggrstheLDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQEKEE 1578
Cdd:COG1579 91 YEALQKEIESLKRRISD-------LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
.
gi 127773 1579 E 1579
Cdd:COG1579 164 E 164
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1492-1669 |
1.65e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1492 IGALRRENKNLADEIHDLTDQLSEggrstheLDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDK 1571
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1572 RIQEKEEEFDNTRRNH--QRALESMQAsLEAEAKGKADAMRIKKKLEQDINELEVALDASnrgKAEMEKTVKRYQQQIRE 1649
Cdd:COG1579 92 EALQKEIESLKRRISDleDEILELMER-IEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAELEELEAEREE 167
|
170 180
....*....|....*....|.
gi 127773 1650 MQTSIEEEQRQR-DEARESYN 1669
Cdd:COG1579 168 LAAKIPPELLALyERIRKRKN 188
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
850-1111 |
1.67e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 850 LKQMDKMKEDLAKterikkELEEQNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQIKELeerlldeeda 929
Cdd:PHA02562 165 LSEMDKLNKDKIR------ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEE---------- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 930 AADLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHiGKLNKEKKALEEANKKTSdSLQA 1009
Cdd:PHA02562 229 AKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKG-GVCPTCTQQISEGPDRIT-KIKD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1010 EEDKCNH-LNKLKAKLEQaLDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLN 1088
Cdd:PHA02562 307 KLKELQHsLEKLDTAIDE-LEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQ 385
|
250 260
....*....|....*....|...
gi 127773 1089 sklEDEQNLVSQLQRKIKELQAR 1111
Cdd:PHA02562 386 ---DELDKIVKTKSELVKEKYHR 405
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1691-1912 |
1.70e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1691 QAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADAA----RLADEL 1766
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEerreELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1767 RAEQDHSNQVEKVRKNLESQ-VKEFQIRLD------EAEASSLKGGKKMIQKLESRVHELEAELDNEQRRHAETQKNMRK 1839
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSEsFSDFLDRLSalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 127773 1840 ADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEAEEIAAINLAKYRKAQHELEEAEERADTADS 1912
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1300-1694 |
1.82e-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: 49.51 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1300 KEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRskfeseganr 1379
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASS---------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1380 tEELEDQKRKLLGKLSEAEQtteaanaKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRafdkttaEWQAKVNS 1459
Cdd:pfam07888 111 -EELSEEKDALLAQRAAHEA-------RIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRK-------EEEAERKQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1460 LQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEK---EE 1536
Cdd:pfam07888 176 LQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASErkvEG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1537 LQAALEEAEGALEQEEAKVMRAQLEIATVRNEI-DKRIQEKEEefdntRRNHQRALESMQASLEAEakgkadamriKKKL 1615
Cdd:pfam07888 256 LGEELSSMAAQRDRTQAELHQARLQAAQLTLQLaDASLALREG-----RARWAQERETLQQSAEAD----------KDRI 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127773 1616 EqdinelevaldasnRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERrctlmsgEVEELRAALEQAER 1694
Cdd:pfam07888 321 E--------------KLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRR-------ELQELKASLRVAQK 378
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1439-1598 |
1.93e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1439 MEKKQRA------FDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQ 1512
Cdd:COG1579 2 MPEDLRAlldlqeLDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1513 LSEGGRS------THELDKARRR---LEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQEKEEEFDNT 1583
Cdd:COG1579 82 LGNVRNNkeyealQKEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|....*
gi 127773 1584 RRNHQRALESMQASL 1598
Cdd:COG1579 162 EAEREELAAKIPPEL 176
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
768-1357 |
2.22e-05 |
|
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: 49.73 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 768 GNLeemrDERLSKIISMFQAHIRGYLIRKAY-KKLQDQRIGLSVIQRNIRKWLVLRNWQWWKLYSKVKPLLSiaRQEEEM 846
Cdd:pfam15921 373 GNL----DDQLQKLLADLHKREKELSLEKEQnKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKS--ECQGQM 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 847 KEQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNDLFLQLQTLEDSmgdqeerveklimqkadfesqikeleerllde 926
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS-------------------------------- 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 927 edaaadlegikkkmeadnanlKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEkkaleeankktSDS 1006
Cdd:pfam15921 495 ---------------------ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE-----------GDH 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1007 LQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEqdlkstqenvedLERVKRELEENVRRKEaeiss 1086
Cdd:pfam15921 543 LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQ------------VEKAQLEKEINDRRLE----- 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1087 lnskLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELgerldeaggatsaqieLNkkrea 1166
Cdd:pfam15921 606 ----LQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL----------------LN----- 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1167 ELLKIRRDLEEASLQHEaqisALRKKHQDAANEMADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTHNMKNKGCSEKVM 1246
Cdd:pfam15921 661 EVKTSRNELNSLSEDYE----VLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQI 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1247 KQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLedaehrvSVLSKEKSQLSSQLEdARRSLEEetrarsKL 1326
Cdd:pfam15921 737 TAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQEL-------STVATEKNKMAGELE-VLRSQER------RL 802
|
570 580 590
....*....|....*....|....*....|.
gi 127773 1327 QNEVRNMHADMDAIREQLEEEQESksdVQRQ 1357
Cdd:pfam15921 803 KEKVANMEVALDKASLQFAECQDI---IQRQ 830
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1485-1855 |
2.37e-05 |
|
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: 49.24 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1485 IEEYQDSIgaLRRENKNLADEIH----DLTDQLSEGGRS-THELDKARRRLEME-----KEELQAALEEAEGALEQEEAK 1554
Cdd:NF033838 63 VESHLEKI--LSEIQKSLDKRKHtqnvALNKKLSDIKTEyLYELNVLKEKSEAEltsktKKELDAAFEQFKKDTLEPGKK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1555 VMRAQLEIATVRNeidKRIQEKEEEFDNTRRNHQRALESMQASLEAEAKgKADAMRIKKKLEQDINELEValdasNRGKA 1634
Cdd:NF033838 141 VAEATKKVEEAEK---KAKDQKEEDRRNYPTNTYKTLELEIAESDVEVK-KAELELVKEEAKEPRDEEKI-----KQAKA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1635 EMEKTvkryqqqiREMQTSIEEEQRQRDEARESynmAERRCTLMSGEVEELRAALEQAE----RARKASDNELADANDRV 1710
Cdd:NF033838 212 KVESK--------KAEATRLEKIKTDREKAEEE---AKRRADAKLKEAVEKNVATSEQDkpkrRAKRGVLGEPATPDKKE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1711 NELTSQVSSVQGQKrklegdinamqTDLDEMHGELKGADerCKKAMADAARLADELRaEQDHSNQVEKVRKNLESQVKEF 1790
Cdd:NF033838 281 NDAKSSDSSVGEET-----------LPSPSLKPEKKVAE--AEKKVEEAKKKAKDQK-EEDRRNYPTNTYKTLELEIAES 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 127773 1791 QIRLDEAEASSLKGGKKMIQKlESRVHELEAELDN---EQRRHAETQKNMRKADRRLKELAfqADEDR 1855
Cdd:NF033838 347 DVKVKEAELELVKEEAKEPRN-EEKIKQAKAKVESkkaEATRLEKIKTDRKKAEEEAKRKA--AEEDK 411
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1690-1920 |
2.77e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1690 EQAERARKASDNELADANDRVNELTSQVSSVQGQKRKlegdinAMQtdldemHGELKGADERckkamADAARLADELRAE 1769
Cdd:COG1196 175 EEAERKLEATEENLERLEDILGELERQLEPLERQAEK------AER------YRELKEELKE-----LEAELLLLKLREL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1770 QDHSNQVEKVRKNLESQVKEFQIRLDEAEASslkggkkmIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAF 1849
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAE--------LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 127773 1850 QADEDRKNQERLQELIDKLNAKIKTFKRQVEEAEEiaainlakyrkaqhELEEAEERADTADSTLQKFRAK 1920
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEE--------------ELEEAEEELEEAEAELAEAEEA 366
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1258-1360 |
3.28e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.09 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1258 ARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEksqlssqLEDARRSLEEETRARsklqNEVRNMHADM 1337
Cdd:COG2433 406 RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERE-------LSEARSEERREIRKD----REISRLDREI 474
|
90 100
....*....|....*....|...
gi 127773 1338 DAIREQLEEEQESKSDVQRQLSK 1360
Cdd:COG2433 475 ERLERELEEERERIEELKRKLER 497
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1017-1175 |
3.31e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.70 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1017 LNKLKAKLEQALDELEDNLEREKkVRGDV------EKAKRKVEQDLKSTQENVEdlERVKRELEENVRRKEAEISSLNSK 1090
Cdd:COG2433 345 YDAYKNKFERVEKKVPPDVDRDE-VKARVirglsiEEALEELIEKELPEEEPEA--EREKEHEERELTEEEEEIRRLEEQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1091 LEDEQNLVSQLQRKIKELQARIEELEEELEAER-NARAKVEKQR---------AELNRELEELGERLDEaggatsAQIEL 1160
Cdd:COG2433 422 VERLEAEVEELEAELEEKDERIERLERELSEARsEERREIRKDReisrldreiERLERELEEERERIEE------LKRKL 495
|
170
....*....|....*
gi 127773 1161 NKKREAELLKIRRDL 1175
Cdd:COG2433 496 ERLKELWKLEHSGEL 510
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1327-1884 |
3.93e-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: 48.86 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1327 QNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFEseganrteELEDQKRKLLGKLSEAeqtteaaNA 1406
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIK--------ILEQQIKDLNDKLKKN-------KD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1407 KCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTtaewQAKVNSlqsELENSQKESRGYSAELYRIKASIE 1486
Cdd:TIGR04523 97 KINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKN----IDKFLT---EIKKKEKELEKLNNKYNDLKKQKE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1487 EYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRR---LEMEKEELQAALEEAEGALEQEEAKVMRAQLEIA 1563
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKnksLESQISELKKQNNQLKDNIEKKQQEINEKTTEIS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1564 TVRNEIDKRIQEKEEEfdntrrnhQRALESMQASLEaeakgkaDAMRIKKKLEQDINELEVALDASNRGKA-----EMEK 1638
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKI--------KKQLSEKQKELE-------QNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1639 TVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNELTSQVS 1718
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1719 SVQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAE 1798
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1799 ASslkggkkmIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQ 1878
Cdd:TIGR04523 475 RS--------INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
....*.
gi 127773 1879 VEEAEE 1884
Cdd:TIGR04523 547 LNKDDF 552
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1687-1920 |
4.60e-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: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1687 AALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAmadaarladel 1766
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL----------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1767 raeqdhSNQVEKVRKNLESQVKEFQIRLDEAEASSLKGGKKMIQKLESrVHELEAELDNEQRRHAETQKNMRKADRRLKE 1846
Cdd:COG4942 89 ------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPED-FLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 127773 1847 LAFQADEDRKNQERLQELIDKLNAKiktfKRQVEEAEEIAAINLAKYRKAQHELEEAEERADTADSTLQKFRAK 1920
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1639-1826 |
5.42e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1639 TVKRYQQQIREMQ---TSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNELTS 1715
Cdd:COG1579 1 AMPEDLRALLDLQeldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1716 QVSSVQGQKrklegDINAMQTDLDEMHGELKGADERCKKAMADAARLADELRAEQDhsnQVEKVRKNLESQVKEFQIRLD 1795
Cdd:COG1579 81 QLGNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEA---ELAELEAELEEKKAELDEELA 152
|
170 180 190
....*....|....*....|....*....|.
gi 127773 1796 EAEASslkggkkmIQKLESRVHELEAELDNE 1826
Cdd:COG1579 153 ELEAE--------LEELEAEREELAAKIPPE 175
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1306-1560 |
5.91e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1306 SSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEeeqesksDVQRQLSKANNEIQqwrskfeseganrteELED 1385
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-------ALERRIAALARRIR---------------ALEQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1386 QKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMS----IEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQ 1461
Cdd:COG4942 77 ELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGrqppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1462 SELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAAL 1541
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250
....*....|....*....
gi 127773 1542 EEAEGALEQEEAKVMRAQL 1560
Cdd:COG4942 237 AAAAERTPAAGFAALKGKL 255
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1482-1760 |
6.76e-05 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 48.06 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1482 KASIEEYQDSigALRRENK-NLADEIHDLTDQLSEGGRSTH---ELDKARRRLEMEKE-----ELQAALEEA-----EGA 1547
Cdd:pfam13779 406 RALIEQRRRL--ALDRENRpRVARALDALTLAPEEFGPDAGvylGLRSALARLELARSdealdEVADLLWELalrieDGD 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1548 LEQEEAKVMRAQ--LEIATVRN----EIDKRIQE-----------------------KEEEFDNTRRNHQRALESMQASL 1598
Cdd:pfam13779 484 LSDAERRLRAAQerLSEALERGasdeEIAKLMQElrealddymqalaeqaqqnpqdlQQPDDPNAQEMTQQDLQRMLDRI 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1599 E--AEAKGKADAMRIKKKLEQDINELEVAL--DASNRGKAEMektvkryQQQIREMQTSIEEEQRQRDEARESYNMAERR 1674
Cdd:pfam13779 564 EelARSGRRAEAQQMLSQLQQMLENLQAGQpqQQQQQGQSEM-------QQAMDELGDLLREQQQLLDETFRQLQQQGGQ 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1675 CTLMSGE--------VEELRAALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDinAMQTDLDEMHGELK 1746
Cdd:pfam13779 637 QQGQPGQqgqqgqgqQPGQGGQQPGAQMPPQGGAEALGDLAERQQALRRRLEELQDELKELGGK--EPGQALGDAGRAMR 714
|
330
....*....|....
gi 127773 1747 GADERCKKAMADAA 1760
Cdd:pfam13779 715 DAEEALGQGDLAGA 728
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
950-1166 |
7.51e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 950 DIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALEEAnkktSDSLQAEedkcnhLNKLKAKLEQALD 1029
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE----IDKLQAE------IAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1030 ELEDNLEREKKVRGDVEKAKRKVE----QDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNlvsQLQRKI 1105
Cdd:COG3883 87 ELGERARALYRSGGSVSYLDVLLGsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLA---ELEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 127773 1106 KELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGATSAQIELNKKREA 1166
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1255-1906 |
7.57e-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: 47.82 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1255 DLNARLEDSQRSINELQSQKsrLQAENSDLTRQLEDAEHRVS-VLSKEKSQLSSQLEDARRsLEEETRA--RSKLQNEVR 1331
Cdd:pfam07111 19 DVLERRLDTQRPTVTMWEQD--VSGDGQGPGRRGRSLELEGSqALSQQAELISRQLQELRR-LEEEVRLlrETSLQQKMR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1332 --NMHADMDAIREQLEEEQESKSDVQRQLSKAnneiQQWRSKFESEGANRTEELEDQKRKLLGKLSEA-EQTTEAANAKC 1408
Cdd:pfam07111 96 leAQAMELDALAVAEKAGQAEAEGLRAALAGA----EMVRKNLEEGSQRELEEIQRLHQEQLSSLTQAhEEALSSLTSKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1409 SALEKaksrlqqeledmsievdranaSVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKEsrgysaelyrikasIEEY 1488
Cdd:pfam07111 172 EGLEK---------------------SLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEE--------------LEAQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1489 QDSIGALRRE-NKNLADEIHDLTDQLSEggrstHELDKARRRLEMEKEELQAALEEAEgaleqeeAKVMRAQLEIATVRN 1567
Cdd:pfam07111 217 VTLVESLRKYvGEQVPPEVHSQTWELER-----QELLDTMQHLQEDRADLQATVELLQ-------VRVQSLTHMLALQEE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1568 EIDKRIQEK---EEEF----DNTRRNHQRALESMQASLEAEAKGKADAMrikKKLEQDINELEVALDASNRGKAEMEKTV 1640
Cdd:pfam07111 285 ELTRKIQPSdslEPEFpkkcRSLLNRWREKVFALMVQLKAQDLEHRDSV---KQLRGQVAELQEQVTSQSQEQAILQRAL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1641 KRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNELTSQVSSV 1720
Cdd:pfam07111 362 QDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYA 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1721 QGQKRKLEGDInAMQTDLDEMHGELKGADERCKKAMADAARLADELRAEQDhsnqvekvRKNLESQVKEFQIRLDEAEAS 1800
Cdd:pfam07111 442 VRKVHTIKGLM-ARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERN--------RLDAELQLSAHLIQQEVGRAR 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1801 slKGGKKMIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDRKN------------QERLQELIDKL 1868
Cdd:pfam07111 513 --EQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQEltqqqeiygqalQEKVAEVETRL 590
|
650 660 670
....*....|....*....|....*....|....*...
gi 127773 1869 NAKIKTFKRQVEEAEEIAAINLAKYRKAQHELEEAEER 1906
Cdd:pfam07111 591 REQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKER 628
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1339-1671 |
7.61e-05 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 47.41 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1339 AIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEGANRTEELEDQKRKLlgklseaeqttEAANAKCSALEKAKSRL 1418
Cdd:pfam03528 5 DLQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRQNAVL-----------QEAQVELDALQNQLALA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1419 QQELEDMsievdRANASVNQmEKKQRAFDKTTAEWQAKVNSLQSELENSQKESR-GYSAELYRIKASIEEYQDSIgalrr 1497
Cdd:pfam03528 74 RAEMENI-----KAVATVSE-NTKQEAIDEVKSQWQEEVASLQAIMKETVREYEvQFHRRLEQERAQWNQYRESA----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1498 enknlADEIHDLTDQLSEGgrstheldkarrrleMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKrIQEKE 1577
Cdd:pfam03528 143 -----EREIADLRRRLSEG---------------QEEENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTE-AEDKI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1578 EEFDNTRrnhqraLESMQASLEAEAKGKADamrikkkleqdineLEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEE 1657
Cdd:pfam03528 202 KELEASK------MKELNHYLEAEKSCRTD--------------LEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQE 261
|
330
....*....|....
gi 127773 1658 QRQRDEARESYNMA 1671
Cdd:pfam03528 262 RQQHNQLKHTWQKA 275
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
816-1145 |
7.73e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 816 RKWLVLRNWQWWKLYSKVKPLLSIARQEEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNdlflqlqtledsm 895
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK------------- 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 896 gDQEERVEKLIMQKADFESQIKELEERLLDEEDAAADLEGikKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTL 975
Cdd:PTZ00121 1642 -EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA--KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA 1718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 976 QGEISQQDEHIGKLNKEKKALEEaNKKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLER--EKKVRGDVEKAKRKVE 1053
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAKKEAEE-DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAviEEELDEEDEKRRMEVD 1797
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1054 QDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQlqrKIKELQARIEELEEELEAERNARAKVEKQR 1133
Cdd:PTZ00121 1798 KKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLE---EADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
|
330
....*....|..
gi 127773 1134 AELNRELEELGE 1145
Cdd:PTZ00121 1875 DLKEDDEEEIEE 1886
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1427-1590 |
1.01e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 46.65 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1427 IEVDRANASVNQMEKKQRAFDKTTAEWQAKVN---SLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRREnknla 1503
Cdd:pfam00529 51 LDPTDYQAALDSAEAQLAKAQAQVARLQAELDrlqALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQID----- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1504 deIHDLTDQLSEGGRSTHELDKARRRLemekEELQAALEEAEGALEQEEAKVMRAQLE-IATVRNEIDK---RIQEKEEE 1579
Cdd:pfam00529 126 --LARRRVLAPIGGISRESLVTAGALV----AQAQANLLATVAQLDQIYVQITQSAAEnQAEVRSELSGaqlQIAEAEAE 199
|
170
....*....|.
gi 127773 1580 FDNTRRNHQRA 1590
Cdd:pfam00529 200 LKLAKLDLERT 210
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1066-1231 |
1.03e-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: 45.69 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1066 LERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEEleeeleaernARAKVEKQRAEL-----NREL 1140
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE----------VEARIKKYEEQLgnvrnNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1141 EELgerldeaggatSAQIELNKKReaellkiRRDLEEASLQHEAQISALRKKHQDAANEMADQVDQLQKVKSKLEKDKKD 1220
Cdd:COG1579 92 EAL-----------QKEIESLKRR-------ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170
....*....|.
gi 127773 1221 LKREMDDLESQ 1231
Cdd:COG1579 154 LEAELEELEAE 164
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1760-1919 |
1.10e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 46.77 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1760 ARLADEL--RAEQDHSNQVEKVRKNLEsQVKEFQIR---LD-EAEASSLKGgkkMIQKLESRVHELEAELDNEQRRHAET 1833
Cdd:COG3524 172 ERAREDAvrFAEEEVERAEERLRDARE-ALLAFRNRngiLDpEATAEALLQ---LIATLEGQLAELEAELAALRSYLSPN 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1834 QKNMRKADRRLkelafqadedrknqERLQELIDKLNAKIKTfkrqvEEAEEIAAINLAKYRKAQHELEEAEERADTADST 1913
Cdd:COG3524 248 SPQVRQLRRRI--------------AALEKQIAAERARLTG-----ASGGDSLASLLAEYERLELEREFAEKAYTSALAA 308
|
....*.
gi 127773 1914 LQKFRA 1919
Cdd:COG3524 309 LEQARI 314
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1530-1694 |
1.38e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 46.19 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1530 LEMEKEELQAALEEAEGALEQEEAKVMRAQLEIAT--VRNEIDKRIQEKEEEFDNTRRNHQRalesMQASLEAEAKGKAD 1607
Cdd:COG1566 74 ARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGAeaEIAAAEAQLAAAQAQLDLAQRELER----YQALYKKGAVSQQE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1608 AMRIKKKLEQDINELEVAldasnrgkaemektvkryQQQIREMQTSIEEEQrQRDEAREsynmaerrctlmsgEVEELRA 1687
Cdd:COG1566 150 LDEARAALDAAQAQLEAA------------------QAQLAQAQAGLREEE-ELAAAQA--------------QVAQAEA 196
|
....*..
gi 127773 1688 ALEQAER 1694
Cdd:COG1566 197 ALAQAEL 203
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1181-1416 |
1.50e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1181 QHEAQISALRKKHQDAANE---MADQVDQLQKVKSKLEKDKKDLKREMDDLESQMthnmknkgcsEKVMKQFESQMSDLN 1257
Cdd:COG3883 20 AKQKELSELQAELEAAQAEldaLQAELEELNEEYNELQAELEALQAEIDKLQAEI----------AEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1258 ARLEDSQRSINELQSQKSRLQAEN-SDLTRQLEdaehRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHAD 1336
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESfSDFLDRLS----ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1337 MDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEGANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKS 1416
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1456-1916 |
1.50e-04 |
|
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: 46.94 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1456 KVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIgalrrenKNLADEIHDLTDQLSEGGRSTHELDKARRRLEME-- 1533
Cdd:TIGR04523 41 KLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKI-------KILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEik 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1534 -KEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQEKEEEFDNTRRnHQRALESMQASLEAEAKGKADAMR-- 1610
Cdd:TIGR04523 114 nDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKK-QKEELENELNLLEKEKLNIQKNIDki 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1611 ------------IKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLM 1678
Cdd:TIGR04523 193 knkllklelllsNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1679 SGEVEELRAALEQAERARKASDNELADAN-----DRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMHGELKgaderck 1753
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNnqkeqDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS------- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1754 kamadaarladELRAEQDHSNQvEKVRKNLESQVKEFQIRLDEAEASSLKggkKMIQKLESRVHELEAELDNEQRRHAET 1833
Cdd:TIGR04523 346 -----------QLKKELTNSES-ENSEKQRELEEKQNEIEKLKKENQSYK---QEIKNLESQINDLESKIQNQEKLNQQK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1834 QKnmrkadrRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQvEEAEEIAAINLAKYRKAQHE-LEEAEERADTADS 1912
Cdd:TIGR04523 411 DE-------QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ-DSVKELIIKNLDNTRESLETqLKVLSRSINKIKQ 482
|
....
gi 127773 1913 TLQK 1916
Cdd:TIGR04523 483 NLEQ 486
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1165-1374 |
1.60e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1165 EAELLKIRRDLEEAslqhEAQISALRKKHQD-AANEMADQVDQlqkvksklekdkkdlkrEMDDLESQMThnmknkgcse 1243
Cdd:COG3206 181 EEQLPELRKELEEA----EAALEEFRQKNGLvDLSEEAKLLLQ-----------------QLSELESQLA---------- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1244 kvmkQFESQMSDLNARLEDSQRSINELQSQKSRLQA--ENSDLTRQLEDAEHRVSVLSK---EKS----QLSSQLEDARR 1314
Cdd:COG3206 230 ----EARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSArytPNHpdviALRAQIAALRA 305
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 127773 1315 SLEEET-RARSKLQNEVRNMHADMDAIREQLEE-EQESKS--DVQRQLSKANNEIQQWRSKFES 1374
Cdd:COG3206 306 QLQQEAqRILASLEAELEALQAREASLQAQLAQlEARLAElpELEAELRRLEREVEVARELYES 369
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
929-1313 |
1.62e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.43 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 929 AAADLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQ 1008
Cdd:pfam07888 53 ANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1009 AEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLn 1088
Cdd:pfam07888 133 ELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQL- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1089 skledeQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRaelnRELEELGERLDEAGGATS-AQIELNKKR-EA 1166
Cdd:pfam07888 212 ------QDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASE----RKVEGLGEELSSMAAQRDrTQAELHQARlQA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1167 ELLKIRrdLEEASLQHEAQISALRKKHQDAANEMADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTHNMKNKGCSekvm 1246
Cdd:pfam07888 282 AQLTLQ--LADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCN---- 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 1247 kqfESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDAR 1313
Cdd:pfam07888 356 ---RVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADAKWSEAALTSTER 419
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1528-1769 |
1.65e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 45.40 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1528 RRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRneidKRIQEKEEEFDNTrrnhQRALESMQASLEaeakgkad 1607
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALN----RRIQLLEEELERT----EERLAEALEKLE-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1608 amrikkkleqdinELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRA 1687
Cdd:pfam00261 68 -------------EAEKAADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1688 ALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADAARLADELR 1767
Cdd:pfam00261 135 RAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELE 214
|
..
gi 127773 1768 AE 1769
Cdd:pfam00261 215 AE 216
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1326-1862 |
1.72e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.74 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1326 LQNEVRNMHADMDAIREQLEEeQESKsdvqrqLSKANNEIQQ-WRSKFESEGANRTEE------LEDQKRKLLGKLSEAE 1398
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDI-KESK------LGSSMNSIKTfWSPELKKERALRKEEaarisvLKEQYRVTQEENQHLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1399 QTTEAanakcsalekaksrLQQELedmsievdRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSE-LENSQKESRGYSAE 1477
Cdd:pfam10174 74 LTIQA--------------LQDEL--------RAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEEnFRRLQSEHERQAKE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1478 LYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGG---RSTHELDKARRRLEmekeELQAALEEAEGALEQEEak 1554
Cdd:pfam10174 132 LFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLQSKGlpkKSGEEDWERTRRIA----EAEMQLGHLEVLLDQKE-- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1555 vmraqLEIATVRNEIDKRIQEKEEEfDNTRRNHQ---------RALESMQASLEAEAKG-KADAMRIKKKLEQDINELEV 1624
Cdd:pfam10174 206 -----KENIHLREELHRRNQLQPDP-AKTKALQTviemkdtkiSSLERNIRDLEDEVQMlKTNGLLHTEDREEEIKQMEV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1625 ALDASNRGKAEMEKT---VKRYQQQIREMQTSIEEEQRQRDEAR-------ESYNMAERRCTLMSGEVEELRAALEQAER 1694
Cdd:pfam10174 280 YKSHSKFMKNKIDQLkqeLSKKESELLALQTKLETLTNQNSDCKqhievlkESLTAKEQRAAILQTEVDALRLRLEEKES 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1695 ARKASDNELADANDRVNELTSQVSSVQG----QKRK---LEGDINAMQTDLDEMHGELKGADERCKKAMADAARLADELR 1767
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDmldvKERKinvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALT 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1768 AEQDHSNQVEKVRKNLESQV-KEFQIRLDEAEASslkggKKMIQKLESRVHELEAELD------NEQRRHAETQ-KNMRK 1839
Cdd:pfam10174 440 TLEEALSEKERIIERLKEQReREDRERLEELESL-----KKENKDLKEKVSALQPELTekesslIDLKEHASSLaSSGLK 514
|
570 580
....*....|....*....|...
gi 127773 1840 ADRRLKELAFQADEDRKNQERLQ 1862
Cdd:pfam10174 515 KDSKLKSLEIAVEQKKEECSKLE 537
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1258-1515 |
1.76e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.82 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1258 ARLEDSQRsINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQ---LSSQLEDARRSLEEETRAR----------- 1323
Cdd:PLN02939 150 ARLQALED-LEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHveiLEEQLEKLRNELLIRGATEglcvhslskel 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1324 SKLQNEVRNMHADMDAIREQLEEEQESKSDV---QRQLSKANNEIQQWRSKFESEGANRTEELEDQKRKLLGKLSEAEQT 1400
Cdd:PLN02939 229 DVLKEENMLLKDDIQFLKAELIEVAETEERVfklEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDCWWEKVENLQDL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1401 TEAANAKcsaLEKAKSRLQQElEDMSIEVDRANASVNqmEKKQRAFDKTTAE-WQAKVNSLQSELENSQKESRGYsAELY 1479
Cdd:PLN02939 309 LDRATNQ---VEKAALVLDQN-QDLRDKVDKLEASLK--EANVSKFSSYKVElLQQKLKLLEERLQASDHEIHSY-IQLY 381
|
250 260 270
....*....|....*....|....*....|....*.
gi 127773 1480 riKASIEEYQDSIGALRRENKNLADEiHDLTDQLSE 1515
Cdd:PLN02939 382 --QESIKEFQDTLSKLKEESKKRSLE-HPADDMPSE 414
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1024-1152 |
1.78e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1024 LEQALDELEDnlEREKKVRGDVEKAKRKVEQDLKSTQENVEDLE-RVKR------ELEENVRRKEAEISSLNSKLEDE-- 1094
Cdd:COG2433 378 IEEALEELIE--KELPEEEPEAEREKEHEERELTEEEEEIRRLEeQVERleaeveELEAELEEKDERIERLERELSEArs 455
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 1095 ---------------QNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEEL----GERLDEAGG 1152
Cdd:COG2433 456 eerreirkdreisrlDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFtkeaIRRLEEEYG 532
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1322-1466 |
1.96e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1322 ARSKLQNEVRNMHADMDAIREQLEEEQESKSdvQRQLSKANNEIQQWRSKFESEGANRTEELEDQKRKLLgklseaeQTT 1401
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLL-------QKE 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127773 1402 EAANAKCSALEKAKSRLQQELEdmsievdranasvnQMEKKQRAFDKTTAEWQAKVNSLQSELEN 1466
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEK--------------ELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1124-1881 |
1.97e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.72 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1124 NARAKvekQRAELnreLEELGErlDEAGGATSAQI-ELNKKREAELLKIRRDLEEASLQHEAQISALrkkhQDAANEMAD 1202
Cdd:PRK10246 163 NAKPK---ERAEL---LEELTG--TEIYGQISAMVfEQHKSARTELEKLQAQASGVALLTPEQVQSL----TASLQVLTD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1203 QVDQLQKVKSKLEKDKKDLKREmDDLESQMTHNMKnkgcsekvmkqfesqmsdlnaRLEDSQRSINELQSQKSRLQAENS 1282
Cdd:PRK10246 231 EEKQLLTAQQQQQQSLNWLTRL-DELQQEASRRQQ---------------------ALQQALAAEEKAQPQLAALSLAQP 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1283 dlTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEeQESKSDVQRQLSkan 1362
Cdd:PRK10246 289 --ARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNT-WLAEHDRFRQWN--- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1363 NEIQQWRSKFESEGANRteeleDQKRKLLGKLSEAEQtteaanaKCSALEKAKSRLQQEledmsiEVDRANASVNQMEK- 1441
Cdd:PRK10246 363 NELAGWRAQFSQQTSDR-----EQLRQWQQQLTHAEQ-------KLNALPAITLTLTAD------EVAAALAQHAEQRPl 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1442 KQR--AFDKTTAEWQAKVNSLQSELENSQKESRGYSAEL----YRIKASIEEYQDSIGALRREnknlaDEIHDLTDQ--- 1512
Cdd:PRK10246 425 RQRlvALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALnemrQRYKEKTQQLADVKTICEQE-----ARIKDLEAQraq 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1513 LSEG------GRSTHELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATvrneidKRIQEKEEEfdntrrn 1586
Cdd:PRK10246 500 LQAGqpcplcGSTSHPAVEAYQALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALT------KQLQRDESE------- 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1587 HQRALESMQAsLEAEAKGKADAMRIKKKLEQDIN-------ELEVALDA-SNRGK-----AEMEKTVKRYQQQIREMQTS 1653
Cdd:PRK10246 567 AQSLRQEEQA-LTQQWQAVCASLNITLQPQDDIQpwldaqeEHERQLRLlSQRHElqgqiAAHNQQIIQYQQQIEQRQQQ 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1654 IEEEQRQ-----RDEARESYNMAER------------RCTLMSGEVEELRAALE--------QAERARKASDNeLADAND 1708
Cdd:PRK10246 646 LLTALAGyaltlPQEDEEASWLATRqqeaqswqqrqnELTALQNRIQQLTPLLEtlpqsddlPHSEETVALDN-WRQVHE 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1709 RVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMHGELKGADerckKAMADAARLADELRAeqdhsnQVEKVRKNLESQvk 1788
Cdd:PRK10246 725 QCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDD----QQAFLAALLDEETLT------QLEQLKQNLENQ-- 792
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1789 efqirLDEAEASSLKGGKKMIQKLESRVHELEAELDNEQRRHAETQ--KNMRKADRRLKELAFQADEDRKNQERLQELId 1866
Cdd:PRK10246 793 -----RQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQlaQQLRENTTRQGEIRQQLKQDADNRQQQQALM- 866
|
810
....*....|....*
gi 127773 1867 klnAKIKTFKRQVEE 1881
Cdd:PRK10246 867 ---QQIAQATQQVED 878
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1018-1177 |
2.08e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1018 NKLKAKLEQALDELEDNLEREKKvrgDVEKAKRKVEQDLKstqenvEDLERVKRELEENVRRKEAEISSLNSKLEDEQnl 1097
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKK---EAEAIKKEALLEAK------EEIHKLRNEFEKELRERRNELQKLEKRLLQKE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1098 vSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGATSAQI------ELNKKREAELLKI 1171
Cdd:PRK12704 96 -ENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAkeilleKVEEEARHEAAVL 174
|
....*.
gi 127773 1172 RRDLEE 1177
Cdd:PRK12704 175 IKEIEE 180
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1530-1674 |
2.10e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 45.49 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1530 LEMEKEELQAALEEAEGALEQEEAKVMRAQLEI----------ATVRNEIDKRIQEKEEEFDNtRRNHQRALESMQASLE 1599
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELdrlqaleselAISRQDYDGATAQLRAAQAA-VKAAQAQLAQAQIDLA 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127773 1600 AEAKGKADAMRIKKKLEQDINELEVALDASNRGKAEMEKT----VKRYQQQIREMQTSIEEEQRQRDEARESYNMAERR 1674
Cdd:pfam00529 128 RRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIyvqiTQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLD 206
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
836-1136 |
2.11e-04 |
|
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: 46.50 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 836 LLSIARQEEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQ 915
Cdd:pfam02463 681 LQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 916 IKELEERLLDEEDAAADLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQ----QDEHIGKLNK 991
Cdd:pfam02463 761 EKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQeekiKEEELEELAL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 992 EKKALEEANKKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKR 1071
Cdd:pfam02463 841 ELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIE 920
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 127773 1072 ELEENVRRKEAEISSLNSKLEDEQ---------NLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAEL 1136
Cdd:pfam02463 921 ERIKEEAEILLKYEEEPEELLLEEadekekeenNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDE 994
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1088-1450 |
2.74e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1088 NSKLEDEQNLVSQLQRkIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELgERLDEAGGATSAQIELNKK--RE 1165
Cdd:pfam17380 261 NGQTMTENEFLNQLLH-IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERR-RKLEEAEKARQAEMDRQAAiyAE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1166 AELLKIRRDLEEASLQHEAQISALRKKHQDaanEMADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTHNMKNKGCSEKV 1245
Cdd:pfam17380 339 QERMAMERERELERIRQEERKRELERIRQE---EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1246 MKQFES----QMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLE-----DAEHRVSVLSKEKSQLSSQL--EDARR 1314
Cdd:pfam17380 416 QQQKVEmeqiRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVErlrqqEEERKRKKLELEKEKRDRKRaeEQRRK 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1315 SLEEETRARSKLQNEVRNMhadmdaiREQLEEEQEsksdvQRQlskanNEIQQWRSKFESEGANRTEELEDQKRKLLGKL 1394
Cdd:pfam17380 496 ILEKELEERKQAMIEEERK-------RKLLEKEME-----ERQ-----KAIYEEERRREAEEERRKQQEMEERRRIQEQM 558
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 127773 1395 SEAEQtteaANAKCSALEKAKSRLQQELEDmsievdranasvnqmEKKQRAFDKTT 1450
Cdd:pfam17380 559 RKATE----ERSRLEAMEREREMMRQIVES---------------EKARAEYEATT 595
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1583-1880 |
2.81e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1583 TRRNHQRALESM-QASLEAEAKGKADAMRIKKKLEQDINELEVALDASNRGKAEMEKTV---KRYQQQIREMQTSIEEEQ 1658
Cdd:pfam17380 285 SERQQQEKFEKMeQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAmerERELERIRQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1659 -RQRDEARESYNMAERRCTLMSGEV--EELRAALEQA--------ERARKASDNELADANDRvnelTSQVSSVQGQKRKL 1727
Cdd:pfam17380 365 iRQEEIAMEISRMRELERLQMERQQknERVRQELEAArkvkileeERQRKIQQQKVEMEQIR----AEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1728 EGDINAMQTDLDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVEKV-RKNLESQVKEFQIRLDEAEASslkggK 1806
Cdd:pfam17380 441 EEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQrRKILEKELEERKQAMIEEERK-----R 515
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 127773 1807 KMIQK-LESRVHELEAEldnEQRRHAETQKNMRK---ADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVE 1880
Cdd:pfam17380 516 KLLEKeMEERQKAIYEE---ERRREAEEERRKQQemeERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
834-1208 |
2.95e-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: 45.84 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 834 KPLLSIARQEEEMKEQLKQMDKMKEDLakteRIKKELEEQNVTLLEQKNDLFLQL----QTLEDSMGDQEERVEKLIMQK 909
Cdd:pfam05622 59 KKYLLLQKQLEQLQEENFRLETARDDY----RIKCEELEKEVLELQHRNEELTSLaeeaQALKDEMDILRESSDKVKKLE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 910 ADFESQIKELEERlldeedaaADLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDN---QISTLQGEISQQDEHI 986
Cdd:pfam05622 135 ATVETYKKKLEDL--------GDLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETykrQVQELHGKLSEESKKA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 987 GKLNKEKKALEEANkktsDSLQAEEDKcnhLNKLKAKLEQALDELednleREKKVRGDVEKAKRKVEQDLKSTQENVEDl 1066
Cdd:pfam05622 207 DKLEFEYKKLEEKL----EALQKEKER---LIIERDTLRETNEEL-----RCAQLQQAELSQADALLSPSSDPGDNLAA- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1067 ERVKRELEENVRRKEAEISSLNSKLEdeqnlvSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGER 1146
Cdd:pfam05622 274 EIMPAEIREKLIRLQHENKMLRLGQE------GSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKA 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 127773 1147 LDEAGGATSAQIELNKKREAELLKirrdLEEASLQHEAQISALRKKHQDAANEMADQVDQLQ 1208
Cdd:pfam05622 348 LQEQGSKAEDSSLLKQKLEEHLEK----LHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQ 405
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1247-1471 |
3.06e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1247 KQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQledaehRVSVLSKEksQLSSQLEDARRSLEEetrarskL 1326
Cdd:PRK11281 76 DRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRE------TLSTLSLR--QLESRLAQTLDQLQN-------A 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1327 QNEVRNMHADMDAIREQLEEeqesksdVQRQLSKANNEIQQWRSKFESEGANRTEELEDQKRKLLGKLS------EAEQT 1400
Cdd:PRK11281 141 QNDLAEYNSQLVSLQTQPER-------AQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQAllnaqnDLQRK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1401 TEAANAKCSALEKAK--------SRLQQELEDMS--IEVDRANASVNQMEKKQRAFDKTtaewQAKVNSL-QSELENSQK 1469
Cdd:PRK11281 214 SLEGNTQLQDLLQKQrdyltariQRLEHQLQLLQeaINSKRLTLSEKTVQEAQSQDEAA----RIQANPLvAQELEINLQ 289
|
..
gi 127773 1470 ES 1471
Cdd:PRK11281 290 LS 291
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1736-1895 |
3.13e-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: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1736 TDLDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEASSLKGG---------- 1805
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyealqk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1806 -----KKMIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELafqadedrknQERLQELIDKLNAKIKTFKRQVE 1880
Cdd:COG1579 97 eieslKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK----------KAELDEELAELEAELEELEAERE 166
|
170
....*....|....*.
gi 127773 1881 E-AEEIAAINLAKYRK 1895
Cdd:COG1579 167 ElAAKIPPELLALYER 182
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1414-1884 |
3.21e-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: 45.87 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1414 AKSRLQQELEDmsIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSlqSELENSQKESRGYSaELYRIKASIEEYQDSIG 1493
Cdd:pfam05483 24 AKSNLSKNGEN--IDSDPAFQKLNFLPMLEQVANSGDCHYQEGLKD--SDFENSEGLSRLYS-KLYKEAEKIKKWKVSIE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1494 ALRRENKN-----------------------------LADEIHDLTDQLSEGGRSTHELD----------KARRRLEMEK 1534
Cdd:pfam05483 99 AELKQKENklqenrkiieaqrkaiqelqfenekvslkLEEEIQENKDLIKENNATRHLCNllketcarsaEKTKKYEYER 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1535 EE-------LQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQEKEEEFDNTRRNHQRALESMQASLEAEAKGKAD 1607
Cdd:pfam05483 179 EEtrqvymdLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1608 AMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSgevEELRA 1687
Cdd:pfam05483 259 LTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLT---EEKEA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1688 ALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADAARLADELR 1767
Cdd:pfam05483 336 QMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILA 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1768 AEQ---DHSNQVEKVRKNLESQVKE--FQIRLDEAEASSLKGGKKMIQKLES----RVHELEAELDNEQRRHAETQKNMR 1838
Cdd:pfam05483 416 EDEkllDEKKQFEKIAEELKGKEQEliFLLQAREKEIHDLEIQLTAIKTSEEhylkEVEDLKTELEKEKLKNIELTAHCD 495
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 127773 1839 KADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEAEE 1884
Cdd:pfam05483 496 KLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEE 541
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1016-1210 |
3.69e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1016 HLNKLKAKLEQALDELEDNLEREKKvrgdveKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQ 1095
Cdd:PRK05771 47 KLRSLLTKLSEALDKLRSYLPKLNP------LREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1096 NLVSQLQ-------------------------RKIKELQARIEELEEELEAERNARAKV-------EKQRAELNRELEEL 1143
Cdd:PRK05771 121 QEIERLEpwgnfdldlslllgfkyvsvfvgtvPEDKLEELKLESDVENVEYISTDKGYVyvvvvvlKELSDEVEEELKKL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1144 G-ERLDEAGGATSAQI---------ELNKKRE---AELLKIRRDLEEASLQHEAQISALRKKhQDAANEMA--------- 1201
Cdd:PRK05771 201 GfERLELEEEGTPSELireikeeleEIEKEREsllEELKELAKKYLEELLALYEYLEIELER-AEALSKFLktdktfaie 279
|
250
....*....|....
gi 127773 1202 -----DQVDQLQKV 1210
Cdd:PRK05771 280 gwvpeDRVKKLKEL 293
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1286-1920 |
3.71e-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: 45.71 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1286 RQLEDAEHRVSVLSKEKSQLSsqleDARRSLEEETRARS----------KLQNEVRNMHADMDAIREQLEEEQ------- 1348
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELS----ARESDLEQDYQAASdhlnlvqtalRQQEKIERYQEDLEELTERLEEQEevveeaa 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1349 ESKSDVQRQLSKANNEIQQWRSKFesegANRTEELEDQKRKllgklseAEQTTEAANAkcsaLEKAKSRLQqeLEDMSIE 1428
Cdd:COG3096 375 EQLAEAEARLEAAEEEVDSLKSQL----ADYQQALDVQQTR-------AIQYQQAVQA----LEKARALCG--LPDLTPE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1429 vdranasvnqmekkqrAFDKTTAEWQAKVNSLQSE-LENSQK-----ESRGYSAELYRIKASI-------EEYQDSIGAL 1495
Cdd:COG3096 438 ----------------NAEDYLAAFRAKEQQATEEvLELEQKlsvadAARRQFEKAYELVCKIageversQAWQTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1496 R--RENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEG-ALEQEEAKVMRAQLEiATVRNEIDKR 1572
Cdd:COG3096 502 RryRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEElEELLAELEAQLEELE-EQAAEAVEQR 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1573 IQekeeefdntRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDINE-LE--VALDASNRGKAEMEKTVKRYQQQIRE 1649
Cdd:COG3096 581 SE---------LRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEaLAdsQEVTAAMQQLLEREREATVERDELAA 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1650 MQTSIEEEQRQ-----RDEARESYNMAER-RCTLMSGEVEE---------------LRAA-----LEQAERARKASDNEL 1703
Cdd:COG3096 652 RKQALESQIERlsqpgGAEDPRLLALAERlGGVLLSEIYDDvtledapyfsalygpARHAivvpdLSAVKEQLAGLEDCP 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1704 AD----------ANDRVNELTSQ-----VSSVQGQKR-----------------KLEgDINAMQTDLDEMHGELKGADER 1751
Cdd:COG3096 732 EDlyliegdpdsFDDSVFDAEELedavvVKLSDRQWRysrfpevplfgraarekRLE-ELRAERDELAEQYAKASFDVQK 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1752 CKKAMADAARL-------------ADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDeaeasSLKGGKKMIQKL------ 1812
Cdd:COG3096 811 LQRLHQAFSQFvgghlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLD-----QLKEQLQLLNKLlpqanl 885
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1813 ------ESRVHELEAELDNEQRRHAETQKNmRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQV------- 1879
Cdd:COG3096 886 ladetlADRLEELREELDAAQEAQAFIQQH-GKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIfalsevv 964
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 127773 1880 --------EEAEEIAAINLAKYRKAQHELEEAEERADTADSTLQKFRAK 1920
Cdd:COG3096 965 qrrphfsyEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQ 1013
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
886-1058 |
3.86e-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: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 886 LQLQTLEDSMGDQEERVEKLIMQKADFESQIKEleerlldEEDAAADLEGIKKKMEADNANLKKDIGDLENTLQKAE--Q 963
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 964 DKAHKDNQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLERE-KKVR 1042
Cdd:COG1579 83 GNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAElEELE 162
|
170
....*....|....*.
gi 127773 1043 GDVEKAKRKVEQDLKS 1058
Cdd:COG1579 163 AEREELAAKIPPELLA 178
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1384-1573 |
3.86e-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: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1384 EDQKRKLLgKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSE 1463
Cdd:COG1579 3 PEDLRALL-DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1464 LEN--SQKESRGYSAElyrikasieeyqdsIGALRRENKNLADEIHDLTDQLSEggrSTHELDKARRRLEMEKEELQAAL 1541
Cdd:COG1579 82 LGNvrNNKEYEALQKE--------------IESLKRRISDLEDEILELMERIEE---LEEELAELEAELAELEAELEEKK 144
|
170 180 190
....*....|....*....|....*....|..
gi 127773 1542 EEAEGALEQEEAKVMRAQLEIATVRNEIDKRI 1573
Cdd:COG1579 145 AELDEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
775-1142 |
4.15e-04 |
|
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: 45.39 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 775 DERLSKIISmfqaHIRGYLIRKAYKKLQDQRIGLSVIQRN-IRKWLVLRNWQWWKLYSKVKPLLSIARqEEEMKEQLKQM 853
Cdd:NF033838 64 ESHLEKILS----EIQKSLDKRKHTQNVALNKKLSDIKTEyLYELNVLKEKSEAELTSKTKKELDAAF-EQFKKDTLEPG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 854 DKMKEDLAKTERIKKELEEQNVTllEQKNDLFLQLQTLEDSMGDQEERVEK----LIMQKADF---ESQIKELEERLLDE 926
Cdd:NF033838 139 KKVAEATKKVEEAEKKAKDQKEE--DRRNYPTNTYKTLELEIAESDVEVKKaeleLVKEEAKEprdEEKIKQAKAKVESK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 927 EDAAADLEGIKK-----KMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLqGEISQQDEhigklnKEKKAleeank 1001
Cdd:NF033838 217 KAEATRLEKIKTdrekaEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVL-GEPATPDK------KENDA------ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1002 KTSDSLQAEEDKCNHLNKLKAKLEQAldelednlerEKKVRGDVEKAKRKVEQDLKSTQENVedLERVKREL-EENVRRK 1080
Cdd:NF033838 284 KSSDSSVGEETLPSPSLKPEKKVAEA----------EKKVEEAKKKAKDQKEEDRRNYPTNT--YKTLELEIaESDVKVK 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 127773 1081 EAEIsslnsKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEE 1142
Cdd:NF033838 352 EAEL-----ELVKEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEAKRKAAE 408
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
839-1143 |
4.54e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 839 IARQEEEMKEQLKQMDKMKEDLAKTerikKELEEQNVTLLEQKNDLFLQLQ----TLEDSMGDQEERVEKlimQKADFES 914
Cdd:PRK04778 107 INEIESLLDLIEEDIEQILEELQEL----LESEEKNREEVEQLKDLYRELRksllANRFSFGPALDELEK---QLENLEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 915 QIKELEERLLDEEDAAAdlEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKK 994
Cdd:PRK04778 180 EFSQFVELTESGDYVEA--REILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHLDHLDIEKE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 995 aLEEANKKTSDSLQA-EEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQEN----VEDLERV 1069
Cdd:PRK04778 258 -IQDLKEQIDENLALlEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQnkelKEEIDRV 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1070 KR------ELEENVRRKEAEISSLNSKLED------EQNLV-SQLQRKIKELQARIEELEEELEAERNARAKVEKQRAEL 1136
Cdd:PRK04778 337 KQsytlneSELESVRQLEKQLESLEKQYDEiteriaEQEIAySELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEA 416
|
....*..
gi 127773 1137 NRELEEL 1143
Cdd:PRK04778 417 REKLERY 423
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
961-1109 |
4.62e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 45.44 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 961 AEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCNHLNK-LKAKL---EQALDELEDNLE 1036
Cdd:pfam05911 654 SEIDNLSSDPEIPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENLEsTKSQLqesEQLIAELRSELA 733
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 127773 1037 REKKvrgdvekAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQ 1109
Cdd:pfam05911 734 SLKE-------SNSLAETQLKCMAESYEDLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQ 799
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1747-1920 |
4.99e-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: 44.75 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1747 GADERCKKAMADAARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEA------SSLKGGKKMIQKLESRVHELE 1820
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARriraleQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1821 AELDNEQRRHAE------------------TQKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEA 1882
Cdd:COG4942 97 AELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 127773 1883 EEIAAINLAKYRKAQHELEEAEERADTADSTLQKFRAK 1920
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1523-1708 |
5.03e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 43.66 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1523 LDKA---RRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRiqekeeefdntrrnHQRALESMQASLE 1599
Cdd:COG1842 18 LDKAedpEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKW--------------EEKARLALEKGRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1600 AEAKgkaDAMRIKKKLEQDINELEVALDASnrgkaemEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRC---- 1675
Cdd:COG1842 84 DLAR---EALERKAELEAQAEALEAQLAQL-------EEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEkvne 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 127773 1676 TLMSGEVEELRAALEQAER------ARKASDNELADAND 1708
Cdd:COG1842 154 ALSGIDSDDATSALERMEEkieemeARAEAAAELAAGDS 192
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1528-1864 |
5.53e-04 |
|
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: 44.96 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1528 RRLEMEKEELQAALEEAEG------ALEQEEAKVMRAQLEIATVRNEIDKRIQEKEEEfdnTRRNHQRALESMQASLEAE 1601
Cdd:pfam02463 145 EIIAMMKPERRLEIEEEAAgsrlkrKKKEALKKLIEETENLAELIIDLEELKLQELKL---KEQAKKALEYYQLKEKLEL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1602 AKGKADAMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGE 1681
Cdd:pfam02463 222 EEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1682 VEELRAALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMhgelkgADERCKKAMADAAR 1761
Cdd:pfam02463 302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL------EKLQEKLEQLEEEL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1762 LADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEASSLKGG--KKMIQKLESRVHELEAELDNEQRRHAETQKNMRK 1839
Cdd:pfam02463 376 LAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDllKEEKKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
330 340
....*....|....*....|....*
gi 127773 1840 ADRRLKELAFQADEDRKNQERLQEL 1864
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLV 480
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1243-1349 |
6.08e-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: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1243 EKVMKQFESQMSDLNARLEDSQRSINELQSQKsrlqaENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRA 1322
Cdd:COG1579 58 EKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE 132
|
90 100
....*....|....*....|....*..
gi 127773 1323 RSKLQNEVRNMHADMDAIREQLEEEQE 1349
Cdd:COG1579 133 LAELEAELEEKKAELDEELAELEAELE 159
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1488-1795 |
6.21e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1488 YQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELdkarrrLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRN 1567
Cdd:pfam00038 16 YIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSL------YEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1568 ----EIDKRiQEKEEEFDNTRRNHQrALESMQASLEAEAKGKADAMRIKKKL-EQDINELEVALDASNRgKAEMEKTVK- 1641
Cdd:pfam00038 90 kyedELNLR-TSAENDLVGLRKDLD-EATLARVDLEAKIESLKEELAFLKKNhEEEVRELQAQVSDTQV-NVEMDAARKl 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1642 RYQQQIREMQTSIEEE-QRQRDEARESYnmaerrctlmSGEVEELRAALEQAERARKASDNELADANDRVNELTSQVSSV 1720
Cdd:pfam00038 167 DLTSALAEIRAQYEEIaAKNREEAEEWY----------QSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127773 1721 QGQKRKLEgdinamqtdldemhGELKGADERCKKAMADAARLADELRAEqdhsnqVEKVRKNLESQVKEFQIRLD 1795
Cdd:pfam00038 237 KKQKASLE--------------RQLAETEERYELQLADYQELISELEAE------LQETRQEMARQLREYQELLN 291
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1738-1906 |
6.49e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1738 LDEMHGELKGADErcKKAMADAARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEASslkggkkmIQKLESRVH 1817
Cdd:COG2433 382 LEELIEKELPEEE--PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDER--------IERLERELS 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1818 ELEAELDNEQRRHAETQKNMRKADRRLKELafqaDEDRKNQERLQELIDKLnakiKTFKRQVEEAEEIAAINLAKYRKaq 1897
Cdd:COG2433 452 EARSEERREIRKDREISRLDREIERLEREL----EEERERIEELKRKLERL----KELWKLEHSGELVPVKVVEKFTK-- 521
|
....*....
gi 127773 1898 HELEEAEER 1906
Cdd:COG2433 522 EAIRRLEEE 530
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
1249-1597 |
6.91e-04 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 44.68 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1249 FESQMSDLNARLEDSQRSIN---ELQSQKSRLQAEnsdltrqledAEHRVSVLSK-EKSQLSSQLEDARRSLEEETRARS 1324
Cdd:COG4192 36 WNSLSNQIRYILDDSLPKLQaslKLEENSNELVAA----------LPEFAAATNTtERSQLRNQLNTQLADIEELLAELE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1325 KLQNEVRNMHADMDAIREQLEEEQ---ESKSDVQRQLSKANNEIQQWRSKFESEGANRTEELEDQKRKLLGKLSEAEQTT 1401
Cdd:COG4192 106 QLTQDAGDLRAAVADLRNLLQQLDsllTQRIALRRRLQELLEQINWLHQDFNSELTPLLQEASWQQTRLLDSVETTESLR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1402 EaanakcsalekaksrLQQELEDMSievdRANASVNQMekkqrafdkttaewqakvNSLQSELEnSQKESRGYSAELYRI 1481
Cdd:COG4192 186 N---------------LQNELQLLL----RLLAIENQI------------------VSLLREVA-AARDQADVDNLFDRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1482 KASIEEYQDSIGALrrenKNLADEI--HDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEGALEQeeakvmraq 1559
Cdd:COG4192 228 QYLKDELDRNLQAL----KNYPSTItlRQLIDELLAIGSGEGGLPSLRRDELAAQATLEALAEENNSILEQ--------- 294
|
330 340 350
....*....|....*....|....*....|....*...
gi 127773 1560 leiatVRNEIDKRIQEKEEEFDNTrrnHQRALESMQAS 1597
Cdd:COG4192 295 -----LRTQISGLVGNSREQLVAL---NQETAQLVQQS 324
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1250-1372 |
7.43e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1250 ESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNE 1329
Cdd:PRK09039 73 RQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQ 152
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 127773 1330 VRNMHADMDAIREQLEEEQESKSDVQRQLSKA----NNEIQQWRSKF 1372
Cdd:PRK09039 153 LAALEAALDASEKRDRESQAKIADLGRRLNVAlaqrVQELNRYRSEF 199
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1585-1765 |
7.62e-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: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1585 RNHQRALESMQAsLEAEAkgkADAMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEA 1664
Cdd:COG1579 3 PEDLRALLDLQE-LDSEL---DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1665 RESYNMA--ERrctlmsgEVEELRAALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMH 1742
Cdd:COG1579 79 EEQLGNVrnNK-------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180
....*....|....*....|...
gi 127773 1743 GELKGADERCKKAMADAARLADE 1765
Cdd:COG1579 152 AELEAELEELEAEREELAAKIPP 174
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1345-1545 |
7.66e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1345 EEEQESKSDVQRQLSKANNEIQQWRSKFESEG-------ANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSR 1417
Cdd:PRK05771 39 ELSNERLRKLRSLLTKLSEALDKLRSYLPKLNplreekkKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1418 LQQELE------DMSIEVDRANA-----------SVNQMEKKQRAFDKTTAEW--QAK------VNSLQSELENSQKESR 1472
Cdd:PRK05771 119 LEQEIErlepwgNFDLDLSLLLGfkyvsvfvgtvPEDKLEELKLESDVENVEYisTDKgyvyvvVVVLKELSDEVEEELK 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127773 1473 GYSAELYRIKAS------IEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELdkarrrLEMEKEELQAALEEAE 1545
Cdd:PRK05771 199 KLGFERLELEEEgtpselIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY------LEIELERAEALSKFLK 271
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1304-1575 |
8.64e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1304 QLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEeqesksdvqrqLSKANNEIQQWrskfeseganrtEEL 1383
Cdd:COG0497 155 ELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEE-----------LEAAALQPGEE------------EEL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1384 EDQKRKLlgklSEAEQTTEAANAKCSALEKaksrlqqelEDMSIeVDRANASVNQMEKKQRaFDKTTAEWQAKVNSLQSE 1463
Cdd:COG0497 212 EEERRRL----SNAEKLREALQEALEALSG---------GEGGA-LDLLGQALRALERLAE-YDPSLAELAERLESALIE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1464 LENSQKESRGYSAEL----YRIkASIEEYQDSIGALRRENKNLADEIHDLTDQLSEggrsthELDKARRRlEMEKEELQA 1539
Cdd:COG0497 277 LEEAASELRRYLDSLefdpERL-EEVEERLALLRRLARKYGVTVEELLAYAEELRA------ELAELENS-DERLEELEA 348
|
250 260 270
....*....|....*....|....*....|....*.
gi 127773 1540 ALEEAEGALEQEEAKVMRAQLEIATvrnEIDKRIQE 1575
Cdd:COG0497 349 ELAEAEAELLEAAEKLSAARKKAAK---KLEKAVTA 381
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1415-1824 |
9.89e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1415 KSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSElensqkesrgysaelyrikasieeyqdsIGA 1494
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESR----------------------------VAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1495 LRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKR-I 1573
Cdd:pfam07888 85 LKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAgA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1574 QEKEEEFDntRRNHQRALESMQA---SLEAEAKGKADAMRIKK----KLEQDINELEVALDASNRGKAEMEKTVKryqqq 1646
Cdd:pfam07888 165 QRKEEEAE--RKQLQAKLQQTEEelrSLSKEFQELRNSLAQRDtqvlQLQDTITTLTQKLTTAHRKEAENEALLE----- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1647 irEMQTsieeeqrqrdeARESYNMAERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNELTSQV----SSVQG 1722
Cdd:pfam07888 238 --ELRS-----------LQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALregrARWAQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1723 QKRKLEGDINAMQTDLDEMHGELKGADERCKKAMADAARLADELRAEQDhSNQVEKVRKNLESQVKEFQIRLDEAEASSL 1802
Cdd:pfam07888 305 ERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKD-CNRVQLSESRRELQELKASLRVAQKEKEQL 383
|
410 420
....*....|....*....|..
gi 127773 1803 KGGKkmiQKLESRVHELEAELD 1824
Cdd:pfam07888 384 QAEK---QELLEYIRQLEQRLE 402
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
993-1442 |
1.04e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.97 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 993 KKALEEANKKT------------SDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQ 1060
Cdd:pfam07111 131 RKNLEEGSQREleeiqrlhqeqlSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQ 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1061 ENVED----LERVKRELEENVrrkEAEISSLNSKLEDEQNL--VSQLQRKIKELQARIEELEEELEAERNARAKVEKQ-- 1132
Cdd:pfam07111 211 EELEAqvtlVESLRKYVGEQV---PPEVHSQTWELERQELLdtMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEElt 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1133 ---------RAELNRELEELGERLDEAGGATSAQIELNKKREAELLKIRRD----LEEASLQHEAQISALRKKHQDAANE 1199
Cdd:pfam07111 288 rkiqpsdslEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGqvaeLQEQVTSQSQEQAILQRALQDKAAE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1200 ----------MADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTHNMKNKGCSEKVMKQFESQMSDLNARLEDSQRSINE 1269
Cdd:pfam07111 368 vevermsakgLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHT 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1270 LQSQKSR------LQAENSDLTRQLEDAEHRVSV----LSKEKSQLSSQLEDARRSLEEET-RARSKLQNEVRNMHADMD 1338
Cdd:pfam07111 448 IKGLMARkvalaqLRQESCPPPPPAPPVDADLSLeleqLREERNRLDAELQLSAHLIQQEVgRAREQGEAERQQLSEVAQ 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1339 AIREQLEEEQESKSDVQRQLSKAnneiQQWRSKFESEGANRTEELEDQKRKLLGKLSEAEQTTEaanakcSALEKAKSRL 1418
Cdd:pfam07111 528 QLEQELQRAQESLASVGQQLEVA----RQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVE------TRLREQLSDT 597
|
490 500
....*....|....*....|....
gi 127773 1419 QQELEDMSIEVDRANASVNQMEKK 1442
Cdd:pfam07111 598 KRRLNEARREQAKAVVSLRQIQHR 621
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1235-1470 |
1.04e-03 |
|
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: 43.99 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1235 NMKNKGCSEKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEhrvsvlskeKSQLSSQLEDARR 1314
Cdd:pfam18971 547 DLNNLAITSFVRRNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAVAEAK---------STGNYDEVKKAQK 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1315 SLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQwrskfESEGANRTEELEDQKRKLLGKL 1394
Cdd:pfam18971 618 DLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEANR-----DARAIAYTQNLKGIKRELSDKL 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1395 SE--------AEQTTEAANAKCSALEKAKSRLQQ---ELEDMSI------EVDRANASVNQMEK-KQRAFDKTTaewQAK 1456
Cdd:pfam18971 693 EKiskdlkdfSKSFDEFKNGKNKDFSKAEETLKAlkgSVKDLGInpewisKVENLNAALNEFKNgKNKDFSKVT---QAK 769
|
250
....*....|....
gi 127773 1457 vnslqSELENSQKE 1470
Cdd:pfam18971 770 -----SDLENSVKD 778
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1274-1424 |
1.07e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1274 KSRLQAENSDLTRQLEDAEHRVSVLSKEKsqlssqLEDARrslEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSD 1353
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEA------LLEAK---EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 127773 1354 VQRQLSKANNEIQQWRSKFEsegaNRTEELEDQKRKLLGKLSEAEQTTEaanaKCSAL--EKAKSRLQQELED 1424
Cdd:PRK12704 101 KLELLEKREEELEKKEKELE----QKQQELEKKEEELEELIEEQLQELE----RISGLtaEEAKEILLEKVEE 165
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
841-1136 |
1.13e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 841 RQEEEmkEQLKQMDKMKEdLAKTERIKKELEEQNVTLLEQKNDLFLQLQTLEDSMGDQEERVEKLIMQKADFESQIKELE 920
Cdd:pfam17380 302 RQEKE--EKAREVERRRK-LEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 921 ERLLDEEDAAADLEGIKKKMEAdnanlKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQqdehigklnKEKKALEEAN 1000
Cdd:pfam17380 379 ELERLQMERQQKNERVRQELEA-----ARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ---------REVRRLEEER 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1001 KKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKV-EQDLKSTQENVEDLERVKRELE----- 1074
Cdd:pfam17380 445 AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEkemee 524
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 127773 1075 ------ENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKvEKQRAEL 1136
Cdd:pfam17380 525 rqkaiyEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVES-EKARAEY 591
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1340-1559 |
1.37e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1340 IREQLEEEQESKSDVQRQLSKAN-NEIQQWRSKFESEGANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRL 1418
Cdd:PRK11281 27 ARAASNGDLPTEADVQAQLDALNkQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1419 QQELEDMSIEvDRANASVNQMEKKQRAFDKTTAEWQAKVN-------SLQSELENSQKESRGYSAELYRIKASIEEYQDS 1491
Cdd:PRK11281 107 KDDNDEETRE-TLSTLSLRQLESRLAQTLDQLQNAQNDLAeynsqlvSLQTQPERAQAALYANSQRLQQIRNLLKGGKVG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1492 IGALRRENKN-LADEIHDL-------------TDQLSEGGRSTHELDKAR-RRLEMEKEELQAALEEAEgaLEQEEAKVM 1556
Cdd:PRK11281 186 GKALRPSQRVlLQAEQALLnaqndlqrkslegNTQLQDLLQKQRDYLTARiQRLEHQLQLLQEAINSKR--LTLSEKTVQ 263
|
...
gi 127773 1557 RAQ 1559
Cdd:PRK11281 264 EAQ 266
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
898-1373 |
1.58e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 898 QEERVEKLIMQKA--DFESQIKELEERLLDEEDAAADLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTL 975
Cdd:PRK01156 335 QKDYNDYIKKKSRydDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 976 QGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEE--DKC----NHLNKlkakleqalDELEDNLEREKKVRGDVEKAK 1049
Cdd:PRK01156 415 NVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgqSVCpvcgTTLGE---------EKSNHIINHYNEKKSRLEEKI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1050 RKVEQDLKSTQENVEDLERVKRELE-ENVRRKEAE---ISSLNSKLEDEQNLVSQLqrKIKELQARIEELEEELEAERNA 1125
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKKRKEYLEsEEINKSINEynkIESARADLEDIKIKINEL--KDKHDKYEEIKNRYKSLKLEDL 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1126 RAKVEkqraelnreleelgERLDEAGGATSAQIELNKKREAELLKIRRDLEEASLQHEAQISALRKKHQDAANEMADQVD 1205
Cdd:PRK01156 564 DSKRT--------------SWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEAN 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1206 QLQKVKSklekDKKDLKREMDDLESQMTHNMKNKGcsekVMKQFESQMSDLNARLEDSQRSINELQSQksrLQAENSDLT 1285
Cdd:PRK01156 630 NLNNKYN----EIQENKILIEKLRGKIDNYKKQIA----EIDSIIPDLKEITSRINDIEDNLKKSRKA---LDDAKANRA 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1286 RQledaEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLqnevrnmhADMDAIREQLeeeqeSKSDVQRQLSKA---- 1361
Cdd:PRK01156 699 RL----ESTIEILRTRINELSDRINDINETLESMKKIKKAI--------GDLKRLREAF-----DKSGVPAMIRKSasqa 761
|
490
....*....|...
gi 127773 1362 -NNEIQQWRSKFE 1373
Cdd:PRK01156 762 mTSLTRKYLFEFN 774
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
1270-1358 |
1.60e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 42.38 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1270 LQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQnEVRNMHADMDAIREQLEEEQE 1349
Cdd:pfam15294 131 LHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGAKKDVKSNLK-EISDLEEKMAALKSDLEKTLN 209
|
....*....
gi 127773 1350 SKSDVQRQL 1358
Cdd:pfam15294 210 ASTALQKSL 218
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
844-1351 |
1.72e-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: 43.27 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 844 EEMKEQLKQMD---------KMKEDLAKTERIKKELEEQNV-----TLLEQKNDLFLQLQTLEDSMGDQEERVEKLimqk 909
Cdd:pfam10174 268 EDREEEIKQMEvykshskfmKNKIDQLKQELSKKESELLALqtkleTLTNQNSDCKQHIEVLKESLTAKEQRAAIL---- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 910 adfESQIKELEERLLDEEDAAADLEGIKKKMEADNANLKKDIGDLENTLQKaeqdkahKDNQISTLQGEISQQDEHIgkl 989
Cdd:pfam10174 344 ---QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV-------KERKINVLQKKIENLQEQL--- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 990 nKEKKALEEANKKTSDSLQaeEDKCNHLNKLkAKLEQALDELEDNLEREKKVRGDVEKAKRkveqdlkstqENVEDLERV 1069
Cdd:pfam10174 411 -RDKDKQLAGLKERVKSLQ--TDSSNTDTAL-TTLEEALSEKERIIERLKEQREREDRERL----------EELESLKKE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1070 KRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQR------AELNRELEEL 1143
Cdd:pfam10174 477 NKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkahnaEEAVRTNPEI 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1144 GERLDEAGGATSAQIELNKKREAE---LLKIRRDLEEASLQHEAQISALRKKhqdAANEMADQVDQLQKVKSKLEKDKKD 1220
Cdd:pfam10174 557 NDRIRLLEQEVARYKEESGKAQAEverLLGILREVENEKNDKDKKIAELESL---TLRQMKEQNKKVANIKHGQQEMKKK 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1221 LKREMDDLESQMTHNMKNKGCS--EKVMKQFESQMSDLNA---RLEDSQRSINELQSQKSRLQAENSdltRQLEDAehrv 1295
Cdd:pfam10174 634 GAQLLEEARRREDNLADNSQQLqlEELMGALEKTRQELDAtkaRLSSTQQSLAEKDGHLTNLRAERR---KQLEEI---- 706
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 127773 1296 sVLSKEKSQLSSQLE-DARRSLEEETRARSK-LQNEVRNMHADMDAIREQLEEEQESK 1351
Cdd:pfam10174 707 -LEMKQEALLAAISEkDANIALLELSSSKKKkTQEEVMALKREKDRLVHQLKQQTQNR 763
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1241-1588 |
1.82e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.14 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1241 CSEKVmKQFESQMSDLNARLEDsqrsINELQSQKSRLQAENSDL---TRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLE 1317
Cdd:pfam05622 126 SSDKV-KKLEATVETYKKKLED----LGDLRRQVKLLEERNAEYmqrTLQLEEELKKANALRGQLETYKRQVQELHGKLS 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1318 EETRARSKLQNEVRNMHADMDAI---REQLEEEQESksdvqrqLSKANNEIQ--QWRSKFESEGANRTEELEDQKRKLLG 1392
Cdd:pfam05622 201 EESKKADKLEFEYKKLEEKLEALqkeKERLIIERDT-------LRETNEELRcaQLQQAELSQADALLSPSSDPGDNLAA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1393 KL--SEAEQTTEAANAKCSAL-EKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQK 1469
Cdd:pfam05622 274 EImpAEIREKLIRLQHENKMLrLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGS 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1470 ESRGYSAelyrIKASIEEYQDSIGALRRENKNLADEIHDLT-DQLSEGGRSTHELDKARRRLEmekEELQAA-------L 1541
Cdd:pfam05622 354 KAEDSSL----LKQKLEEHLEKLHEAQSELQKKKEQIEELEpKQDSNLAQKIDELQEALRKKD---EDMKAMeerykkyV 426
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 127773 1542 EEAEGALEQEEAKVMRAQ-LEIATVRN---EIDKRIQEKEEEFDNTRRNHQ 1588
Cdd:pfam05622 427 EKAKSVIKTLDPKQNPASpPEIQALKNqllEKDKKIEHLERDFEKSKLQRE 477
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1100-1704 |
1.85e-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: 43.09 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1100 QLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEaggatsAQIELNK-KREAELLKIR-RDLE- 1176
Cdd:pfam05701 39 LVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLER------AQTEEAQaKQDSELAKLRvEEMEq 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1177 ----EASLQHEAQISALRKKHQDAANEMA---DQVDQLQKvksklekdkkdlkrEMDDLESQMTHNMKNKGCSEKVMKQF 1249
Cdd:pfam05701 113 giadEASVAAKAQLEVAKARHAAAVAELKsvkEELESLRK--------------EYASLVSERDIAIKRAEEAVSASKEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1250 ESQMSDLNARLEDSQRSINelQSQKSRLQAEnsdltrqledaEHRVSVlSKEKSQLSSQLEDARRSLEEETRarsklqne 1329
Cdd:pfam05701 179 EKTVEELTIELIATKESLE--SAHAAHLEAE-----------EHRIGA-ALAREQDKLNWEKELKQAEEELQ-------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1330 vrnmhadmdaireQLEEEQESKSDVQRQLSKANNEIQQWRSKFesegANRTEeledqkrkllGKLSEAEQTTEAANAKCS 1409
Cdd:pfam05701 237 -------------RLNQQLLSAKDLKSKLETASALLLDLKAEL----AAYME----------SKLKEEADGEGNEKKTST 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1410 ALEKAKSRLQQELEDMSIEVDRANASVNQMekkqrafdKTTAEwqakvnSLQSELENS--------QKESRGySAELYRI 1481
Cdd:pfam05701 290 SIQAALASAKKELEEVKANIEKAKDEVNCL--------RVAAA------SLRSELEKEkaelaslrQREGMA-SIAVSSL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1482 KASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRsthELDKARRRLEMEKEELQAALEEAEgaleqeeakvmRAQLE 1561
Cdd:pfam05701 355 EAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQ---EAEEAKSLAQAAREELRKAKEEAE-----------QAKAA 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1562 IATVrneiDKRIQEKEEEFDNTRRNHQRALESMQASLEAEAKGKADamrikkklEQDINELEVALDASnrgkaEMEKTVK 1641
Cdd:pfam05701 421 ASTV----ESRLEAVLKEIEAAKASEKLALAAIKALQESESSAEST--------NQEDSPRGVTLSLE-----EYYELSK 483
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 127773 1642 RYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQA-ERARKASDNELA 1704
Cdd:pfam05701 484 RAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEERKEALKIAlEKAEKAKEGKLA 547
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1250-1368 |
1.87e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 41.07 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1250 ESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKsqlsSQLEDARRSLEEETRARSKLqne 1329
Cdd:pfam08614 56 EQLLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAER----AQLEEKLKDREEELREKRKL--- 128
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 127773 1330 VRNMHADMDAIREQLeEEQESKSdvqRQLSKANNE-IQQW 1368
Cdd:pfam08614 129 NQDLQDELVALQLQL-NMAEEKL---RKLEKENRElVERW 164
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1345-1695 |
1.90e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.21 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1345 EEEQESKSDVQRQLSKANNEIQQWRSKFESEGANRT--------EELEDQKRKLLGKLSEAE-QTTEAANAKCSALEKAK 1415
Cdd:pfam09731 84 EEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLpkseqekeKALEEVLKEAISKAESATaVAKEAKDDAIQAVKAHT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1416 SRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEW--QAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIG 1493
Cdd:pfam09731 164 DSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLakQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1494 ALRRENKNLADE-----------IHDLTDQLSEGGRSTHE-----LDKARRRLEM-----------EKEELQAALEEAEG 1546
Cdd:pfam09731 244 LVDQYKELVASErivfqqelvsiFPDIIPVLKEDNLLSNDdlnslIAHAHREIDQlskklaelkkrEEKHIERALEKQKE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1547 ALEQEEAKVMRAQleiatvRNEIDKRIQEKEEEFDntrRNHQRALESMQASLEAEAKGKADAM--RIKKKLEQDINELEV 1624
Cdd:pfam09731 324 ELDKLAEELSARL------EEVRAADEAQLRLEFE---REREEIRESYEEKLRTELERQAEAHeeHLKDVLVEQEIELQR 394
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 127773 1625 ALDASNRGKAEMEKTVkrYQQQIREMQTSIEEEQRQRDEARESYNMAeRRCTLMSGEVEELRAALEQAERA 1695
Cdd:pfam09731 395 EFLQDIKEKVEEERAG--RLLKLNELLANLKGLEKATSSHSEVEDEN-RKAQQLWLAVEALRSTLEDGSAD 462
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
777-799 |
2.00e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 37.31 E-value: 2.00e-03
10 20
....*....|....*....|...
gi 127773 777 RLSKIISMFQAHIRGYLIRKAYK 799
Cdd:smart00015 1 RLTRAAIIIQAAWRGYLARKRYK 23
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1270-1882 |
2.15e-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: 42.89 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1270 LQSQKSRLQAENSDLTRQLEDAEHRV-SVLSKEKSQLSSQLEdARRSLEEETRARSKL--------QNEVRNMHADMDAI 1340
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLgSSMNSIKTFWSPELK-KERALRKEEAARISVlkeqyrvtQEENQHLQLTIQAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1341 REQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEGAN---RTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSR 1417
Cdd:pfam10174 80 QDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENfrrLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDES 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1418 LQQELEDMSIEVDRANASVNQMEKKQRafdktTAEWQAKVNSLQSELENSQKESRGYSAELYR-------------IKAS 1484
Cdd:pfam10174 160 IKKLLEMLQSKGLPKKSGEEDWERTRR-----IAEAEMQLGHLEVLLDQKEKENIHLREELHRrnqlqpdpaktkaLQTV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1485 IEEYQDSIGALRRENKNLADEIHDL-------------------------------TDQL-SEGGRSTHELDKARRRLE- 1531
Cdd:pfam10174 235 IEMKDTKISSLERNIRDLEDEVQMLktngllhtedreeeikqmevykshskfmknkIDQLkQELSKKESELLALQTKLEt 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1532 -------------MEKEELQAalEEAEGALEQEEAKVMRAQLEI-ATVRNEIDKRIQEKEEE--------------FDNT 1583
Cdd:pfam10174 315 ltnqnsdckqhieVLKESLTA--KEQRAAILQTEVDALRLRLEEkESFLNKKTKQLQDLTEEkstlageirdlkdmLDVK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1584 RRN---HQRALESMQASLEAEAKGKADAMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQiremqtsIEEEQRQ 1660
Cdd:pfam10174 393 ERKinvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQ-------REREDRE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1661 RDEaresynmaerrctlmsgEVEELRAALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDE 1740
Cdd:pfam10174 466 RLE-----------------ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQ 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1741 MHGELKGADERCKKA--MADAAR----LADELRA-EQDHSNQVEKVRKNlESQVKEFQIRLDEAEASSLKGGKKmIQKLE 1813
Cdd:pfam10174 529 KKEECSKLENQLKKAhnAEEAVRtnpeINDRIRLlEQEVARYKEESGKA-QAEVERLLGILREVENEKNDKDKK-IAELE 606
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127773 1814 SRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTfkRQVEEA 1882
Cdd:pfam10174 607 SLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKT--RQELDA 673
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1321-1487 |
2.16e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1321 RARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKfeseganrteeLEDQKRKLLGKLSEAEQt 1400
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-----------IKKYEEQLGNVRNNKEY- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1401 tEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKqraFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYR 1480
Cdd:COG1579 92 -EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
....*..
gi 127773 1481 IKASIEE 1487
Cdd:COG1579 168 LAAKIPP 174
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1084-1470 |
2.23e-03 |
|
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: 42.75 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1084 ISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAE---LNRELEELGERLDEAGGATSAQIEL 1160
Cdd:pfam19220 12 LGEMADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAygkLRRELAGLTRRLSAAEGELEELVAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1161 NKKREAELLKIRRDLEEASL---QHEAQISALRKKHQDAANE---MADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTH 1234
Cdd:pfam19220 92 LAKLEAALREAEAAKEELRIelrDKTAQAEALERQLAAETEQnraLEEENKALREEAQAAEKALQRAEGELATARERLAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1235 NMKNKGCSEKVMKQFESQMSDLNARLEDSQRSINELQsqksrlqaensdltRQLEDAEHRVSVLSKEKSQLSSQLEDARR 1314
Cdd:pfam19220 172 LEQENRRLQALSEEQAAELAELTRRLAELETQLDATR--------------ARLRALEGQLAAEQAERERAEAQLEEAVE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1315 SLE-EETRARSKLQnEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESeganRTEELEDQKRKLLGK 1393
Cdd:pfam19220 238 AHRaERASLRMKLE-ALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLER----RLAGLEADLERRTQQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1394 LSEAEQTTEAANAKCSALEKAksrlqqeLEDMSIEVDRANASVN----QMEKKQRAFDKTTAEWQAKVNSLQSELENSQK 1469
Cdd:pfam19220 313 FQEMQRARAELEERAEMLTKA-------LAAKDAALERAEERIAslsdRIAELTKRFEVERAALEQANRRLKEELQRERA 385
|
.
gi 127773 1470 E 1470
Cdd:pfam19220 386 E 386
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1062-1208 |
2.36e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.34 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1062 NVEDLERVK----------RELEENVRRKEAEISSLNSKLEDEQNLVSQlQRKIKELQARIeeleeeleaeRNARAKVEK 1131
Cdd:COG1566 60 LVKEGDRVKkgqvlarldpTDLQAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQL----------AAAQAQLDL 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 1132 QRAELNReLEELGERldeagGATSAQiELNKKReAELLKIRRDLEEASLQHEAQISALRKKHQDAANEmaDQVDQLQ 1208
Cdd:COG1566 129 AQRELER-YQALYKK-----GAVSQQ-ELDEAR-AALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQ--AQVAQAE 195
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1382-1708 |
2.40e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1382 ELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQ 1461
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1462 SELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAAL 1541
Cdd:COG4372 94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1542 EEAEGALEQEEAKVMRAQL-EIATVRNEIDKRIQEKEEEFDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDIN 1620
Cdd:COG4372 174 QALSEAEAEQALDELLKEAnRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1621 ELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAERARKASD 1700
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
....*...
gi 127773 1701 NELADAND 1708
Cdd:COG4372 334 ILLAELAD 341
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1587-1915 |
2.41e-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: 42.82 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1587 HQRALESMQASLEAEAKGKADAMRIKKKLEQDINELEVALDAS--------NRGKAEMEKTVKRYQQQIREmQTSIEEEQ 1658
Cdd:pfam09731 91 IPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVlkeaiskaESATAVAKEAKDDAIQAVKA-HTDSLKEA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1659 RQRDE--------------ARESYNMAERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNELTSQVSSVQGQK 1724
Cdd:pfam09731 170 SDTAEisrekatdsalqkaEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1725 RKLEGDINAMQTDLDEMHGEL--------KGADERCKKAMADAARLADELRAEQDHsnQVEKVRKNLESQVKEFQIRLDE 1796
Cdd:pfam09731 250 ELVASERIVFQQELVSIFPDIipvlkednLLSNDDLNSLIAHAHREIDQLSKKLAE--LKKREEKHIERALEKQKEELDK 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1797 AEAsslkggkKMIQKLESRVHELEAELDNE-QRRHAETQKNMR-KADRRLKELAFQADEDRKNQERLQ--ELIDKLNAKI 1872
Cdd:pfam09731 328 LAE-------ELSARLEEVRAADEAQLRLEfEREREEIRESYEeKLRTELERQAEAHEEHLKDVLVEQeiELQREFLQDI 400
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 127773 1873 KTfkrQVEEAEEIAAINLAKYRKAQHELEEA-EERADTADSTLQ 1915
Cdd:pfam09731 401 KE---KVEEERAGRLLKLNELLANLKGLEKAtSSHSEVEDENRK 441
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1781-1888 |
2.53e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1781 KNLESQVKEFQIRLDEAEASSLKGGKKMIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDRKNQER 1860
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKE 493
|
90 100
....*....|....*....|....*...
gi 127773 1861 LQELIDKLNAKIKTFKRQVEEaEEIAAI 1888
Cdd:COG0542 494 LAELEEELAELAPLLREEVTE-EDIAEV 520
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
972-1192 |
2.55e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 972 ISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRK 1051
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1052 VEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEE--LEEELEAERNARAKV 1129
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAleQELQALSEAEAEQAL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 127773 1130 EKQRAELNRELEELGERLDEAGGATSAQIELNKKREAELLKIRRDLEEASLQHEAQISALRKK 1192
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1409-1542 |
2.55e-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: 41.97 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1409 SALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELEN--SQKESRGYSAELYRIKASIE 1486
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDllTDEGGAIARKEIKDLQKELE 189
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 1487 EYQDSIGA-LRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALE 1542
Cdd:cd22656 190 KLNEEYAAkLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIP 246
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1635-1853 |
2.71e-03 |
|
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: 42.74 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1635 EMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEqAERARKASDNELADANDRVNELT 1714
Cdd:pfam13166 290 KLIEKVESAISSLLAQLPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALE-AKRKDPFKSIELDSVDAKIESIN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1715 SQVSSVQgqkrKLEGDINAMQTDLDEmhgelkgADERCKKAMAdaARLADELRAEQDhsnQVEKVRKNLESQVKEFQIRL 1794
Cdd:pfam13166 369 DLVASIN----ELIAKHNEITDNFEE-------EKNKAKKKLR--LHLVEEFKSEID---EYKDKYAGLEKAINSLEKEI 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 127773 1795 DEAEASslkggkkmIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADE 1853
Cdd:pfam13166 433 KNLEAE--------IKKLREEIKELEAQLRDHKPGADEINKLLKAFGFGELELSFNEEG 483
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1092-1363 |
2.75e-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: 43.02 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1092 EDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNREL--------EELGERLDEA----GGATSAQIE 1159
Cdd:COG3096 832 PDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLpqanlladETLADRLEELreelDAAQEAQAF 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1160 LNK--KREAELLKIRRDLEEASLQHEA------QISALRKKHQDAANEMADQVDQLQKVKSKLEKDKKDLKREMDD-LES 1230
Cdd:COG3096 912 IQQhgKALAQLEPLVAVLQSDPEQFEQlqadylQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSDLNEkLRA 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1231 QMTHNMKNKGCSEKVMKQFESQMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQL-EDAEHRVSVlskEKSQLSSQL 1309
Cdd:COG3096 992 RLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQAdAEAEERARI---RRDELHEEL 1068
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 127773 1310 --EDARRSLEEETRARSK-----LQNEVRNMHADMDAIREQLEEEQESKSDVQRqLSKANN 1363
Cdd:COG3096 1069 sqNRSRRSQLEKQLTRCEaemdsLQKRLRKAERDYKQEREQVVQAKAGWCAVLR-LARDND 1128
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1613-1908 |
2.90e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1613 KKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQA 1692
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1693 ERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMHGELKGADERckKAMADAARLADELRAEQDH 1772
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA--EAEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1773 SNQVEKVRKNLESQVKEFQIRLDEAEASSLKGGKKMIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQAD 1852
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 127773 1853 EDRKNQERLQELIDKLNAKIKTFKRQVEEAEEIAAINLAKYRKAQHELEEAEERAD 1908
Cdd:COG4372 279 EIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1073-1212 |
2.91e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1073 LEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGG 1152
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 127773 1153 ATSA--QIELNKKREAELLK-----IRRDLeeASLQHEAQISALRKKHQDAANE---------MADQVDQLQKVKS 1212
Cdd:PRK09039 124 ELDSekQVSARALAQVELLNqqiaaLRRQL--AALEAALDASEKRDRESQAKIAdlgrrlnvaLAQRVQELNRYRS 197
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
971-1085 |
3.38e-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: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 971 QISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEedkcnhLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKR 1050
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAE------LRDELAELEEELEALKARWEAEKELIEEIQELKE 478
|
90 100 110
....*....|....*....|....*....|....*
gi 127773 1051 KVEQDLKSTQENVEDLERVKRELEENVRRKEAEIS 1085
Cdd:COG0542 479 ELEQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1032-1771 |
3.42e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1032 EDNLERekkVRGDVEKAKRKVEQDLKSTQENVEDLERVKR-ELEENVRRKEAEISSLNSKLEDEQNlvsqlQRKIKELQA 1110
Cdd:NF041483 523 EETLER---TRAEAERLRAEAEEQAEEVRAAAERAARELReETERAIAARQAEAAEELTRLHTEAE-----ERLTAAEEA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1111 RIEELEEELEAERNARAKVEKQRAE-------LNRELEELGERL-DEAGGATSAQielnkKREAELLKIRRDLEEAS--- 1179
Cdd:NF041483 595 LADARAEAERIRREAAEETERLRTEaaerirtLQAQAEQEAERLrTEAAADASAA-----RAEGENVAVRLRSEAAAeae 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1180 -LQHEAQISA--LRKKHQDAANEMADQVdqlQKVKSKLEKDKKDLKREMDDLESQMTHNMKNKgcSEKVMKQFESQMSDL 1256
Cdd:NF041483 670 rLKSEAQESAdrVRAEAAAAAERVGTEA---AEALAAAQEEAARRRREAEETLGSARAEADQE--RERAREQSEELLASA 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1257 NARLEDSQ----RSINELQSQKSRLQAENSDLTRQLEDAehrVSVLSKEKSQLSSQLEDARRSLEEetRARSKLQNEVRN 1332
Cdd:NF041483 745 RKRVEEAQaeaqRLVEEADRRATELVSAAEQTAQQVRDS---VAGLQEQAEEEIAGLRSAAEHAAE--RTRTEAQEEADR 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1333 MHADMDAIREQLEEeqesksDVQRQLSKANNEIQQWRSKFESEGANRTEELEdqkrKLLGKLSEAEQT--TEAANAKCSA 1410
Cdd:NF041483 820 VRSDAYAERERASE------DANRLRREAQEETEAAKALAERTVSEAIAEAE----RLRSDASEYAQRvrTEASDTLASA 889
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1411 LEKAKSRLQQELEDMS-IEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAElyRIKASIEEYQ 1489
Cdd:NF041483 890 EQDAARTRADAREDANrIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAA--QAEQLIAEAT 967
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1490 DSIGALRREnknlADEIHDLTDQLSEGGRSthELDKARRRLEMEKEELQA-ALEEAEGALEQEEAKVMRAQLEIAtvrNE 1568
Cdd:NF041483 968 GEAERLRAE----AAETVGSAQQHAERIRT--EAERVKAEAAAEAERLRTeAREEADRTLDEARKDANKRRSEAA---EQ 1038
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1569 IDKRIQEKEEEFDNTRRNHQRalESMQASLEAEAKgkADAMRIKKKLEQDinelEVALDASNRGKAEMEKT--------- 1639
Cdd:NF041483 1039 ADTLITEAAAEADQLTAKAQE--EALRTTTEAEAQ--ADTMVGAARKEAE----RIVAEATVEGNSLVEKArtdadellv 1110
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1640 -VKRYQQQIREMQtsieEEQRQRDEAR-ESYNMAERRCTlmsgeVEELRAALEQAERARKASDNELADANDRVNELTSQV 1717
Cdd:NF041483 1111 gARRDATAIRERA----EELRDRITGEiEELHERARRES-----AEQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDA 1181
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 127773 1718 SSVQGQKR-----KLEGDINAMQTDLDEMHGElkgADERCKKAMADAARLADELRAEQD 1771
Cdd:NF041483 1182 NSEASKVRiaavkKAEGLLKEAEQKKAELVRE---AEKIKAEAEAEAKRTVEEGKRELD 1237
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
991-1362 |
3.71e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 991 KEKKALEEANKKTSDSLQAEEDKCNHLNKLKAKLEQ----ALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVEDL 1066
Cdd:COG5185 226 KEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQntdlRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1067 ERVKRELEENVRRKEAEissLNSKLEDeqnLVSQLQRKIKELQARIEeleeeleaerNARAKVEKQRAELNRELEELGEr 1146
Cdd:COG5185 306 DIKKATESLEEQLAAAE---AEQELEE---SKRETETGIQNLTAEIE----------QGQESLTENLEAIKEEIENIVG- 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1147 ldeaggatsaqielnkkrEAELLKIRRDLEEASLQHEAQISALRKKHQDAANEMADQVDQLQKVKSKLEKDKKDLKREMD 1226
Cdd:COG5185 369 ------------------EVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1227 DLESQMTHNMK-NKGCSEKVMKQFESQMSDLNARLEDSQRSINelqsqkSRLQAENSDLTRQLEDAEHRVSVLSKEKSQL 1305
Cdd:COG5185 431 QATSSNEEVSKlLNELISELNKVMREADEESQSRLEEAYDEIN------RSVRSKKEDLNEELTQIESRVSTLKATLEKL 504
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 127773 1306 SSQLEdarRSLEeetRARSKLQNEVRNMHADM----DAIREQLEEEQESKSDVQRQLSKAN 1362
Cdd:COG5185 505 RAKLE---RQLE---GVRSKLDQVAESLKDFMrargYAHILALENLIPASELIQASNAKTD 559
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
955-1209 |
3.88e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.94 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 955 ENTLQKAEQDK----AHKDNQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCNHLNKLkakLEQALDE 1030
Cdd:pfam05667 211 RNAAELAAAQEweeeWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAEL---LSSFSGS 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1031 LEDNLEREKKVRGDVEKAkrkvEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQA 1110
Cdd:pfam05667 288 STTDTGLTKGSRFTHTEK----LQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLES 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1111 RIEELEEELEAERNARAKVEKQR-----------------AELNRELEELGERLDEAGGatsaqiELNKKREAELLKIRR 1173
Cdd:pfam05667 364 SIKQVEEELEELKEQNEELEKQYkvkkktldllpdaeeniAKLQALVDASAQRLVELAG------QWEKHRVPLIEEYRA 437
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 127773 1174 DLEEASLQHE------AQISALRKKHQDAANEmADQVDQLQK 1209
Cdd:pfam05667 438 LKEAKSNKEDesqrklEEIKELREKIKEVAEE-AKQKEELYK 478
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1260-1713 |
3.88e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.20 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1260 LEDSQRSINELQSQKSRLQAENSDLTRQLEDAEhRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMhadMDA 1339
Cdd:COG5278 78 LEPYEEARAEIDELLAELRSLTADNPEQQARLD-ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKAL---MDE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1340 IRE---QLEEEQESKSDVQRQLSKANNEIQQWRSKFESEGANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKS 1416
Cdd:COG5278 154 IRArllLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1417 RLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALR 1496
Cdd:COG5278 234 LLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1497 RENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQEK 1576
Cdd:COG5278 314 AAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1577 EEEFDNTRRNHQRALESMQASLEAEAKGKADAMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEE 1656
Cdd:COG5278 394 AIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAA 473
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 1657 EQRQRDEARESYNMAERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNEL 1713
Cdd:COG5278 474 LAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1394-1565 |
4.17e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 41.76 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1394 LSEAEQTTEAANAKcsALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFD-KTTAEWQAK-VNSLQSELenSQKEs 1471
Cdd:COG3524 160 LAESEELVNQLSER--AREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDpEATAEALLQlIATLEGQL--AELE- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1472 rgysAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQL--SEGGRSTHELDKARRRLEMEKEELQAALEEAEGALE 1549
Cdd:COG3524 235 ----AELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLtgASGGDSLASLLAEYERLELEREFAEKAYTSALAALE 310
|
170
....*....|....*.
gi 127773 1550 QEEAKVMRAQLEIATV 1565
Cdd:COG3524 311 QARIEAARQQRYLAVI 326
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
942-1204 |
4.22e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.98 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 942 ADNANLKKDIGDLENTLQKAEQdkahkdnQISTLQGEISQQDEHIGKLNKEKKALEEANKKTS--DSLQAEEDKCNHLNK 1019
Cdd:COG0497 151 AGLEELLEEYREAYRAWRALKK-------ELEELRADEAERARELDLLRFQLEELEAAALQPGeeEELEEERRRLSNAEK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1020 LKAKLEQALDELEDNlerEKKVRGDVEKAKRKVEQ---DLKSTQENVEDLERVKRELEENVRrkeaEISSLNSKLE-DEQ 1095
Cdd:COG0497 224 LREALQEALEALSGG---EGGALDLLGQALRALERlaeYDPSLAELAERLESALIELEEAAS----ELRRYLDSLEfDPE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1096 NLVSQLQR--KIKELQarieeleeeleaeRNARAKVEkqraELNRELEELGERLDEAGGATSAQIELnkkrEAELLKIRR 1173
Cdd:COG0497 297 RLEEVEERlaLLRRLA-------------RKYGVTVE----ELLAYAEELRAELAELENSDERLEEL----EAELAEAEA 355
|
250 260 270
....*....|....*....|....*....|.
gi 127773 1174 DLEEASlqheAQISALRKKhqdAANEMADQV 1204
Cdd:COG0497 356 ELLEAA----EKLSAARKK---AAKKLEKAV 379
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1316-1821 |
4.27e-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: 42.25 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1316 LEEETRARSKLQNevrnMHADMDAIREQLEEEQESKSDvqRQLSKanNEIQQWRSKFESE---GANRTEELEDQ----KR 1388
Cdd:COG3096 221 LPENSGVRKAFQD----MEAALRENRMTLEAIRVTQSD--RDLFK--HLITEATNYVAADymrHANERRELSERalelRR 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1389 KLLG---KLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRafdkttaeWQAKVNSLQSELE 1465
Cdd:COG3096 293 ELFGarrQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIER--------YQEDLEELTERLE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1466 nSQKESRGYSAELYrikasiEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAE 1545
Cdd:COG3096 365 -EQEEVVEEAAEQL------AEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCGLPDLTPE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1546 GALEQEEAkvMRAQLEIAT-VRNEIDKRIQEKEEefdnTRRNHQRALESMQASleAEAKGKADAMRIKKKLEQDINELEV 1624
Cdd:COG3096 438 NAEDYLAA--FRAKEQQATeEVLELEQKLSVADA----ARRQFEKAYELVCKI--AGEVERSQAWQTARELLRRYRSQQA 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1625 ALDASNRGKAEMEKTVKRYQQQiREMQTSIEEEQRQrdeARESYNMAErrctlmsgEVEELRAALEQaerarkasdnELA 1704
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQQ-QNAERLLEEFCQR---IGQQLDAAE--------ELEELLAELEA----------QLE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1705 DANDRVNELTSQVSSVQGQKRKLEGDInamqtdldemhGELKGADERCKKAMADAARLADELRAEQDHSNQVEKVRKNLE 1784
Cdd:COG3096 568 ELEEQAAEAVEQRSELRQQLEQLRARI-----------KELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLL 636
|
490 500 510
....*....|....*....|....*....|....*..
gi 127773 1785 SQVKEFQIRLDEAEAsslkggKKmiQKLESRVHELEA 1821
Cdd:COG3096 637 EREREATVERDELAA------RK--QALESQIERLSQ 665
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
965-1320 |
4.28e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.34 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 965 KAHKDNQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCNHLNKLKAK---LEQALDELedNLEREKKV 1041
Cdd:PTZ00108 1030 NAKKKDLVKELKKLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSYdylLSMPIWSL--TKEKVEKL 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1042 RGDVEKAKRKVEQDLKSTQENV--EDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARiEELEEEL 1119
Cdd:PTZ00108 1108 NAELEKKEKELEKLKNTTPKDMwlEDLDKFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEK-KKKKSSA 1186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1120 EAERNARAKVEKQRAELNRELEELGERLDEAGGATSAQIELNKKREAELlkirRDLEEASLQHEAQISALRKKhqdaANE 1199
Cdd:PTZ00108 1187 DKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKP----KKSSVKRLKSKKNNSSKSSE----DND 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1200 MADQVDQLQKVKSKLEKDKKDLKREMDDLESQMTHNMKNKGCSE------KVMKQFESQMSDLNARLEDSQRSINELQSQ 1273
Cdd:PTZ00108 1259 EFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPssptkkKVKKRLEGSLAALKKKKKSEKKTARKKKSK 1338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 127773 1274 KSRLQAENSDLTRQLEdaehRVSVLSKEKSQLSSQLEDARRSLEEET 1320
Cdd:PTZ00108 1339 TRVKQASASQSSRLLR----RPRKKKSDSSSEDDDDSEVDDSEDEDD 1381
|
|
| DUF3498 |
pfam12004 |
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ... |
1450-1630 |
4.80e-03 |
|
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.
Pssm-ID: 463427 [Multi-domain] Cd Length: 511 Bit Score: 41.67 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1450 TAEWQAKVNSLQSELENSQKESRgysaELYRIKasiEEYQDsigalrrenknladEIHDLTDQLSEGGRSTHELDkarRR 1529
Cdd:pfam12004 359 TAAWVLNMNGQYEEEESSGPESR----EELKQA---EKYEQ--------------EISKLKERLRVSNRKLEEYE---RR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1530 LEMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQEKEEEFdntRRNHQraleSMQASLEAeakgkadam 1609
Cdd:pfam12004 415 LLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEEL---KKDHA----EMQAVIDS--------- 478
|
170 180
....*....|....*....|....*
gi 127773 1610 riKKKL----EQDIneleVALDASN 1630
Cdd:pfam12004 479 --KQKIidaqEKRI----ASLDAAN 497
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1252-1501 |
5.32e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1252 QMSDLNARLEDSQRSINELQSQKSRLQAENSDLTRQLEDAEHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVR 1331
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1332 NMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEGANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSAL 1411
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1412 EKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDS 1491
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
250
....*....|
gi 127773 1492 IGALRRENKN 1501
Cdd:COG4372 279 EIAALELEAL 288
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1383-1800 |
5.61e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.60 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1383 LEDQKRKLLG---KLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEWQAKVNS 1459
Cdd:pfam05622 26 LQEEKNSLQQenkKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1460 LQSELENSQK------ESRGYSAELYRIKASIEEYQ---DSIGALRRENKNLADEIhdlTDQLSEGGRSTHELDKA---R 1527
Cdd:pfam05622 106 LTSLAEEAQAlkdemdILRESSDKVKKLEATVETYKkklEDLGDLRRQVKLLEERN---AEYMQRTLQLEEELKKAnalR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1528 RRLEMEKEELQaaleEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQEKE---EEFDNTRRN---------HQRALESMQ 1595
Cdd:pfam05622 183 GQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKErliIERDTLRETneelrcaqlQQAELSQAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1596 ASLEA------------------------EAKGKADAMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQ 1651
Cdd:pfam05622 259 ALLSPssdpgdnlaaeimpaeireklirlQHENKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQ 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1652 TSIEEEQRQrdeARESYNMAERRCTLMSgeveELRAALEQAERArkasDNELADANDRVNELTSQVSSVQGQKrklegdI 1731
Cdd:pfam05622 339 QQVEELQKA---LQEQGSKAEDSSLLKQ----KLEEHLEKLHEA----QSELQKKKEQIEELEPKQDSNLAQK------I 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 127773 1732 NAMQTDLDEMHGELKGADERCKKAMADAARLADELRAEQDHSNQVEKVRknLESQVKEFQIRLDEAEAS 1800
Cdd:pfam05622 402 DELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASPPEIQA--LKNQLLEKDKKIEHLERD 468
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1098-1609 |
5.63e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 41.71 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1098 VSQLQRKIKELQARIEELEEELEAERNARAKvekQRAELNRELEELGERLDEAGGATSAQIELNKKReAELLKIRRDLEE 1177
Cdd:PRK10246 306 LAHTRQQIEEVNTRLQSTMALRARIRHHAAK---QSAELQAQQQSLNTWLAEHDRFRQWNNELAGWR-AQFSQQTSDREQ 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1178 ASLQHEaQISALRKKH------------QDAANEMADQVDQ----------------LQKVKSKLEKDKKDLKREMDDLE 1229
Cdd:PRK10246 382 LRQWQQ-QLTHAEQKLnalpaitltltaDEVAAALAQHAEQrplrqrlvalhgqivpQQKRLAQLQVAIQNVTQEQTQRN 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1230 SQMTHNMKNkgcsekvMKQFESQMSDLNARLEDSQRsINELQSQKSRLQA---------------------ENSDLTRQL 1288
Cdd:PRK10246 461 AALNEMRQR-------YKEKTQQLADVKTICEQEAR-IKDLEAQRAQLQAgqpcplcgstshpaveayqalEPGVNQSRL 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1289 EDAEHRVSVLSKEKSQLSSQL----------EDARRSLEEETRARSKLQNEV-------RNMHADM-DAIREQLEEEQES 1350
Cdd:PRK10246 533 DALEKEVKKLGEEGAALRGQLdaltkqlqrdESEAQSLRQEEQALTQQWQAVcaslnitLQPQDDIqPWLDAQEEHERQL 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1351 KSDVQRQ-LSKANNEIQQWRSKFESEGANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRlQQELEDMSIEV 1429
Cdd:PRK10246 613 RLLSQRHeLQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSWQQR-QNELTALQNRI 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1430 DRANASVNQM----EKKQRAFDKTTAEWQAKVN---SLQSELENSQKESrgySAELYRIKASIEEYQDSIGALRrenknL 1502
Cdd:PRK10246 692 QQLTPLLETLpqsdDLPHSEETVALDNWRQVHEqclSLHSQLQTLQQQD---VLEAQRLQKAQAQFDTALQASV-----F 763
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1503 ADEIHDLTDQLSEggRSTHELDKARRRLEMEKEELQAALEEAEGALEQ---------------EEAKVMRAQL-----EI 1562
Cdd:PRK10246 764 DDQQAFLAALLDE--ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQhqqhrpdgldltvtvEQIQQELAQLaqqlrEN 841
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 127773 1563 ATVRNEIDKRIQEkeeefDNTRRNHQRAL--ESMQASLEAEAKGKADAM 1609
Cdd:PRK10246 842 TTRQGEIRQQLKQ-----DADNRQQQQALmqQIAQATQQVEDWGYLNSL 885
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1450-1919 |
6.10e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.43 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1450 TAEWQAKVNSLQSELENSQKESRGY-----SAELYRIKASIEEYQDSIGALRR------ENKNLADEIHDLTDQLSEGGR 1518
Cdd:COG5278 45 TYEVLRALEELLSALLDAETGQRGYlltgdESFLEPYEEARAEIDELLAELRSltadnpEQQARLDELEALIDQWLAELE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1519 STHELdkarrrleMEKEELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQEKEEEFDNTRRNHQRALESMQASL 1598
Cdd:COG5278 125 QVIAL--------RRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLAL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1599 -------EAEAKGKADAMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMA 1671
Cdd:COG5278 197 aralaalLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1672 ERRCTLMSGEVEELRAALEQAERARKASDNELADANDRVNELTSQVSSVQGQKRKLEGDINAMQTDLDEMHGELKGADER 1751
Cdd:COG5278 277 LAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1752 CKKAMADAARLADELRAEQDHSNQVEKVRKNLESQVKEFQIRLDEAEASSLKGGKKMIQKLESRVHELEAELDNEQRRHA 1831
Cdd:COG5278 357 AAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1832 ETQKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEAEEIAAINLAKYRKAQHELEEAEERADTAD 1911
Cdd:COG5278 437 EEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAA 516
|
....*...
gi 127773 1912 STLQKFRA 1919
Cdd:COG5278 517 LAAALAAA 524
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1295-1592 |
6.27e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1295 VSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFES 1374
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1375 EgANRTEELEDQKRKLLGKLSEAEQTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQMEKKQRAFDKTTAEwQ 1454
Cdd:COG4372 106 L-QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE-Q 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1455 AKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEK 1534
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 127773 1535 EELQAALEEAEGALEQEEAKVMRAQLEIATVRNEIDKRIQEKEEEFDNTRRNHQRALE 1592
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
910-1091 |
6.30e-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: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 910 ADFESQIKEleerlldeedaaadLEGIKKKMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKL 989
Cdd:COG1579 13 QELDSELDR--------------LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 990 nkEKKALEEANKKTSDSLQAEEDKcnhLNKLKAKLEQALDELEDNLEREKKVRGDVEKAKRKVEQDLKSTQENVED-LER 1068
Cdd:COG1579 79 --EEQLGNVRNNKEYEALQKEIES---LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEeLAE 153
|
170 180
....*....|....*....|...
gi 127773 1069 VKRELEENVRRKEAEISSLNSKL 1091
Cdd:COG1579 154 LEAELEELEAEREELAAKIPPEL 176
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1774-1920 |
6.36e-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: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1774 NQVEKVRKNLESQVKEFQIRLDEAEASsLKGGKKMIQKLESRVHELEAELDNEQRRHAETQ------KNMRKADRRLKEL 1847
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEAR-LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvRNNKEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 127773 1848 AFQADEDRKNQERLQELIDKLNAKiktfKRQVEEAEEIAAINLAKYRKAQHELEEAEERADTADSTLQKFRAK 1920
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEEL----EEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1045-1194 |
6.39e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1045 VEKAKRKVEQDLkstqenvEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIeeleeeLEAERN 1124
Cdd:PRK00409 504 IEEAKKLIGEDK-------EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEE------DKLLEE 570
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1125 ARAKVEKQRAELNRELEELGERLDEAGGATSAQIelnkkREAELLKIRRDLEEASLQHEAQISALRKKHQ 1194
Cdd:PRK00409 571 AEKEAQQAIKEAKKEADEIIKELRQLQKGGYASV-----KAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1809-1920 |
6.41e-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: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1809 IQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKELAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEA------ 1882
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkey 91
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 127773 1883 ----EEIAAINLAKyRKAQHELEEAEERADTADSTLQKFRAK 1920
Cdd:COG1579 92 ealqKEIESLKRRI-SDLEDEILELMERIEELEEELAELEAE 132
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1300-1538 |
6.53e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1300 KEKSQLSSQLEDARRSLEEETRARSKLQNEVRNMHAD-MDAIREQLEEEQESKSDVQRQLSKANNEIqqwrSKFESEGAN 1378
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDEL----LNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1379 RTEELEDQKRKLLGKLSEAE-------------------QTTEAANAKCSALEKAKSRLQQELEDMSIEVDRANASVNQM 1439
Cdd:PHA02562 253 PSAALNKLNTAAAKIKSKIEqfqkvikmyekggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEF 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1440 EKKQRafdkttaewqaKVNSLQSELENSQKESRGYSAELYRIKASIEEYQDsigalrrENKNLADEIHDLTDQLSeggrs 1519
Cdd:PHA02562 333 NEQSK-----------KLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA-------EFVDNAEELAKLQDELD----- 389
|
250
....*....|....*....
gi 127773 1520 thELDKARRRLEMEKEELQ 1538
Cdd:PHA02562 390 --KIVKTKSELVKEKYHRG 406
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
939-1204 |
7.14e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 939 KMEADNANLKKDIGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCNHLN 1018
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1019 KLKAKLEQALDELED---NLEREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKR------ELEENVRRKEAEIsSLNS 1089
Cdd:COG1340 82 ELNEKLNELREELDElrkELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKElvekikELEKELEKAKKAL-EKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1090 KLEDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRELEELGERLDEAGGATSaqiELNKKREAELL 1169
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAD---ELHEEIIELQK 237
|
250 260 270
....*....|....*....|....*....|....*
gi 127773 1170 KIRRDLEEASLQHEAQISALRKKHQDAANEMADQV 1204
Cdd:COG1340 238 ELRELRKELKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
975-1161 |
7.37e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.51 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 975 LQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKcnhlnklkakLEQALDELEDNLEREKKVRGDVEKAKRKVEQ 1054
Cdd:pfam09787 52 LRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAES----------SREQLQELEEQLATERSARREAEAELERLQE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1055 DLKStqeNVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQrkikELQARIEELEEELEAERNARAKVEKQRA 1134
Cdd:pfam09787 122 ELRY---LEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQS----ELENRLHQLTETLIQKQTMLEALSTEKN 194
|
170 180
....*....|....*....|....*..
gi 127773 1135 ELNRELEELGERLDEAGGATSAQIELN 1161
Cdd:pfam09787 195 SLVLQLERMEQQIKELQGEGSNGTSIN 221
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1036-1203 |
7.57e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.09 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1036 EREKKVRGDVEKAKRKVEQDLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQLQRK----------- 1104
Cdd:pfam15709 341 ERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKqrlqlqaaqer 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1105 ----IKELQARIEELEEELEAERNARAKVEKQR-AELNRELEELGERLdeAGGATSAQIELNKKREAELLKIRRDLEEAS 1179
Cdd:pfam15709 421 arqqQEEFRRKLQELQRKKQQEEAERAEAEKQRqKELEMQLAEEQKRL--MEMAEEERLEYQRQKQEAEEKARLEAEERR 498
|
170 180
....*....|....*....|....
gi 127773 1180 LQHEAQISALRKKHQDAANEMADQ 1203
Cdd:pfam15709 499 QKEEEAARLALEEAMKQAQEQARQ 522
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
1334-1538 |
7.68e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 39.75 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1334 HADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSKFESEGANRTEELED---QKRKLLGKLSEAEQTTEAANAKCSA 1410
Cdd:pfam14988 3 KFFLEYLAKKTEEKQKKIEKLWNQYVQECEEIERRRQELASRYTQQTAELQTqllQKEKEQASLKKELQALRPFAKLKES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1411 LEKAKSRLQQELEDMSIEVDRANASVN-QMEKKQRAFDKTTAEWqakvNSLQSELENSQKESRGYSAELYRIKASIEEYQ 1489
Cdd:pfam14988 83 QEREIQDLEEEKEKVRAETAEKDREAHlQFLKEKALLEKQLQEL----RILELGERATRELKRKAQALKLAAKQALSEFC 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 127773 1490 DSIgalRRENKNLADEIHDLTDQlseggrsTHELDKARRRLEMEKEELQ 1538
Cdd:pfam14988 159 RSI---KRENRQLQKELLQLIQE-------TQALEAIKSKLENRKQRLK 197
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1022-1371 |
7.88e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1022 AKLEQALDELEDNLEREKkvrgdvekakrkveqdLKSTQENVEDLERVKRELEENVRRKEAEISSLNSKLEDEQNLVSQL 1101
Cdd:PRK04778 82 PDIEEQLFEAEELNDKFR----------------FRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1102 QRKIKELQARIEELEEELEaerNARAKVEKQRAELNRELEELgERLDEAGGATSAQIELNKKREaELLKIRRDLEE---- 1177
Cdd:PRK04778 146 KDLYRELRKSLLANRFSFG---PALDELEKQLENLEEEFSQF-VELTESGDYVEAREILDQLEE-ELAALEQIMEEipel 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1178 -ASLQHE--AQISALRK------------KHQDAANEMADQVDQLQKVKSK--------LEKDKKDLKREMDDLESQMTH 1234
Cdd:PRK04778 221 lKELQTElpDQLQELKAgyrelveegyhlDHLDIEKEIQDLKEQIDENLALleeldldeAEEKNEEIQERIDQLYDILER 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1235 NMKNKgcsekvmKQFESQMSDLNARLEDSQRSINELQSQKSRLQaENSDLTrqlEDAEHRVSVLSKEKSQLSSQLEDARR 1314
Cdd:PRK04778 301 EVKAR-------KYVEKNSDTLPDFLEHAKEQNKELKEEIDRVK-QSYTLN---ESELESVRQLEKQLESLEKQYDEITE 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 127773 1315 SLEEETRARSKLQNEVRNMHADMDAIREQLEEEQESKSDVQRQLSKANNEIQQWRSK 1371
Cdd:PRK04778 370 RIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNK 426
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
949-1333 |
7.97e-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: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 949 KDIGDLENTLQKAEQD-------KAHKDnqISTLQGEISQQDEHIGKLNKEKKALEEANKKTSDSLQAEEDKCNHLNKL- 1020
Cdd:pfam06160 60 KSLPDIEELLFEAEELndkyrfkKAKKA--LDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTl 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1021 ----------KAKLEQALDELEDNLER--EKKVRGDVEKAKR---KVEQDLKSTQENVED----LERVK-------RELE 1074
Cdd:pfam06160 138 lanrfsygpaIDELEKQLAEIEEEFSQfeELTESGDYLEAREvleKLEEETDALEELMEDipplYEELKtelpdqlEELK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1075 ENVRRKEA------------EISSLNSKLEDEQNLVSQL-----QRKIKELQARIEELEEELEAERNARAKVEKQRAELN 1137
Cdd:pfam06160 218 EGYREMEEegyalehlnvdkEIQQLEEQLEENLALLENLeldeaEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1138 RELEELGERLDEaggaTSAQIELNKKR----EAELLKIRrdleeaslQHEAQISALRKKHQDAANEMADQvdqlQKVKSK 1213
Cdd:pfam06160 298 DYLEHAEEQNKE----LKEELERVQQSytlnENELERVR--------GLEKQLEELEKRYDEIVERLEEK----EVAYSE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1214 LEKDKKDLKREMDDLESQMthnmknKGCSEKVMKQFESQMsDLNARLEDSQRSINELQS--QKSRLQAENSDLTRQLEDA 1291
Cdd:pfam06160 362 LQEELEEILEQLEEIEEEQ------EEFKESLQSLRKDEL-EAREKLDEFKLELREIKRlvEKSNLPGLPESYLDYFFDV 434
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 127773 1292 EHRVSVLSKEKSQLSSQLEDARRSLEEETRARSKLQNEVRNM 1333
Cdd:pfam06160 435 SDEIEDLADELNEVPLNMDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1594-1722 |
7.99e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1594 MQASLEAEAKGKADAMrikKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAER 1673
Cdd:PRK09039 40 AQFFLSREISGKDSAL---DRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 127773 1674 RCTLMSGEVEELRAALEQAERarkasdnELADANDRVNELTSQVSSVQG 1722
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALA-------QVELLNQQIAALRRQLAALEA 158
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1301-1722 |
8.44e-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: 41.09 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1301 EKSQLSSQLEDARRSLEEETRARSKLQ---NEVRNMHADMDAIREQLEEEQESKSD----VQRQLsKANNEIQQWRskfe 1373
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQyrlVEMARELEELSARESDLEQDYQAASDhlnlVQTAL-RQQEKIERYQ---- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1374 seganrtEELEDqkrkLLGKLSEAEQTTEAANakcsaleKAKSRLQQELEDMSIEVDRANasvNQMEKKQRAFD--KTTA 1451
Cdd:COG3096 354 -------EDLEE----LTERLEEQEEVVEEAA-------EQLAEAEARLEAAEEEVDSLK---SQLADYQQALDvqQTRA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1452 -EWQAKVNSLqselENSQKESRgySAELyrikaSIEEYQDSIGALRRENKNLADEIHDLTDQLSEGgrsthelDKARRRL 1530
Cdd:COG3096 413 iQYQQAVQAL----EKARALCG--LPDL-----TPENAEDYLAAFRAKEQQATEEVLELEQKLSVA-------DAARRQF 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1531 EmekeELQAALEEAEGALEQEEA-KVMRAQLE-------IATVRNEIDKRIQEKEEEFDNtRRNHQRALESMQASLEAEA 1602
Cdd:COG3096 475 E----KAYELVCKIAGEVERSQAwQTARELLRryrsqqaLAQRLQQLRAQLAELEQRLRQ-QQNAERLLEEFCQRIGQQL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1603 KGKADAMRIKKKLEQDINELEVALDASNRGKAEMEKTVKRYQQQIREM----------QTSIEEEQRQRDEARESynmae 1672
Cdd:COG3096 550 DAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELaarapawlaaQDALERLREQSGEALAD----- 624
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 127773 1673 rrctlmSGEVEELRAALEQAERARKASDNELADANDRVNELTSQVSSVQG 1722
Cdd:COG3096 625 ------SQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGG 668
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1046-1183 |
8.48e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.85 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1046 EKAKRKVEQDLKSTQENVEDLERVKRELEEnvRRKEAEISSLNSKLEDEQNLVSQLQRKIKELQARIEELEEELEAERNA 1125
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLL--RERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEER 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 127773 1126 RAKVEKQRAELNRELEELGERLDEAGGATSAQI--ELNKKREAEL-----LKIRRDLEEASLQHE 1183
Cdd:PRK12705 111 EKALSARELELEELEKQLDNELYRVAGLTPEQArkLLLKLLDAELeeekaQRVKKIEEEADLEAE 175
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1520-1738 |
8.51e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1520 THELDKARRRLEMEKEELQAALEEAEGALEQEEAKVMRAQlEIATVRNEIDKRIQEKEEEFdNTRRNHQRALESMQASLE 1599
Cdd:PRK10929 29 TQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAK-QYQQVIDNFPKLSAELRQQL-NNERDEPRSVPPNMSTDA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1600 aeakgkadamrikkkLEQDInelevaLDASNRgkaEMEKTVKRYQQQ--IREMQTSIEEEQRQRDEARESYNMAERRC-T 1676
Cdd:PRK10929 107 ---------------LEQEI------LQVSSQ---LLEKSRQAQQEQdrAREISDSLSQLPQQQTEARRQLNEIERRLqT 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1677 LMSGE--VEELRAALEQAER-ARKASDNELA----DANDRvNELTSQVSSV-QGQKRKLEGDINAMQTDL 1738
Cdd:PRK10929 163 LGTPNtpLAQAQLTALQAESaALKALVDELElaqlSANNR-QELARLRSELaKKRSQQLDAYLQALRNQL 231
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
951-1292 |
8.86e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 951 IGDLENTLQKAEQDKAHKDNQISTLQGEISQQDEHIGKLnkeKKALEEANKKTSDS-LQAEEDkcnhlnklkakLEQALD 1029
Cdd:PRK04863 832 EADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQA---KEGLSALNRLLPRLnLLADET-----------LADRVE 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1030 ELEDNLERekkvrgdVEKAKRkveqDLKSTQENVEDLERVKRELEEnvrrkeaeisslnskleDEQNLvSQLQRKIKELQ 1109
Cdd:PRK04863 898 EIREQLDE-------AEEAKR----FVQQHGNALAQLEPIVSVLQS-----------------DPEQF-EQLKQDYQQAQ 948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1110 ARieeleeeleaERNARAKVekqraelnRELEELGERLDEAGGATSAQIeLNKkrEAELL-KIRRDLEEAslqhEAQISA 1188
Cdd:PRK04863 949 QT----------QRDAKQQA--------FALTEVVQRRAHFSYEDAAEM-LAK--NSDLNeKLRQRLEQA----EQERTR 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1189 LRKKHQDAANEMADQVDQLQKVKSK---LEKDKKDLKREMDDLESQMTHNMKnkgcsekvmKQFESQMSDLNARLEDSQR 1265
Cdd:PRK04863 1004 AREQLRQAQAQLAQYNQVLASLKSSydaKRQMLQELKQELQDLGVPADSGAE---------ERARARRDELHARLSANRS 1074
|
330 340
....*....|....*....|....*..
gi 127773 1266 SINELQSQKSRLQAENSDLTRQLEDAE 1292
Cdd:PRK04863 1075 RRNQLEKQLTFCEAEMDNLTKKLRKLE 1101
|
|
| PRK09793 |
PRK09793 |
methyl-accepting chemotaxis protein IV; |
1620-1882 |
9.47e-03 |
|
methyl-accepting chemotaxis protein IV;
Pssm-ID: 182079 [Multi-domain] Cd Length: 533 Bit Score: 40.83 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1620 NELEVALDASNRGKAEMEKTVKRYQQQIREMQTSIEEEQRQRDEARESYNMAERRCTLMSGEVEELRAALEQ-AERARKA 1698
Cdd:PRK09793 243 NEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQnADNARQA 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1699 SD--NELAD----ANDRVNELTSQVSSVQGQKRKLeGDIN------AMQTDLDEMHgelkgaderckkAMADAARLADEL 1766
Cdd:PRK09793 323 SElaKNAATtaqaGGVQVSTMTHTMQEIATSSQKI-GDIIsvidgiAFQTNILALN------------AAVEAARAGEQG 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1767 RAEQDHSNQVekvrKNLESQvkefqirldeaEASSLKGGKKMIQKLESRVHELEAELDNEQRRHAETQKNMRKADRRLKE 1846
Cdd:PRK09793 390 RGFAVVAGEV----RNLASR-----------SAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGE 454
|
250 260 270
....*....|....*....|....*....|....*.
gi 127773 1847 LAFQADEDRKNQERLQELIDKLNAKIKTFKRQVEEA 1882
Cdd:PRK09793 455 IASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEA 490
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1477-1640 |
9.53e-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: 39.91 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1477 ELYRIKASIEEYQDSIGALRRENKNLADEIHDLTDQLSEGGRSTHELDKARRRLEMEKEELQAALEEAEGALEQ----EE 1552
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1553 AKVMRAQLEIATVRN--------EIDKRIQEKEEEFDNTrrnhQRALESMQASLEAEakgkadamriKKKLEQDINELEV 1624
Cdd:COG1579 91 YEALQKEIESLKRRIsdledeilELMERIEELEEELAEL----EAELAELEAELEEK----------KAELDEELAELEA 156
|
170
....*....|....*.
gi 127773 1625 ALDASNRGKAEMEKTV 1640
Cdd:COG1579 157 ELEELEAEREELAAKI 172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
836-1139 |
9.83e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 836 LLSIARQEEEMKEQLKQMDKMKEDLAKTERIKKELEEQNVTlleqknDLFLQLQTLEDSMGDQEERVEKLIM-------- 907
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA------AALLALLGLGGSLLSLILTIAGVLFlvlgllal 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 908 -------QKADFESQIKELEERLLDEEDAAADLEGIKKKMEADNANLKKDIGDLENTLQKAEQdkahKDNQISTLQGEIS 980
Cdd:COG4717 289 lflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE----LLREAEELEEELQ 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 981 QQDehigkLNKEKKAL-EEANKKTSDSLQAEEDKCNHLNKLKAKLEQALDELEDNLEREKKVRGDVEKAkrKVEQDLKST 1059
Cdd:COG4717 365 LEE-----LEQEIAALlAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEEL 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 127773 1060 QENVEDLERVKRELEENVRRKEAEISSLnskleDEQNLVSQLQRKIKELQARIEELEEELEAERNARAKVEKQRAELNRE 1139
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQL-----EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| |
